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Conserved domains on  [gi|768032625|ref|XP_011543857|]
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ribosomal protein S6 kinase alpha-3 isoform X1 [Homo sapiens]

Protein Classification

ribosomal protein S6 kinase alpha-3( domain architecture ID 10145002)

ribosomal protein S6 kinase alpha-3 is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; contains an N-terminal kinase domain from the AGC family and a C-terminal kinase domain from the CAMK family

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
72-394 0e+00

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: 736.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05582    1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGT 231
Cdd:cd05582   81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 232 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd05582  161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 312 vnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGF 391
Cdd:cd05582  241 ------GAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGF 314

                 ...
gi 768032625 392 SFV 394
Cdd:cd05582  315 SFV 317
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
408-737 0e+00

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: 716.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 408 VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 487
Cdd:cd14176    1 VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 488 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 567
Cdd:cd14176   81 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 647
Cdd:cd14176  161 FGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 648 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPV 727
Cdd:cd14176  241 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPV 320
                        330
                 ....*....|
gi 768032625 728 GRSTLAQRRG 737
Cdd:cd14176  321 GRSTLAQRRG 330
 
Name Accession Description Interval E-value
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
72-394 0e+00

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: 736.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05582    1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGT 231
Cdd:cd05582   81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 232 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd05582  161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 312 vnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGF 391
Cdd:cd05582  241 ------GAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGF 314

                 ...
gi 768032625 392 SFV 394
Cdd:cd05582  315 SFV 317
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
408-737 0e+00

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: 716.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 408 VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 487
Cdd:cd14176    1 VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 488 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 567
Cdd:cd14176   81 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 647
Cdd:cd14176  161 FGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 648 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPV 727
Cdd:cd14176  241 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPV 320
                        330
                 ....*....|
gi 768032625 728 GRSTLAQRRG 737
Cdd:cd14176  321 GRSTLAQRRG 330
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-333 1.91e-104

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 319.86  E-value: 1.91e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625    68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTG---KLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKKAYS 227
Cdd:smart00220  77 EYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR-KETMTMILKAKLGMPQF---LSPEAQSLLRMLF 303
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdISPEAKDLIRKLL 235
                          250       260       270
                   ....*....|....*....|....*....|
gi 768032625   304 KRNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:smart00220 236 VKDPEKRL-----------TAEEALQHPFF 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
428-685 1.91e-98

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 304.45  E-value: 1.91e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDP-----TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKdreriLREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaENGLLM 582
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LDEDGH---VKLADFGLARQLD-PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFSLSGGYWNsVSDTAKDLV 662
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPEWD-ISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 768032625   663 SKMLHVDPHQRLTAALVLRHPWI 685
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
66-391 2.27e-89

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 283.63  E-value: 2.27e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKhKGTG----EYYAIKCLKKrEILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhek 223
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD--- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:PTZ00263 171 RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 304 KRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDpeftaKTPkDSP--GIPPS 381
Cdd:PTZ00263 251 QTDHTKRL------GTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-----KYP-DSPvdRLPPL 318
                        330
                 ....*....|.
gi 768032625 382 ANAHQ-LFRGF 391
Cdd:PTZ00263 319 TAAQQaEFAGF 329
Pkinase pfam00069
Protein kinase domain;
428-685 1.61e-70

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 229.82  E-value: 1.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdknilrEIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYlhaqgvvhrdlkpsnilyvdesgnpesiricdfgfakqlraeNGLL 581
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES------------------------------------------GSSL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLsggyWNSVSDTAKDL 661
Cdd:pfam00069 118 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL----PSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....
gi 768032625  662 VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:pfam00069 194 LKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
68-310 3.61e-64

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 221.81  E-value: 3.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLK-KATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDL---RLGRPVALKVLRpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE-KKA 225
Cdd:COG0515   86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPE-----AQSLLR 300
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDlppalDAIVLR 245
                        250
                 ....*....|
gi 768032625 301 MLFKrNPANR 310
Cdd:COG0515  246 ALAK-DPEER 254
Pkinase pfam00069
Protein kinase domain;
68-333 5.42e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 204.40  E-value: 5.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALdhlhslgiiyrdlkpenilldeeghikltdfglskesiDHEKKAYS 227
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGL--------------------------------------ESGSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLRMLFK 304
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|....*....
gi 768032625  305 RNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:pfam00069 200 KDPSKRL-----------TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
426-737 8.28e-51

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 184.83  E-value: 8.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQ------HPNIITLKDVYDDGKYVYVVT 499
Cdd:COG0515    7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARalarlnHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFAKQLRAEN- 578
Cdd:COG0515   87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRV---KLIDFGIARALGGATl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 ---GLLMtpcYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWNSVS 655
Cdd:COG0515  163 tqtGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---DGDSPAELLRAHLREPPPPPSELRPDLP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQR 735
Cdd:COG0515  237 PALDAIVLRALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 316

                 ..
gi 768032625 736 RG 737
Cdd:COG0515  317 AA 318
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
428-693 7.79e-44

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 161.14  E-value: 7.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQ------HPNIITLKDVYDDGKYVYVVTEL 501
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSilmelsHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKiLRQ---------KFFSereASAVLftitkTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK 572
Cdd:PTZ00263 100 VVGGELFTH-LRKagrfpndvaKFYH---AELVL-----AFEYLHSKDIIYRDLKPENLL-LDNKGH---VKVTDFGFAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENgllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywN 652
Cdd:PTZ00263 167 KVPDRT---FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFF---DDTPFRIYEKILAGRLKFP----N 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTA-----ALVLRHPWI--VHWDQLPQ 693
Cdd:PTZ00263 237 WFDGRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFhgANWDKLYA 284
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
126-270 3.16e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 98.33  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 126 NHPFIVKLhYAFQTEGKL-YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:NF033483  65 SHPNIVSV-YDVGEDGGIpYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKD 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 205 GHIKLTDFG----LSKESIDHEKkaySFCGTVEYMAPE-----VVNRRghtqsADWWSFGVLMFEMLTGTLPFQG 270
Cdd:NF033483 144 GRVKVTDFGiaraLSSTTMTQTN---SVLGTVHYLSPEqarggTVDAR-----SDIYSLGIVLYEMLTGRPPFDG 210
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
479-632 7.23e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 94.09  E-value: 7.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDES 557
Cdd:NF033483  66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKD-YIREHGpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-ITKD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 558 GNpesIRICDFGFAkqlRAENGLLMTpcYTANFV------APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGpdDT 631
Cdd:NF033483 144 GR---VKVTDFGIA---RALSSTTMT--QTNSVLgtvhylSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF-DG--DS 212

                 .
gi 768032625 632 P 632
Cdd:NF033483 213 P 213
 
Name Accession Description Interval E-value
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
72-394 0e+00

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: 736.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05582    1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGT 231
Cdd:cd05582   81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 232 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd05582  161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 312 vnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQLFRGF 391
Cdd:cd05582  241 ------GAGPDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGF 314

                 ...
gi 768032625 392 SFV 394
Cdd:cd05582  315 SFV 317
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
408-737 0e+00

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: 716.03  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 408 VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 487
Cdd:cd14176    1 VGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 488 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 567
Cdd:cd14176   81 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 647
Cdd:cd14176  161 FGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 648 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPV 727
Cdd:cd14176  241 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPV 320
                        330
                 ....*....|
gi 768032625 728 GRSTLAQRRG 737
Cdd:cd14176  321 GRSTLAQRRG 330
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
427-717 0e+00

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: 657.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd14091   81 LLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFGFAKQLRAENGLLMTPCY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKML 666
Cdd:cd14091  161 TANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKML 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 667 HVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALN 717
Cdd:cd14091  241 HVDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVKGAVAATFRAIN 291
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
426-717 0e+00

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: 613.96  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd14175    1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMTPC 585
Cdd:cd14175   81 ELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPESLRICDFGFAKQLRAENGLLMTPC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKM 665
Cdd:cd14175  161 YTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKM 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 666 LHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDApHLVKGAMAATYSALN 717
Cdd:cd14175  241 LHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQDV-QLVKGAMAATYSALN 291
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
424-717 0e+00

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: 606.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14178    1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLMT 583
Cdd:cd14178   81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPESIRICDFGFAKQLRAENGLLMT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVS 663
Cdd:cd14178  161 PCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDIVS 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDApHLVKGAMAATYSALN 717
Cdd:cd14178  241 KMLHVDPHQRLTAPQVLRHPWIVNREYLSQNQLSRQDV-HLVKGAMAATYFALN 293
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
423-717 0e+00

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: 591.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd14177    1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLLM 582
Cdd:cd14177   81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLRGENGLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLV 662
Cdd:cd14177  161 TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALN 717
Cdd:cd14177  241 SHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAPHLVKGAMAATYSALN 295
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
71-395 9.03e-168

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: 485.37  E-value: 9.03e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLkVR---DRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05584    1 LKVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASI-VRnqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd05584   80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNP 307
Cdd:cd05584  160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 308 ANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSP-GIPPSANAHQ 386
Cdd:cd05584  240 SSRL------GSGPGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVDSPdDSTLSESANQ 313

                 ....*....
gi 768032625 387 LFRGFSFVA 395
Cdd:cd05584  314 VFQGFTYVA 322
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
74-333 2.38e-143

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: 420.00  E-value: 2.38e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd05123    1 LGKGSFGKVLLVRKK---DTGKLYAMKVLRKKEIIKRKEVeHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTV 232
Cdd:cd05123   78 GELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 233 EYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLv 312
Cdd:cd05123  158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRL- 236
                        250       260
                 ....*....|....*....|.
gi 768032625 313 npfligaGPDGVEEIKRHSFF 333
Cdd:cd05123  237 -------GSGGAEEIKAHPFF 250
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
68-395 1.16e-126

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: 380.42  E-value: 1.16e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLY 144
Cdd:cd05614    2 FELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALvqKAKTVEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK- 223
Cdd:cd05614   82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKe 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT----MILKAKLGMPQFLSPEAQSL 298
Cdd:cd05614  162 RTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKNTQSevsrRILKCDPPFPSFIGPVARDL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 299 LRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSP-G 377
Cdd:cd05614  242 LQKLLCKDPKKRL------GAGPQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPaG 315
                        330
                 ....*....|....*...
gi 768032625 378 IPPSANahQLFRGFSFVA 395
Cdd:cd05614  316 TPPSGA--RVFQGYSFIA 331
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
72-394 1.75e-125

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: 376.94  E-value: 1.75e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKkisGSDARQLYAMKVLKKATLKVRDRVR-TKMERDILVEVN-HPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05570    1 KVLGKGSFGKVMLAE---RKKTDELYAIKVLKKEVIIEDDDVEcTMTEKRVLALANrHPFLTGLHACFQTEDRLYFVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05570   78 VNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05570  158 GTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPAR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 310 RLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANA--HQL 387
Cdd:cd05570  238 RL------GCGPKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDSDLLTNidQEE 311

                 ....*..
gi 768032625 388 FRGFSFV 394
Cdd:cd05570  312 FRGFSYI 318
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
428-684 3.67e-123

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: 368.34  E-value: 3.67e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEdeemlrREIEILKRL-DHPNIVKLYEVFEDDKNLYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQLRaENGLL 581
Cdd:cd05117   81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP-IKIIDFGLAKIFE-EGEKL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDL 661
Cdd:cd05117  159 KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFY---GETEQELFEKILKGKYSFDSPEWKNVSEEAKDL 235
                        250       260
                 ....*....|....*....|...
gi 768032625 662 VSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd05117  236 IKRLLVVDPKKRLTAAEALNHPW 258
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
73-336 6.22e-121

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: 363.25  E-value: 6.22e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05583    1 VLGTGAYGKVFLVRKVGGHDAGKLYAMKVLKKATIvqKAKTAEHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK-KAYSF 228
Cdd:cd05583   81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENdRAYSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNR--RGHTQSADWWSFGVLMFEMLTGTLPF--QGKD--RKETMTMILKAKLGMPQFLSPEAQSLLRML 302
Cdd:cd05583  161 CGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFtvDGERnsQSEISKRILKSHPPIPKTFSAEAKDFILKL 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 303 FKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTI 336
Cdd:cd05583  241 LEKDPKKRL------GAGPRGAHEIKEHPFFKGL 268
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
72-394 5.97e-118

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: 357.78  E-value: 5.97e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRTKM-ERDILVE-VNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05575    1 KVIGKGSFGKVLLARHK---AEGKLYAVKVLQKKAILKRNEVKHIMaERNVLLKnVKHPFLVGLHYSFQTKDKLYFVLDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05575   78 VNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05575  158 GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 310 RLvnpfliGAGPDGvEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQL-- 387
Cdd:cd05575  238 RL------GSGNDF-LEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVPASVGKSADSVAVSAsv 310
                        330
                 ....*....|...
gi 768032625 388 ------FRGFSFV 394
Cdd:cd05575  311 qeadnaFDGFSYV 323
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
72-395 2.59e-116

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: 353.20  E-value: 2.59e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd05571    1 KVLGKGTFGKVILCRE---KATGELYAIKILKKEVIIAKDEVaHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCG 230
Cdd:cd05571   78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05571  158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 311 LvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQL--- 387
Cdd:cd05571  238 L------GGGPRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESVELTPPDRGDLLGLEEeer 311
                        330
                 ....*....|
gi 768032625 388 --FRGFSFVA 395
Cdd:cd05571  312 phFEQFSYSA 321
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
66-364 2.08e-113

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: 344.56  E-value: 2.08e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKA-TLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05580    1 DDFEFLKTLGTGSFGRVRLVKHK---DSGKYYALKILKKAkIIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidhEKK 224
Cdd:cd05580   78 MVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRV---KDR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFK 304
Cdd:cd05580  155 TYTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLV 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 305 RNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFD 364
Cdd:cd05580  235 VDLTKRL------GNLKNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
68-352 2.69e-111

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: 339.28  E-value: 2.69e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLY 144
Cdd:cd05613    2 FELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIvqKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI-DHEK 223
Cdd:cd05613   82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLlDENE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVN--RRGHTQSADWWSFGVLMFEMLTGTLPF----QGKDRKETMTMILKAKLGMPQFLSPEAQS 297
Cdd:cd05613  162 RAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKD 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 298 LLRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05613  242 IIQRLLMKDPKKRL------GCGPNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
66-393 3.67e-105

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: 325.39  E-value: 3.67e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDK---DTGQVYAMKILRKSDMLKREQIAhVRAERDILADADSPWIVRLHYAFQDEDHLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKK 224
Cdd:cd05573   78 LVMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMNKSGDR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 -----------------------------AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKE 275
Cdd:cd05573  158 esylndsvntlfqdnvlarrrphkqrrvrAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVE 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 276 TMTMIL--KAKLGMP--QFLSPEAQSLLRMLFKRnPANRLvnpfligagpDGVEEIKRHSFFSTIDWNKLyrREIHPPFK 351
Cdd:cd05573  238 TYSKIMnwKESLVFPddPDVSPEAIDLIRRLLCD-PEDRL----------GSAEEIKAHPFFKGIDWENL--RESPPPFV 304
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 352 PATGRPEDTFYFD--PEFTAKTPKDSPGIPPSANAHQL-FRGFSF 393
Cdd:cd05573  305 PELSSPTDTSNFDdfEDDLLLSEYLSNGSPLLGKGKQLaFVGFTF 349
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
72-394 5.72e-105

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: 323.95  E-value: 5.72e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05592    1 KVLGKGSFGKVMLAEL---KGTNQYFAIKALKKDVVLEDDDVECTMiERRVLaLASQHPFLTHLFCTFQTESHLFFVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05592   78 LNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05592  158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 310 RLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSP---GIPPSANAHQ 386
Cdd:cd05592  238 RL------GVPECPAGDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPvdkKLLASMDQEQ 311

                 ....*...
gi 768032625 387 lFRGFSFV 394
Cdd:cd05592  312 -FKGFSFT 318
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
68-333 1.91e-104

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 319.86  E-value: 1.91e-104
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625    68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTG---KLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKKAYS 227
Cdd:smart00220  77 EYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR-KETMTMILKAKLGMPQF---LSPEAQSLLRMLF 303
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdISPEAKDLIRKLL 235
                          250       260       270
                   ....*....|....*....|....*....|
gi 768032625   304 KRNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:smart00220 236 VKDPEKRL-----------TAEEALQHPFF 254
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
432-685 1.89e-102

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: 316.93  E-value: 1.89e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIIdkSKR-DPTEEIEILlRYGQ-HPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd14092   12 EALGDGSFSVCRKCVHKKTGQEFAVKIV--SRRlDTSREVQLL-RLCQgHPNIVKLHEVFQDELHTYLVMELLRGGELLE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKqLRAENGLLMTPCYTAN 589
Cdd:cd14092   89 RIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDAE-IKIVDFGFAR-LKPENQPLKTPCFTLP 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 590 FVAPEVLKR----QGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSK 664
Cdd:cd14092  167 YAAPEVLKQalstQGYDESCDLWSLGVILYTMLSGQVPFqSPSRNESAAEIMKRIKSGDFSFDGEEWKNVSSEAKSLIQG 246
                        250       260
                 ....*....|....*....|.
gi 768032625 665 MLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14092  247 LLTVDPSKRLTMSELRNHPWL 267
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
71-394 4.94e-102

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: 316.26  E-value: 4.94e-102
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKiSGSDarQLYAMKVLKKATLKVRDRVR-TKMERDILVEVNHP-FIVKLHYAFQTEGKLYLILD 148
Cdd:cd05587    1 LMVLGKGSFGKVMLAER-KGTD--ELYAIKILKKDVIIQDDDVEcTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSF 228
Cdd:cd05587   78 YVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPA 308
Cdd:cd05587  158 CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPA 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 309 NRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPP-SANAHQ- 386
Cdd:cd05587  238 KRL------GCGPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLvIMNIDQs 311

                 ....*...
gi 768032625 387 LFRGFSFV 394
Cdd:cd05587  312 EFEGFSFV 319
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
68-395 1.26e-101

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: 315.39  E-value: 1.26e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVN---HPFIVKLHYAFQTEGK 142
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEyKPTG----ELFAIKALKKGDIIARDEVESLMcEKRIFETVNsarHPFLVNLFACFQTPEH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd05589   77 VCFVMEYAAGGDLMMHIHEDV-FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRML 302
Cdd:cd05589  156 DRTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRL 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 303 FKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPP-- 380
Cdd:cd05589  236 LRKNPERRL------GASERDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPPKEPrp 309
                        330
                 ....*....|....*.
gi 768032625 381 -SANAHQLFRGFSFVA 395
Cdd:cd05589  310 lTEEEQALFKDFDYVA 325
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
66-359 2.24e-101

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: 314.56  E-value: 2.24e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05574    1 DHFKKIKLLGKGDVGRVYLVRLKGTG---KLFAMKVLDKEEMIKRNKVkRVLTEREILATLDHPFLPTLYASFQTSTHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK------ 216
Cdd:cd05574   78 FVMDYCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKqssvtp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ----------------ESIDHEKKAY-------SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR 273
Cdd:cd05574  158 ppvrkslrkgsrrssvKSIEKETFVAepsarsnSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 274 KETMTMILKAKLGMPQ--FLSPEAQSLLRMLFKRNPANRLvnpfligAGPDGVEEIKRHSFFSTIDWNKLyrREIHPPFK 351
Cdd:cd05574  238 DETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRL-------GSKRGASEIKRHPFFRGVNWALI--RNMTPPII 308

                 ....*...
gi 768032625 352 PATGRPED 359
Cdd:cd05574  309 PRPDDPID 316
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
72-376 9.49e-100

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: 310.40  E-value: 9.49e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05595    1 KLLGKGTFGKVILVReKATG----RYYAMKILRKEVIIAKDEVaHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05595   77 ANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05595  157 GTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQ 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 310 RLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSP 376
Cdd:cd05595  237 RL------GGGPSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITP 297
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
66-397 5.20e-99

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: 308.39  E-value: 5.20e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKK---DTGHVYAMKKLRKSEMLEKEQVaHVRAERDILAEADNPWVVKLYYSFQDEENLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKK 224
Cdd:cd05599   78 LIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMPQ--FLSPEAQSLLR 300
Cdd:cd05599  157 AYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIE 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 301 MLFKrNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLyrREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPP 380
Cdd:cd05599  237 RLLC-DAEHRL--------GANGVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFDEFEEVDLQIPSSPEAG 305
                        330
                 ....*....|....*..
gi 768032625 381 SANAHQLFRGFSFVAIT 397
Cdd:cd05599  306 KDSKELKSKDWVFIGYT 322
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
428-685 1.91e-98

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 304.45  E-value: 1.91e-98
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDP-----TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKdreriLREIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaENGLLM 582
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL-LDEDGH---VKLADFGLARQLD-PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFSLSGGYWNsVSDTAKDLV 662
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPEWD-ISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 768032625   663 SKMLHVDPHQRLTAALVLRHPWI 685
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
73-393 1.58e-97

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: 304.49  E-value: 1.58e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05585    1 VIGKGSFGKVMQVRK---KDTSRIYALKTIRKAHIVSRSEVtHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGT 231
Cdd:cd05585   78 GGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 232 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRL 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 312 vnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDS--PGIPPSANAHQLFR 389
Cdd:cd05585  238 --------GYNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSvvDDSHLSESVQQQFE 309

                 ....
gi 768032625 390 GFSF 393
Cdd:cd05585  310 GWSY 313
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
72-394 1.92e-96

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: 301.89  E-value: 1.92e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSdarQLYAMKVL-KKATLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDG---KFYAVKVLqKKTILKKKEQNHIMAERNVLLKnLKHPFLVGLHYSFQTSEKLYFVLDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05603   78 VNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05603  158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 310 RLvnpfliGAGPDgVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPP-----SANA 384
Cdd:cd05603  238 RL------GAKAD-FLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSVGRTPdltasSSSS 310
                        330
                 ....*....|
gi 768032625 385 HQLFRGFSFV 394
Cdd:cd05603  311 SSAFLGFSYA 320
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
63-393 1.32e-94

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: 297.70  E-value: 1.32e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  63 ADPSQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVL-KKATLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTE 140
Cdd:cd05602    4 AKPSDFHFLKVIGKGSFGKVLLARHKS---DEKFYAVKVLqKKAILKKKEEKHIMSERNVLLKnVKHPFLVGLHFSFQTT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd05602   81 DKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLR 300
Cdd:cd05602  161 PNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 301 MLFKRNPANRLvnpfligAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPP 380
Cdd:cd05602  241 GLLQKDRTKRL-------GAKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQSP 313
                        330       340
                 ....*....|....*....|.
gi 768032625 381 SA--------NAHQLFRGFSF 393
Cdd:cd05602  314 DSilvtasikEAAEAFLGFSY 334
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
71-393 1.57e-94

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: 296.87  E-value: 1.57e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVK-KISGsdarQLYAMKVL-KKATLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05604    1 LKVIGKGSFGKVLLAKrKRDG----KYYAVKVLqKKVILNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTDKLYFVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd05604   77 DFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNP 307
Cdd:cd05604  157 FCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDR 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 308 ANRLvnpfliGAGPDgVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDS------PGIPPS 381
Cdd:cd05604  237 QLRL------GAKED-FLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSvcvssdYSIVNA 309
                        330
                 ....*....|....
gi 768032625 382 A--NAHQLFRGFSF 393
Cdd:cd05604  310 SvlEADDAFVGFSY 323
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
74-393 2.21e-93

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: 294.09  E-value: 2.21e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgSDARQLYAMKVL-KKATLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05586    1 IGKGTFGQVYQVRK---KDTRRIYAMKVLsKKVIVAKKEVAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05586   78 MSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ-FLSPEAQSLLRMLFKRNP 307
Cdd:cd05586  158 GTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 308 ANRLvnpfliGAgPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIP-------P 380
Cdd:cd05586  238 KHRL------GA-HDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTNASLLNANIVPwaqrpglP 310
                        330       340
                 ....*....|....*....|
gi 768032625 381 SANAHQL-------FRGFSF 393
Cdd:cd05586  311 GATSTPLspsvqanFRGFTF 330
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
66-393 3.02e-93

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: 293.84  E-value: 3.02e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05598    1 SMFEKIKTIGVGAFGEVSLVRKK---DTNALYAMKTLRKKDVLKRNQVaHVKAERDILAEADNEWVVKLYYSFQDKENLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL-SKESIDHEK 223
Cdd:cd05598   78 FVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLcTGFRWTHDS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 K---AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMPQF--LSPEAQ 296
Cdd:cd05598  158 KyylAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLSPEAK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 297 SLLRMLFkRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREihPPFKPATGRPEDTFYFDP---EFTAKTPK 373
Cdd:cd05598  238 DLILRLC-CDAEDRL--------GRNGADEIKAHPFFAGIDWEKLRKQK--APYIPTIRHPTDTSNFDPvdpEKLRSSDE 306
                        330       340
                 ....*....|....*....|...
gi 768032625 374 --DSPGIPPSANAHQ-LFRGFSF 393
Cdd:cd05598  307 epTTPNDPDNGKHPEhAFYEFTF 329
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
60-376 9.76e-93

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: 293.14  E-value: 9.76e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  60 HEKADPSQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAF 137
Cdd:cd05593    9 HKRKTMNDFDYLKLLGKGTFGKVILVReKASG----KYYAMKILKKEVIIAKDEVaHTLTESRVLKNTRHPFLTSLKYSF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE 217
Cdd:cd05593   85 QTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQS 297
Cdd:cd05593  165 GITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKS 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 298 LLRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSP 376
Cdd:cd05593  245 LLSGLLIKDPNKRL------GGGPDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITP 317
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
68-394 2.68e-91

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: 288.44  E-value: 2.68e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKiSGSDarQLYAMKVLKKATLKVRDRVRTKM--ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05616    2 FNFLMVLGKGSFGKVMLAER-KGTD--ELYAVKILKKDVVIQDDDVECTMveKRVLALSGKPPFLTQLHSCFQTMDRLYF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd05616   79 VMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd05616  159 KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTK 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 306 NPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP-ATGRpeDTFYFDPEFTAKTPKDSPgiPPSANA 384
Cdd:cd05616  239 HPGKRL------GCGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPkACGR--NAENFDRFFTRHPPVLTP--PDQEVI 308
                        330
                 ....*....|....
gi 768032625 385 HQL----FRGFSFV 394
Cdd:cd05616  309 RNIdqseFEGFSFV 322
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
68-395 3.23e-91

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: 289.62  E-value: 3.23e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05594   27 FEYLKLLGKGTFGKVILVKeKATG----RYYAMKILKKEVIVAKDEVaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHS-LGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKK 224
Cdd:cd05594  103 VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGAT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFK 304
Cdd:cd05594  183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLK 262
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 305 RNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAK----TPKDSPGIPP 380
Cdd:cd05594  263 KDPKQRL------GGGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQmitiTPPDQDDSME 336
                        330
                 ....*....|....*..
gi 768032625 381 SANAHQL--FRGFSFVA 395
Cdd:cd05594  337 TVDNERRphFPQFSYSA 353
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
76-338 6.49e-91

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: 285.65  E-value: 6.49e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  76 QGSFGKVFLVKKISGSDarqLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 154
Cdd:cd05579    3 RGAYGRVYLAKKKSTGD---LYAIKVIKKRDMIRKNQVdSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 155 LFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK---------------ESI 219
Cdd:cd05579   80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvrrqiklsiqkkSNG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF--LSPEAQS 297
Cdd:cd05579  160 APEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpeVSDEAKD 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 298 LLRMLFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDW 338
Cdd:cd05579  240 LISKLLTPDPEKRL--------GAKGIEEIKNHPFFKGIDW 272
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
72-395 4.54e-90

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: 285.26  E-value: 4.54e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd05590    1 RVLGKGSFGKVMLARlKESG----RLYAVKVLKKDVILQDDDVECTMtEKRILsLARNHPFLTQLYCCFQTPDRLFFVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSF 228
Cdd:cd05590   77 FVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPA 308
Cdd:cd05590  157 CGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPT 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 309 NRLvnpfliGAGPDGVEE-IKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSP---GIPPSANA 384
Cdd:cd05590  237 MRL------GSLTLGGEEaILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPieeSLLPMINQ 310
                        330
                 ....*....|.
gi 768032625 385 HQlFRGFSFVA 395
Cdd:cd05590  311 DE-FRNFSYTA 320
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
74-340 5.77e-90

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: 282.58  E-value: 5.77e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd05572    1 LGVGGFGRVELVQLKSKG---RTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKKAYSFCGTV 232
Cdd:cd05572   78 GELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK-KLGSGRKTWTFCGTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 233 EYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK--ETMTMILKA--KLGMPQFLSPEAQSLLRMLFKRNPA 308
Cdd:cd05572  157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPE 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 309 NRLvnpfliGAGPDGVEEIKRHSFFSTIDWNK 340
Cdd:cd05572  237 ERL------GYLKGGIRDIKKHKWFEGFDWEG 262
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
67-332 7.55e-90

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: 282.06  E-value: 7.55e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLkvrdrVRTKMERDILVEV------NHPFIVKLHYAFQT 139
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAReKKSG----FIVALKVISKSQL-----QKSGLEHQLRREIeiqshlRHPNILRLYGYFED 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd14007   72 KKRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKaySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLL 299
Cdd:cd14007  152 SNRRK--TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLI 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 300 RMLFKRNPANRLvnpfligagpdGVEEIKRHSF 332
Cdd:cd14007  230 SKLLQKDPSKRL-----------SLEQVLNHPW 251
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
66-391 2.27e-89

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 283.63  E-value: 2.27e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVRIAKhKGTG----EYYAIKCLKKrEILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhek 223
Cdd:PTZ00263  94 YFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPD--- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:PTZ00263 171 RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLL 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 304 KRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDpeftaKTPkDSP--GIPPS 381
Cdd:PTZ00263 251 QTDHTKRL------GTLKGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFE-----KYP-DSPvdRLPPL 318
                        330
                 ....*....|.
gi 768032625 382 ANAHQ-LFRGF 391
Cdd:PTZ00263 319 TAAQQaEFAGF 329
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
67-333 1.19e-86

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: 273.75  E-value: 1.19e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05578    1 HFQILRVIGKGSFGKVCIVQK---KDTKKMFAMKYMNKQKCIEKDSVRNVLnELEILQELEHPFLVNLWYSFQDEEDMYM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhEKKA 225
Cdd:cd05578   78 VVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTD-GTLA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK---ETMTMILKAKLGMPQFLSPEAQSLLRML 302
Cdd:cd05578  157 TSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTsieEIRAKFETASVLYPAGWSEEAIDLINKL 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 303 FKRNPANRLVNPfligagpdgvEEIKRHSFF 333
Cdd:cd05578  237 LERDPQKRLGDL----------SDLKNHPYF 257
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
72-394 4.04e-86

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: 274.75  E-value: 4.04e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKiSGSDarQLYAMKVLKKATLKVRDRVRTKM-ERDILV-EVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05591    1 KVLGKGSFGKVMLAER-KGTD--EVYAIKVLKKDVILQDDDVDCTMtEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05591   78 VNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05591  158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 310 RLvnpfliG--AGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANA--H 385
Cdd:cd05591  238 RL------GcvASQGGEDAIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQinQ 311

                 ....*....
gi 768032625 386 QLFRGFSFV 394
Cdd:cd05591  312 EEFRGFSFV 320
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
428-684 9.78e-86

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: 271.31  E-value: 9.78e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEIL--LRygqHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIeekikrEIEIMklLN---HPNIIKLYEVIETENKIYLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaENG 579
Cdd:cd14003   79 EYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL-LDKNGN---LKIIDFGLSNEFR-GGS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGKFSlsggYWNSVSDTA 658
Cdd:cd14003  154 LLKTFCGTPAYAAPEVLLGRKYDGpKADVWSLGVILYAMLTGYLPF-DDDND--SKLFRKILKGKYP----IPSHLSPDA 226
                        250       260
                 ....*....|....*....|....*.
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14003  227 RDLIRRMLVVDPSKRITIEEILNHPW 252
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
66-333 1.23e-84

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: 269.47  E-value: 1.23e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05581    1 NDFKFGKPLGEGSYSTVVLAKEK---ETGKEYAIKVLDKRHIIKEKKVKYvTIEKEVLSRLAHPGIVKLYYTFQDESKLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-------- 216
Cdd:cd05581   78 FVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdssp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 -------ESIDHE--KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGM 287
Cdd:cd05581  158 estkgdaDSQIAYnqARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEF 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 288 PQFLSPEAQSLLRMLFKRNPANRLvnpfliGAGPD-GVEEIKRHSFF 333
Cdd:cd05581  238 PENFPPDAKDLIQKLLVLDPSKRL------GVNENgGYDELKAHPFF 278
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
434-718 1.43e-84

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: 270.37  E-value: 1.43e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKIL 512
Cdd:cd14179   15 LGEGSFSICRKCLHKKTNQEYAVKIVSKRMEANTQrEIAALKLCEGHPNIVKLHEVYHDQLHTFLVMELLKGGELLERIK 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 513 RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQLRAENGLLMTPCYTANFVA 592
Cdd:cd14179   95 KKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE-IKIIDFGFARLKPPDNQPLKTPCFTLHYAA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 593 PEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDD----TPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHV 668
Cdd:cd14179  174 PELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctSAEEIMKKIKQGDFSFEGEAWKNVSQEAKDLIQGLLTV 253
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 669 DPHQRLTAALVLRHPWIVHWDQLPQYQLNRQD----APHLVKGAMAATYSALNR 718
Cdd:cd14179  254 DPNKRIKMSGLRYNEWLQDGSQLSSNPLMTPDilgsSGASVHTCVKATFHAFNK 307
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
67-311 1.65e-84

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: 268.19  E-value: 1.65e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVhKKTG----EEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKEsIDHE 222
Cdd:cd05117   77 VMELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSL 298
Cdd:cd05117  156 EKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDL 235
                        250
                 ....*....|...
gi 768032625 299 LRMLFKRNPANRL 311
Cdd:cd05117  236 IKRLLVVDPKKRL 248
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
67-330 7.77e-84

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: 266.31  E-value: 7.77e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14003    1 NYELGKTLGEGSFGKVKLARhKLTG----EKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESiDHEKKA 225
Cdd:cd14003   77 VMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF-RGGSLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRG-HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFK 304
Cdd:cd14003  156 KTFCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLV 235
                        250       260
                 ....*....|....*....|....*.
gi 768032625 305 RNPANRLvnpfligagpdGVEEIKRH 330
Cdd:cd14003  236 VDPSKRI-----------TIEEILNH 250
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
66-394 2.38e-83

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: 267.94  E-value: 2.38e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKkISGSDarQLYAMKVLKKATLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05619    5 EDFVLHKMLGKGSFGKVFLAE-LKGTN--QFFAIKALKKDVVLMDDDVECTMvEKRVLsLAWEHPFLTHLFCTFQTKENL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd05619   82 FFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd05619  162 KTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLF 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 304 KRNPANRLvnpfligaGPDGveEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSAN 383
Cdd:cd05619  242 VREPERRL--------GVRG--DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSFADRALIN 311
                        330
                 ....*....|...
gi 768032625 384 A--HQLFRGFSFV 394
Cdd:cd05619  312 SmdQNMFRNFSFV 324
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
66-366 6.62e-83

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: 265.45  E-value: 6.62e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKkatlkVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQ 138
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRdRISE----HYYALKVMA-----IPEVIRLKQeqhvhnEKRVLKEVSHPFIIRLFWTEH 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd05612   72 DQRFLYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDhekKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSL 298
Cdd:cd05612  152 RD---RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDL 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 299 LRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFD--PE 366
Cdd:cd05612  229 IKKLLVVDRTRRL------GNMKNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDdyPE 292
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
67-364 8.48e-82

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: 262.34  E-value: 8.48e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGsdaRQLYAMKVL-KKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKET---GNYYAMKILdKQKVVKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHekkA 225
Cdd:cd14209   79 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGR---T 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd14209  156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 306 NPANRLVNpfLIgagpDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFD 364
Cdd:cd14209  236 DLTKRFGN--LK----NGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFD 288
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
72-394 1.58e-81

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: 262.57  E-value: 1.58e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVfLVKKISGSDarQLYAMKVLKKATLKVRDRVRTKM--ERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd05620    1 KVLGKGSFGKV-LLAELKGKG--EYFAVKALKKDVVLIDDDVECTMveKRVLALAWENPFLTHLYCTFQTKEHLFFVMEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd05620   78 LNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd05620  158 GTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 310 RLvnpfligaGPDGveEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDS---PGIPPSANaHQ 386
Cdd:cd05620  238 RL--------GVVG--NIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSysdKNLIDSMD-QS 306

                 ....*...
gi 768032625 387 LFRGFSFV 394
Cdd:cd05620  307 AFAGFSFI 314
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
66-394 4.03e-81

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: 262.24  E-value: 4.03e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKiSGSDarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHP-FIVKLHYAFQTEGKL 143
Cdd:cd05615   10 TDFNFLMVLGKGSFGKVMLAER-KGSD--ELYAIKILKKDVVIQDDDVECTMvEKRVLALQDKPpFLTQLHSCFQTVDRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd05615   87 YFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGV 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd05615  167 TTRTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLM 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 304 KRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPAT-GRPEDTfyFDPEFTAKTPKDSPgiPPS- 381
Cdd:cd05615  247 TKHPAKRL------GCGPEGERDIREHAFFRRIDWDKLENREIQPPFKPKVcGKGAEN--FDKFFTRGQPVLTP--PDQl 316
                        330
                 ....*....|....*.
gi 768032625 382 --ANAHQL-FRGFSFV 394
Cdd:cd05615  317 viANIDQAdFEGFSYV 332
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
72-394 8.08e-80

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: 258.50  E-value: 8.08e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLKVR---DRVRTkmERDIL-VEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05588    1 RVIGRGSYAKVLMVELKK---TKRIYAMKVIKKELVNDDediDWVQT--EKHVFeTASNHPFLVGLHSCFQTESRLFFVI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd05588   76 EFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQ---GKDRKETMT------MILKAKLGMPQFLSPEAQSL 298
Cdd:cd05588  156 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDivgSSDNPDQNTedylfqVILEKPIRIPRSLSVKAASV 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 299 LRMLFKRNPANRLvnpfliGAGPD-GVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPG 377
Cdd:cd05588  236 LKGFLNKNPAERL------GCHPQtGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPD 309
                        330
                 ....*....|....*....
gi 768032625 378 IPPSANA--HQLFRGFSFV 394
Cdd:cd05588  310 DPDVIEKidQSEFEGFEYV 328
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
66-393 1.08e-79

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: 258.05  E-value: 1.08e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKA-TLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKS---TEKVYAMKILNKWeMLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlSKESIDHEK 223
Cdd:cd05597   78 LVMDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SCLKLREDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSF--CGTVEYMAPEVV--NRRGHTQ---SADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMP---QFL 291
Cdd:cd05597  157 TVQSSvaVGTPDYISPEILqaMEDGKGRygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPddeDDV 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 292 SPEAQSLLRMLFKRnPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLyrREIHPPFKPATGRPEDTFYFDPEFTAKT 371
Cdd:cd05597  237 SEEAKDLIRRLICS-RERRL--------GQNGIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFDVDDDDLR 305
                        330       340
                 ....*....|....*....|....*..
gi 768032625 372 PKDSpgIPPSANA----HQL-FRGFSF 393
Cdd:cd05597  306 HTDS--LPPPSNAafsgLHLpFVGFTY 330
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
66-393 5.23e-79

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: 258.42  E-value: 5.23e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05600   11 SDFQILTQVGQGGYGSVFLARK---KDTGEICALKIMKKKVLFKLNEVNhVLTERDILTTTNSPWLVKLLYAFQDPENVY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK- 223
Cdd:cd05600   88 LAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKi 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 ------------------------------------KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLP 267
Cdd:cd05600  168 esmkirleevkntafleltakerrniyramrkedqnYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPP 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 268 FQGKDRKETMTMIL--KAKLGMPQF--------LSPEAQSLLRMLFKrNPANRLVNPfligagpdgvEEIKRHSFFSTID 337
Cdd:cd05600  248 FSGSTPNETWANLYhwKKTLQRPVYtdpdlefnLSDEAWDLITKLIT-DPQDRLQSP----------EQIKNHPFFKNID 316
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 338 WNKLyRREIHPPFKPATGRPEDTFYFDpEFTAKTPKDS-------------PGIPPSANAHQ-LFRGFSF 393
Cdd:cd05600  317 WDRL-REGSKPPFIPELESEIDTSYFD-DFNDEADMAKykdvhekqkslegSGKNGGDNGNRsLFVGFTF 384
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
434-720 8.22e-79

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: 255.18  E-value: 8.22e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKIL 512
Cdd:cd14180   14 LGEGSFSVCRKCRHRQSGQEYAVKIISRRMEANTQrEVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLRGGELLDRIK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 513 RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpESIRICDFGFAKQLRAENGLLMTPCYTANFVA 592
Cdd:cd14180   94 KKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDG-AVLKVIDFGFARLRPQGSRPLQTPCFTLQYAA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 593 PEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPD----DTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHV 668
Cdd:cd14180  173 PELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGkmfhNHAADIMHKIKEGDFSLEGEAWKGVSEEAKDLVRGLLTV 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 669 DPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPH----LVKGAMAATYSALNRNQ 720
Cdd:cd14180  253 DPAKRLKLSELRESDWLQGGSALSSTPLMTPDVLEssgpAVRTGVNATFMAFNRGK 308
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
68-386 1.54e-78

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: 256.70  E-value: 1.54e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05629    3 FHTVKVIGKGAFGEVRLVQKK---DTGKIYAMKTLLKSEMFKKDQLaHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS----------- 215
Cdd:cd05629   80 MEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsay 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 -------------------------------KESIDHEKK-----AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMF 259
Cdd:cd05629  160 yqkllqgksnknridnrnsvavdsinltmssKDQIATWKKnrrlmAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 260 EMLTGTLPFQGKDRKETMTMIL--KAKLGMPQ--FLSPEAQSLLRMLFKrNPANRLvnpfligaGPDGVEEIKRHSFFST 335
Cdd:cd05629  240 ECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRRLIT-NAENRL--------GRGGAHEIKSHPFFRG 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 336 IDWNKLyrREIHPPFKPATGRPEDTFYFDPEFTAKTPkDSPGIPPSANAHQ 386
Cdd:cd05629  311 VDWDTI--RQIRAPFIPQLKSITDTSYFPTDELEQVP-EAPALKQAAPAQQ 358
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
68-394 3.26e-78

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: 254.16  E-value: 3.26e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDarqLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGD---IYAMKVLKKsETLAQEEVSFFEEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlSKESIDHEKKA 225
Cdd:cd05601   80 MEYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG-SAAKLSSDKTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSF--CGTVEYMAPEV---VNRRG---HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMPQ--FLSP 293
Cdd:cd05601  159 TSKmpVGTPDYIAPEVltsMNGGSkgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPEdpKVSE 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 294 EAQSLLRMLFKrNPANRLvnpfligagpdGVEEIKRHSFFSTIDWNKLyrREIHPPFKPATGRPEDTFYFDpEFTAKtpK 373
Cdd:cd05601  239 SAVDLIKGLLT-DAKERL-----------GYEGLCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFD-EFEPK--K 301
                        330       340
                 ....*....|....*....|....*..
gi 768032625 374 DSPGIPPSANAHQL------FRGFSFV 394
Cdd:cd05601  302 TRPSYENFNKSKGFsgkdlpFVGFTFT 328
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
428-684 4.15e-78

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: 251.48  E-value: 4.15e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmienEVAILRRV-KHPNIVQLIEEYDTDTELYLVMELV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRaenGLLM 582
Cdd:cd14095   81 KGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLKLADFGLATEVK---EPLF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLV 662
Cdd:cd14095  158 TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFR-SPDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14095  237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
424-684 4.93e-76

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: 246.50  E-value: 4.93e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------------EIEILLRYGQHPNIITLKDVYDD 491
Cdd:cd14093    1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSEneaeelreatrrEIEILRQVSGHPNIIELHDVFES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 492 GKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFA 571
Cdd:cd14093   81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENIL-LDDNLN---VKISDFGFA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLrAENGLLMTPCYTANFVAPEVLKRQ------GYDAACDIWSLGVLLYTMLTGYTPFANGPDDTpeeILARIGSGKFS 645
Cdd:cd14093  157 TRL-DEGEKLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMV---MLRNIMEGKYE 232
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 646 LSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14093  233 FGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
425-684 1.84e-75

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: 244.59  E-value: 1.84e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK---SKRDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14083    2 RDKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKkalKGKEDSLENEIaVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQlrAENGL 580
Cdd:cd14083   82 LVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPDEDSK-IMISDFGLSKM--EDSGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKD 660
Cdd:cd14083  159 MSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFY---DENDSKLFAQILKAEYEFDSPYWDDISDSAKD 235
                        250       260
                 ....*....|....*....|....
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14083  236 FIRHLMEKDPNKRYTCEQALEHPW 259
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
74-352 1.43e-73

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: 240.12  E-value: 1.43e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd05577    1 LGRGGFGEVCACQV---KATGKMYACKKLDKKRIKKKKGETMALnEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKKAYSFCG 230
Cdd:cd05577   78 GDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQ----GKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd05577  157 THGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRqrkeKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 306 NPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05577  237 DPERRL------GCRGGSADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
71-339 2.63e-73

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: 238.92  E-value: 2.63e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKISGSDarqLYAMKVLKKATLKVRDRVR-TKMERDIL-VEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd05611    1 LKPISKGAFGSVYLAKKRSTGD---YFAIKVLKKSDMIAKNQVTnVKAERAIMmIQGESPYVAKLYYSFQSKDYLYLVME 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID--HEKKay 226
Cdd:cd05611   78 YLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEkrHNKK-- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 sFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRML 302
Cdd:cd05611  156 -FVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRL 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 303 FKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWN 339
Cdd:cd05611  235 LCMDPAKRL--------GANGYQEIKSHPFFKSINWD 263
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
65-394 3.22e-73

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: 241.90  E-value: 3.22e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05596   25 AEDFDVIKVIGRGAFGEVQLVRH---KSTKKVYAMKLLSKfEMIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKeVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG----LSKESI 219
Cdd:cd05596  102 YMVMDYMPGGDLVNLMSN-YDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGtcmkMDKDGL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAysfCGTVEYMAPEVVNRRGHT----QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMP--QFL 291
Cdd:cd05596  181 VRSDTA---VGTPDYISPEVLKSQGGDgvygRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhKNSLQFPddVEI 257
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 292 SPEAQSLLRMlFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKT 371
Cdd:cd05596  258 SKDAKSLICA-FLTDREVRL--------GRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDDIEEDET 328
                        330       340
                 ....*....|....*....|....
gi 768032625 372 PKDSPGIPPSANAHQL-FRGFSFV 394
Cdd:cd05596  329 PEETFPVPKAFVGNHLpFVGFTYS 352
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
73-352 3.86e-73

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: 238.88  E-value: 3.86e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNH----PFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05606    1 IIGRGGFGEVYGCRK---ADTGKMYAMKCLDKKRIKMKQGETLALnERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFIL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidHEKKAYS 227
Cdd:cd05606   78 DLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF--SKKKPHA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGTLPF---QGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd05606  156 SVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 304 KRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05606  236 QRDVSKRL------GCLGRGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
428-684 2.41e-72

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: 236.42  E-value: 2.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEV-KEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRdpteEIEILLRYGQHPNIITLKDVY----DDGKYVYVVT 499
Cdd:cd14089    2 YTIsKQVLGLGINGKVLECFHKKTGEKFALKVLrdnPKARR----EVELHWRASGCPHIVRIIDVYentyQGRKCLLVVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnPESI-RICDFGFAKQLRA 576
Cdd:cd14089   78 ECMEGGELFSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKG--PNAIlKLTDFGFAKETTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 eNGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF--ANGPDDTPeEILARIGSGKFSLSGGYWNSV 654
Cdd:cd14089  156 -KKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFysNHGLAISP-GMKKRIRNGQYEFPNPEWSNV 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 655 SDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14089  234 SEEAKDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
426-685 3.07e-72

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: 236.93  E-value: 3.07e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDI-GVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14090    1 DLYKLTGELlGEGAYASVQTCINLYTGKEYAVKIIEKhpghSRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAENGL 580
Cdd:cd14090   81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENIL-CESMDKVSPVKICDFDLGSGIKLSSTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 --------LMTPCYTANFVAPEVL-----KRQGYDAACDIWSLGVLLYTMLTGYTPFAN--GPD----------DTPEEI 635
Cdd:cd14090  160 mtpvttpeLLTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGrcGEDcgwdrgeacqDCQELL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 636 LARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14090  240 FHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
68-352 2.47e-71

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: 234.56  E-value: 2.47e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRD-RVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQvRATG----KMYACKKLEKKRIKKRKgEAMALNEKQILEKVNSRFVVSLAYAYETKDALCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd05605   78 VLTIMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK----DRKETMTMILKAKLGMPQFLSPEAQSLL 299
Cdd:cd05605  157 TIRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKEDQEEYSEKFSEEAKSIC 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 300 RMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05605  237 SQLLQKDPKTRL------GCRGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
Pkinase pfam00069
Protein kinase domain;
428-685 1.61e-70

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 229.82  E-value: 1.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdknilrEIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYlhaqgvvhrdlkpsnilyvdesgnpesiricdfgfakqlraeNGLL 581
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES------------------------------------------GSSL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLsggyWNSVSDTAKDL 661
Cdd:pfam00069 118 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL----PSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....
gi 768032625  662 VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:pfam00069 194 LKKLLKKDPSKRLTATQALQHPWF 217
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
67-316 3.37e-70

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 230.43  E-value: 3.37e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDG---KLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRL----SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd08215   78 MEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG-MPQFLSPEAQSLLRM 301
Cdd:cd08215  158 DLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNS 237
                        250       260
                 ....*....|....*....|.
gi 768032625 302 LFKRNPANR------LVNPFL 316
Cdd:cd08215  238 MLQKDPEKRpsaneiLSSPFI 258
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
68-394 3.81e-70

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: 233.76  E-value: 3.81e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKkISGSDarQLYAMKVLKKATLKVRDRVR-TKMERDILVEVN-HPFIVKLHYAFQTEGKLYL 145
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVR-LKKND--QIYAMKVVKKELVHDDEDIDwVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT-------MILKAKLGMPQFLSPEAQSL 298
Cdd:cd05617  174 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNtedylfqVILEKPIRIPRFLSVKASHV 253
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 299 LRMLFKRNPANRLVNPFligagPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAK----TPKD 374
Cdd:cd05617  254 LKGFLNKDPKERLGCQP-----QTGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEpvqlTPDD 328
                        330       340
                 ....*....|....*....|
gi 768032625 375 SPGIPPSANAHqlFRGFSFV 394
Cdd:cd05617  329 EDVIKRIDQSE--FEGFEYI 346
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
67-338 4.50e-70

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: 230.76  E-value: 4.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRH---RETRQRFAMKKINKQNLILRNQIqQVFVERDILTFAENPFVVSMYCSFETKRHLCM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--------- 216
Cdd:cd05609   78 VMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmslttn 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ---ESIDHEKKAYS---FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ- 289
Cdd:cd05609  158 lyeGHIEKDTREFLdkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEg 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 290 --FLSPEAQSLLRMLFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDW 338
Cdd:cd05609  238 ddALPDDAQDLITRLLQQNPLERL--------GTGGAEEVKQHPFFQDLDW 280
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
426-701 5.55e-69

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: 228.46  E-value: 5.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDkSKRDPTEEIEILLRYG------QHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIIN-TKKLSARDHQKLEREAricrllKHPNIVRLHDSISEEGFHYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPeSIRICDFGFAKQLRAEN- 578
Cdd:cd14086   80 DLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGA-AVKLADFGLAIEVQGDQq 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 ---GLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVS 655
Cdd:cd14086  159 awfGFAGTPGY----LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFW---DEDQHRLYAQIKAGAYDYPSPEWDTVT 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQlPQYQLNRQDA 701
Cdd:cd14086  232 PEAKDLINQMLTVNPAKRITAAEALKHPWICQRDR-VASMVHRQET 276
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
428-686 1.62e-68

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: 225.82  E-value: 1.62e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-RDPTE------EIEI--LLRygqHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlQKSGLehqlrrEIEIqsHLR---HPNILRLYGYFEDKKRIYLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQlrAEN 578
Cdd:cd14007   79 LEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENIL-LGSNGE---LKLADFGWSVH--APS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSlsggYWNSVSDTA 658
Cdd:cd14007  153 NRRKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFE---SKSHQETYKRIQNVDIK----FPSSVSPEA 225
                        250       260
                 ....*....|....*....|....*...
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd14007  226 KDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
68-394 2.75e-68

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: 229.15  E-value: 2.75e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVR-TKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05618   22 FDLLRVIGRGSYAKVLLVRL---KKTERIYAMKVVKKELVNDDEDIDwVQTEKHVFEQAsNHPFLVGLHSCFQTESRLFF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd05618   99 VIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQ---GKDRKETMT------MILKAKLGMPQFLSPEAQ 296
Cdd:cd05618  179 STFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDivgSSDNPDQNTedylfqVILEKQIRIPRSLSVKAA 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 297 SLLRMLFKRNPANRLvnpfliGAGPD-GVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAK----T 371
Cdd:cd05618  259 SVLKSFLNKDPKERL------GCHPQtGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEpvqlT 332
                        330       340
                 ....*....|....*....|...
gi 768032625 372 PKDSPGIPPSANAHqlFRGFSFV 394
Cdd:cd05618  333 PDDDDIVRKIDQSE--FEGFEYI 353
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
434-684 5.86e-68

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: 224.07  E-value: 5.86e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDK 510
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIpkrDKKKEAVLREISIL-NQLQHPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 511 ILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAEnGLLMTPCYTANF 590
Cdd:cd14006   80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSP--QIKIIDFGLARKLNPG-EELKEIFGTPEF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 591 VAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDP 670
Cdd:cd14006  157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFL---GEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEP 233
                        250
                 ....*....|....
gi 768032625 671 HQRLTAALVLRHPW 684
Cdd:cd14006  234 RKRPTAQEALQHPW 247
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
428-685 7.20e-68

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: 224.33  E-value: 7.20e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKsKRDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET-KCRGREVCESelnVLRRVRHTNIIQLIEVFETKERVYMVMELATG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDeSGNPESIRICDFGFAKQLR-AENGLLMT 583
Cdd:cd14087   82 GELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYH-PGPDSKIMITDFGLASTRKkGPNCLMKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVS 663
Cdd:cd14087  161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPF---DDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFID 237
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14087  238 RLLTVNPGERLSATQALKHPWI 259
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
423-685 1.19e-67

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: 224.19  E-value: 1.19e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK------------RDPTEEIEILLRYgQHPNIITLKDVYD 490
Cdd:cd14084    3 ELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrreinkpRNIETEIEILKKL-SHPCIIKIEDFFD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPeSIRICDFGF 570
Cdd:cd14084   82 AEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEC-LIKITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLrAENGLLMTPCYTANFVAPEVLK---RQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFSLS 647
Cdd:cd14084  161 SKIL-GETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSE--EYTQMSLKEQILSGKYTFI 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 648 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14084  238 PKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
66-377 2.00e-67

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: 227.20  E-value: 2.00e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05626    1 SMFVKIKTLGIGAFGEVCLACKV---DTHALYAMKTLRKKDVLNRNQVaHVKAERDILAEADNEWVVKLYYSFQDKDNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL---------- 214
Cdd:cd05626   78 FVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthns 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 ------------SKESID------------------------HEK-KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVL 257
Cdd:cd05626  158 kyyqkgshirqdSMEPSDlwddvsncrcgdrlktleqratkqHQRcLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 258 MFEMLTGTLPFQGKDRKETMTMIL--KAKLGMPQ--FLSPEAQSLLRMLFKrNPANRLvnpfligaGPDGVEEIKRHSFF 333
Cdd:cd05626  238 LFEMLVGQPPFLAPTPTETQLKVInwENTLHIPPqvKLSPEAVDLITKLCC-SAEERL--------GRNGADDIKAHPFF 308
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 768032625 334 STIDWNKLYRREiHPPFKPATGRPEDTFYFDPEFTAKTPKDSPG 377
Cdd:cd05626  309 SEVDFSSDIRTQ-PAPYVPKISHPMDTSNFDPVEEESPWNDASG 351
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
428-684 2.23e-67

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: 222.90  E-value: 2.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI---EILL-RYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14185    2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMiesEILIiKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLraeNGLLMT 583
Cdd:cd14185   82 GGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYV---TGPIFT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVS 663
Cdd:cd14185  159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPF-RSPERDQEELFQIIQLGHYEFLPPYWDNISEAAKDLIS 237
                        250       260
                 ....*....|....*....|.
gi 768032625 664 KMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14185  238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
428-685 6.42e-67

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: 222.56  E-value: 6.42e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPlsRDSSLENEIaVLKRIKHENIVTLEDIYESTTHYYLVMQLVSG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQlrAENGLLMTP 584
Cdd:cd14166   85 GELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDENSK-IMITDFGLSKM--EQNGIMSTA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSK 664
Cdd:cd14166  162 CGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY---EETESRLFEKIKEGYYEFESPFWDDISESAKDFIRH 238
                        250       260
                 ....*....|....*....|.
gi 768032625 665 MLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14166  239 LLEKNPSKRYTCEKALSHPWI 259
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
426-684 6.71e-66

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: 219.13  E-value: 6.71e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14184    1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKccgKEHLIENEVsILRRVKHPNIIMLIEEMDTPAELYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLraeNGLL 581
Cdd:cd14184   81 VKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVV---EGPL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDL 661
Cdd:cd14184  158 YTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF-RSENNLQEDLFDQILLGKLEFPSPYWDNITDSAKEL 236
                        250       260
                 ....*....|....*....|...
gi 768032625 662 VSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14184  237 ISHMLQVNVEARYTAEQILSHPW 259
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
425-685 1.21e-65

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: 219.26  E-value: 1.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEV--KEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEeIEILLRYGQHPNIITLKDVYDDG---------- 492
Cdd:cd14171    3 LEEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKILLDRPKARTE-VRLHMMCSGHPNIVQIYDVYANSvqfpgesspr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 493 KYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAK 572
Cdd:cd14171   82 ARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDAP-IKLCDFGFAK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 qlrAENGLLMTPCYTANFVAPEVLKRQ-----------------GYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDT-PE 633
Cdd:cd14171  161 ---VDQGDLMTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFySEHPSRTiTK 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 634 EILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14171  238 DMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
66-365 3.40e-65

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: 221.46  E-value: 3.40e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05625    1 SMFVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVaHVKAERDILAEADNEWVVRLYYSFQDKDNLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-------- 216
Cdd:cd05625   78 FVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTgfrwthds 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ---ESIDHEKK------------------------------------AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVL 257
Cdd:cd05625  158 kyyQSGDHLRQdsmdfsnewgdpencrcgdrlkplerraarqhqrclAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 258 MFEMLTGTLPFQGKDRKETMTMILKAKLGM---PQF-LSPEAQSLLRMLFkRNPANRLvnpfligaGPDGVEEIKRHSFF 333
Cdd:cd05625  238 LFEMLVGQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEASDLIIKLC-RGPEDRL--------GKNGADEIKAHPFF 308
                        330       340       350
                 ....*....|....*....|....*....|..
gi 768032625 334 STIDWNKLYRREiHPPFKPATGRPEDTFYFDP 365
Cdd:cd05625  309 KTIDFSSDLRQQ-SAPYIPKITHPTDTSNFDP 339
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
424-711 4.14e-65

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: 218.16  E-value: 4.14e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14085    1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTvdKKIVRTEIGVLLRL-SHPNIIKLKEIFETPTEISLVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnPES-IRICDFGFAKQLraENGL 580
Cdd:cd14085   80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPA--PDApLKIADFGLSKIV--DQQV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LM-TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14085  156 TMkTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYD--ERGDQYMFKRILNCDYDFVSPWWDDVSLNAK 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI-------VHWDQlPQYQLNRQDAPHLVKGAMAA 711
Cdd:cd14085  234 DLVKKLIVLDPKKRLTTQQALQHPWVtgkaanfAHMDT-AQKKLQEFNARRKLKAAVKA 291
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
68-402 6.33e-65

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: 221.42  E-value: 6.33e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05624   74 FEIIKVIGRGAFGEVAVVKM---KNTERIYAMKILNKwEMLKRAETACFREERNVLVNGDCQWITTLHYAFQDENYLYLV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS-KESIDHEKK 224
Cdd:cd05624  151 MDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSClKMNDDGTVQ 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRR-----GHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMPQFL---SPE 294
Cdd:cd05624  231 SSVAVGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhEERFQFPSHVtdvSEE 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 295 AQSLL-RMLFKRNpaNRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLyrREIHPPFKPATGRPEDTFYFDPEftAKTPK 373
Cdd:cd05624  311 AKDLIqRLICSRE--RRL--------GQNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTSNFDVD--DDVLR 376
                        330       340       350
                 ....*....|....*....|....*....|.
gi 768032625 374 DSPGIPPSanAHQLFRGF--SFVAITSDDES 402
Cdd:cd05624  377 NPEILPPS--SHTGFSGLhlPFVGFTYTTES 405
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
426-685 1.30e-64

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: 215.66  E-value: 1.30e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE---EIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14167    3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKEtsiENEIaVLHKIKHPNIVALDDIYESGGHLYLIMQL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY--VDESgnpESIRICDFGFAKqLRAENG 579
Cdd:cd14167   83 VSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYysLDED---SKIMISDFGLSK-IEGSGS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14167  159 VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY---DENDAKLFEQILKAEYEFDSPYWDDISDSAK 235
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14167  236 DFIQHLMEKDPEKRFTCEQALQHPWI 261
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
68-310 3.61e-64

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 221.81  E-value: 3.61e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLK-KATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:COG0515    9 YRILRLLGRGGMGVVYLARDL---RLGRPVALKVLRpELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE-KKA 225
Cdd:COG0515   86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPE-----AQSLLR 300
Cdd:COG0515  166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDlppalDAIVLR 245
                        250
                 ....*....|
gi 768032625 301 MLFKrNPANR 310
Cdd:COG0515  246 ALAK-DPEER 254
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
68-393 1.24e-63

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: 216.85  E-value: 1.24e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05627    4 FESLKVIGRGAFGEVRLVQK---KDTGHIYAMKILRKADMLEKEQVaHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL------------ 214
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkkahrtef 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 ------------------SKESIDHEKK-----AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK 271
Cdd:cd05627  161 yrnlthnppsdfsfqnmnSKRKAETWKKnrrqlAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 272 DRKETMTMILKAKLGM---PQFLSPEAQSLLRMLFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREIHP 348
Cdd:cd05627  241 TPQETYRKVMNWKETLvfpPEVPISEKAKDLILRFCTDAENRI--------GSNGVEEIKSHPFFEGVDWEHIRERPAAI 312
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 349 PFKPATgrPEDTFYFD--PEFTAKTPKDSPGIPPSANAHQLFRGFSF 393
Cdd:cd05627  313 PIEIKS--IDDTSNFDdfPESDILQPAPNTTEPDYKSKDWVFLNYTY 357
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
66-408 2.58e-63

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: 215.31  E-value: 2.58e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEV----NHPFIVKLHYAFQTEG 141
Cdd:cd05633    5 NDFSVHRIIGRGGFGEVYGCRK---ADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidH 221
Cdd:cd05633   82 KLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDF--S 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGTLPF---QGKDRKETMTMILKAKLGMPQFLSPEAQS 297
Cdd:cd05633  160 KKKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSFSPELKS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 298 LLRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDpeFTAKTPKDSPG 377
Cdd:cd05633  240 LLEGLLQRDVSKRL------GCHGRGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFD--IGSFDEEDTKG 311
                        330       340       350
                 ....*....|....*....|....*....|.
gi 768032625 378 IPPSANAHQLFRGFSFVaITSDDESQAMQTV 408
Cdd:cd05633  312 IKLLDSDQELYKNFPLV-ISERWQQEVAETV 341
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
67-370 6.04e-63

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: 214.36  E-value: 6.04e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05610    5 EFVIVKPISRGAFGKVYLGRK---KNNSKLYAVKVVKKADMINKNMVhQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE--- 222
Cdd:cd05610   82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRElnm 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 ------------KKAYS--------------------------------------FCGTVEYMAPEVVNRRGHTQSADWW 252
Cdd:cd05610  162 mdilttpsmakpKNDYSrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWW 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 253 SFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP---QFLSPEAQSLLRMLFKRNPANRlvnpfligagpDGVEEIKR 329
Cdd:cd05610  242 ALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKR-----------AGLKELKQ 310
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 768032625 330 HSFFSTIDWNKLYRREihPPFKPATGRPEDTFYFDPEFTAK 370
Cdd:cd05610  311 HPLFHGVDWENLQNQT--MPFIPQPDDETDTSYFEARNNAQ 349
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
68-395 7.64e-63

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: 216.03  E-value: 7.64e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05623   74 FEILKVIGRGAFGEVAVVKL---KNADKVFAMKILNKwEMLKRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS-KESIDHEKK 224
Cdd:cd05623  151 MDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSClKLMEDGTVQ 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVN-----RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL--KAKLGMPQFL---SPE 294
Cdd:cd05623  231 SSVAVGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKERFQFPTQVtdvSEN 310
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 295 AQSLLRMLFKRNpANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLyrREIHPPFKPATGRPEDTFYFDPEftAKTPKD 374
Cdd:cd05623  311 AKDLIRRLICSR-EHRL--------GQNGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSNFDVD--DDCLKN 377
                        330       340
                 ....*....|....*....|....*.
gi 768032625 375 SPGIPPSANA-----HQLFRGFSFVA 395
Cdd:cd05623  378 CETMPPPTHTafsghHLPFVGFTYTS 403
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
67-332 1.05e-62

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: 210.34  E-value: 1.05e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDArqlYAMKVLKKATLkVRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGES---VAIKIIDKEQV-AREGMVEQIKREIAImkLLRHPNIVELHEVMATKTKIF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS--KESIDHE 222
Cdd:cd14663   77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRM 301
Cdd:cd14663  157 GLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKR 236
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 302 LFKRNPANRLVnpfligagpdgVEEIKRHSF 332
Cdd:cd14663  237 ILDPNPSTRIT-----------VEQIMASPW 256
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
424-684 1.22e-62

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: 210.93  E-value: 1.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID------------KSKRDPT-EEIEILLRYGQHPNIITLKDVYD 490
Cdd:cd14182    1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgggsfspeevQELREATlKEIDILRKVSGHPNIIQLKDTYE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGF 570
Cdd:cd14182   81 TNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM----NIKLTDFGF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLrAENGLLMTPCYTANFVAPEVLK------RQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTpeeILARIGSGKF 644
Cdd:cd14182  157 SCQL-DPGEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQML---MLRMIMSGNY 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 645 SLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14182  233 QFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPF 272
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
68-391 9.94e-62

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: 209.90  E-value: 9.94e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEV----NHPFIVKLHYAFQTEGKL 143
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRK---ADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidHEK 223
Cdd:cd14223   79 SFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDF--SKK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRR-GHTQSADWWSFGVLMFEMLTGTLPF---QGKDRKETMTMILKAKLGMPQFLSPEAQSLL 299
Cdd:cd14223  157 KPHASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 300 RMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDpeFTAKTPKDSPGIP 379
Cdd:cd14223  237 EGLLQRDVNRRL------GCMGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPPRGEVNAADAFD--IGSFDEEDTKGIK 308
                        330
                 ....*....|..
gi 768032625 380 PSANAHQLFRGF 391
Cdd:cd14223  309 LLESDQELYRNF 320
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
423-684 1.32e-61

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: 208.29  E-value: 1.32e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-----------KSKRDPT-EEIEILLRYGQHPNIITLKDVYD 490
Cdd:cd14181    7 EFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeqlEEVRSSTlKEIHILRQVSGHPSIITLIDSYE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGF 570
Cdd:cd14181   87 SSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENIL-LDDQLH---IKLSDFGF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLRAeNGLLMTPCYTANFVAPEVLK------RQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTpeeILARIGSGKF 644
Cdd:cd14181  163 SCHLEP-GEKLRELCGTPGYLAPEILKcsmdetHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQML---MLRMIMEGRY 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 645 SLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14181  239 QFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
425-685 1.37e-61

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: 207.93  E-value: 1.37e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-----EIEILLRYgQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14183    5 SERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmiqnEVSILRRV-KHPNIVLLIEEMDMPTELYLVM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLraeNG 579
Cdd:cd14183   84 ELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATVV---DG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTpEEILARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14183  161 PLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQ-EVLFDQILMGQVDFPSPYWDNVSDSAK 239
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14183  240 ELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
427-685 1.77e-61

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: 208.44  E-value: 1.77e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEF-AVKIIDK-----------SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKY 494
Cdd:cd14096    2 NYRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRKadlssdnlkgsSRANILKEVQIMKRL-SHPNIVKLLDFQESDEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY--------------------- 553
Cdd:cd14096   81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkadddetk 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 554 VDE--------SGNPESIRICDFGFAKQLRAENglLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFA 625
Cdd:cd14096  161 VDEgefipgvgGGGIGIVKLADFGLSKQVWDSN--TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFY 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 626 ngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14096  239 ---DESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
428-685 1.82e-61

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: 207.11  E-value: 1.82e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-----EIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14081    3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvlmkvEREIaIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKqLRAENGLL 581
Cdd:cd14081   83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLL-LDEKNN---IKIADFGMAS-LQPEGSLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYD-AACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSggywNSVSDTAKD 660
Cdd:cd14081  158 ETSCGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPF---DDDNLRQLLEKVKRGVFHIP----HFISPDAQD 230
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14081  231 LLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
72-333 2.91e-61

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: 206.64  E-value: 2.91e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKvRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd14099    7 KFLGKGGFAKCYEVTDMSTG---KVYAGKVVPKSSLT-KPKQREKLKSEIKIhrSLKHPNIVKFHDCFEDEENVYILLEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS-KESIDHEKKaYSF 228
Cdd:cd14099   83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAaRLEYDGERK-KTL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFL--SPEAQSLLRMLFKR 305
Cdd:cd14099  162 CGTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQP 241
                        250       260
                 ....*....|....*....|....*...
gi 768032625 306 NPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14099  242 DPTKRPS-----------LDEILSHPFF 258
Pkinase pfam00069
Protein kinase domain;
68-333 5.42e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 204.40  E-value: 5.42e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALdhlhslgiiyrdlkpenilldeeghikltdfglskesiDHEKKAYS 227
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGL--------------------------------------ESGSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLRMLFK 304
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|....*....
gi 768032625  305 RNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:pfam00069 200 KDPSKRL-----------TATQALQHPWF 217
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
68-352 9.57e-61

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: 206.03  E-value: 9.57e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQvRATG----KMYACKKLEKKRIKKRKGEAMALnEKQILEKVNSRFVVSLAYAYETKDALCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd05630   78 VLTLMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK----ETMTMILKAKLGMPQFLSPEAQSLL 299
Cdd:cd05630  157 TIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKikreEVERLVKEVPEEYSEKFSPQARSLC 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 300 RMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05630  237 SMLLCKDPAERL------GCRGGGAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
68-382 1.25e-60

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: 208.74  E-value: 1.25e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05628    3 FESLKVIGRGAFGEVRLVQK---KDTGHVYAMKILRKADMLEKEQVgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL------------ 214
Cdd:cd05628   80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkahrtef 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 ------------------SKESIDHEKK-----AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK 271
Cdd:cd05628  160 yrnlnhslpsdftfqnmnSKRKAETWKRnrrqlAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 272 DRKETMTMILKAKLGM---PQFLSPEAQSLLRMLFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREIHP 348
Cdd:cd05628  240 TPQETYKKVMNWKETLifpPEVPISEKAKDLILRFCCEWEHRI--------GAPGVEEIKTNPFFEGVDWEHIRERPAAI 311
                        330       340       350
                 ....*....|....*....|....*....|....
gi 768032625 349 PFKPATgrPEDTFYFDpEFtaktpKDSPGIPPSA 382
Cdd:cd05628  312 PIEIKS--IDDTSNFD-EF-----PDSDILKPSV 337
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
74-310 1.66e-60

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: 202.89  E-value: 1.66e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd00180    1 LGKGSFGKVYKARdKETG----KKVAVKVIPKEKLK-KLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ESIDHEKKAYSFC 229
Cdd:cd00180   76 GSLKDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMltgtlpfqgkdrketmtmilkaklgmpqflsPEAQSLLRMLFKRNPAN 309
Cdd:cd00180  156 TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKK 204

                 .
gi 768032625 310 R 310
Cdd:cd00180  205 R 205
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
426-685 1.97e-60

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: 205.26  E-value: 1.97e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDI-GVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14173    1 DVYQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKrpghSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAENGL 580
Cdd:cd14173   81 KMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENIL-CEHPNQVSPVKICDFDLGSGIKLNSDC 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 -------LMTPCYTANFVAPEVLKRQG-----YDAACDIWSLGVLLYTMLTGYTPFAN--GPD---DTPEE-------IL 636
Cdd:cd14173  160 spistpeLLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGrcGSDcgwDRGEAcpacqnmLF 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 637 ARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14173  240 ESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
428-684 6.91e-60

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: 202.63  E-value: 6.91e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-------RDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQvaregmvEQIKREIAIM-KLLRHPNIVELHEVMATKTKIFFVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFA--KQLRAEN 578
Cdd:cd14663   81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLL-LDEDGN---LKISDFGLSalSEQFRQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVLKRQGYD-AACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywNSVSDT 657
Cdd:cd14663  157 GLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFD---DENLMALYRKIMKGEFEYP----RWFSPG 229
                        250       260
                 ....*....|....*....|....*..
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14663  230 AKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
434-684 1.27e-59

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: 201.59  E-value: 1.27e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK-------RDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEiikrkevEHTLNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASavLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd05123   80 LFSHLSKEGRFPEERAR--FYAaeIVLALEYLHSLGIIYRDLKPENIL-LDSDGH---IKLTDFGLAKELSSDGDRTYTF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSK 664
Cdd:cd05123  154 CGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF---YAENRKEIYEKILKSPLKFP----EYVSPEAKSLISG 226
                        250       260
                 ....*....|....*....|...
gi 768032625 665 MLHVDPHQRLTAAL---VLRHPW 684
Cdd:cd05123  227 LLQKDPTKRLGSGGaeeIKAHPF 249
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
428-685 1.49e-59

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: 202.81  E-value: 1.49e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKAlrgKEAMVENEIaVLRRINHENIVSLEDIYESPTHLYLAMELVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQlrAENGLLMT 583
Cdd:cd14169   85 GGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEDSK-IMISDFGLSKI--EAQGMLST 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVS 663
Cdd:cd14169  162 ACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFY---DENDSELFNQILKAEYEFDSPYWDDISESAKDFIR 238
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14169  239 HLLERDPEKRFTCEQALQHPWI 260
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
434-685 1.65e-59

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: 201.30  E-value: 1.65e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREdvrnEIEIM-NQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILRQKFF-SEREAsaVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRaENGLLMTPCY 586
Cdd:cd14103   80 RVVDDDFElTERDC--ILFMrqICEGVQYMHKQGILHLDLKPENILCVSRTGN--QIKIIDFGLARKYD-PDKKLKVLFG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKrqgYDA---ACDIWSLGVLLYTMLTGYTPFAnGPDDTpeEILARIGSGKFSLSGGYWNSVSDTAKDLVS 663
Cdd:cd14103  155 TPEFVAPEVVN---YEPisyATDMWSVGVICYVLLSGLSPFM-GDNDA--ETLANVTRAKWDFDDEAFDDISDEAKDFIS 228
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14103  229 KLLVKDPRKRMSAAQCLQHPWL 250
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
427-685 1.68e-59

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: 202.03  E-value: 1.68e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIH-KATNME-FAVKIIDKsKRDPTE--------EIEILLRYgQHPNIITLKDVYDDGKYVY 496
Cdd:cd14080    1 GYRLGKTIGEGSYSKVKLAEYtKSGLKEkVACKIIDK-KKAPKDflekflprELEILRKL-RHPNIIQVYSIFERGSKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRA 576
Cdd:cd14080   79 IFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENIL-LDSNNN---VKLSDFGFARLCPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLM--TPCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFangpDDT-PEEILARIGSGKFSLSGGYWN 652
Cdd:cd14080  155 DDGDVLskTFCGSAAYAAPEILQGIPYDPkKYDIWSLGVILYIMLCGSMPF----DDSnIKKMLKDQQNRKVRFPSSVKK 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 653 sVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14080  231 -LSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
67-316 1.83e-59

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: 201.60  E-value: 1.83e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFL-VKKISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLaLNLDTG----ELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ESIDHEK 223
Cdd:cd06606   77 FLEYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF-QGKDRKETMTMILKAKLG--MPQFLSPEAQSLLR 300
Cdd:cd06606  157 GTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGEPppIPEHLSEEAKDFLR 236
                        250       260
                 ....*....|....*....|..
gi 768032625 301 MLFKRNPANR------LVNPFL 316
Cdd:cd06606  237 KCLQRDPKKRptadelLQHPFL 258
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
432-685 6.02e-59

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: 201.41  E-value: 6.02e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKnaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAENGL------- 580
Cdd:cd14174   88 LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL-CESPDKVSPVKICDFDLGSGVKLNSACtpittpe 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVL-----KRQGYDAACDIWSLGVLLYTMLTGYTPFAN--GPD---DTPE-------EILARIGSGK 643
Cdd:cd14174  167 LTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGhcGTDcgwDRGEvcrvcqnKLFESIQEGK 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 644 FSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14174  247 YEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
428-684 7.68e-59

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: 200.39  E-value: 7.68e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-----RDP---TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvagndKNLqlfQREINILKSL-EHPGIVRLIDWYEDDQHIYLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgNPESIRICDFGFAKqLRAENG 579
Cdd:cd14098   81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQD--DPVIVKISDFGLAK-VIHTGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLK------RQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNS 653
Cdd:cd14098  158 FLVTFCGTMAYLAPEILMskeqnlQGGYSNLVDMWSVGCLVYVMLTGALPFD---GSSQLPVEKRIRKGRYTQPPLVDFN 234
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14098  235 ISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
428-685 8.69e-59

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: 199.70  E-value: 8.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS-------KRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14099    3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltkpkqREKLKSEIKIH-RSLKHPNIVKFHDCFEDEENVYILLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd14099   82 LCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLF-LDENMN---VKIGDFGLAARLEYDGER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGywNSVSDTAK 659
Cdd:cd14099  158 KKTLCGTPNYIAPEVLeKKKGHSFEVDIWSLGVILYTLLVGKPPFE---TSDVKETYKRIKKNEYSFPSH--LSISDEAK 232
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14099  233 DLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
67-310 3.02e-58

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: 198.58  E-value: 3.02e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISgsDARQlYAMKVLKkATLKVRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTL--LGRP-VAIKVLR-PELAEDEEFRERFLReaRALARLSHPNIVRVYDVGEDDGRPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-ESIDHEK 223
Cdd:cd14014   77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARaLGDSGLT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLL 299
Cdd:cd14014  157 QTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPsplnPDVPPALDAII 236
                        250
                 ....*....|.
gi 768032625 300 RMLFKRNPANR 310
Cdd:cd14014  237 LRALAKDPEER 247
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
425-685 4.55e-58

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: 198.29  E-value: 4.55e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEV-KEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRdPTEEIEILLRYGQHPNIITLKDVYDD----GKYVYVVT 499
Cdd:cd14172    2 TDDYKLsKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPK-ARREVEHHWRASGGPHIVHILDVYENmhhgKRCLLIIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQLRAE 577
Cdd:cd14172   81 ECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAV-LKLTDFGFAKETTVQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLlMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSGKFSLSGGYWNSVSD 656
Cdd:cd14172  160 NAL-QTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFySNTGQAISPGMKRRIRMGQYGFPNPEWAEVSE 238
                        250       260
                 ....*....|....*....|....*....
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14172  239 EAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
67-333 5.62e-58

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: 197.48  E-value: 5.62e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLkVRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKL 143
Cdd:cd14081    2 PYRLGKTLGKGQTGLVKLAKhCVTG----QKVAIKIVNKEKL-SKESVLMKVEREIAIMklIEHPNVLKLYDVYENKKYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhEK 223
Cdd:cd14081   77 YLVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPE-GS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRML 302
Cdd:cd14081  156 LLETSCGSPHYACPEVIkGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRM 235
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 303 FKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14081  236 LEVNPEKRIT-----------IEEIKKHPWF 255
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
68-364 1.08e-57

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 199.82  E-value: 1.08e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARqlYAMKVLKKATLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:PTZ00426  32 FNFIRTLGTGSFGRVILATYKNEDFPP--VAIKRFEKSKIIKQKQVdHVFSERKILNYINHPFCVNLYGSFKDESYLYLV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidhEKKAY 226
Cdd:PTZ00426 110 LEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV---DTRTY 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRN 306
Cdd:PTZ00426 187 TLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHD 266
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 307 PANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFD 364
Cdd:PTZ00426 267 LTKRY------GNLKKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
56-393 1.22e-57

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: 201.77  E-value: 1.22e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  56 VKEGHEKADpsQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFIVKLH 134
Cdd:cd05622   65 IRDLRMKAE--DYEVVKVIGRGAFGEVQLVRHKS---TRKVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPWVVQLF 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGKLYLILDFLRGGDLFTRLSKEVMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05622  140 YAFQDDRYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 S-KESIDHEKKAYSFCGTVEYMAPEVVNRRG----HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK--LGM 287
Cdd:cd05622  219 CmKMNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTF 298
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 288 PQ--FLSPEAQSLLrMLFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPEDTFYFDP 365
Cdd:cd05622  299 PDdnDISKEAKNLI-CAFLTDREVRL--------GRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDD 369
                        330       340
                 ....*....|....*....|....*....
gi 768032625 366 EFTAKTPKDSPGIPPSANAHQL-FRGFSF 393
Cdd:cd05622  370 LEEDKGEEETFPIPKAFVGNQLpFVGFTY 398
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
424-685 1.64e-57

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: 196.80  E-value: 1.64e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEV-KEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR--DPTEEI--EI--LLRYGQHPNIITLKDVYDDGKYVY 496
Cdd:cd14106    5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRgqDCRNEIlhEIavLELCKDCPRVVNLHEVYETRSELI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpESIRICDFGFAKQLRA 576
Cdd:cd14106   85 LILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPL-GDIKLCDFGISRVIGE 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGL---LMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNS 653
Cdd:cd14106  164 GEEIreiLGTPDY----VAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGG---DDKQETFLNISQCNLDFPEELFKD 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14106  237 VSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
52-393 1.83e-57

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: 200.23  E-value: 1.83e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  52 ITHHVKEGHEKADpsQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKK-ATLKVRDRVRTKMERDILVEVNHPFI 130
Cdd:cd05621   40 IVNKIRELQMKAE--DYDVVKVIGRGAFGEVQLVRHKA---SQKVYAMKLLSKfEMIKRSDSAFFWEERDIMAFANSPWV 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 131 VKLHYAFQTEGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLT 210
Cdd:cd05621  115 VQLFCAFQDDKYLYMVMEYMPGGDL-VNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 211 DFG----LSKESIDHEKKAysfCGTVEYMAPEVVNRRG----HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL- 281
Cdd:cd05621  194 DFGtcmkMDETGMVHCDTA---VGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMd 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 282 -KAKLGMPQ--FLSPEAQSLLrMLFKRNPANRLvnpfligaGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKPATGRPE 358
Cdd:cd05621  271 hKNSLNFPDdvEISKHAKNLI-CAFLTDREVRL--------GRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDI 341
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 768032625 359 DTFYFDPEFTAKTPKDSPGIPPSANAHQL-FRGFSF 393
Cdd:cd05621  342 DTSNFDDIEDDKGDVETFPIPKAFVGNQLpFVGFTY 377
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
68-316 1.93e-57

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: 195.88  E-value: 1.93e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARhKKTG----QIVAIKKINLESKEKKESILN--EIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLfTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKK 224
Cdd:cd05122   76 MEFCSGGSL-KDLLKNTNktLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LSDGKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK---AKLGMPQFLSPEAQSLLRM 301
Cdd:cd05122  154 RNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATngpPGLRNPKKWSKEFKDFLKK 233
                        250       260
                 ....*....|....*....|.
gi 768032625 302 LFKRNPANR------LVNPFL 316
Cdd:cd05122  234 CLQKDPEKRptaeqlLKHPFI 254
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
426-685 2.67e-57

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: 196.17  E-value: 2.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK-----SKRDPT-EEIE---ILLRYGQHPNIITLKDVYDDGKYVY 496
Cdd:cd14105    5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKrrskaSRRGVSrEDIErevSILRQVLHPNIITLHDVFENKTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRA 576
Cdd:cd14105   85 LILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFGLAHKIED 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENgLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSD 656
Cdd:cd14105  165 GN-EFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG---DTKQETLANITAVNYDFDDEYFSNTSE 240
                        250       260
                 ....*....|....*....|....*....
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14105  241 LAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
428-685 1.40e-56

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: 195.27  E-value: 1.40e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQLVS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgNPESIRICDFGFAKqLRAENGLLMT 583
Cdd:cd14168   92 GGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQD-EESKIMISDFGLSK-MEGKGDVMST 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVS 663
Cdd:cd14168  170 ACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFY---DENDSKLFEQILKADYEFDSPYWDDISDSAKDFIR 246
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14168  247 NLMEKDPNKRYTCEQALRHPWI 268
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
426-685 2.07e-56

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: 193.70  E-value: 2.07e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK----------SKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYV 495
Cdd:cd14194    5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKrrtkssrrgvSREDIEREVSIL-KEIQHPNVITLHEVYENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLR 575
Cdd:cd14194   84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKID 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AEN---GLLMTPcytaNFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWN 652
Cdd:cd14194  164 FGNefkNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG---DTKQETLANVSAVNYEFEDEYFS 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14194  237 NTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
68-352 2.44e-56

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: 194.06  E-value: 2.44e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQvRATG----KMYACKKLEKKRIKKRKGEAMALnEKRILEKVNSRFVVSLAYAYETKDALCL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd05631   78 VLTIMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK----DRKETMTMILKAKLGMPQFLSPEAQSLL 299
Cdd:cd05631  157 TVRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkervKREEVDRRVKEDQEEYSEKFSEDAKSIC 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 300 RMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05631  237 RMLLTKNPKERL------GCRGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
74-333 3.82e-56

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: 192.77  E-value: 3.82e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLK-------VRDRVRTKMER-----DILVEVNHPFIVKLHYAF--QT 139
Cdd:cd14008    1 LGRGSFGKVKLALDT---ETGQLYAIKIFNKSRLRkrregknDRGKIKNALDDvrreiAIMKKLDHPNIVRLYEVIddPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKe 217
Cdd:cd14008   78 SDKLYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSE- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 sIDHEKKAYSFC--GTVEYMAPEVVNRRGHTQS---ADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL--GMPQF 290
Cdd:cd14008  157 -MFEDGNDTLQKtaGTPAFLAPELCDGDSKTYSgkaADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDefPIPPE 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 291 LSPEAQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14008  236 LSPELKDLLRRMLEKDPEKRIT-----------LKEIKEHPWV 267
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
434-683 7.00e-56

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: 190.56  E-value: 7.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT-----EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleellREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DKILRQ-KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLL--MTPC 585
Cdd:cd00180   80 DLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENIL-LDSDGT---VKLADFGLAKDLDSDDSLLktTGGT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMltgytpfangpddtpeeilarigsgkfslsggywnsvsDTAKDLVSKM 665
Cdd:cd00180  156 TPPYYAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------------EELKDLIRRM 197
                        250
                 ....*....|....*...
gi 768032625 666 LHVDPHQRLTAALVLRHP 683
Cdd:cd00180  198 LQYDPKKRPSAKELLEHL 215
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
68-352 9.08e-56

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: 193.65  E-value: 9.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05632    4 FRQYRVLGKGGFGEVCACQvRATG----KMYACKRLEKKRIKKRKGESMALnEKQILEKVNSQFVVNLAYAYETKDALCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd05632   80 VLTIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK----DRKETMTMILKAKLGMPQFLSPEAQSLL 299
Cdd:cd05632  159 SIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRkekvKREEVDRRVLETEEVYSAKFSEEAKSIC 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 300 RMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05632  239 KMLLTKDPKQRL------GCQEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP 285
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
426-697 1.98e-55

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: 192.17  E-value: 1.98e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDI-GVGSYSVCKRCIHKATNMEFAVKIID---KSKRdpteEIEILLRYGQHPNIITLKDVYDD----GKYVYV 497
Cdd:cd14170    1 DDYKVTSQVlGLGINGKVLQIFNKRTQEKFALKMLQdcpKARR----EVELHWRASQCPHIVRIVDVYENlyagRKCLLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdeSGNPESI-RICDFGFAKQL 574
Cdd:cd14170   77 VMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYT--SKRPNAIlKLTDFGFAKET 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGLlMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSGKFSLSGGYWNS 653
Cdd:cd14170  155 TSHNSL-TTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKTRIRMGQYEFPNPEWSE 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLN 697
Cdd:cd14170  234 VSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQSTKVPQTPLH 277
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
424-708 3.37e-55

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: 191.60  E-value: 3.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---------RDPTEEIEILLRYgQHPNIITLKDVYDDGKY 494
Cdd:cd14094    1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsspglstEDLKREASICHML-KHPHIVELLETYSSDGM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgNPESIRICDFGF 570
Cdd:cd14094   80 LYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKE-NSAPVKLGGFGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLrAENGLLMT-PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpddTPEEILARIGSGKFSLSGG 649
Cdd:cd14094  159 AIQL-GESGLVAGgRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPR 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 650 YWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQY--------QLNRQDAPHLVKGA 708
Cdd:cd14094  234 QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRYAYRihlpetveQLRKFNARRKLKGA 300
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
423-685 5.12e-55

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: 190.17  E-value: 5.12e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIE---ILLRYGQHPNIITLKDVYDDGK 493
Cdd:cd14196    2 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsrEEIErevSILRQVLHPNIITLHDVYENRT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 YVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQ 573
Cdd:cd14196   82 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 LraENGLLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWN 652
Cdd:cd14196  162 I--EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG---DTKQETLANITAVSYDFDEEFFS 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14196  237 HTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
68-333 3.30e-54

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: 187.39  E-value: 3.30e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARQLyAMKVLKKAtlKVRDRVRTKM---ERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAEYTKSGLKEKV-ACKIIDKK--KAPKDFLEKFlprELEILRKLRHPNIIQVYSIFERGSKVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKK 224
Cdd:cd14080   79 IFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYS--FCGTVEYMAPEVVnrRG---HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP---QFLSPEAQ 296
Cdd:cd14080  159 VLSktFCGSAAYAAPEIL--QGipyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECK 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 297 SLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:cd14080  237 DLIDQLLEPDPTKRA-----------TIEEILNHPWL 262
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
428-685 3.52e-54

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: 187.02  E-value: 3.52e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESIlnEIaILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLrAENGLLM 582
Cdd:cd05122   82 GSLKD-LLKNTNktLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANIL-LTSDG---EVKLIDFGLSAQL-SDGKTRN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIG-SGKFSLSGGYWNsvSDTAKDL 661
Cdd:cd05122  156 TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY---SELPPMKALFLIAtNGPPGLRNPKKW--SKEFKDF 230
                        250       260
                 ....*....|....*....|....
gi 768032625 662 VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd05122  231 LKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
67-311 3.82e-54

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: 187.21  E-value: 3.82e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDN---QVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVM----FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKesIDHE 222
Cdd:cd08530   78 MEYAPFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG-MPQFLSPEAQSLLRM 301
Cdd:cd08530  156 NLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPpIPPVYSQDLQQIIRS 235
                        250
                 ....*....|
gi 768032625 302 LFKRNPANRL 311
Cdd:cd08530  236 LLQVNPKKRP 245
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
68-352 7.51e-54

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: 187.40  E-value: 7.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05608    3 FLDFRVLGKGGFGEVSACQmRATG----KLYACKKLNKKRLKKRKGYEGAMvEKRILAKVHSRFIVSLAYAFQTKTDLCL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDL----FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd05608   79 VMTIMNGGDLryhiYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK----DRKETMTMILKAKLGMPQFLSPEAQS 297
Cdd:cd05608  159 QTKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKS 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 298 LLRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05608  239 ICEALLAKDPEKRL------GFRDGNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
428-685 1.00e-53

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: 186.22  E-value: 1.00e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14097    3 YTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSavklleREVDIL-KHVNHAHIIHLEEVFETPKRMYLVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY---VDESGNPESIRICDFGFA--KQLRA 576
Cdd:cd14097   82 CEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssIIDNNDKLNIKVTDFGLSvqKYGLG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTpCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpddTPEEILARIGSGKFSLSGGYWNSVSD 656
Cdd:cd14097  162 EDMLQET-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAK---SEEKLFEEIRKGDLTFTQSVWQSVSD 237
                        250       260
                 ....*....|....*....|....*....
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14097  238 AAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
434-685 1.60e-53

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: 185.42  E-value: 1.60e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:cd06606    8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEElealEREIrILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DkiLRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd06606   88 S--LLKKFgkLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL-VDSDGV---VKLADFGCAKRLAEIATGEGTKSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 --TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDdtPEEILARIGSGKfsLSGGYWNSVSDTAKDLVSK 664
Cdd:cd06606  162 rgTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGN--PVAALFKIGSSG--EPPPIPEHLSEEAKDFLRK 237
                        250       260
                 ....*....|....*....|.
gi 768032625 665 MLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06606  238 CLQRDPKKRPTADELLQHPFL 258
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
426-685 2.14e-53

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: 185.59  E-value: 2.14e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK-----SKRDPT-EEIEI---LLRYGQHPNIITLKDVYDDGKYVY 496
Cdd:cd14195    5 DHYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKrrlssSRRGVSrEEIERevnILREIQHPNIITLHDIFENKTDVV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRA 576
Cdd:cd14195   85 LILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 EN---GLLMTPcytaNFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNS 653
Cdd:cd14195  165 GNefkNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG---ETKQETLTNISAVNYDFDEEYFSN 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14195  238 TSELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
74-311 2.87e-53

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: 184.73  E-value: 2.87e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14009    1 IGRGSFATVWKGRHK---QTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKeSIDHEKKAYSFCG 230
Cdd:cd14009   78 DLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFAR-SLQPASMAETLCG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKD----RKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRN 306
Cdd:cd14009  157 SPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNhvqlLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLRRD 236

                 ....*
gi 768032625 307 PANRL 311
Cdd:cd14009  237 PAERI 241
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
74-311 2.93e-53

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: 184.39  E-value: 2.93e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVF-LVKKISGsdarQLYAMKVLKKatlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd14006    1 LGRGRFGVVKrCIEKATG----REFAAKFIPK---RDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE--EGHIKLTDFGLSKEsIDHEKKAYSFCG 230
Cdd:cd14006   74 GELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADrpSPQIKIIDFGLARK-LNPGEELKEIFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG----MPQFLSPEAQSLLRMLFKRN 306
Cdd:cd14006  153 TPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseeYFSSVSQEAKDFIRKLLVKE 232

                 ....*
gi 768032625 307 PANRL 311
Cdd:cd14006  233 PRKRP 237
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
434-685 3.16e-53

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 185.06  E-value: 3.16e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK--------------RDPTE----EIEIL--LRygqHPNIITLKDVYDD-- 491
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRlrkrregkndrgkiKNALDdvrrEIAIMkkLD---HPNIVRLYEVIDDpe 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 492 GKYVYVVTELMKGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFG 569
Cdd:cd14008   78 SDKLYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL-LTADGT---VKISDFG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 570 FAKQLRAENGLLMTPCYTANFVAPEVLK--RQGYDA-ACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSgkFS 645
Cdd:cd14008  154 VSEMFEDGNDTLQKTAGTPAFLAPELCDgdSKTYSGkAADIWALGVTLYCLVFGRLPFnGDNILELYEAIQNQNDE--FP 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 646 LSGGywnsVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14008  232 IPPE----LSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
72-311 4.35e-53

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: 184.90  E-value: 4.35e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLKVR--------DRVRTKMErdILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14084   12 RTLGSGACGEVKLAYDKS---TCKKVAIKIINKRKFTIGsrreinkpRNIETEIE--ILKKLSHPCIIKIEDFFDAEDDY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKeSID 220
Cdd:cd14084   87 YIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSK-ILG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVN---RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT-MILKAKL--GMPQF--LS 292
Cdd:cd14084  166 ETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLKeQILSGKYtfIPKAWknVS 245
                        250
                 ....*....|....*....
gi 768032625 293 PEAQSLLRMLFKRNPANRL 311
Cdd:cd14084  246 EEAKDLVKKMLVVDPSRRP 264
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
68-352 8.50e-53

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: 184.72  E-value: 8.50e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQvKNTG----QMYACKKLDKKRLKKKSGEKMALlEKEILEKVNSPFIVSLAYAFETKTHLCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd05607   80 VMSLMNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFqgKDRKETM--------TMILKAKLGMPQFlSPEA 295
Cdd:cd05607  159 PITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPF--RDHKEKVskeelkrrTLEDEVKFEHQNF-TEEA 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 296 QSLLRMLFKRNPANRLvnpfligAGPDGVEEIKRHSFFSTIDWNKLYRREIHPPFKP 352
Cdd:cd05607  236 KDICRLFLAKKPENRL-------GSRTNDDDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
423-685 8.83e-53

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: 183.69  E-value: 8.83e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDiGVGSYSVCKRcihkatnmeFAVKIIDKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd14088   13 EFCEIFRAKDK-TTGKLYTCKK---------FLKRDGRKVRKAAKNEINIL-KMVKHPNILQLVDVFETRKEYFIFLELA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKqlrAENGLLM 582
Cdd:cd14088   82 TGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNSK-IVISDFHLAK---LENGLIK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEE-----ILARIGSGKFSLSGGYWNSVSDT 657
Cdd:cd14088  158 EPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknLFRKILAGDYEFDSPYWDDISQA 237
                        250       260
                 ....*....|....*....|....*...
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14088  238 AKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
427-685 4.71e-52

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: 181.51  E-value: 4.71e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID------KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlsnmseKEREEALNEVKLLSKL-KHPNIVKYYESFEENGKLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRA 576
Cdd:cd08215   80 YADGGDLAQKIKKQKkkgqPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIF-LTKDGV---VKLGDFGISKVLES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFS-LSGGYwnsvS 655
Cdd:cd08215  156 TTDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFE---ANNLPALVYKIVKGQYPpIPSQY----S 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08215  229 SELRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
428-685 5.53e-52

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: 181.05  E-value: 5.53e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEI--LLRygqHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEnlkkiyREVQImkMLN---HPHIIKLYQVMETKDMLYLVT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEnG 579
Cdd:cd14071   79 EYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLL-LDANMN---IKIADFGFSNFFKPG-E 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFaNGPddTPEEILARIGSGKFSLSggYWnsVSDTA 658
Cdd:cd14071  154 LLKTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPF-DGS--TLQTLRDRVLSGRFRIP--FF--MSTDC 226
                        250       260
                 ....*....|....*....|....*..
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14071  227 EHLIRRMLVLDPSKRLTIEQIKKHKWM 253
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
66-310 2.34e-51

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: 179.71  E-value: 2.34e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKkatLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd06623    1 SDLERVKVLGQGSSGVVYKVRhKPTG----KIYALKKIH---VDGDEEFRKQLLRElkTLRSCESPYVVKCYGAFYKEGE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHS-LGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd06623   74 ISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFL-----SPEAQ 296
Cdd:cd06623  154 LDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPSLpaeefSPEFR 233
                        250
                 ....*....|....
gi 768032625 297 SLLRMLFKRNPANR 310
Cdd:cd06623  234 DFISACLQKDPKKR 247
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
427-684 3.15e-51

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: 179.00  E-value: 3.15e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-------EIEILlRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14079    3 NYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDmeekirrEIQIL-KLFRHPHIIRLYEVIETPTDIFMVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENg 579
Cdd:cd14079   82 EYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLL-LDSNMN---VKIADFGLSNIMRDGE- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFangpDDtpEEI---LARIGSGKFSLSGgywnSVS 655
Cdd:cd14079  157 FLKTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPF----DD--EHIpnlFKKIKSGIYTIPS----HLS 226
                        250       260
                 ....*....|....*....|....*....
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14079  227 PGARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
68-311 3.84e-51

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: 179.00  E-value: 3.84e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLK---VRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLARE---KQSKFILALKVLFKAQLEkagVEHQLRREVE--IQSHLRHPNILRLYGYFHDATRVY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKK 224
Cdd:cd14116   82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 aySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFK 304
Cdd:cd14116  162 --TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK 239

                 ....*..
gi 768032625 305 RNPANRL 311
Cdd:cd14116  240 HNPSQRP 246
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
428-693 5.94e-51

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: 179.70  E-value: 5.94e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE------ILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEhvlnekRILSEVRHPFIVNLLGSFQDDRNLYMVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaenGLL 581
Cdd:cd05580   83 VPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLL-LDSDGH---IKITDFGFAKRVK---DRT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSlsggYWNSVSDTAKDL 661
Cdd:cd05580  156 YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFF---DENPMKIYEKILEGKIR----FPSFFDPDAKDL 228
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 662 VSKMLHVDPHQRL-----TAALVLRHPWI--VHWDQLPQ 693
Cdd:cd05580  229 IKRLLVVDLTKRLgnlknGVEDIKNHPWFagIDWDALLQ 267
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
426-737 8.28e-51

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 184.83  E-value: 8.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQ------HPNIITLKDVYDDGKYVYVVT 499
Cdd:COG0515    7 GRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPELAADPEARERFRREARalarlnHPNIVRVYDVGEEDGRPYLVM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFAKQLRAEN- 578
Cdd:COG0515   87 EYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRV---KLIDFGIARALGGATl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 ---GLLMtpcYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWNSVS 655
Cdd:COG0515  163 tqtGTVV---GTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---DGDSPAELLRAHLREPPPPPSELRPDLP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQR 735
Cdd:COG0515  237 PALDAIVLRALAKDPEERYQSAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 316

                 ..
gi 768032625 736 RG 737
Cdd:COG0515  317 AA 318
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
428-685 9.28e-51

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: 177.79  E-value: 9.28e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID---KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRlrkQNKELIINEILIMKEC-KHPNIVDYYDSYLVGDELWVVMEYMDG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAE----N 578
Cdd:cd06614   81 GSLTD-IITQNPvrMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNIL-LSKDG---SVKLADFGFAAQLTKEkskrN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPcYtanFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGS-GKFSLSGGywNSVSDT 657
Cdd:cd06614  156 SVVGTP-Y---WMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYL---EEPPLRALFLITTkGIPPLKNP--EKWSPE 226
                        250       260
                 ....*....|....*....|....*...
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06614  227 FKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
428-685 1.36e-50

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: 177.61  E-value: 1.36e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEIL-----LRYGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFqevrcMKLVQHPNVVRLYEVIDTQTKLYLILELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILR-QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpeSIRICDFGFAKQLRaENGLL 581
Cdd:cd14074   85 DGGDMYDYIMKhENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQ-PGEKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFANGPDdtpEEILARIGSGKFSLSggywNSVSDTAKD 660
Cdd:cd14074  161 ETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEAND---SETLTMIMDCKYTVP----AHVSPECKD 233
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14074  234 LIRRMLIRDPKKRASLEEIENHPWL 258
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
427-677 1.40e-50

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: 177.39  E-value: 1.40e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-------EIEILLRYgQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfrerflrEARALARL-SHPNIVRVYDVGEDDGRPYIVM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLrAENG 579
Cdd:cd14014   80 EYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANIL-LTEDGR---VKLTDFGIARAL-GDSG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTP--CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWNSVSDT 657
Cdd:cd14014  155 LTQTGsvLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPF---DGDSPAAVLAKHLQEAPPPPSPLNPDVPPA 231
                        250       260
                 ....*....|....*....|
gi 768032625 658 AKDLVSKMLHVDPHQRLTAA 677
Cdd:cd14014  232 LDAIILRALAKDPEERPQSA 251
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
68-310 3.41e-50

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: 176.29  E-value: 3.41e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDRVrtkMERDILV--EVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14185    2 YEIGRTIGDGNFA---VVKECRHWNENQEYAMKIIDKSKLKGKEDM---IESEILIikSLSHPNIVKLFEVYETEKEIYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFGLSKESIdh 221
Cdd:cd14185   76 ILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 eKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR-KETMTMILkaKLGMPQFLSP------- 293
Cdd:cd14185  154 -GPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERdQEELFQII--QLGHYEFLPPywdnise 230
                        250
                 ....*....|....*..
gi 768032625 294 EAQSLLRMLFKRNPANR 310
Cdd:cd14185  231 AAKDLISRLLVVDPEKR 247
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
68-311 3.50e-50

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: 176.36  E-value: 3.50e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDArqlYAMKVLKKATLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKE---YALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG----HIKLTDFGLSKESidhEK 223
Cdd:cd14095   78 ELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEV---KE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR--KETMTMILKAKLgmpQFLSP-------E 294
Cdd:cd14095  155 PLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRdqEELFDLILAGEF---EFLSPywdnisdS 231
                        250
                 ....*....|....*..
gi 768032625 295 AQSLLRMLFKRNPANRL 311
Cdd:cd14095  232 AKDLISRMLVVDPEKRY 248
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
427-684 1.04e-49

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: 175.21  E-value: 1.04e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID--KSKRDPTEEI--EILL-RYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14069    2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDmkRAPGDCPENIkkEVCIqKMLSHKNVVRFYGHRREGEFQYLFLEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENG-- 579
Cdd:cd14069   82 ASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLL-LDENDN---LKISDFGLATVFRYKGKer 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFaNGPDDTPEEILARIGSGKFSLsgGYWNSVSDTA 658
Cdd:cd14069  158 LLNKMCGTLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAGELPW-DQPSDSCQEYSDWKENKKTYL--TPWKKIDTAA 234
                        250       260
                 ....*....|....*....|....*.
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14069  235 LSLLRKILTENPNKRITIEDIKKHPW 260
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
428-685 1.23e-49

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: 174.88  E-value: 1.23e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RD-PTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14078    5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgDDlPRVKTEIeALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGF-AKQLRAENGLLM 582
Cdd:cd14078   85 GGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLL-LDEDQN---LKLIDFGLcAKPKGGMDHHLE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTANFVAPEVLKRQGY-DAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSggYWNSVSdtAKDL 661
Cdd:cd14078  161 TCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPF---DDDNVMALYRKIQSGKYEEP--EWLSPS--SKLL 233
                        250       260
                 ....*....|....*....|....
gi 768032625 662 VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14078  234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
74-310 2.60e-49

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: 173.49  E-value: 2.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKkISGSDArqlyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd13999    1 IGSGSFGEVYKGK-WRGTDV----AIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTV 232
Cdd:cd13999   76 SLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 233 EYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKD-RKETMTMILKAK-LGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd13999  156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSpIQIAAAVVQKGLrPPIPPDCPPELSKLIKRCWNEDPEKR 235
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
66-333 9.77e-49

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: 172.52  E-value: 9.77e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISGSDArqlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGK-LY 144
Cdd:cd14069    1 EDWDLVQTLGEGAFGEVFLAVNRNTEEA---VAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRF-YGHRREGEfQY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI--DHE 222
Cdd:cd14069   77 LFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRykGKE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRG-HTQSADWWSFGVLMFEMLTGTLPF-QGKDRKETMTMILKAK---LGMPQFLSPEAQS 297
Cdd:cd14069  157 RLLNKMCGTLPYVAPELLAKKKyRAEPVDVWSCGIVLFAMLAGELPWdQPSDSCQEYSDWKENKktyLTPWKKIDTAALS 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 298 LLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14069  237 LLRKILTENPNKRIT-----------IEDIKKHPWY 261
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
434-684 9.93e-49

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: 172.02  E-value: 9.93e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK-----RDPTE-EIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKlnkklQENLEsEIAIL-KSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFAKQLrAENGLLMTPCYT 587
Cdd:cd14009   80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGDDPV-LKIADFGFARSL-QPASMAETLCGS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDdtPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLH 667
Cdd:cd14009  158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPF-RGSN--HVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLR 234
                        250
                 ....*....|....*..
gi 768032625 668 VDPHQRLTAALVLRHPW 684
Cdd:cd14009  235 RDPAERISFEEFFAHPF 251
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-333 1.53e-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: 171.96  E-value: 1.53e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISgsDaRQLYAMKVLKKATLKVRDRvrtKM---ERDILVEVNHPFIVKLHYAF--QTEG 141
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKS--D-GKILVWKEIDYGKMSEKEK---QQlvsEVNILRELKHPNIVRYYDRIvdRANT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDL---FTRLSKEVMFTEED-VKFYLAELALALDHLHSLG-----IIYRDLKPENILLDEEGHIKLTDF 212
Cdd:cd08217   75 TLYIVMEYCEGGDLaqlIKKCKKENQYIPEEfIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDF 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 213 GLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG-MPQFL 291
Cdd:cd08217  155 GLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFPrIPSRY 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 292 SPEAQSLLRMLFKRNPANRlvnpfligagPDgVEEIKRHSFF 333
Cdd:cd08217  235 SSELNEVIKSMLNVDPDKR----------PS-VEELLQLPLI 265
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
434-689 4.14e-48

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: 170.87  E-value: 4.14e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEI----EILLRyGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhivQTRQQEHIfsekEILEE-CNSPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDkILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGlLMTPC 585
Cdd:cd05572   80 LWT-ILRDRgLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLL-LDSNG---YVKLVDFGFAKKLGSGRK-TWTFC 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDTPEEILARIGSGKFSLsgGYWNSVSDTAKDLVSKM 665
Cdd:cd05572  154 GTPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPF-GGDDEDPMKIYNIILKGIDKI--EFPKYIDKNAKNLIKQL 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 666 LHVDPHQRL-----TAALVLRHPW--IVHWD 689
Cdd:cd05572  231 LRRNPEERLgylkgGIRDIKKHKWfeGFDWE 261
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
428-684 1.37e-47

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 169.70  E-value: 1.37e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS------KRDP-TEEIEILLRYGqHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiikekKVKYvTIEKEVLSRLA-HPGIVKLYYTFQDESKLYFVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd05581   82 YAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENIL-LDEDMH---IKITDFGTAKVLGPDSSP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTP-----------------CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGK 643
Cdd:cd05581  158 ESTKgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR---GSNEYLTFQKIVKLE 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 644 FSLSggywNSVSDTAKDLVSKMLHVDPHQRLTAAL------VLRHPW 684
Cdd:cd05581  235 YEFP----ENFPPDAKDLIQKLLVLDPSKRLGVNEnggydeLKAHPF 277
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
427-684 1.96e-47

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: 168.63  E-value: 1.96e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKsKRDPTE--------EIEILlRYGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14162    1 GYIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSK-KKAPEDylqkflprEIEVI-KGLKHPNLICFYEAIETTSRVYII 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK-QLRAE 577
Cdd:cd14162   79 MELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLL-LDKNNN---LKITDFGFARgVMKTK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NG---LLMTPCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFangpDDTP-EEILARIGSG-KFSLSggyw 651
Cdd:cd14162  155 DGkpkLSETYCGSYAYASPEILRGIPYDPfLSDIWSMGVVLYTMVYGRLPF----DDSNlKVLLKQVQRRvVFPKN---- 226
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 652 NSVSDTAKDLVSKMLHVDPhQRLTAALVLRHPW 684
Cdd:cd14162  227 PTVSEECKDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
68-333 2.08e-47

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 168.18  E-value: 2.08e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKkatLKVRDRVRTKMERDILVEVN----HPFIVKLHYAF--QTEG 141
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARD---KVTGEKVAIKKIK---NDFRHPKAALREIKLLKHLNdvegHPNIVKLLDVFehRGGN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLrGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE-GHIKLTDFGLSKesI 219
Cdd:cd05118   75 HLCLVFELM-GMNLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLAR--S 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMPQFLspeaqSL 298
Cdd:cd05118  152 FTSPPYTPYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR-LLGTPEAL-----DL 225
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 299 LRMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd05118  226 LSKMLKYDPAKRIT-----------ASQALAHPYF 249
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
428-685 4.31e-47

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: 167.90  E-value: 4.31e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDP------TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14075    4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQktqrllSREISSMEKL-HHPNIIRLYEVVETLSKLHLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAENgLL 581
Cdd:cd14075   83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYA----SNNCVKVGDFGFSTHAKRGE-TL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGY-DAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGgywnSVSDTAKD 660
Cdd:cd14075  158 NTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFRA---ETVAKLKKCILEGTYTIPS----YVSEPCQE 230
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14075  231 LIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
66-310 5.15e-47

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: 167.57  E-value: 5.15e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVflvKKISGSDARQLYAMKVLKKATLKVR-DRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14073    1 HRYELLETLGKGTYGKV---KLAIERATGREVAIKSIKKDKIEDEqDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKK 224
Cdd:cd14073   78 IVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSN-LYSKDKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRG-HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSpEAQSLLRMLF 303
Cdd:cd14073  157 LQTFCGSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWML 235

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd14073  236 TVNPKRR 242
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
428-685 9.93e-47

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: 166.79  E-value: 9.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-------RDP-----TEEIEIL--LRYGQHPNIITLKDVYDDGK 493
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdtwvRDRklgtvPLEIHILdtLNKRSHPNIVKLLDFFEDDE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 YVYVVTELMKGG-ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAK 572
Cdd:cd14004   82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVI-LDGNG---TIKLIDFGSAA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLraENGLLMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFANgpddtPEEILAriGSGKFSlsggyw 651
Cdd:cd14004  158 YI--KSGPFDTFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFYN-----IEEILE--ADLRIP------ 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14004  223 YAVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
425-685 1.12e-46

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: 166.72  E-value: 1.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14191    1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKaysaKEKENIRQEISIMNCL-HHPKLVQCVDAFEEKANIVMVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAEnG 579
Cdd:cd14191   80 MVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--KIKLIDFGLARRLENA-G 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14191  157 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMG---DNDNETLANVTSATWDFDDEAFDEISDDAK 233
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14191  234 DFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
67-316 2.05e-46

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: 165.89  E-value: 2.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLV-KKISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGrRKYTG----QVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd14002   78 VTEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd14002  157 TSIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNK 236
                        250
                 ....*....|.
gi 768032625 306 NPANRLVNPFL 316
Cdd:cd14002  237 DPSKRLSWPDL 247
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
67-310 2.18e-46

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: 165.75  E-value: 2.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkiSGSDARQlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd08218    1 KYVRIKKIGEGSFGKALLVK--SKEDGKQ-YVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKE--VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKK 224
Cdd:cd08218   78 MDYCDGGDLYKRINAQrgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVEL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL-GMPQFLSPEAQSLLRMLF 303
Cdd:cd08218  158 ARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLF 237

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd08218  238 KRNPRDR 244
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
434-684 3.92e-46

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: 164.75  E-value: 3.92e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDK--SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKI 511
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKkmKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 512 LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQL---RAENGLLMTPcyta 588
Cdd:cd14115   81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQIsghRHVHHLLGNP---- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 589 NFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHV 668
Cdd:cd14115  156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFL---DESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQE 232
                        250
                 ....*....|....*.
gi 768032625 669 DPHQRLTAALVLRHPW 684
Cdd:cd14115  233 DPRRRPTAATCLQHPW 248
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
428-685 1.04e-45

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: 163.56  E-value: 1.04e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT---EEIEILLRYG---QHPNIITLKDVYDD--GKYVYVVT 499
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKHLNdveGHPNIVKLLDVFEHrgGNHLCLVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMkgGELLDKILR--QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRICDFGFAKQLRae 577
Cdd:cd05118   81 ELM--GMNLYELIKdyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI---NLELGQLKLADFGLARSFT-- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 ngllmTPCYTANFV-----APEVLKR-QGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSLSGgyw 651
Cdd:cd05118  154 -----SPPYTPYVAtrwyrAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLF---PGDSEVDQLAKI----VRLLG--- 218
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 652 nsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd05118  219 ---TPEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
424-685 1.19e-45

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: 163.99  E-value: 1.19e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDP-TEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14113    5 FDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKlmKRDQvTHELGVLQSL-QHPQLVGLLDTFETPTSYILVLE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLRAE--- 577
Cdd:cd14113   84 MADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENIL-VDQSLSKPTIKLADFGDAVQLNTTyyi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPcytaNFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNSVSDT 657
Cdd:cd14113  163 HQLLGSP----EFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFL---DESVEETCLNICRLDFSFPDDYFKGVSQK 235
                        250       260
                 ....*....|....*....|....*...
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14113  236 AKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-316 1.43e-45

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: 163.59  E-value: 1.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkiSGSDARQLyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd08225    1 RYEIIKKIGEGSFGKIYLAK--AKSDSEHC-VIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKE--VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI-KLTDFGLSKESIDHEK 223
Cdd:cd08225   78 MEYCDGGDLMKRINRQrgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSME 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG--MPQFlSPEAQSLLRM 301
Cdd:cd08225  158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApiSPNF-SRDLRSLISQ 236
                        250       260
                 ....*....|....*....|.
gi 768032625 302 LFKRNPANR------LVNPFL 316
Cdd:cd08225  237 LFKVSPRDRpsitsiLKRPFL 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
428-684 1.81e-45

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: 163.14  E-value: 1.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEIEILLRYGqHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14107    4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIplrSSTRARAFQERDILARLS-HRRLTCLLDQFETRKTLILILELCSS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdeSGNPESIRICDFGFAKQLRAENgLLMTP 584
Cdd:cd14107   83 EELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMV--SPTREDIKICDFGFAQEITPSE-HQFSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDtpEEILARIGSGKFSLSGGYWNSVSDTAKDLVSK 664
Cdd:cd14107  160 YGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFA-GEND--RATLLNVAEGVVSWDTPEITHLSEDAKDFIKR 236
                        250       260
                 ....*....|....*....|
gi 768032625 665 MLHVDPHQRLTAALVLRHPW 684
Cdd:cd14107  237 VLQPDPEKRPSASECLSHEW 256
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
74-332 2.03e-45

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: 162.89  E-value: 2.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVflvkKISGSD-ARQLYAMKVLKKAtlKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14075   10 LGSGNFSQV----KLGIHQlTKEKVAIKILDKT--KLDQKTQRLLSREIssMEKLHHPNIIRLYEVVETLSKLHLVMEYA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESiDHEKKAYSFCG 230
Cdd:cd14075   84 SGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHA-KRGETLNTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVV---NRRGHtqSADWWSFGVLMFEMLTGTLPFqgkdRKETM----TMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd14075  163 SPPYAAPELFkdeHYIGI--YVDIWALGVLLYFMVTGVMPF----RAETVaklkKCILEGTYTIPSYVSEPCQELIRGIL 236
                        250       260
                 ....*....|....*....|....*....
gi 768032625 304 KRNPANRLvnpfligagpdGVEEIKRHSF 332
Cdd:cd14075  237 QPVPSDRY-----------SIDEIKNSEW 254
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
66-311 3.32e-45

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: 162.70  E-value: 3.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKatlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14087    1 AKYDIKALIGRGSFSRVVRVEHRV---TRQPYAIKMIET---KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH---IKLTDFGL-SKESIDH 221
Cdd:cd14087   75 VMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLaSTRKKGP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGM-PQF---LSPEAQS 297
Cdd:cd14087  155 NCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsGEPwpsVSNLAKD 234
                        250
                 ....*....|....
gi 768032625 298 LLRMLFKRNPANRL 311
Cdd:cd14087  235 FIDRLLTVNPGERL 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
429-685 3.35e-45

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: 162.76  E-value: 3.35e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 429 EVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdKSKRDPTE------EIEILLRyGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd06623    4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFrkqllrELKTLRS-CESPYVVKCYGAFYKEGEISIVLEYM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLraENGLL 581
Cdd:cd06623   82 DGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLL-INSKGE---VKIADFGISKVL--ENTLD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCY--TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSG-KFSLSGGYWnsvSDTA 658
Cdd:cd06623  156 QCNTFvgTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGpPPSLPAEEF---SPEF 232
                        250       260
                 ....*....|....*....|....*..
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06623  233 RDFISACLQKDPKKRPSAAELLQHPFI 259
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
426-685 4.97e-45

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: 161.98  E-value: 4.97e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS----KRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14114    2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPhesdKETVRKEIQIMNQL-HHPKLINLHDAFEDDNEMVLILEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGL 580
Cdd:cd14114   81 LSGGELFERIAAEHYkMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSN--EVKLIDFGLATHLDPKESV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDtpeEILARIGSGKFSLSGGYWNSVSDTAKD 660
Cdd:cd14114  159 KVTTG-TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDD---ETLRNVKSCDWNFDDSAFSGISEEAKD 234
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14114  235 FIRKLLLADPNKRMTIHQALEHPWL 259
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
428-685 1.14e-44

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: 161.02  E-value: 1.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-RDPTE------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiEDEQDmvrirrEIEIMSSL-NHPHIIRIYEVFENKDKIVIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAkQLRAENGL 580
Cdd:cd14073   82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENIL-LDQNGN---AKIADFGLS-NLYSKDKL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFangpDDTPEEILAR-IGSGKFslsggYWNSVSDTA 658
Cdd:cd14073  157 LQTFCGSPLYASPEIVNGTPYQGPeVDCWSLGVLLYTLVYGTMPF----DGSDFKRLVKqISSGDY-----REPTQPSDA 227
                        250       260
                 ....*....|....*....|....*..
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14073  228 SGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
97-332 1.20e-44

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: 161.31  E-value: 1.20e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  97 YAMK-VLKKATLKVRDRVRTkmerdiLVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLA 175
Cdd:cd14010   28 VAIKcVDKSKRPEVLNEVRL------THELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLETLLRQDGNLPESSVRKFGR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 176 ELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK----------------ESIDHEKKAYSFCGTVEYMAPEV 239
Cdd:cd14010  102 DLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkelfgqfsdeGNVNKVSKKQAKRGTPYYMAPEL 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 240 VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA-----KLGMPQFLSPEAQSLLRMLFKRNPANRLvnp 314
Cdd:cd14010  182 FQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEdppppPPKVSSKPSPDFKSLLKGLLEKDPAKRL--- 258
                        250
                 ....*....|....*...
gi 768032625 315 fligagpdGVEEIKRHSF 332
Cdd:cd14010  259 --------SWDELVKHPF 268
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
68-311 1.76e-44

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: 160.63  E-value: 1.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14078    5 YELHETIGSGGFAKVKLAThILTG----EKVAIKIMDKKALG-DDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL---SKESIDHEk 223
Cdd:cd14078   80 LEYCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcakPKGGMDHH- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 kAYSFCGTVEYMAPEVVNRRGHTQS-ADWWSFGVLMFEMLTGTLPFqgkDRKETMTM---ILKAKLGMPQFLSPEAQSLL 299
Cdd:cd14078  159 -LETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPF---DDDNVMALyrkIQSGKYEEPEWLSPSSKLLL 234
                        250
                 ....*....|..
gi 768032625 300 RMLFKRNPANRL 311
Cdd:cd14078  235 DQMLQVDPKKRI 246
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
428-685 1.92e-44

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: 160.47  E-value: 1.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSvckrCIHKATNME----FAVKIIDKSKRDPTE------EIEiLLRYGQHPNIITLKDVYDDGKYVYV 497
Cdd:cd06627    2 YQLGDLIGRGAFG----SVYKGLNLNtgefVAIKQISLEKIPKSDlksvmgEID-LLKKLNHPNIVKYIGSVKTKDSLYI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAE 577
Cdd:cd06627   77 ILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKD----GLVKLADFGVATKLNEV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFS-LSGGywnsVSD 656
Cdd:cd06627  153 EKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYY---DLQPMAALFRIVQDDHPpLPEN----ISP 225
                        250       260
                 ....*....|....*....|....*....
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06627  226 ELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
68-311 2.30e-44

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: 160.80  E-value: 2.30e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLkVRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14117    8 FDIGRPLGKGKFGNVYLARE---KQSKFIVALKVLFKSQI-EKEGVEHQLRREIEIQshLRHPNILRLYNYFHDRKRIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKa 225
Cdd:cd14117   84 ILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRR- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 ySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd14117  163 -TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRY 241

                 ....*.
gi 768032625 306 NPANRL 311
Cdd:cd14117  242 HPSERL 247
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
427-683 2.31e-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: 160.25  E-value: 2.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID------KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNlgslsqKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRa 576
Cdd:cd08530   80 YAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLS----AGDLVKIGDLGISKVLK- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 eNGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGpdDTPEEILARIGSGKFS-LSGGYwnsvS 655
Cdd:cd08530  155 -KNLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPF-EA--RTMQELRYKVCRGKFPpIPPVY----S 226
                        250       260
                 ....*....|....*....|....*...
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd08530  227 QDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
66-310 2.60e-44

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: 160.23  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGSdarqLYAMKVLKKATLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGK 142
Cdd:cd14083    3 DKYEFKEVLGTGAFSEVVLAEdKATGK----LVAIKCIDKKALKGKE---DSLENEIAVlrKIKHPNIVQLLDIYESKSH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL---LDEEGHIKLTDFGLSKesI 219
Cdd:cd14083   76 LYLVMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--M 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLgmpQFLSP------ 293
Cdd:cd14083  154 EDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEY---EFDSPywddis 230
                        250
                 ....*....|....*...
gi 768032625 294 -EAQSLLRMLFKRNPANR 310
Cdd:cd14083  231 dSAKDFIRHLMEKDPNKR 248
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
434-688 2.60e-44

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: 160.46  E-value: 2.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEI----EILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKKRdmiRKNQVDSVlaerNILSQA-QNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLdKILRQ-KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK------------- 572
Cdd:cd05579   80 LY-SLLENvGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNIL-IDANGH---LKLTDFGLSKvglvrrqiklsiq 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 ------QLRAENGLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFsl 646
Cdd:cd05579  155 kksngaPEKEDRRIVGTPDY----LAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFH---AETPEEIFQNILNGKI-- 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 647 sggYW---NSVSDTAKDLVSKMLHVDPHQRL---TAALVLRHPWI--VHW 688
Cdd:cd05579  226 ---EWpedPEVSDEAKDLISKLLTPDPEKRLgakGIEEIKNHPFFkgIDW 272
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
67-310 6.40e-44

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: 158.84  E-value: 6.40e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKI-SGSDArqlyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14072    1 NYRLLKTIGKGNFAKVKLARHVlTGREV----AIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKKA 225
Cdd:cd14072   77 VMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNE-FTPGNKL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVN-RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFK 304
Cdd:cd14072  156 DTFCGSPPYAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLV 235

                 ....*.
gi 768032625 305 RNPANR 310
Cdd:cd14072  236 LNPSKR 241
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
428-693 7.79e-44

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 161.14  E-value: 7.79e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQ------HPNIITLKDVYDDGKYVYVVTEL 501
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSilmelsHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKiLRQ---------KFFSereASAVLftitkTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK 572
Cdd:PTZ00263 100 VVGGELFTH-LRKagrfpndvaKFYH---AELVL-----AFEYLHSKDIIYRDLKPENLL-LDNKGH---VKVTDFGFAK 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENgllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywN 652
Cdd:PTZ00263 167 KVPDRT---FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFF---DDTPFRIYEKILAGRLKFP----N 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTA-----ALVLRHPWI--VHWDQLPQ 693
Cdd:PTZ00263 237 WFDGRARDLVKGLLQTDHTKRLGTlkggvADVKNHPYFhgANWDKLYA 284
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
72-311 1.16e-43

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: 159.82  E-value: 1.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKatlkvrdRVRTKMERDI----LVEvNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd14179   13 KPLGEGSFS---ICRKCLHKKTNQEYAVKIVSK-------RMEANTQREIaalkLCE-GHPNIVKLHEVYHDQLHTFLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG---HIKLTDFGLSKESIDHEKK 224
Cdd:cd14179   82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFARLKPPDNQP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT----MILKAKLGMPQF-------LSP 293
Cdd:cd14179  162 LKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTCTsaeeIMKKIKQGDFSFegeawknVSQ 241
                        250
                 ....*....|....*...
gi 768032625 294 EAQSLLRMLFKRNPANRL 311
Cdd:cd14179  242 EAKDLIQGLLTVDPNKRI 259
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
427-685 1.23e-43

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: 158.41  E-value: 1.23e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RDPTE-----EIEILLRYgQHPNIITLKDVYD--DGKyVYV 497
Cdd:cd14165    2 GYILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKapDDFVEkflprELEILARL-NHKSIIKTYEIFEtsDGK-VYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL-RA 576
Cdd:cd14165   80 VMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLL-LDKDFN---IKLTDFGFSKRClRD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLM---TPCYTANFVAPEVLKRQGYDAAC-DIWSLGVLLYTMLTGYTPFangpDDTPEEILARIgsgKFSLSGGYWN 652
Cdd:cd14165  156 ENGRIVlskTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPY----DDSNVKKMLKI---QKEHRVRFPR 228
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 653 SVSDTA--KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14165  229 SKNLTSecKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-318 1.35e-43

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: 158.27  E-value: 1.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKR---TQKLVAIKCIAKKALEGKE---TSIENEIAVlhKIKHPNIVALDDIYESGGHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL---LDEEGHIKLTDFGLSKesIDHE 222
Cdd:cd14167   79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSK--IEGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSF-CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLgmpQFLSP-------E 294
Cdd:cd14167  157 GSVMSTaCGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEY---EFDSPywddisdS 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 295 AQSLLRMLFKRNPANR------LVNPFLIG 318
Cdd:cd14167  234 AKDFIQHLMEKDPEKRftceqaLQHPWIAG 263
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
67-310 1.46e-43

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: 157.77  E-value: 1.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkkiSGSDAR--QLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd06627    1 NYQLGDLIGRGAFGSVY-----KGLNLNtgEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKK 224
Cdd:cd06627   76 IILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK-AKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd06627  156 ENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQdDHPPLPENISPELRDFLLQCF 235

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd06627  236 QKDPTLR 242
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
68-333 1.63e-43

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: 158.29  E-value: 1.63e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVN-------HPFIVKLHYAFQT 139
Cdd:cd14093    5 YEPKEILGRGVSSTVRrCIEKETG----QEFAVKIIDITGEKSSENEAEELREATRREIEilrqvsgHPNIIELHDVFES 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsI 219
Cdd:cd14093   81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR-L 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVV------NRRGHTQSADWWSFGVLMFEMLTGTLPFQgkDRKEtMTMILKAKLGMPQFLSP 293
Cdd:cd14093  160 DEGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFW--HRKQ-MVMLRNIMEGKYEFGSP 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 294 E-------AQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14093  237 EwddisdtAKDLISKLLVVDPKKRLT-----------AEEALEHPFF 272
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
72-333 1.72e-43

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: 157.78  E-value: 1.72e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDArqlYAMKVLKKATL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14189    7 RLLGKGGFARCYEMTDLATNKT---YAVKVIPHSRVaKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCG 230
Cdd:cd14189   84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14189  164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDR 243
                        250       260
                 ....*....|....*....|...
gi 768032625 311 LVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14189  244 LT-----------LDQILEHEFF 255
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
426-702 2.01e-43

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: 158.72  E-value: 2.01e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE------ILLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14209    1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEhtlnekRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRaenG 579
Cdd:cd14209   81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLL-IDQQG---YIKVTDFGFAKRVK---G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYwnsvSDTAK 659
Cdd:cd14209  154 RTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFA---DQPIQIYEKIVSGKVRFPSHF----SSDLK 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 660 DLVSKMLHVDPHQRL-----TAALVLRHPWIVHWDQLPQYQlNRQDAP 702
Cdd:cd14209  227 DLLRNLLQVDLTKRFgnlknGVNDIKNHKWFATTDWIAIYQ-RKVEAP 273
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
67-310 2.16e-43

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: 157.42  E-value: 2.16e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGsdarQLYAMKVLKKATLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14161    4 RYEFLETLGKGTYGRVKKARDSSG----RLVAIKSIRKDRIKdEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKKA 225
Cdd:cd14161   80 VMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSN-LYNQDKFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSpEAQSLLRMLFK 304
Cdd:cd14161  159 QTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLM 237

                 ....*.
gi 768032625 305 RNPANR 310
Cdd:cd14161  238 VNPERR 243
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
428-685 5.60e-43

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: 156.84  E-value: 5.60e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII------------------DKSKRDPTEEIEILLRYGQHPNIITLKDVY 489
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkerekrlekEISRDIRTIREAALSSLLNHPHICRLRDFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 490 DDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFG 569
Cdd:cd14077   83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL-ISKSGN---IKIIDFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 570 FAKQLRAENgLLMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFangpDDTPEEIL-ARIGSGKFSls 647
Cdd:cd14077  159 LSNLYDPRR-LLRTFCGSLYFAAPELLQAQPYTGPeVDVWSFGVVLYVLVCGKVPF----DDENMPALhAKIKKGKVE-- 231
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 648 ggYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14077  232 --YPSYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
67-310 5.97e-43

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 156.48  E-value: 5.97e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVflvKKISGSDARQLYAMKVLKKATLKVRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14098    1 KYQIIDRLGSGTFAEV---KKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQReiNILKSLEHPGIVRLIDWYEDDQHIY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG--HIKLTDFGLSKeSIDHE 222
Cdd:cd14098   78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAK-VIHTG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRR------GHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFL----S 292
Cdd:cd14098  157 TFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVdfniS 236
                        250
                 ....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANR 310
Cdd:cd14098  237 EEAIDFILRLLDVDPEKR 254
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
68-311 7.46e-43

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: 155.79  E-value: 7.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKI-SGSDArqlyAMKVL-KKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLhTGLEV----AIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLfTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd14186   79 VLEMCHNGEM-SRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd14186  158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLL 237

                 ....*...
gi 768032625 304 KRNPANRL 311
Cdd:cd14186  238 RKNPADRL 245
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
68-310 8.35e-43

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: 156.03  E-value: 8.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKI-SGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14074    5 YDLEETLGRGHFAVVKLARHVfTG----EKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDV-KFYLAELALALDHLHSLGIIYRDLKPENILLDEE-GHIKLTDFGLSKESIDHEKK 224
Cdd:cd14074   81 LELGDGGDMYDYIMKHENGLNEDLaRKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKqGLVKLTDFGFSNKFQPGEKL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSfCGTVEYMAPEVVNRRGHTQSA-DWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd14074  161 ETS-CGSLAYSAPEILLGDEYDAPAvDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRML 239

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd14074  240 IRDPKKR 246
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
424-685 9.57e-43

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: 156.25  E-value: 9.57e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVK--EDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR------DPTEEIEILLRYGQHPNIITLKDVYDDGKYV 495
Cdd:cd14197    5 FQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKgqdcrmEIIHEIAVLELAQANPWVINLHEVYETASEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKIL--RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDES--GNpesIRICDFGFA 571
Cdd:cd14197   85 ILVLEYAAGGEIFNQCVadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplGD---IKIVDFGLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLRAENGL---LMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSG 648
Cdd:cd14197  162 RILKNSEELreiMGTPEY----VAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLG---DDKQETFLNISQMNVSYSE 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 649 GYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14197  235 EEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
426-685 1.13e-42

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: 155.98  E-value: 1.13e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPteEIEILLRYGQ------HPNIITLKDVYDDGKYVYVVT 499
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQT--SMDELRKEIQamsqcnHPNVVSYYTSFVVGDELWLVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDkILRQKF----FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFA---- 571
Cdd:cd06610   79 PLLSGGSLLD-IMKSSYprggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNIL-LGEDG---SVKIADFGVSasla 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 ----KQLRAENGLLMTPCYtanfVAPEVLKR-QGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIGSGKF-S 645
Cdd:cd06610  154 tggdRTRKVRKTFVGTPCW----MAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYP---PMKVLMLTLQNDPpS 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 646 LSGGYWNSV-SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06610  227 LETGADYKKySKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
67-310 1.25e-42

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: 156.44  E-value: 1.25e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvKKISGSDARQLYAMKVLKKATLKvrDRVRTKMERD-ILVEVN------HPFIVKLHYAFQT 139
Cdd:cd14096    2 NYRLINKIGEGAFSNVY--KAVPLRNTGKPVAIKVVRKADLS--SDNLKGSSRAnILKEVQimkrlsHPNIVKLLDFQES 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL------------------- 200
Cdd:cd14096   78 DEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkaddd 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 201 ---LDEE-----------GHIKLTDFGLSKESIDHEKKaySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTL 266
Cdd:cd14096  158 etkVDEGefipgvggggiGIVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 267 PFQgKDRKETMTMilKAKLGMPQFLSP-------EAQSLLRMLFKRNPANR 310
Cdd:cd14096  236 PFY-DESIETLTE--KISRGDYTFLSPwwdeiskSAKDLISHLLTVDPAKR 283
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
428-684 1.58e-42

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: 154.93  E-value: 1.58e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR-DPTEEIEIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKiDENVQREIInHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPEsIRICDFGFAK------QLRAENG 579
Cdd:cd14662   82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSPAPR-LKICDFGYSKssvlhsQPKSTVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 llmTPCYtanfVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFANgPDDtPEEI---LARIGSGKFSLSGgyWNSVS 655
Cdd:cd14662  160 ---TPAY----IAPEVLSRKEYDGkVADVWSCGVTLYVMLVGAYPFED-PDD-PKNFrktIQRIMSVQYKIPD--YVRVS 228
                        250       260
                 ....*....|....*....|....*....
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14662  229 QDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
67-310 1.60e-42

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: 155.13  E-value: 1.60e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISgSDarQLYAMKVLK--KATLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVN-SD--QKYAMKEIRlpKSSSAVED---SRKEAVLLAKMKHPNIVAFKESFEADGHLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTR--LSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd08219   75 IVMEYCDGGDLMQKikLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKEtmtMILKAKLG----MPQFLSPEAQSL 298
Cdd:cd08219  155 AYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKN---LILKVCQGsykpLPSHYSYELRSL 231
                        250
                 ....*....|..
gi 768032625 299 LRMLFKRNPANR 310
Cdd:cd08219  232 IKQMFKRNPRSR 243
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
72-311 1.70e-42

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: 156.69  E-value: 1.70e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKV-FLVKKISGsdarQLYAMKVLKKatlkvrdRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd14092   12 EALGDGSFSVCrKCVHKKTG----QEFAVKIVSR-------RLDTSREVQLLRLCqGHPNIVKLHEVFQDELHTYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKESIDHEKKAy 226
Cdd:cd14092   81 LRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQPLK- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRR----GHTQSADWWSFGVLMFEMLTGTLPFQGKDRK----ETMTMILKAKLGMP----QFLSPE 294
Cdd:cd14092  160 TPCFTLPYAAPEVLKQAlstqGYDESCDLWSLGVILYTMLSGQVPFQSPSRNesaaEIMKRIKSGDFSFDgeewKNVSSE 239
                        250
                 ....*....|....*..
gi 768032625 295 AQSLLRMLFKRNPANRL 311
Cdd:cd14092  240 AKSLIQGLLTVDPSKRL 256
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
66-311 1.76e-42

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: 156.04  E-value: 1.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14086    1 DEYDLKEELGKGAFSVVRrCVQKSTG----QEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKESIDH 221
Cdd:cd14086   77 LVFDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ----FLSPEAQS 297
Cdd:cd14086  157 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKD 236
                        250
                 ....*....|....
gi 768032625 298 LLRMLFKRNPANRL 311
Cdd:cd14086  237 LINQMLTVNPAKRI 250
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
428-685 1.85e-42

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: 155.02  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT-------EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAgmvqrvrNEVEIHCQL-KHPSILELYNYFEDSNYVYLVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKIL-RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENG 579
Cdd:cd14186   82 MCHNGEMSRYLKnRKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNM----NIKIADFGLATQLKMPHE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggywNSVSDTAK 659
Cdd:cd14186  158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDT---DTVKNTLNKVVLADYEMP----AFLSREAQ 230
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14186  231 DLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-318 2.12e-42

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: 155.54  E-value: 2.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLkVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTG---KLYALKCIKKSPL-SRD---SSLENEIAVlkRIKHENIVTLEDIYESTTHYYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKesIDHE 222
Cdd:cd14166   78 VMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--MEQN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgkdrKETMTMIL-KAKLGMPQFLSP-------E 294
Cdd:cd14166  156 GIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY----EETESRLFeKIKEGYYEFESPfwddiseS 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 295 AQSLLRMLFKRNPANR------LVNPFLIG 318
Cdd:cd14166  232 AKDFIRHLLEKNPSKRytcekaLSHPWIIG 261
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
72-311 2.35e-42

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: 154.82  E-value: 2.35e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVF-LVKKISGSDarqlYAMKVLKKatlkvrdRVRTKMER-DILVEV-------NHPFIVKLHYAFQTEGK 142
Cdd:cd14106   14 TPLGRGKFAVVRkCIHKETGKE----YAAKFLRK-------RRRGQDCRnEILHEIavlelckDCPRVVNLHEVYETRSE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKeSI 219
Cdd:cd14106   83 LILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISR-VI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFL----SPEA 295
Cdd:cd14106  162 GEGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLA 241
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14106  242 IDFIKRLLVKDPEKRL 257
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
427-685 2.43e-42

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: 154.34  E-value: 2.43e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSvcKRCI--HKATNMEFAVKIIDKSK-------RDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYV 497
Cdd:cd05578    1 HFQILRVIGKGSFG--KVCIvqKKDTKKMFAMKYMNKQKciekdsvRNVLNELEILQEL-EHPFLVNLWYSFQDEEDMYM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaE 577
Cdd:cd05578   78 VVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNIL-LDEQGH---VHITDFNIATKLT-D 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSlsggYWNSVSDT 657
Cdd:cd05578  153 GTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVL----YPAGWSEE 228
                        250       260
                 ....*....|....*....|....*....
gi 768032625 658 AKDLVSKMLHVDPHQRL-TAALVLRHPWI 685
Cdd:cd05578  229 AIDLINKLLERDPQKRLgDLSDLKNHPYF 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
69-310 3.09e-42

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: 154.24  E-value: 3.09e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625    69 ELLKVLGQGSFGKVFLVK-KISGSDARQLYAMKVLKK-ATLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlKGKGDGKEVEVAVKTLKEdASEQQIEEFL--REARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   147 LDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidHEKK 224
Cdd:smart00221  80 MEYMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL--YDDD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   225 AYSFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQSLL 299
Cdd:smart00221 158 YYKVKGGklpIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYrLPKPPNCPPELYKLM 237
                          250
                   ....*....|.
gi 768032625   300 RMLFKRNPANR 310
Cdd:smart00221 238 LQCWAEDPEDR 248
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
74-311 5.38e-42

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: 153.15  E-value: 5.38e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd14103    1 LGRGKFGTVYrCVEKATG----KELAAKFIKCRKAKDREDVR--NEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMF-TEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEGH-IKLTDFGLSKEsIDHEKKAYSFC 229
Cdd:cd14103   75 GELFERVVDDDFElTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARK-YDPDKKLKVLF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK--LGMPQF--LSPEAQSLLRMLFKR 305
Cdd:cd14103  154 GTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKwdFDDEAFddISDEAKDFISKLLVK 233

                 ....*.
gi 768032625 306 NPANRL 311
Cdd:cd14103  234 DPRKRM 239
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
57-333 6.00e-42

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: 154.36  E-value: 6.00e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  57 KEGHEKADPSQfellkVLGQGSFGkvfLVKKISGSDARQLYAMKVLK----KATLKVRDRVR--TKMERDILVEV-NHPF 129
Cdd:cd14181    6 KEFYQKYDPKE-----VIGRGVSS---VVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVRssTLKEIHILRQVsGHPS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 130 IVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd14181   78 IITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 210 TDFGLSKEsIDHEKKAYSFCGTVEYMAPEVV------NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKa 283
Cdd:cd14181  158 SDFGFSCH-LEPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIME- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 284 klGMPQFLSPE-------AQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14181  236 --GRYQFSSPEwddrsstVKDLISRLLVVDPEIRLT-----------AEQALQHPFF 279
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
432-684 6.04e-42

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: 153.34  E-value: 6.04e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI-----LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGgE 506
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLrnevaILQQLSHPGVVNLECMFETPERVFVVMEKLHG-D 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPEsIRICDFGFA-----KQLRaeNG 579
Cdd:cd14082   88 MLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFPQ-VKLCDFGFAriigeKSFR--RS 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangpdDTPEEILARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14082  165 VVGTPAY----LAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDINDQIQNAAFMYPPNPWKEISPDAI 235
                        250       260
                 ....*....|....*....|....*
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14082  236 DLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
426-696 6.40e-42

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: 154.52  E-value: 6.40e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-------KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd05612    1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAipevirlKQEQHVHNEKRVLKEV-SHPFIIRLFWTEHDQRFLYML 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN 578
Cdd:cd05612   80 MEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-LDKEGH---IKLTDFGFAKKLRDRT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 gllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywNSVSDTA 658
Cdd:cd05612  156 ---WTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFF---DDNPFGIYEKILAGKLEFP----RHLDLYA 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 659 KDLVSKMLHVDPHQRL-----TAALVLRHPWI--VHWDQLPQYQL 696
Cdd:cd05612  226 KDLIKKLLVVDRTRRLgnmknGADDVKNHRWFksVDWDDVPQRKL 270
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
72-310 2.02e-41

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: 152.39  E-value: 2.02e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14187   13 RFLGKGGFAKCY---EITDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL-SKESIDHEKKAySFC 229
Cdd:cd14187   90 RRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLaTKVEYDGERKK-TLC 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd14187  169 GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA 248

                 .
gi 768032625 310 R 310
Cdd:cd14187  249 R 249
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
66-316 3.34e-41

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: 151.73  E-value: 3.34e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKkATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRhRPSG----QIMAVKVIR-LEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLfTRLSKEVMFTEEDvkfYLAELALA----LDHLHS-LGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd06605   76 ICMEYMDGGSL-DKILKEVGRIPER---ILGKIAVAvvkgLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DheKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI--LKAKLGMP------QFL 291
Cdd:cd06605  152 D--SLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFelLSYIVDEPppllpsGKF 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 292 SPEAQSLLRMLFKRNPANR------LVNPFL 316
Cdd:cd06605  230 SPDFQDFVSQCLQKDPTERpsykelMEHPFI 260
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
425-685 3.58e-41

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: 151.27  E-value: 3.58e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEV--KEDIGVGSYSVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14192    1 NSYYAVcpHEVLGGGRFGQVHKCTELSTGLTLAAKIIKvkgaKEREEVKNEINIMNQL-NHVNLIQLYDAFESKTNLTLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFfSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRA 576
Cdd:cd14192   80 MEYVDGGELFDRITDESY-QLTELDAILFTrqICEGVHYLHQHYILHLDLKPENILCVNSTGN--QIKIIDFGLARRYKP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTpCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSD 656
Cdd:cd14192  157 REKLKVN-FGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLG---ETDAETMNNIVNCKWDFDAEAFENLSE 232
                        250       260
                 ....*....|....*....|....*....
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14192  233 EAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
68-310 3.96e-41

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: 151.02  E-value: 3.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVR---KVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEV--MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd08529   79 EYAENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQSLLRMLFK 304
Cdd:cd08529  159 QTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKyPPISASYSQDLSQLIDSCLT 238

                 ....*.
gi 768032625 305 RNPANR 310
Cdd:cd08529  239 KDYRQR 244
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
434-673 4.14e-41

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: 150.77  E-value: 4.14e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMefAVKIIDKSK------RDPTEEIEIL--LRygqHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd13999    1 IGSGSFGEVYKGKWRGTDV--AIKKLKVEDdndellKEFRREVSILskLR---HPNIVQFIGACLSPPPLCIVTEYMPGG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd13999   76 SLYDLLHKKKIpLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNIL-LDENFT---VKIADFGLSRIKNSTTEKMTGV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAN------------------GPDDTPEEIlarigsgkfsl 646
Cdd:cd13999  152 VGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKElspiqiaaavvqkglrppIPPDCPPEL----------- 220
                        250       260
                 ....*....|....*....|....*..
gi 768032625 647 sggywnsvsdtaKDLVSKMLHVDPHQR 673
Cdd:cd13999  221 ------------SKLIKRCWNEDPEKR 235
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
428-685 4.33e-41

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: 151.63  E-value: 4.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-KSKRDPTEEI--EI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDlEEAEDEIEDIqqEIqFLSQCDSPYITKYYGSFLKGSKLWIIMEYCG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFfSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMT 583
Cdd:cd06609   83 GGSVLDLLKPGPL-DETYIAFILREVLLGLEYLHSEGKIHRDIKAANIL-LSEEGD---VKLADFGVSGQLTSTMSKRNT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKF-SLSGGYWnsvSDTAKDLV 662
Cdd:cd06609  158 FVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLS---DLHPMRVLFLIPKNNPpSLEGNKF---SKPFKDFV 231
                        250       260
                 ....*....|....*....|...
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06609  232 ELCLNKDPKERPSAKELLKHKFI 254
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
461-702 5.24e-41

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: 152.94  E-value: 5.24e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 461 KSKRDPTEEIeillrygQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG 540
Cdd:cd05584   48 KAERNILEAV-------KHPFIVDLHYAFQTGGKLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 541 VVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTG 620
Cdd:cd05584  121 IIYRDLKPENIL-LDAQGH---VKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTG 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 621 YTPF-ANGPDDTPEEILarigSGKFSLSggywNSVSDTAKDLVSKMLHVDPHQRL-----TAALVLRHPWIVH--WDQLp 692
Cdd:cd05584  197 APPFtAENRKKTIDKIL----KGKLNLP----PYLTNEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPFFRHinWDDL- 267
                        250
                 ....*....|
gi 768032625 693 qyqLNRQDAP 702
Cdd:cd05584  268 ---LAKKVEP 274
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
428-685 6.55e-41

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: 150.83  E-value: 6.55e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKED--IGVGSYSVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14193    4 YNVNKEeiLGGGRFGQVHKCEEKSSGLKLAAKIIKarsqKEKEEVKNEIEVMNQL-NHANLIQLYDAFESRNDIVLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFfSEREASAVLF--TITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENG 579
Cdd:cd14193   83 VDGGELFDRIIDENY-NLTELDTILFikQICEGIQYMHQMYILHLDLKPENILCVSREAN--QVKIIDFGLARRYKPREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTpCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTpeEILARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14193  160 LRVN-FGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFL-GEDDN--ETLNNILACQWDFEDEEFADISEEAK 235
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14193  236 DFISKLLIKEKSWRMSASEALKHPWL 261
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
72-333 7.19e-41

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: 150.55  E-value: 7.19e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKvRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTN---KVYAAKIIPHSRVS-KPHQREKIDKEIELHriLHHKHVVQFYHYFEDKENIYILLEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd14188   83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTIC 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd14188  163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPED 242
                        250       260
                 ....*....|....*....|....
gi 768032625 310 RlvnPFLigagpdgvEEIKRHSFF 333
Cdd:cd14188  243 R---PSL--------DEIIRHDFF 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
428-685 9.43e-41

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: 150.33  E-value: 9.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATN-----MEFAVKIIDKSK-RDPTEEIEI-----LLRYGQHPNIITLKDVYDDGKYVY 496
Cdd:cd14076    3 YILGRTLGEGEFGKVKLGWPLPKAnhrsgVQVAIKLIRRDTqQENCQTSKImreinILKGLTHPNIVRLLDVLKTKKYIG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRA 576
Cdd:cd14076   83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLL-LDKNRN---LVITDFGFANTFDH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLM-TPCYTANFVAPE--VLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNS 653
Cdd:cd14076  159 FNGDLMsTSCGSPCYAAPElvVSDSMYAGRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLYRYICNTPLIFPEY 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14076  239 VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
68-311 1.23e-40

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: 150.33  E-value: 1.23e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDR--VRTKMERD--ILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14105    7 YDIGEELGSGQFA---VVKKCREKSTGLEYAAKFIKKRRSKASRRgvSREDIEREvsILRQVLHPNIITLHDVFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG----HIKLTDFGLSKEsI 219
Cdd:cd14105   84 VLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAHK-I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFL----SPEA 295
Cdd:cd14105  163 EDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYfsntSELA 242
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14105  243 KDFIRQLLVKDPRKRM 258
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
428-685 1.80e-40

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: 149.21  E-value: 1.80e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSslqklfREVRIM-KILNHPNIVKLFEVIETEKTLYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGlL 581
Cdd:cd14072   81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLL-LDADMN---IKIADFGFSNEFTPGNK-L 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggYWnsVSDTAKD 660
Cdd:cd14072  156 DTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPFDG---QNLKELRERVLRGKYRIP--FY--MSTDCEN 228
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14072  229 LLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
67-361 2.00e-40

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: 150.09  E-value: 2.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFL-VKKISgsdaRQLYAMKVLKKATLKVRDRVrtkmerDILVEV-NHPFIVKLHYAFQTEGKLY 144
Cdd:cd14091    1 EYEIKEEIGKGSYSVCKRcIHKAT----GKEYAVKIIDKSKRDPSEEI------EILLRYgQHPNIITLRDVYDDGNSVY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-DEEGH---IKLTDFGLSKESID 220
Cdd:cd14091   71 LVTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQLRA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFqGKDRKETMTMILKaKLGMPQF---------L 291
Cdd:cd14091  151 ENGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILA-RIGSGKIdlsggnwdhV 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 292 SPEAQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFFStiDWNKLYRREIHPPFKPAT--GRPEDTF 361
Cdd:cd14091  229 SDSAKDLVRKMLHVDPSQRPT-----------AAQVLQHPWIR--NRDSLPQRQLTDPQDAALvkGAVAATF 287
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
69-310 2.68e-40

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 148.83  E-value: 2.68e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625    69 ELLKVLGQGSFGKVFLVK-KISGSDARQLYAMKVLKK-ATLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlKGKGGKKKVEVAVKTLKEdASEQQIEEFLR--EARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   147 LDFLRGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidHEKKA 225
Cdd:smart00219  80 MEYMEGGDLLSYLrKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDL--YDDDY 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   226 YSFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQSLLR 300
Cdd:smart00219 158 YRKRGGklpIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYrLPQPPNCPPELYDLML 237
                          250
                   ....*....|
gi 768032625   301 MLFKRNPANR 310
Cdd:smart00219 238 QCWAEDPEDR 247
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
433-685 2.87e-40

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: 149.43  E-value: 2.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-----------------------RDPTE----EIEILLRYgQHPNIITL 485
Cdd:cd14118    1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKllkqagffrrppprrkpgalgkpLDPLDrvyrEIAILKKL-DHPNVVKL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 486 KDVYDD--GKYVYVVTELMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSI 563
Cdd:cd14118   80 VEVLDDpnEDNLYMVFELVDKGAVME-VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLL-LGDDG---HV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 564 RICDFGFAKQLRAENGLLMTPCYTANFVAPEVLK--RQGYDA-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIG 640
Cdd:cd14118  155 KIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSesRKKFSGkALDIWAMGVTLYCFVFGRCPFE---DDHILGLHEKIK 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 641 SG--KFSLSggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14118  232 TDpvVFPDD----PVVSEQLKDLILRMLDKNPSERITLPEIKEHPWV 274
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
68-310 2.99e-40

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: 148.80  E-value: 2.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   68 FELLKVLGQGSFGKVFLVK-KISGSDARQLYAMKVLKKATlkvRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLY 144
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTlKGEGENTKIKVAVKTLKEGA---DEEEREDFLEEASImkKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  145 LILDFLRGGDL--FTRLSKEVMFTEEDVKFyLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKesiDHE 222
Cdd:pfam07714  78 IVTEYMPGGDLldFLRKHKRKLTLKDLLSM-ALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR---DIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  223 KKAYSFCGT-----VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEA 295
Cdd:pfam07714 154 DDDYYRKRGggklpIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGYrLPQPENCPDEL 233
                         250
                  ....*....|....*
gi 768032625  296 QSLLRMLFKRNPANR 310
Cdd:pfam07714 234 YDLMKQCWAYDPEDR 248
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
67-333 3.13e-40

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: 148.57  E-value: 3.13e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDrVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14079    3 NYILGKTLGVGSFGKVKLAEhELTG----HKVAVKILNRQKIKSLD-MEEKIRREIqiLKLFRHPHIIRLYEVIETPTDI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd14079   78 FMVMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSfCGTVEYMAPEVVNRRGHTQS-ADWWSFGVLMFEMLTGTLPFqgkDRKETMTMILKAKLGM---PQFLSPEAQSLL 299
Cdd:cd14079  158 LKTS-CGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPF---DDEHIPNLFKKIKSGIytiPSHLSPGARDLI 233
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 300 RMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14079  234 KRMLVVDPLKRIT-----------IPEIRQHPWF 256
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
74-311 6.18e-40

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: 148.08  E-value: 6.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKIsgsDARQLYAMKVL---KKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14097    9 LGQGSFGVVIEATHK---ETQTKWAIKKInreKAGSSAVKLLER---EVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-------DEEGHIKLTDFGLSKE----SI 219
Cdd:cd14097   83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGLSVQkyglGE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKkaySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEA 295
Cdd:cd14097  163 DMLQ---ETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAA 239
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14097  240 KNVLQQLLKVDPAHRM 255
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
74-311 7.03e-40

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: 147.43  E-value: 7.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvKKISGSDARQLYAMKVLKKATLK--VRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd14121    3 LGSGTYATVY--KAYRKSGAREVVAVKCVSKSSLNkaSTENLLTEIE--LLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG--HIKLTDFGLSKeSIDHEKKAYSFC 229
Cdd:cd14121   79 GGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQ-HLKPNDEAHSLR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK-LGMPQF--LSPEAQSLLRMLFKRN 306
Cdd:cd14121  158 GSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQRD 237

                 ....*
gi 768032625 307 PANRL 311
Cdd:cd14121  238 PDRRI 242
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
72-310 7.15e-40

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: 147.66  E-value: 7.15e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFL-VKKISGSDArqlyAMKVLKKATLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd14070    8 RKLGEGSFAKVREgLHAVTGEKV----AIKVIDKKKAKKDSYVTKNLRREgrIQQMIRHPNITQLLDILETENSYYLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ESIDHEKKAY 226
Cdd:cd14070   84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcaGILGYSDPFS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKD---RKETMTMILKAKLGMPQFLSPEAQSLLRMLF 303
Cdd:cd14070  164 TQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfslRALHQKMVDKEMNPLPTDLSPGAISFLRSLL 243

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd14070  244 EPDPLKR 250
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
431-685 1.14e-39

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: 146.99  E-value: 1.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd14190    9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEmvllEIQVMNQL-NHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMTpC 585
Cdd:cd14190   88 LFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH--QVKIIDFGLARRYNPREKLKVN-F 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTpeEILARIGSGKFSLSGGYWNSVSDTAKDLVSKM 665
Cdd:cd14190  165 GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFL-GDDDT--ETLNNVLMGNWYFDEETFEHVSDEAKDFVSNL 241
                        250       260
                 ....*....|....*....|
gi 768032625 666 LHVDPHQRLTAALVLRHPWI 685
Cdd:cd14190  242 IIKERSARMSATQCLKHPWL 261
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
431-685 1.31e-39

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: 147.38  E-value: 1.31e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR------DPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14198   13 SKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRgqdcraEILHEIAVLELAKSNPRVVNLHEVYETTSEIILILEYAAG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNP-ESIRICDFGFAKQLrAENGLL 581
Cdd:cd14198   93 GEIFNLCVPDlaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILL--SSIYPlGDIKIVDFGMSRKI-GHACEL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILaRIGSGKFSLSGGYWNSVSDTAKDL 661
Cdd:cd14198  170 REIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVG--EDNQETFL-NISQVNVDYSEETFSSVSQLATDF 246
                        250       260
                 ....*....|....*....|....
gi 768032625 662 VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14198  247 IQKLLVKNPEKRPTAEICLSHSWL 270
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
77-333 1.50e-39

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 146.92  E-value: 1.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  77 GSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRvRTKMERDIlvevnhPFIVKLHYAFQTEGKLYLILDFLRGGDLF 156
Cdd:cd05576   10 GVIDKVLLVMD---TRTQETFILKGLRKSSEYSRER-KTIIPRCV------PNMVCLRKYIISEESVFLVLQHAEGGKLW 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 157 TRLSK----------------------EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05576   80 SYLSKflndkeihqlfadlderlaaasRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDhekkaySFCG-TVE--YMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQ----GKDRKETmtmilkakLGM 287
Cdd:cd05576  160 WSEVED------SCDSdAIEnmYCAPEVGGISEETEACDWWSLGALLFELLTGKALVEchpaGINTHTT--------LNI 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 288 PQFLSPEAQSLLRMLFKRNPANRLvnpfliGAGPDGVEEIKRHSFF 333
Cdd:cd05576  226 PEWVSEEARSLLQQLLQFNPTERL------GAGVAGVEDIKSHPFF 265
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
428-685 1.67e-39

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: 147.24  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTEE-I------EI-LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK---KIRLDNEEEgIpstalrEIsLLKELKHPNIVKLLDVIHTENKLYLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELM----KGgeLLDKILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR 575
Cdd:cd07829   78 EYCdqdlKK--YLDKRPGP--LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLL-INRDGV---LKLADFGLARAFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AEngllmTPCYTANFV-----APEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSLSG- 648
Cdd:cd07829  150 IP-----LRTYTHEVVtlwyrAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLF---PGDSEIDQLFKI----FQILGt 217
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 649 ------------GYWNSV----------------SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07829  218 pteeswpgvtklPDYKPTfpkwpkndlekvlprlDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
68-316 1.94e-39

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: 146.73  E-value: 1.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLKVRD----RVRTKM-ERDILVEV-NHPFIVKLHYAFQTEG 141
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLR---TGRKYAIKCLYKSGPNSKDgndfQKLPQLrEIDLHRRVsRHPNIITLHDVFETEV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLFT--RLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EEGHIKLTDFGLSKEs 218
Cdd:cd13993   79 AIYIVLEYCPNGDLFEaiTENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFGLATT- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 idhEKKAYSF-CGTVEYMAPEVVNRRGH------TQSADWWSFGVLMFEMLTGTLPFQ--GKDRKETMTMILKAKLGMPQ 289
Cdd:cd13993  158 ---EKISMDFgVGSEFYMAPECFDEVGRslkgypCAAGDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPNLFDV 234
                        250       260
                 ....*....|....*....|....*....
gi 768032625 290 FL--SPEAQSLLRMLFKRNPANRLVNPFL 316
Cdd:cd13993  235 ILpmSDDFYNLLRQIFTVNPNNRILLPEL 263
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
66-311 2.12e-39

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: 146.96  E-value: 2.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14169    3 SVYELKEKLGEGAFSEVVLAQE---RGSQRLVALKCIPKKALRGKEAM-VENEIAVLRRINHENIVSLEDIYESPTHLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD---EEGHIKLTDFGLSKesIDHE 222
Cdd:cd14169   79 AMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLgmpQFLSP-------EA 295
Cdd:cd14169  157 GMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEY---EFDSPywddiseSA 233
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14169  234 KDFIRHLLERDPEKRF 249
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
67-332 2.47e-39

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: 146.07  E-value: 2.47e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkisGSDARQLYAMKVLKKAtLKVRDRVrtkmERDIL--VEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14662    1 RYELVKDIGSGNFGVARLMR---NKETKELVAVKYIERG-LKIDENV----QREIInhRSLRHPNIIRFKEVVLTPTHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EEGHIKLTDFGLSKESIDHE 222
Cdd:cd14662   73 IVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAySFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQG----KDRKETMTMILKAKLGMPQF--LSPEA 295
Cdd:cd14662  153 QPK-STVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDpddpKNFRKTIQRIMSVQYKIPDYvrVSQDC 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 296 QSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSF 332
Cdd:cd14662  232 RHLLSRIFVANPAKRIT-----------IPEIKNHPW 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
428-684 3.18e-39

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: 145.90  E-value: 3.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR-DPTEEIEIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKiDENVQREIInHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPEsIRICDFGFAK------QLRAENG 579
Cdd:cd14665   82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSPAPR-LKICDFGYSKssvlhsQPKSTVG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 llmTPCYtanfVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFANgPDDTPE--EILARIGSGKFSLSGgyWNSVSD 656
Cdd:cd14665  160 ---TPAY----IAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFED-PEEPRNfrKTIQRILSVQYSIPD--YVHISP 229
                        250       260
                 ....*....|....*....|....*...
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14665  230 ECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
66-330 4.50e-39

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: 145.85  E-value: 4.50e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFL-VKKISGsdarQLYAMKV--LKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd06609    1 ELFTLLERIGKGSFGEVYKgIDKRTN----QVVAIKVidLEEAEDEIEDIQQ---EIQFLSQCDSPYITKYYGSFLKGSK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTrLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd06609   74 LWIIMEYCGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTM 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA---KLGMPQFlSPEAQSLL 299
Cdd:cd06609  153 SKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNnppSLEGNKF-SKPFKDFV 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 300 RMLFKRNPANR------LVNPFLIGAGPDG-----VEEIKRH 330
Cdd:cd06609  232 ELCLNKDPKERpsakelLKHKFIKKAKKTSyltllIERIKKW 273
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
426-695 4.54e-39

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: 148.20  E-value: 4.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPT----EEIEILLRYgQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd05573    1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSdmlKREQIahvrAERDILADA-DSPWIVRLHYAFQDEDHLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR--- 575
Cdd:cd05573   80 MEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNIL-LDADGH---IKLADFGLCTKMNksg 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 -------AENGLLM-------------------TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpd 629
Cdd:cd05573  156 dresylnDSVNTLFqdnvlarrrphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYS--- 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 630 DTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLhVDPHQRLT-AALVLRHPWI--VHWDQLPQYQ 695
Cdd:cd05573  233 DSLVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGsAEEIKAHPFFkgIDWENLRESP 300
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
72-316 6.69e-39

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: 144.85  E-value: 6.69e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLvkKISGSDArQLYAMKVLKKATL-KVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd06632    6 QLLGSGSFGSVYE--GFNGDTG-DFFAVKEVSLVDDdKKSRESVKQLEQEIalLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ESIDHEKkay 226
Cdd:cd06632   83 YVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKhvEAFSFAK--- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRR--GHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL--GMPQFLSPEAQSLLRML 302
Cdd:cd06632  160 SFKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLC 239
                        250       260
                 ....*....|....*....|
gi 768032625 303 FKRNPANR------LVNPFL 316
Cdd:cd06632  240 LQRDPEDRptasqlLEHPFV 259
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-316 7.24e-39

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: 144.89  E-value: 7.24e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKisGSDARQlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTE-GKLYL 145
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRH--KRDRKQ-YVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEdGFLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLS--KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd08223   78 VMGFCEGGDLYTRLKeqKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL-GMPQFLSPEAQSLLRML 302
Cdd:cd08223  158 MATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAM 237
                        250       260
                 ....*....|....*....|
gi 768032625 303 FKRNPANR------LVNPFL 316
Cdd:cd08223  238 LHQDPEKRpsvkriLRQPYI 257
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
428-688 8.20e-39

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: 146.90  E-value: 8.20e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDKSKRDPTE------EIEILlRYGQHPNIITLKDV-----YDDGKYV 495
Cdd:cd07834    2 YELLKPIGSGAYgVVCS-AYDKRTGRKVAIKKISNVFDDLIDakrilrEIKIL-RHLKHENIIGLLDIlrppsPEEFNDV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMkggEL-LDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESgnpESIRICDFGFAKQ 573
Cdd:cd07834   80 YIVTELM---ETdLHKVIKSPqPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNIL-VNSN---CDLKICDFGLARG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 LRA-ENGLLMTPcytanFV------APEV-LKRQGYDAACDIWSLGVLLYTMLTGyTPFANGPD------------DTP- 632
Cdd:cd07834  153 VDPdEDKGFLTE-----YVvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTR-KPLFPGRDyidqlnlivevlGTPs 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 633 EEILARIGSGKF-----SLS---GGYWNSVSDT----AKDLVSKMLHVDPHQRLTAALVLRHPWIVHW 688
Cdd:cd07834  227 EEDLKFISSEKArnylkSLPkkpKKPLSEVFPGaspeAIDLLEKMLVFNPKKRITADEALAHPYLAQL 294
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
68-330 1.15e-38

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: 144.07  E-value: 1.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGSDArqlyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14071    2 YDIERTIGKGNFAVVKLARhRITKTEV----AIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKKAY 226
Cdd:cd14071   78 TEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSN-FFKPGELLK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd14071  157 TWCGSPPYAAPEVFEGKEYEgPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVL 236
                        250       260
                 ....*....|....*....|....*
gi 768032625 306 NPANRLvnpfligagpdGVEEIKRH 330
Cdd:cd14071  237 DPSKRL-----------TIEQIKKH 250
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
428-685 1.19e-38

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: 143.95  E-value: 1.19e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSY-SVCKrCIHKATNMEFAVKI--IDKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06612    5 FDILEKLGEGSYgSVYK-AIHKETGQVVAIKVvpVEEDLQEIIKEISIL-KQCDSPYIVKYYGSYFKNTDLWIVMEYCGA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL----RAENG 579
Cdd:cd06612   83 GSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNIL-LNEEGQ---AKLADFGVSGQLtdtmAKRNT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIG---SGKFSlSGGYWnsvSD 656
Cdd:cd06612  159 VIGTPFW----MAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIH---PMRAIFMIPnkpPPTLS-DPEKW---SP 227
                        250       260
                 ....*....|....*....|....*....
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06612  228 EFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
426-685 1.22e-38

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 144.19  E-value: 1.22e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEV-KEDIGVGSYSVCKRCIHKATNMEFAVKI--IDKSKrdpTEEIEILLRYgQHPNIITLKDVYDD-GKYVYVVTEL 501
Cdd:cd14109    3 ELYEIgEEDEKRAAQGAPFHVTERSTGRNFLAQLryGDPFL---MREVDIHNSL-DHPNIVQMHDAYDDeKLAVTVIDNL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELL-DKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpesIRICDFGFAKQLraENG 579
Cdd:cd14109   79 ASTIELVrDNLLPGKdYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDDK-----LKLADFGQSRRL--LRG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTpeEILARIGSGKFSLSGGYWNSVSDTA 658
Cdd:cd14109  152 KLTTLIYgSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFL-GDNDR--ETLTNVRSGKWSFDSSPLGNISDDA 228
                        250       260
                 ....*....|....*....|....*..
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14109  229 RDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
425-684 1.29e-38

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: 143.89  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID---KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14108    1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvraKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVVIIVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesGNPESIRICDFGFAKQLRAENgll 581
Cdd:cd14108   80 CHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMAD--QKTDQVRICDFGNAQELTPNE--- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 mtPCY----TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTpeeILARIGSGKFSLSGGYWNSVSDT 657
Cdd:cd14108  154 --PQYckygTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRT---TLMNIRNYNVAFEESMFKDLCRE 228
                        250       260
                 ....*....|....*....|....*..
gi 768032625 658 AKDLVSKMLhVDPHQRLTAALVLRHPW 684
Cdd:cd14108  229 AKGFIIKVL-VSDRLRPDAEETLEHPW 254
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
74-310 1.35e-38

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: 144.00  E-value: 1.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRtkmERDILVEVN-HPFIVKLH-YAFQTEGKLYLILDFL 150
Cdd:cd13987    1 LGEGTYGKVLLAVhKGSG----TKMALKFVPKPSTKLKDFLR---EYNISLELSvHPHIIKTYdVAFETEDYYVFAQEYA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-DEE-GHIKLTDFGLSKeSIDHEKKAYSf 228
Cdd:cd13987   74 PYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTR-RVGSTVKRVS- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 cGTVEYMAPEVVNRRGHT-----QSADWWSFGVLMFEMLTGTLPFQ---GKDRK-ETMTMILKAKLGMP--QF--LSPEA 295
Cdd:cd13987  152 -GTIPYTAPEVCEAKKNEgfvvdPSIDVWAFGVLLFCCLTGNFPWEkadSDDQFyEEFVRWQKRKNTAVpsQWrrFTPKA 230
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd13987  231 LRMFKKLLAPEPERR 245
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
67-332 1.51e-38

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: 143.97  E-value: 1.51e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKAtlkvrDRVRTKMERDIL--VEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14665    1 RYELVKDIGSGNFGVARLMRD---KQTKELVAVKYIERG-----EKIDENVQREIInhRSLRHPNIVRFKEVILTPTHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EEGHIKLTDFGLSKESIDHE 222
Cdd:cd14665   73 IVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVLHS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAySFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQG----KDRKETMTMILKAKLGMPQF--LSPEA 295
Cdd:cd14665  153 QPK-STVGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYvhISPEC 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 296 QSLLRMLFKRNPANRLVNPfligagpdgveEIKRHSF 332
Cdd:cd14665  232 RHLISRIFVADPATRITIP-----------EIRNHEW 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
432-684 1.74e-38

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: 143.58  E-value: 1.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEF-AVKIIDKSK--RDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14121    1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSKSSlnKASTEnlltEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCSG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdESGNPeSIRICDFGFAKQLRAEN---GLL 581
Cdd:cd14121   80 GDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLS-SRYNP-VLKLADFGFAQHLKPNDeahSLR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGK-FSLSGGywNSVSDTAKD 660
Cdd:cd14121  158 GSPLY----MAPEMILKKKYDARVDLWSVGVILYECLFGRAPFAS---RSFEELEEKIRSSKpIEIPTR--PELSADCRD 228
                        250       260
                 ....*....|....*....|....
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14121  229 LLLRLLQRDPDRRISFEEFFAHPF 252
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
74-268 1.76e-38

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: 143.99  E-value: 1.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISgSDARQLYAMKVLKKATL-----KVRDRVRTkmERDILVEVNHPFIVKLHYAFQTE-GKLYLIL 147
Cdd:cd13994    1 IGKGATSVVRIVTKKN-PRSGVLYAVKEYRRRDDeskrkDYVKRLTS--EYIISSKLHHPNIVKVLDLCQDLhGKWCLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS-KESIDHEKKAY 226
Cdd:cd13994   78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKESP 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 227 SF---CGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd13994  158 MSaglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPW 203
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
448-689 2.17e-38

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: 143.78  E-value: 2.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 448 KATNMEFAVKIIDKSKRDPTEEIE-------ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSER 520
Cdd:cd05611   18 RSTGDYFAIKVLKKSDMIAKNQVTnvkaeraIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCASLIKTLGGLPED 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 521 EASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK--QLRAENGLLMTpcyTANFVAPEVLKR 598
Cdd:cd05611   98 WAKQYIAEVVLGVEDLHQRGIIHRDIKPENLL-IDQTGH---LKLTDFGLSRngLEKRHNKKFVG---TPDYLAPETILG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 599 QGYDAACDIWSLGVLLYTMLTGYTPFANGpddTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTA-- 676
Cdd:cd05611  171 VGDDKMSDWWSLGCVIFEFLFGYPPFHAE---TPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKRLGAng 247
                        250
                 ....*....|....*.
gi 768032625 677 -ALVLRHPWI--VHWD 689
Cdd:cd05611  248 yQEIKSHPFFksINWD 263
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
434-684 2.44e-38

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: 143.17  E-value: 2.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RDP------TEEIEILLRYgQHPNIITLKDV-YDDGKY-VYVVTELMK 503
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrRIPngeanvKREIQILRRL-NHRNVIKLVDVlYNEEKQkLYMVMEYCV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GG--ELLDKIlRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLR--AENG 579
Cdd:cd14119   80 GGlqEMLDSA-PDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLT----TDGTLKISDFGVAEALDlfAEDD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDA--ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGgywnSVSDT 657
Cdd:cd14119  155 TCTTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFE---GDNIYKLFENIGKGEYTIPD----DVDPD 227
                        250       260
                 ....*....|....*....|....*..
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14119  228 LQDLLRGMLEKDPEKRFTIEQIRQHPW 254
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
72-310 2.70e-38

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: 143.06  E-value: 2.70e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLkvrDRVRTKMERDILV--EVNHPFIVKLhYAFQTE-GKLYLILD 148
Cdd:cd00192    1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDAS---ESERKDFLKEARVmkKLGHPNVVRL-LGVCTEeEPLYLVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEV---------MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsI 219
Cdd:cd00192   77 YMEGGDLLDFLRKSRpvfpspepsTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD-I 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILK-AKLGMPQFLSPE 294
Cdd:cd00192  156 YDDDYYRKKTGGklpIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKgYRLPKPENCPDE 235
                        250
                 ....*....|....*.
gi 768032625 295 AQSLLRMLFKRNPANR 310
Cdd:cd00192  236 LYELMLSCWQLDPEDR 251
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
60-316 2.78e-38

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: 143.90  E-value: 2.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  60 HEKADPSQfellkVLGQGSFGkvfLVKKISGSDARQLYAMKVL------KKATLKVRD-RVRTKMERDILVEVN-HPFIV 131
Cdd:cd14182    2 YEKYEPKE-----ILGRGVSS---VVRRCIHKPTRQEYAVKIIditgggSFSPEEVQElREATLKEIDILRKVSgHPNII 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 132 KLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTD 211
Cdd:cd14182   74 QLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 212 FGLSKEsIDHEKKAYSFCGTVEYMAPEVV------NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKakl 285
Cdd:cd14182  154 FGFSCQ-LDPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMS--- 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 286 GMPQFLSPE-------AQSLLRMLFKRNPANR------LVNPFL 316
Cdd:cd14182  230 GNYQFGSPEwddrsdtVKDLISRFLVVQPQKRytaeeaLAHPFF 273
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
57-331 3.28e-38

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 148.63  E-value: 3.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  57 KEGHEKADPSQ--FELLKVLGQGSFGKVFLVKKisGSDARQlyamKVLKKATLKVRDRVRT--KMERDILVEVNHPFIVK 132
Cdd:PTZ00267  56 EEVPESNNPREhmYVLTTLVGRNPTTAAFVATR--GSDPKE----KVVAKFVMLNDERQAAyaRSELHCLAACDHFGIVK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 133 LHYAFQTEGKLYLILDFLRGGDLFT----RLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIK 208
Cdd:PTZ00267 130 HFDDFKSDDKLLLIMEYGSGGDLNKqikqRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIK 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSKESIDHEK--KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG 286
Cdd:PTZ00267 210 LGDFGFSKQYSDSVSldVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYD 289
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 287 -MPQFLSPEAQSLLRMLFKRNPANR-----LVNPFLIGAGPDGVEEIKRHS 331
Cdd:PTZ00267 290 pFPCPVSSGMKALLDPLLSKNPALRpttqqLLHTEFLKYVANLFQDIVRHS 340
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
64-343 3.76e-38

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: 144.02  E-value: 3.76e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLK-KATLKVRDRVrtkMERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd06644    9 DPNEvWEIIGELGDGAFGKVY---KAKNKETGALAAAKVIEtKSEEELEDYM---VEIEILATCNHPYIVKLLGAFYWDG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDL-FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06644   83 KLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVV-----NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK---LGMPQFLS 292
Cdd:cd06644  163 TLQRRDSFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWS 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 293 PEAQSLLRMLFKRNPANRlvnpfligagPDGVEEIKrHSFFSTIDWNKLYR 343
Cdd:cd06644  243 MEFRDFLKTALDKHPETR----------PSAAQLLE-HPFVSSVTSNRPLR 282
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
67-316 4.75e-38

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: 142.40  E-value: 4.75e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd06612    4 VFDILEKLGEGSYGSVY---KAIHKETGQVVAIKVVPVEE----DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGG---DLFTRLSKEvmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd06612   77 MEYCGAGsvsDIMKITNKT--LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK---AKLGMPQFLSPEAQSLLR 300
Cdd:cd06612  155 KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNkppPTLSDPEKWSPEFNDFVK 234
                        250       260
                 ....*....|....*....|..
gi 768032625 301 MLFKRNPANR------LVNPFL 316
Cdd:cd06612  235 KCLVKDPEERpsaiqlLQHPFI 256
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
68-310 4.92e-38

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 142.59  E-value: 4.92e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAMKV--------LKKATLKVRDR-----VRTKMERDILVEVNHPFIVKLH 134
Cdd:cd14077    3 WEFVKTIGAGSMGKVKLAKHIR---TGEKCAIKIiprasnagLKKEREKRLEKeisrdIRTIREAALSSLLNHPHICRLR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd14077   80 DFLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKeSIDHEKKAYSFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSP 293
Cdd:cd14077  160 SN-LYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSS 238
                        250
                 ....*....|....*..
gi 768032625 294 EAQSLLRMLFKRNPANR 310
Cdd:cd14077  239 ECKSLISRMLVVDPKKR 255
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
68-311 4.94e-38

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: 142.85  E-value: 4.94e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDR--VRTKMERD--ILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14194    7 YDTGEELGSGQFA---VVKKCREKSTGLQYAAKFIKKRRTKSSRRgvSREDIEREvsILKEIQHPNVITLHEVYENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG----HIKLTDFGLSKEsI 219
Cdd:cd14194   84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHK-I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ-FLSPE---A 295
Cdd:cd14194  163 DFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeYFSNTsalA 242
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14194  243 KDFIRRLLVKDPKKRM 258
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
434-685 8.30e-38

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: 142.06  E-value: 8.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHK--ATNMEFAVKIIdksKRDPTEEIE-----------ILLRYGQHPNIITLKDVYDDGKYVYV-VT 499
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKEY---RRRDDESKRkdyvkrltseyIISSKLHHPNIVKVLDLCQDLHGKWClVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR--AE 577
Cdd:cd13994   78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENIL-LDEDGV---LKLTDFGTAEVFGmpAE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMT--PCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFANgPDDTPEEILARIGSGKFSLSG--GYWN 652
Cdd:cd13994  154 KESPMSagLCGSEPYMAPEVFTSGSYDGrAVDVWSCGIVLFALFTGRFPWRS-AKKSDSAYKAYEKSGDFTNGPyePIEN 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd13994  233 LLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-311 8.68e-38

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: 143.47  E-value: 8.68e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGkvfLVKKISGSDARQLYAMKVLKKatlkvrdRVRTKMERDI----LVEvNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd14180   14 LGEGSFS---VCRKCRHRQSGQEYAVKIISR-------RMEANTQREVaalrLCQ-SHPNIVALHEVLHDQYHTYLVMEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH---IKLTDFGLSKESIDHEKKAY 226
Cdd:cd14180   83 LRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK-------ETMTMILKAKLGMP----QFLSPEA 295
Cdd:cd14180  163 TPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEgeawKGVSEEA 242
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14180  243 KDLVRGLLTVDPAKRL 258
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
428-685 1.14e-37

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: 142.41  E-value: 1.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--------------------------RDPTEEI--EI-LLRYGQ 478
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraapegctqpRGPIERVyqEIaILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYDDGK--YVYVVTELMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDE 556
Cdd:cd14199   84 HPNVVKLVEVLDDPSedHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL-VGE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 557 SGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLK--RQGYDA-ACDIWSLGVLLYTMLTGYTPFANgpddtpE 633
Cdd:cd14199  162 DGH---IKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSetRKIFSGkALDVWAMGVTLYCFVFGQCPFMD------E 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 634 EILA---RIGSGKFSLSGGYwnSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14199  233 RILSlhsKIKTQPLEFPDQP--DISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
428-685 1.31e-37

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: 141.11  E-value: 1.31e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqAEEKQGVLQEYEIL-KSLHHERIMALHEAYITPRYLVLIAEFCSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLraeNGLLMTP 584
Cdd:cd14111   84 KELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVT----NLNAIKIVDFGSAQSF---NPLSLRQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CY----TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWNsVSDTAKD 660
Cdd:cd14111  157 LGrrtgTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE---DQDPQETEAKILVAKFDAFKLYPN-VSQSASL 232
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14111  233 FLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
74-333 1.37e-37

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: 141.46  E-value: 1.37e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVflvKKISGSDARQLYAMKVL--KKATLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQT-EGKLYLILDFL 150
Cdd:cd14165    9 LGEGSYAKV---KSAYSERLKCNVAIKIIdkKKAPDDFVEKFLPR-ELEILARLNHKSIIKTYEIFETsDGKVYIVMELG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI-DHEKK---AY 226
Cdd:cd14165   85 VQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLrDENGRivlSK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVnrRGHT---QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ--FLSPEAQSLLRM 301
Cdd:cd14165  165 TFCGSAAYAAPEVL--QGIPydpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRskNLTSECKDLIYR 242
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 302 LFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd14165  243 LLQPDVSQRLC-----------IDEVLSHPWL 263
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
428-685 1.39e-37

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: 141.14  E-value: 1.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI-----LLRYGQHPNIITLKDVYDD--GKYVYVVTE 500
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLvsevnILRELKHPNIVRYYDRIVDraNTTLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQK----FFSEREASAVLFTITKTVEYLH----AQGVV-HRDLKPSNIlYVDESGNpesIRICDFGFA 571
Cdd:cd08217   82 YCEGGDLAQLIKKCKkenqYIPEEFIWKIFTQLLLALYECHnrsvGGGKIlHRDLKPANI-FLDSDNN---VKLGDFGLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLRAENGL----LMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANgpddTPEEILARIGSGKFS- 645
Cdd:cd08217  158 RVLSHDSSFaktyVGTPYY----MSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFqAA----NQLELAKKIKEGKFPr 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 646 LSGGYwnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08217  230 IPSRY----SSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
427-685 1.44e-37

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: 140.90  E-value: 1.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKrDPTEEIEILL-------RYGQHPNIITLKDVYD--DGKyVYV 497
Cdd:cd14163    1 GYQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSG-GPEEFIQRFLprelqivERLDHKNIIHVYEMLEsaDGK-IYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPESIRICDFGFAKQL-RA 576
Cdd:cd14163   79 VMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-----QGFTLKLTDFGFAKQLpKG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTPCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFangpDDTP-EEILARIGSGkFSLSGGYwnSV 654
Cdd:cd14163  154 GRELSQTFCGSTAYAAPEVLQGVPHDSrKGDIWSMGVVLYVMLCAQLPF----DDTDiPKMLCQQQKG-VSLPGHL--GV 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 655 SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14163  227 SRTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
66-334 1.72e-37

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 141.15  E-value: 1.72e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLG--QGSFGKVFLVKKisgSDARQLYAMKVLKKatlkvrdrvrtKMERDILVEV-----NHPFIVKLHYAFQ 138
Cdd:PHA03390  14 KNCEIVKKLKliDGKFGKVSVLKH---KPTQKLFVQKIIKA-----------KNFNAIEPMVhqlmkDNPNFIKLYYSVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE-EGHIKLTDFGLSKe 217
Cdd:PHA03390  80 TLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLCDYGLCK- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 sIDHEKKAYSfcGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgKDRKETMTM-----ILKAKLGMPQFLS 292
Cdd:PHA03390 159 -IIGTPSCYD--GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK-EDEDEELDLesllkRQQKKLPFIKNVS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 293 PEAQSLLRMLFKRNPANRLVNpfligagpdgVEEIKRHSFFS 334
Cdd:PHA03390 235 KNANDFVQSMLKYNINYRLTN----------YNEIIKHPFLK 266
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
67-284 1.91e-37

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: 141.10  E-value: 1.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSdaRQLYAMKVLKKATLKVRdrvRTKMERD-----ILVEVN-------HPFIVKLH 134
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVRKKSNG--QTLLALKEINMTNPAFG---RTEQERDksvgdIISEVNiikeqlrHPNIVRYY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGKLYLILDFLRG---GDLFTRL-SKEVMFTEEDVKFYLAELALALDHLH-SLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd08528   76 KTFLENDRLYIVMELIEGaplGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTI 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 210 TDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK 284
Cdd:cd08528  156 TDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAE 230
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
428-684 1.96e-37

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: 141.69  E-value: 1.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTEEI-------EI-LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK---KFKESEDDEDvkktalrEVkVLRQLRHENIVNLKEAFRRKGRLYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMkGGELLDKILRQKFFSEREA-SAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAEN 578
Cdd:cd07833   80 EYV-ERTLLELLEASPGGLPPDAvRSYIWQLLQAIAYCHSHNIIHRDIKPENIL-VSESG---VLKLCDFGFARALTARP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPcYTAN--FVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFAN--------------GPDDTPEEIL----A 637
Cdd:cd07833  155 ASPLTD-YVATrwYRAPELLvGDTNYGKPVDVWAIGCIMAELLDGEPLFPGdsdidqlyliqkclGPLPPSHQELfssnP 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 638 RIGSGKF-------SLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07833  234 RFAGVAFpepsqpeSLERRYPGKVSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
67-316 2.10e-37

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: 140.64  E-value: 2.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARQLyamKVLKK---ATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd08222    1 RYRVVRKLGSGNFGTVYLVSDLKATADEEL---KVLKEisvGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLS----KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLdEEGHIKLTDFGLSKESI 219
Cdd:cd08222   78 CIVTEYCEGGDLDDKISeykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISRILM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL-GMPQFLSPEAQSL 298
Cdd:cd08222  157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAI 236
                        250       260
                 ....*....|....*....|....
gi 768032625 299 LRMLFKRNPANR------LVNPFL 316
Cdd:cd08222  237 YSRMLNKDPALRpsaaeiLKIPFI 260
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
426-689 2.48e-37

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: 140.56  E-value: 2.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdksKRDPTEEI--EIL-----LRYGQHPNIITL-KDVYDDGKyVYV 497
Cdd:cd06605    1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVI---RLEIDEALqkQILreldvLHKCNSPYIVGFyGAFYSEGD-ISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELlDKILRQ-KFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLr 575
Cdd:cd06605   77 CMEYMDGGSL-DKILKEvGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNIL-VNSRGQ---VKLCDFGVSGQL- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 aENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAN---GPDDTPEEILARI--------GSGKF 644
Cdd:cd06605  151 -VDSLAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPpnaKPSMMIFELLSYIvdepppllPSGKF 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 645 SLSggywnsvsdtAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWD 689
Cdd:cd06605  230 SPD----------FQDFVSQCLQKDPTERPSYKELMEHPFIKRYE 264
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
428-684 3.82e-37

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: 140.93  E-value: 3.82e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD---PTE---EIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEggiPNQalrEIKALQACQGHPYVVKLRDVFPHGTGFVLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGelLDKILR--QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENG 579
Cdd:cd07832   82 MLSS--LSEVLRdeERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLL-ISSTG---VLKIADFGLARLFSEEDP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTP-CYTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGyTPFANGPDDTpeEILARI----GSGKFSLSGGY--- 650
Cdd:cd07832  156 RLYSHqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNG-SPLFPGENDI--EQLAIVlrtlGTPNEKTWPELtsl 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 651 ---------------WN----SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07832  233 pdynkitfpeskgirLEeifpDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
431-630 4.43e-37

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 140.15  E-value: 4.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSYSVCKRCIHKAT-NMEFAVKIID-----KSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14202    7 KDLIGHGAFAVVFKGRHKEKhDLEVAVKCINkknlaKSQTLLGKEIKIL-KELKHENIVALYDFQEIANSVYLVMEYCNG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESG---NPESIRI--CDFGFAKQLRAeNG 579
Cdd:cd14202   86 GDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksNPNNIRIkiADFGFARYLQN-NM 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDD 630
Cdd:cd14202  165 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFqASSPQD 216
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
447-734 5.57e-37

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: 141.20  E-value: 5.57e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 447 HKATNMEFAVKIIDKSKRDPTEEIE-------ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSE 519
Cdd:cd05570   16 RKKTDELYAIKVLKKEVIIEDDDVEctmtekrVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGGDLMFHIQRARRFTE 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 520 REASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQ 599
Cdd:cd05570   96 ERARFYAAEICLALQFLHERGIIYRDLKLDNVL-LDAEGH---IKIADFGMCKEGIWGGNTTSTFCGTPDYIAPEILREQ 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 600 GYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSlsggYWNSVSDTAKDLVSKMLHVDPHQRL----- 674
Cdd:cd05570  172 DYGFSVDWWALGVLLYEMLAGQSPF---EGDDEDELFEAILNDEVL----YPRWLSREAVSILKGLLTKDPARRLgcgpk 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 675 TAALVLRHPW--IVHWDQLpqyqLNRQDAPHL---VKGAM-AATYSALNRNQSPVLEPVGRSTLAQ 734
Cdd:cd05570  245 GEADIKAHPFfrNIDWDKL----EKKEVEPPFkpkVKSPRdTSNFDPEFTSESPRLTPVDSDLLTN 306
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
426-686 6.53e-37

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: 139.32  E-value: 6.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT-------EEIEILlRYGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14116    5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAgvehqlrREVEIQ-SHLRHPNILRLYGYFHDATRVYLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAkqLRAEN 578
Cdd:cd14116   84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL----GSAGELKIADFGWS--VHAPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSlsggYWNSVSDTA 658
Cdd:cd14116  158 SRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEA---NTYQETYKRISRVEFT----FPDFVTEGA 230
                        250       260
                 ....*....|....*....|....*...
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd14116  231 RDLISRLLKHNPSQRPMLREVLEHPWIT 258
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
66-310 7.14e-37

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: 139.25  E-value: 7.14e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKkatLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14107    2 SVYEVKEEIGRGTFG---FVKRVTHKGNGECCAAKFIP---LRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLIL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL--DEEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd14107   76 ILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQE-ITPSE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL--GMPQF--LSPEAQSLL 299
Cdd:cd14107  155 HQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVswDTPEIthLSEDAKDFI 234
                        250
                 ....*....|.
gi 768032625 300 RMLFKRNPANR 310
Cdd:cd14107  235 KRVLQPDPEKR 245
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
418-684 9.92e-37

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: 141.28  E-value: 9.92e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 418 HRNSIQFT-----DGYEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDKSKRDPT------EEIEiLLRYGQHPNIITL 485
Cdd:cd07851    2 YRQELNKTvwevpDRYQNLSPVGSGAYgQVCS-AFDTKTGRKVAIKKLSRPFQSAIhakrtyRELR-LLKHMKHENVIGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 486 KDVY------DDGKYVYVVTELMkgGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDEsgN 559
Cdd:cd07851   80 LDVFtpasslEDFQDVYLVTHLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLA-VNE--D 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 560 PEsIRICDFGFAKQLRAEngllMTPcYTAN--FVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPD------- 629
Cdd:cd07851  155 CE-LKILDFGLARHTDDE----MTG-YVATrwYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFP-GSDhidqlkr 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 630 -----DTP-EEILARIGSgkfSLSGGYWNSVSDTAK---------------DLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07851  228 imnlvGTPdEELLKKISS---ESARNYIQSLPQMPKkdfkevfsganplaiDLLEKMLVLDPDKRITAAEALAHPY 300
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
434-683 1.12e-36

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 138.66  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKA-TNMEFAVKIID-----KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd14120    1 IGHGAFAVVFKGRHRKkPDLPVAIKCITkknlsKSQNLLGKEIKILKEL-SHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESG-NPE----SIRICDFGFAKQLraeNGLLM 582
Cdd:cd14120   80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrKPSpndiRLKIADFGFARFL---QDGMM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 --TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANgpddTPEEiLARIGSGKFSLSGGYWNSVSDTAK 659
Cdd:cd14120  157 aaTLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFqAQ----TPQE-LKAFYEKNANLRPNIPSGTSPALK 231
                        250       260
                 ....*....|....*....|....
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14120  232 DLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
68-333 1.25e-36

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: 138.58  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVflvKKISGSDARQLYAMKVLKKAtlKVRDRVRTK-MERDILV--EVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14162    2 YIVGKTLGHGSYAVV---KKAYSTKHKCKVAIKIVSKK--KAPEDYLQKfLPREIEVikGLKHPNLICFYEAIETTSRVY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK---ESIDH 221
Cdd:cd14162   77 IIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgvmKTKDG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKK-AYSFCGTVEYMAPEVVnrRG---HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMP--QFLSPEA 295
Cdd:cd14162  157 KPKlSETYCGSYAYASPEIL--RGipyDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR-RVVFPknPTVSEEC 233
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 296 QSLL-RMLfkrNPANRLVNpfligagpdgVEEIKRHSFF 333
Cdd:cd14162  234 KDLIlRML---SPVKKRIT----------IEEIKRDPWF 259
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
74-271 1.91e-36

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: 137.97  E-value: 1.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd13978    1 LGSGGFGTVSKARHVS---WFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLA-ELALALDHLHSL--GIIYRDLKPENILLDEEGHIKLTDFGLSK-----ESIDHEKKA 225
Cdd:cd13978   78 SLKSLLEREIQDVPWSLRFRIIhEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRGT 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 226 YSFCGTVEYMAPEVVN--RRGHTQSADWWSFGVLMFEMLTGTLPFQGK 271
Cdd:cd13978  158 ENLGGTPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLTRKEPFENA 205
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
74-311 2.07e-36

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 137.89  E-value: 2.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISGSDarQLYAMKVLKKATLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPD--LPVAIKCITKKNLSKSQNLLGK-EIKILKELSHENVVALLDCQETSSSVYLVMEYCNGG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG---------HIKLTDFGLSKeSIDHEKK 224
Cdd:cd14120   78 DLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFAR-FLQDGMM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLRM 301
Cdd:cd14120  157 AATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIpsgTSPALKDLLLG 236
                        250
                 ....*....|
gi 768032625 302 LFKRNPANRL 311
Cdd:cd14120  237 LLKRNPKDRI 246
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
64-346 2.73e-36

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: 138.24  E-value: 2.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQF-ELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKatlKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd06643    2 NPEDFwEIVGELGDGAFGKVY---KAQNKETGILAAAKVIDT---KSEEELEDYMvEIDILASCDHPNIVKLLDAFYYEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDL-FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06643   76 NLWILIEFCAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTR 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVV-----NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK---LGMPQFLS 292
Cdd:cd06643  156 TLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWS 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 293 PEAQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFFSTIDWNKLYRREI 346
Cdd:cd06643  236 PEFKDFLRKCLEKNVDARWT-----------TSQLLQHPFVSVLVSNKPLRELI 278
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
426-685 2.92e-36

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: 137.00  E-value: 2.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK---SKRDPT---EEIEILlRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14002    1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKrgkSEKELRnlrQEIEIL-RKLNHPNIIEMLDSFETKKEFVVVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLrAENG 579
Cdd:cd14002   80 EYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILI----GKGGVVKLCDFGFARAM-SCNT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLM-----TPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF------------ANGPDDTPEEIlarigsg 642
Cdd:cd14002  154 LVLtsikgTPLY----MAPELVQEQPYDHTADLWSLGCILYELFVGQPPFytnsiyqlvqmiVKDPVKWPSNM------- 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 643 kfslsggywnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14002  223 ------------SPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
72-311 3.93e-36

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: 137.02  E-value: 3.93e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDArqlYAMKVLKKATLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd14192   10 EVLGGGRFGQVHKCTELSTGLT---LAAKIIKVKGAKEREEV--KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEGH-IKLTDFGLSKESIDHEKKAYSF 228
Cdd:cd14192   85 GGELFDRITDEsYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVNF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 cGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRMLFK 304
Cdd:cd14192  165 -GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLV 243

                 ....*..
gi 768032625 305 RNPANRL 311
Cdd:cd14192  244 KEKSCRM 250
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
73-316 3.94e-36

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: 137.28  E-value: 3.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFL-VKKISGsdarQLYAMK--VLKKATLKVRDRVRT-----KMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd06628    7 LIGSGSFGSVYLgMNASSG----ELMAVKqvELPSVSAENKDRKKSmldalQREIALLRELQHENIVQYLGSSSDANHLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE------S 218
Cdd:cd06628   83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleanslS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRketMTMILK----AKLGMPQFLSPE 294
Cdd:cd06628  163 TKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ---MQAIFKigenASPTIPSNISSE 239
                        250       260
                 ....*....|....*....|....*...
gi 768032625 295 AQSLLRMLF-----KRNPANRLV-NPFL 316
Cdd:cd06628  240 ARDFLEKTFeidhnKRPTADELLkHPFL 267
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
67-310 5.29e-36

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: 136.70  E-value: 5.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14184    2 KYKIGKVIGDGNFA---VVKECVERSTGKEFALKIIDKAKCCGKEHL-IENEVSILRRVKHPNIIMLIEEMDTPAELYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFGLSKESidhE 222
Cdd:cd14184   78 MELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV---E 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKD--RKETMTMILKAKLGMPQ----FLSPEAQ 296
Cdd:cd14184  155 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSpywdNITDSAK 234
                        250
                 ....*....|....
gi 768032625 297 SLLRMLFKRNPANR 310
Cdd:cd14184  235 ELISHMLQVNVEAR 248
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
428-685 6.80e-36

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: 136.24  E-value: 6.80e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCiHKATNMEFAVKIIDKSK-RDPTE------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14161    5 YEFLETLGKGTYGRVKKA-RDSSGRLVAIKSIRKDRiKDEQDllhirrEIEIMSSL-NHPHIISVYEVFENSSKIVIVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENgL 580
Cdd:cd14161   83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENIL-LDANGN---IKIADFGLSNLYNQDK-F 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGKFSLSggywNSVSDtAK 659
Cdd:cd14161  158 LQTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPF-DGHDY--KILVKQISSGAYREP----TKPSD-AC 229
                        250       260
                 ....*....|....*....|....*.
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14161  230 GLIRWLLMVNPERRATLEDVASHWWV 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
74-331 8.02e-36

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: 136.72  E-value: 8.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVR----------------DRVRTKMER-----DILVEVNHPFIVK 132
Cdd:cd14118    2 IGKGSYG---IVKLAYNEEDNTLYAMKILSKKKLLKQagffrrppprrkpgalGKPLDPLDRvyreiAILKKLDHPNVVK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 133 LHYAFQ--TEGKLYLILDFLRGGdlftrlskEVM-------FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE 203
Cdd:cd14118   79 LVEVLDdpNEDNLYMVFELVDKG--------AVMevptdnpLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 204 EGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQS---ADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI 280
Cdd:cd14118  151 DGHVKIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKI 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 281 LKAKLGMPQ--FLSPEAQSLLRMLFKRNPANRLVNPfligagpdgveEIKRHS 331
Cdd:cd14118  231 KTDPVVFPDdpVVSEQLKDLILRMLDKNPSERITLP-----------EIKEHP 272
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-310 8.19e-36

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: 137.49  E-value: 8.19e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATG---KLFAVKCIPKKALKGKE---SSIENEIAVlrKIKHENIVALEDIYESPNHLYL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKESIDHE 222
Cdd:cd14168   86 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSfCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA--KLGMPQF--LSPEAQSL 298
Cdd:cd14168  166 VMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyEFDSPYWddISDSAKDF 244
                        250
                 ....*....|..
gi 768032625 299 LRMLFKRNPANR 310
Cdd:cd14168  245 IRNLMEKDPNKR 256
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
428-685 8.92e-36

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: 136.21  E-value: 8.92e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd06647   89 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTM 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGS-GKFSLSGGywNSVSDTAKDLVS 663
Cdd:cd06647  164 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIATnGTPELQNP--EKLSAIFRDFLN 238
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06647  239 RCLEMDVEKRGSAKELLQHPFL 260
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
434-685 1.24e-35

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: 135.65  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRREllfnEVVIMRDY-QHPNIVEMYSSYLVGDELWVVMEFLEGGALTD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 kILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAE----NGLLMTPC 585
Cdd:cd06648   94 -IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSIL-LTSDGR---VKLSDFGFCAQVSKEvprrKSLVGTPY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTAnfvaPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIGSGKFSLSGGYWNsVSDTAKDLVSKM 665
Cdd:cd06648  169 WMA----PEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEP---PLQAMKRIRDNEPPKLKNLHK-VSPRLRSFLDRM 240
                        250       260
                 ....*....|....*....|
gi 768032625 666 LHVDPHQRLTAALVLRHPWI 685
Cdd:cd06648  241 LVRDPAQRATAAELLNHPFL 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
68-316 1.38e-35

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: 135.42  E-value: 1.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFL-VKKISGsdarQLYAMKVLKkatLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd06614    2 YKNLEKIGEGASGEVYKaTDRATG----KEVAIKKMR---LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVV 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLS-KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG----LSKEsidH 221
Cdd:cd06614   75 MEYMDGGSLTDIITqNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGfaaqLTKE---K 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIlkAKLGMPQF-----LSPEAQ 296
Cdd:cd06614  152 SKRN-SVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPLRALFLI--TTKGIPPLknpekWSPEFK 228
                        250       260
                 ....*....|....*....|....*.
gi 768032625 297 SLLRMLFKRNPANR------LVNPFL 316
Cdd:cd06614  229 DFLNKCLVKDPEKRpsaeelLQHPFL 254
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
428-693 2.07e-35

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: 137.06  E-value: 2.07e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS-------KRDPTEEIEILLRyGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSetlaqeeVSFFEEERDIMAK-ANSPWITKLQYAFQDSENLYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENG 579
Cdd:cd05601   82 YHPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENIL-IDRTGH---IKLADFGSAAKLSSDKT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LL-MTPCYTANFVAPEVL------KRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWN 652
Cdd:cd05601  158 VTsKMPVGTPDYIAPEVLtsmnggSKGTYGVECDWWSLGIVAYEMLYGKTPFT---EDTVIKTYSNIMNFKKFLKFPEDP 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 653 SVSDTAKDLVSKMLhVDPHQRLTAALVLRHPWI--VHWDQLPQ 693
Cdd:cd05601  235 KVSESAVDLIKGLL-TDAKERLGYEGLCCHPFFsgIDWNNLRQ 276
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
447-689 2.15e-35

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: 136.60  E-value: 2.15e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 447 HKATNMEFAVKIIDKS---KRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQ--KFF 517
Cdd:cd05574   22 LKGTGKLFAMKVLDKEemiKRNKVKrvltEREILATL-DHPFLPTLYASFQTSTHLCFVMDYCPGGELFRLLQKQpgKRL 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL--------RAENGLLMTPCY--- 586
Cdd:cd05574  101 PEEVARFYAAEVLLALEYLHLLGFVYRDLKPENIL-LHESGH---IMLTDFDLSKQSsvtpppvrKSLRKGSRRSSVksi 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 ------------------TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSG 648
Cdd:cd05574  177 eketfvaepsarsnsfvgTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKG---SNRDETFSNILKKELTFPE 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 649 GywNSVSDTAKDLVSKMLHVDPHQRL----TAALVLRHPWI--VHWD 689
Cdd:cd05574  254 S--PPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPFFrgVNWA 298
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
64-340 2.29e-35

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: 135.64  E-value: 2.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQF-ELLKVLGQGSFGKVFLVKKisgsdaRQLYAMKVLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd06611    2 NPNDIwEIIGELGDGAFGKVYKAQH------KETGLFAAAKIIQIESEEELEDFMvEIDILSECKHPNIVGLYEAYFYEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06611   76 KLWILIEFCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVN-----RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA---KLGMPQFLS 292
Cdd:cd06611  156 TLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSeppTLDQPSKWS 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANRlvnpflIGAGpdgveEIKRHSFFSTIDWNK 340
Cdd:cd06611  236 SSFNDFLKSCLVKDPDDR------PTAA-----ELLKHPFVSDQSDNK 272
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
428-685 3.22e-35

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: 135.08  E-value: 3.22e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---------RDPT---------------------EEIEILLRYg 477
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygfprRPPPrgskaaqgeqakplaplervyQEIAILKKL- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 478 QHPNIITLKDVYDDGKY--VYVVTELMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVD 555
Cdd:cd14200   81 DHVNIVKLIEVLDDPAEdnLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 556 ESgnpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVL--KRQGYDA-ACDIWSLGVLLYTMLTGYTPFANgpddtp 632
Cdd:cd14200  160 DG----HVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLsdSGQSFSGkALDVWAMGVTLYCFVYGKCPFID------ 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 633 EEILA---RIGSGKFSLSGGywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14200  230 EFILAlhnKIKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
72-333 3.25e-35

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: 134.41  E-value: 3.25e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFL-VKKISGsdaRQLyAMKVL------KKATLKVRdrvrtKMERDI--LVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd06625    6 KLLGQGAFGQVYLcYDADTG---REL-AVKQVeidpinTEASKEVK-----ALECEIqlLKNLQHERIVQYYGCLQDEKS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ESID 220
Cdd:cd06625   77 LSIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTIC 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgkdRKETMTMILK-----AKLGMPQFLSPEA 295
Cdd:cd06625  157 SSTGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWA---EFEPMAAIFKiatqpTNPQLPPHVSEDA 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 296 QSLLRMLFKRNPANRlvnpfligagPDGvEEIKRHSFF 333
Cdd:cd06625  234 RDFLSLIFVRNKKQR----------PSA-EELLSHSFV 260
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
70-332 3.40e-35

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: 134.53  E-value: 3.40e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVFLVKKISGSDAR--QLYAMKVLKKATLKVRDRVrTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14076    5 LGRTLGEGEFGKVKLGWPLPKANHRsgVQVAIKLIRRDTQQENCQT-SKIMREIniLKGLTHPNIVRLLDVLKTKKYIGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKKA 225
Cdd:cd14076   84 VLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANT-FDHFNGD 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 Y--SFCGTVEYMAPEVVNRRG--HTQSADWWSFGVLMFEMLTGTLPF-------QGKDRKETMTMILKAKLGMPQFLSPE 294
Cdd:cd14076  163 LmsTSCGSPCYAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPK 242
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 295 AQSLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSF 332
Cdd:cd14076  243 ARDLLRRILVPNPRKRI-----------RLSAIMRHAW 269
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
434-746 4.09e-35

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: 135.91  E-value: 4.09e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEI----EILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKailKRNEVKHImaerNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05575   83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENIL-LDSQGH---VVLTDFGLCKEGIEPSDTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTpEEILARIGSGKFSLSggywNSVSDTAKDLVSKML 666
Cdd:cd05575  159 TPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYS--RDT-AEMYDNILHKPLRLR----TNVSPSARDLLEGLL 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 667 HVDPHQRLTAAL----VLRHPWI--VHWDQLPQYQLNRQDAPHlVKGAMAAtysalnRNQSP--VLEPVGRSTLAQRRGC 738
Cdd:cd05575  232 QKDRTKRLGSGNdfleIKNHSFFrpINWDDLEAKKIPPPFNPN-VSGPLDL------RNIDPefTREPVPASVGKSADSV 304

                 ....*...
gi 768032625 739 LHFAGLPK 746
Cdd:cd05575  305 AVSASVQE 312
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
74-333 4.77e-35

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (AMPK) and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 133.92  E-value: 4.77e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVflvKKISGSDARQLYAMKVLKKATLKV----RDRVRTKMErdILVEVNHPFIVKLHYAFQTE--GKLYLIL 147
Cdd:cd14119    1 LGEGSYGKV---KEVLDTETLCRRAVKILKKRKLRRipngEANVKREIQ--ILRRLNHRNVIKLVDVLYNEekQKLYMVM 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGdlftrlSKEVMFTEEDVKF-------YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES-- 218
Cdd:cd14119   76 EYCVGG------LQEMLDSAPDKRLpiwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEALdl 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEVVN--RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQ 296
Cdd:cd14119  150 FAEDDTCTTSQGSPAFQPPEIANgqDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQ 229
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 297 SLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:cd14119  230 DLLRGMLEKDPEKRF-----------TIEQIRQHPWF 255
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
68-310 4.84e-35

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: 134.34  E-value: 4.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKkatLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd13996    8 FEEIELLGSGGFGSVYKVRNKVDG---VTYAIKKIR---LTEKSSASEKVLREVkaLAKLNHPNIVRYYTAWVEEPPLYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYL---AELALALDHLHSLGIIYRDLKPENILLDEE-GHIKLTDFGLSKESIDH 221
Cdd:cd13996   82 QMELCEGGTLRDWIDRRNSSSKNDRKLALelfKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAY--------------SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLtgtLPFQ-GKDRKETMTMILKAKLg 286
Cdd:cd13996  162 KRELNnlnnnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKtAMERSTILTDLRNGIL- 237
                        250       260
                 ....*....|....*....|....*...
gi 768032625 287 mPQFLS----PEAQSLLRMLfKRNPANR 310
Cdd:cd13996  238 -PESFKakhpKEADLIQSLL-SKNPEER 263
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
428-685 5.01e-35

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: 134.60  E-value: 5.01e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT---EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVlvkKEISIL-NIARHRNILRLHESFESHEELVMIFEFISG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMT 583
Cdd:cd14104   81 VDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGS--YIKIIEFGQSRQLKPGDKFRLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 pcYT-ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLV 662
Cdd:cd14104  159 --YTsAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEA---ETNQQTIENIRNAEYAFDDEAFKNISIEALDFV 233
                        250       260
                 ....*....|....*....|...
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14104  234 DRLLVKERKSRMTAQEALNHPWL 256
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
428-685 5.02e-35

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: 136.15  E-value: 5.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEILLRYGQHPNIITLKDVY--DDGKYVYVVT 499
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDaqrtfrEIMFLQELNDHPNIIKLLNVIraENDKDIYLVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGelLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPE-SIRICDFGFAKQLRAEN 578
Cdd:cd07852   89 EYMETD--LHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILL-----NSDcRVKLADFGLARSLSQLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTaNFVA------PEVL-KRQGYDAACDIWSLGVLLYTMLTGyTPFANG--------------PDDTPEEILA 637
Cdd:cd07852  162 EDDENPVLT-DYVAtrwyraPEILlGSTRYTKGVDMWSVGCILGEMLLG-KPLFPGtstlnqlekiieviGRPSAEDIES 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 638 rIGSG-------------KFSLSgGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07852  240 -IQSPfaatmleslppsrPKSLD-ELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
428-684 5.53e-35

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: 134.58  E-value: 5.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDKSKRDPTE-----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd07830    1 YKVIKQLGDGTFgSVYL-ARNKETGELVAIKKMKKKFYSWEEcmnlrEVKSLRKLNEHPNIVKLKEVFRENDELYFVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGgELLDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAEng 579
Cdd:cd07830   80 MEG-NLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVS----GPEVVKIADFGLAREIRSR-- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 llmtPCYTAnFV------APEVLKRQG-YDAACDIWSLGVL---LYTMltgyTPFANGPDDTPE--EILARIGSGKFSls 647
Cdd:cd07830  153 ----PPYTD-YVstrwyrAPEILLRSTsYSSPVDIWALGCImaeLYTL----RPLFPGSSEIDQlyKICSVLGTPTKQ-- 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 648 ggYWN--------------------------SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07830  222 --DWPegyklasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
434-680 5.62e-35

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: 133.91  E-value: 5.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS-------KRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllkphqKEKMSMEIAIH-RSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd14187   94 LLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM----EVKIGDFGLATKVEYDGERKKTLCG 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKML 666
Cdd:cd14187  170 TPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFET---SCLKETYLRIKKNEYSIP----KHINPVAASLIQKML 242
                        250
                 ....*....|....
gi 768032625 667 HVDPHQRLTAALVL 680
Cdd:cd14187  243 QTDPTARPTINELL 256
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
68-311 7.64e-35

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: 133.54  E-value: 7.64e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDR--VRTKMER--DILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14196    7 YDIGEELGSGQFA---IVKKCREKSTGLEYAAKFIKKRQSRASRRgvSREEIERevSILRQVLHPNIITLHDVYENRTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG----HIKLTDFGLSKEsI 219
Cdd:cd14196   84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIKLIDFGLAHE-I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGM-PQFLSPE---A 295
Cdd:cd14196  163 EDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdEEFFSHTselA 242
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14196  243 KDFIRKLLVKETRKRL 258
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
68-310 8.29e-35

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: 132.89  E-value: 8.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLV-KKISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 145
Cdd:cd13997    2 FHELEQIGSGSFSEVFKVrSKVDG----CLYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGG---DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE---SI 219
Cdd:cd13997   78 QMELCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRletSG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKkaysfcGTVEYMAPEVVN-RRGHTQSADWWSFGVLMFEMLTGT-LPFQGKDRKEtmtmILKAKLGMP--QFLSPEA 295
Cdd:cd13997  158 DVEE------GDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEpLPRNGQQWQQ----LRQGKLPLPpgLVLSQEL 227
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd13997  228 TRLLKVMLDPDPTRR 242
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
66-283 8.32e-35

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: 133.51  E-value: 8.32e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFEL--LKVLGQGSFGKVF-LVKKISGSDarqlYAMKVLKKATLKVRDRVRTKMerDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd14190    2 STFSIhsKEVLGGGKFGKVHtCTEKRTGLK----LAAKVINKQNSKDKEMVLLEI--QVMNQLNHRNLIQLYEAIETPNE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-DEEGH-IKLTDFGLSKESI 219
Cdd:cd14190   76 IVLFMEYVEGGELFERIVDEdYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYN 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 220 DHEKKAYSFcGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA 283
Cdd:cd14190  156 PREKLKVNF-GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMG 218
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
427-685 9.27e-35

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: 133.06  E-value: 9.27e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT-------EEIEILLRYgQHPNIITLKDVYD-DGKYVYVV 498
Cdd:cd14164    1 GYTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfvqkflpRELSILRRV-NHPNIVQMFECIEvANGRLYIV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TElMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRICDFGFAKQLRAEN 578
Cdd:cd14164   80 ME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL---SADDRKIKIADFGFARFVEDYP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVLKRQGYDAA-CDIWSLGVLLYTMLTGYTPFangpDDTPEEILARIGSGKFSLSGgywNSVSDT 657
Cdd:cd14164  156 ELSTTFCGSRAYTPPEVILGTPYDPKkYDVWSLGVVLYVMVTGTMPF----DETNVRRLRLQQRGVLYPSG---VALEEP 228
                        250       260
                 ....*....|....*....|....*...
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14164  229 CRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
68-311 9.98e-35

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: 133.09  E-value: 9.98e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14114    4 YDILEELGTGAFGVVHrCTERATG----NNFAAKFIMTPHESDKETVRK--EIQIMNQLHHPKLINLHDAFEDDNEMVLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EEGHIKLTDFGLSKEsIDHEK 223
Cdd:cd14114   78 LEFLSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH-LDPKE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLL 299
Cdd:cd14114  157 SVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFI 236
                        250
                 ....*....|..
gi 768032625 300 RMLFKRNPANRL 311
Cdd:cd14114  237 RKLLLADPNKRM 248
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
423-685 1.09e-34

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: 135.19  E-value: 1.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILlRYGQHPNIITLKDV------YD 490
Cdd:cd07855    2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTtakrtlRELKIL-RHFKHDNIIAIRDIlrpkvpYA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGF 570
Cdd:cd07855   81 DFKDVYVVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL-VNENC---ELKIGDFGM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQL---RAENGLLMTPcYTAN--FVAPEV-LKRQGYDAACDIWSLGVLLYTMLtGYTPFANGPD-------------DT 631
Cdd:cd07855  156 ARGLctsPEEHKYFMTE-YVATrwYRAPELmLSLPEYTQAIDMWSVGCIFAEML-GRRQLFPGKNyvhqlqliltvlgTP 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 632 PEEILARIGSGKF--------SLSGGYWNSV----SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07855  234 SQAVINAIGADRVrryiqnlpNKQPVPWETLypkaDQQALDLLSQMLRFDPSERITVAEALQHPFL 299
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
67-333 1.23e-34

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: 133.78  E-value: 1.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkisGSDARQLYAMK-VLKKATLKVRdrvrtkmERDILVEVNHPFIVKLHYAFQTEGK--- 142
Cdd:cd14137    5 SYTIEKVIGSGSFGVVYQAK---LLETGEVVAIKkVLQDKRYKNR-------ELQIMRRLKHPNIVKLKYFFYSSGEkkd 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 ---LYLILDFLrGGDLF-----TRLSKEVMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE-GHIKLTDFG 213
Cdd:cd14137   75 evyLNLVMEYM-PETLYrvirhYSKNKQTI-PIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLCDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LSKESIDHEK-KAYsFCgTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP--- 288
Cdd:cd14137  153 SAKRLVPGEPnVSY-IC-SRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKV-LGTPtre 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 289 QFLS---------------------------PEAQSLLRMLFKRNPANRLvNPFligagpdgveEIKRHSFF 333
Cdd:cd14137  230 QIKAmnpnytefkfpqikphpwekvfpkrtpPDAIDLLSKILVYNPSKRL-TAL----------EALAHPFF 290
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
66-310 1.30e-34

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: 133.26  E-value: 1.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KIsgsDARQlYAMKvlkkatlKVRDRVRTKMERDILVEV------NHPFIVKLHYAFQ 138
Cdd:cd14046    6 TDFEELQVLGKGAFGQVVKVRnKL---DGRY-YAIK-------KIKLRSESKNNSRILREVmllsrlNHQHVVRYYQAWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-- 216
Cdd:cd14046   75 ERANLYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATsn 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 --------------------ESIDHEKKAysfcGTVEYMAPEVVNRRG--HTQSADWWSFGVLMFEMltgTLPFQ-GKDR 273
Cdd:cd14046  155 klnvelatqdinkstsaalgSSGDLTGNV----GTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM---CYPFStGMER 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 274 KETMTMILKAKLGMPQ-FLS---PEAQSLLRMLFKRNPANR 310
Cdd:cd14046  228 VQILTALRSVSIEFPPdFDDnkhSKQAKLIRWLLNHDPAKR 268
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
434-685 1.46e-34

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: 132.53  E-value: 1.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIE---ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKEVslvddDKKSRESVKQLEqeiALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLdKILrQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLLM- 582
Cdd:cd06632   88 SIH-KLL-QRYGAFEEPVIRLYTrqILSGLAYLHSRNTVHRDIKGANIL-VDTNG---VVKLADFGMAKHVEAFSFAKSf 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 --TPCYtanfVAPEVLKRQ--GYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggYWNSVSDTA 658
Cdd:cd06632  162 kgSPYW----MAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWS---QYEGVAAIFKIGNSGELPP--IPDHLSPDA 232
                        250       260
                 ....*....|....*....|....*..
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06632  233 KDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
67-316 1.72e-34

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: 132.44  E-value: 1.72e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARqlYAMKVLKKATLKVRDRVRTKmERDILVEVNHPFIVKLhYAFQT-EGKLYL 145
Cdd:cd14202    3 EFSRKDLIGHGAFAVVFKGRHKEKHDLE--VAVKCINKKNLAKSQTLLGK-EIKILKELKHENIVAL-YDFQEiANSVYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG---------HIKLTDFGLSK 216
Cdd:cd14202   79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFAR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 eSIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKL---GMPQFLSP 293
Cdd:cd14202  159 -YLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSlspNIPRETSS 237
                        250       260
                 ....*....|....*....|....*....
gi 768032625 294 EAQSLLRMLFKRNPANRLV------NPFL 316
Cdd:cd14202  238 HLRQLLLGLLQRNQKDRMDfdeffhHPFL 266
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
66-333 2.02e-34

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: 132.48  E-value: 2.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISgsdarqlYAMKV-LKKATLkvrDRVRTKMErDILVEV------NHPFIVKLHYAFQ 138
Cdd:cd06610    1 DDYELIEVIGSGATAVVYAAYCLP-------KKEKVaIKRIDL---EKCQTSMD-ELRKEIqamsqcNHPNVVSYYTSFV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGG---DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd06610   70 VGDELWLVMPLLSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 ----KESIDHEKKAYSFCGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaklGMPQF 290
Cdd:cd06610  150 aslaTGGDRTRKVRKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQ---NDPPS 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 291 LSPEAQS---------LLRMLFKRNPANRlvnpfligagPDGvEEIKRHSFF 333
Cdd:cd06610  227 LETGADYkkysksfrkMISLCLQKDPSKR----------PTA-EELLKHKFF 267
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
428-684 2.26e-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: 132.42  E-value: 2.26e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd14010    2 YVLYDEIGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQ-KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK-------------- 572
Cdd:cd14010   82 ET-LLRQdGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNIL-LDGNGT---LKLSDFGLARregeilkelfgqfs 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 ------QLRAENGLLMTPCYTAnfvaPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSL 646
Cdd:cd14010  157 degnvnKVSKKQAKRGTPYYMA----PELFQGGVHSFASDLWALGCVLYEMFTGKPPFVA---ESFTELVEKILNEDPPP 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 647 SGGYWNSVSDTA-KDLVSKMLHVDPHQRLTAALVLRHP-W 684
Cdd:cd14010  230 PPPKVSSKPSPDfKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
72-310 2.27e-34

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: 132.04  E-value: 2.27e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd06626    6 NKIGEGTFGKVYTAVNL---DTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH-----EKKAY 226
Cdd:cd06626   83 EGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNtttmaPGEVN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVN---RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDrKETMTMIlkaKLGM---PQF-----LSPEA 295
Cdd:cd06626  163 SLVGTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWSELD-NEWAIMY---HVGMghkPPIpdslqLSPEG 238
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd06626  239 KDFLSRCLESDPKKR 253
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
68-310 2.30e-34

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: 131.74  E-value: 2.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLK----VRDRVRTK--MERDILVEVN---HPFIVKLHYAFQ 138
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKS---KGKEVVIKFIFKERILvdtwVRDRKLGTvpLEIHILDTLNkrsHPNIVKLLDFFE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILD-FLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSke 217
Cdd:cd14004   79 DDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA-- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SIDHEKKAYSFCGTVEYMAPEVV--NR-RGHTQsaDWWSFGVLMFEMLTGTLPFQGKDRketmtmILKAKLGMPQFLSPE 294
Cdd:cd14004  157 AYIKSGPFDTFVGTIDYAAPEVLrgNPyGGKEQ--DIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSED 228
                        250
                 ....*....|....*.
gi 768032625 295 AQSLLRMLFKRNPANR 310
Cdd:cd14004  229 LIDLISRMLNRDVGDR 244
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
428-685 2.35e-34

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: 132.01  E-value: 2.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEILLRYGQHP-----NIITLKDVYDDGKYVYVVT 499
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKdylDQSLDEIRLLELLNKKDkadkyHIVRLKDVFYFKNHLCIVF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGG--ELLdKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnPESIRICDFGFAkqlrae 577
Cdd:cd14133   81 ELLSQNlyEFL-KQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYS--RCQIKIIDFGSS------ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 ngllmtpCYTANFV----------APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGS--GKFS 645
Cdd:cd14133  152 -------CFLTQRLysyiqsryyrAPEVILGLPYDEKIDMWSLGCILAELYTGEPLF---PGASEVDQLARIIGtiGIPP 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 646 lSGGYWNSVSDTAK--DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14133  222 -AHMLDQGKADDELfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
428-628 2.41e-34

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: 131.86  E-value: 2.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-RDPTEEIEILLRYGQ------HPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd14070    4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKaKKDSYVTKNLRREGRiqqmirHPNITQLLDILETENSYYLVME 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd14070   84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLL-LDENDN---IKLIDFGLSNCAGILGYS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 --LMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGP 628
Cdd:cd14070  160 dpFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEP 209
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
68-311 2.45e-34

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: 132.43  E-value: 2.45e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDR--VRTKMER--DILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14195    7 YEMGEELGSGQFA---IVRKCREKGTGKEYAAKFIKKRRLSSSRRgvSREEIERevNILREIQHPNIITLHDIFENKTDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG----HIKLTDFGLSKEsI 219
Cdd:cd14195   84 VLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHK-I 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ----FLSPEA 295
Cdd:cd14195  163 EAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEeyfsNTSELA 242
                        250
                 ....*....|....*.
gi 768032625 296 QSLLRMLFKRNPANRL 311
Cdd:cd14195  243 KDFIRRLLVKDPKKRM 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
428-630 6.41e-34

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 131.28  E-value: 6.41e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIH-KATNMEFAVKIIDKSKRDPTE-----EIEILlRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14201    8 YSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQillgkEIKIL-KELQHENIVALYDVQEMPNSVFLVMEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIL--YVDESGNPES---IRICDFGFAKQLRA 576
Cdd:cd14201   87 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILlsYASRKKSSVSgirIKIADFGFARYLQS 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 577 eNGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDD 630
Cdd:cd14201  167 -NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFqANSPQD 220
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
73-311 6.64e-34

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: 131.38  E-value: 6.64e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVF-LVKKISGSDarqlYAMKVLKKATLKVRDRVRTKMErdILVEV-NHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14090    9 LLGEGAYASVQtCINLYTGKE----YAVKIIEKHPGHSRSRVFREVE--TLHQCqGHPNILQLIEYFEDDERFYLVFEKM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI---KLTDFGLSKESIDHEKKA-- 225
Cdd:cd14090   83 RGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICDFDLGSGIKLSSTSMtp 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 ------YSFCGTVEYMAPEVVNR---RGHT--QSADWWSFGVLMFEMLTGTLPFQGK-------DRKET--------MTM 279
Cdd:cd14090  163 vttpelLTPVGSAEYMAPEVVDAfvgEALSydKRCDLWSLGVILYIMLCGYPPFYGRcgedcgwDRGEAcqdcqellFHS 242
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 280 ILKAKLGMP----QFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14090  243 IQEGEYEFPekewSHISAEAKDLISHLLVRDASQRY 278
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
67-315 8.89e-34

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: 131.30  E-value: 8.89e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDArqlyamKVLKKATLKVR-DRVRTKMERDI--LVEVN-HPFIVKLHYAFQTEGK 142
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGET------VALKKVALRKLeGGIPNQALREIkaLQACQgHPYVVKLRDVFPHGTG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLrGGDLFTRLSKEVM-FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd07832   75 FVLVFEYM-LSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSF-CGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPQFLS-PEAQSL 298
Cdd:cd07832  154 DPRLYSHqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRT-LGTPNEKTwPELTSL 232
                        250       260
                 ....*....|....*....|
gi 768032625 299 LR---MLFKRNPANRLVNPF 315
Cdd:cd07832  233 PDynkITFPESKGIRLEEIF 252
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
67-311 1.11e-33

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 131.12  E-value: 1.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDRVRT---KMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd14094    4 VYELCEVIGKGPFS---VVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTedlKREASICHMLKHPHIVELLETYSSDGML 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDL----FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSK 216
Cdd:cd14094   81 YMVFEFMDGADLcfeiVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKdRKETMTMILKAKLGM--PQF--LS 292
Cdd:cd14094  161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMnpRQWshIS 239
                        250
                 ....*....|....*....
gi 768032625 293 PEAQSLLRMLFKRNPANRL 311
Cdd:cd14094  240 ESAKDLVRRMLMLDPAERI 258
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
68-316 1.51e-33

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: 130.29  E-value: 1.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLK-------VRdrvrtkmERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDK---KTGEIVALKKIRLDNEEegipstaLR-------EISLLKELKHPNIVKLLDVIHTE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGgDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSI 219
Cdd:cd07829   71 NKLYLVFEYCDQ-DLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLAR-AF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYsfcgTVE-----YMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLG------- 286
Cdd:cd07829  149 GIPLRTY----THEvvtlwYRAPEIlLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQ-ILGtpteesw 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 287 ------------MPQF-----------LSPEAQSLLRMLFKRNPANR------LVNPFL 316
Cdd:cd07829  224 pgvtklpdykptFPKWpkndlekvlprLDPEGIDLLSKMLQYNPAKRisakeaLKHPYF 282
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
68-333 2.04e-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: 129.96  E-value: 2.04e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLKKATLKVRDRVRTKmERDILVEVN-HPFIVKLHYAFQTEGKLYLI 146
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKE---TGELVAIKKMKKKFYSWEECMNLR-EVKSLRKLNeHPNIVKLKEVFRENDELYFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGgDLF--TRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESidHEKK 224
Cdd:cd07830   77 FEYMEG-NLYqlMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI--RSRP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AY-SFCGTVEYMAPEVVNRRGHTQSA-DWWSFGVLMFEMLTGTLPFQGKDRKETMTMI-----------------LKAKL 285
Cdd:cd07830  154 PYtDYVSTRWYRAPEILLRSTSYSSPvDIWALGCIMAELYTLRPLFPGSSEIDQLYKIcsvlgtptkqdwpegykLASKL 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 286 G--MPQFL-----------SPEAQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFF 333
Cdd:cd07830  234 GfrFPQFAptslhqlipnaSPEAIDLIKDMLRWDPKKRPT-----------ASQALQHPYF 283
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
72-310 2.07e-33

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: 129.67  E-value: 2.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATlKVRDrVRTKMERDILV---EVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd14197   15 RELGRGKFA---VVRKCVEKDSGKEFAAKFMRKRR-KGQD-CRMEIIHEIAVlelAQANPWVINLHEVYETASEMILVLE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRL--SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE---GHIKLTDFGLSKeSIDHEK 223
Cdd:cd14197   90 YAAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLSR-ILKNSE 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLL 299
Cdd:cd14197  169 ELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSeeefEHLSESAIDFI 248
                        250
                 ....*....|.
gi 768032625 300 RMLFKRNPANR 310
Cdd:cd14197  249 KTLLIKKPENR 259
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
74-268 2.91e-33

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: 129.88  E-value: 2.91e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKV-RDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKL-YLI 146
Cdd:cd13989    1 LGSGGFGYVTLWKH---QDTGEYVAIKKCRQELSPSdKNRERWCLEVQIMKKLNHPNVVSArdvppELEKLSPNDLpLLA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDL---FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL-DEEGHI--KLTDFGLSKEsID 220
Cdd:cd13989   78 MEYCSGGDLrkvLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqQGGGRViyKLIDLGYAKE-LD 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd13989  157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
67-303 3.10e-33

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 128.96  E-value: 3.10e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14183    7 RYKVGRTIGDGNFA---VVKECVERSTGREYALKIINKSKCRGKEHM-IQNEVSILRRVKHPNIVLLIEEMDMPTELYLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFGLSKESidhE 222
Cdd:cd14183   83 MELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVV---D 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQG--KDRKETMTMILKAKLGMP----QFLSPEAQ 296
Cdd:cd14183  160 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFPspywDNVSDSAK 239

                 ....*..
gi 768032625 297 SLLRMLF 303
Cdd:cd14183  240 ELITMML 246
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
425-685 3.11e-33

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: 128.50  E-value: 3.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT---EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14110    2 EKTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQlvlREYQVLRRL-SHPRIAQLHSAYLSPRHLVLIEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesgnPESIRICDFGFAKQLRAENGLL 581
Cdd:cd14110   81 CSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITE----KNLLKIVDLGNAQPFNQGKVLM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPC-YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYwNSVSDTAKD 660
Cdd:cd14110  157 TDKKgDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSS---DLNWERDRNIRKGKVQLSRCY-AGLSGGAVN 232
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14110  233 FLKSTLCAKPWGRPTASECLQNPWL 257
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
68-311 3.43e-33

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: 129.56  E-value: 3.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd14085    5 FEIESELGRGATSVVYRCRQ---KGTQKPYAVKKLKKTV----DKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL---LDEEGHIKLTDFGLSKeSIDHEKK 224
Cdd:cd14085   78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLyatPAPDAPLKIADFGLSK-IVDQQVT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETM-TMILKAKLgmpQFLSP-------EAQ 296
Cdd:cd14085  157 MKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMfKRILNCDY---DFVSPwwddvslNAK 233
                        250
                 ....*....|....*
gi 768032625 297 SLLRMLFKRNPANRL 311
Cdd:cd14085  234 DLVKKLIVLDPKKRL 248
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
53-310 4.99e-33

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 133.84  E-value: 4.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  53 THHVKEGHEKADPSQFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVK 132
Cdd:PTZ00283  19 TFAKDEATAKEQAKKYWISRVLGSGATGTVLCAKRVSDG---EPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 133 LHYAFQTEGK--------LYLILDFLRGGDLF----TRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL 200
Cdd:PTZ00283  96 CHEDFAKKDPrnpenvlmIALVLDYANAGDLRqeikSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANIL 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 201 LDEEGHIKLTDFGLSKE-----SIDHEKkaySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKE 275
Cdd:PTZ00283 176 LCSNGLVKLGDFGFSKMyaatvSDDVGR---TFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEE 252
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 276 TMTMILKAKLG-MPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:PTZ00283 253 VMHKTLAGRYDpLPPSISPEMQEIVTALLSSDPKRR 288
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
428-697 6.02e-33

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: 128.36  E-value: 6.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEIL--LRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLnldtdDDDVSDIQKEVALLsqLKLGQPKNIIKYYGSYLKGPSLWIIMD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELlDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd06917   83 YCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANIL-VTNTGN---VKLCDFGVAASLNQNSSK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKR-QGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKF-SLSGgywNSVSDTA 658
Cdd:cd06917  158 RSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYS---DVDALRAVMLIPKSKPpRLEG---NGYSPLL 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLN 697
Cdd:cd06917  232 KEFVAACLDEEPKDRLSADELLKSKWIKQHSKTPTSVLK 270
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
73-316 6.54e-33

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: 128.20  E-value: 6.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFLVKKISGSDARqlYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd14201   13 LVGHGAFAVVFKGRHRKKTDWE--VAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG---------HIKLTDFGLSKeSIDHEK 223
Cdd:cd14201   90 GDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFAR-YLQSNM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLR 300
Cdd:cd14201  169 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIpreTSPYLADLLL 248
                        250       260
                 ....*....|....*....|..
gi 768032625 301 MLFKRNPANRL------VNPFL 316
Cdd:cd14201  249 GLLQRNQKDRMdfeaffSHPFL 270
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
72-268 7.84e-33

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: 127.53  E-value: 7.84e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVF-LVKKISGSDArqlyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14082    9 EVLGSGQFGIVYgGKHRKTGRDV----AIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEV-MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG---HIKLTDFGLSKesIDHEKK-A 225
Cdd:cd14082   85 HGDMLEMILSSEKgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR--IIGEKSfR 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14082  163 RSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
72-311 8.28e-33

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: 127.79  E-value: 8.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVF-LVKKISGsdarQLYAMKVLkkatlkvRDRVRTKMERDILVEV-NHPFIVKLH--YA--FQTEGKLYL 145
Cdd:cd14089    7 QVLGLGINGKVLeCFHKKTG----EKFALKVL-------RDNPKARREVELHWRAsGCPHIVRIIdvYEntYQGRKCLLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH---IKLTDFGLSKEsiD 220
Cdd:cd14089   76 VMECMEGGELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKE--T 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAY-SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgKDRKETMTMILKAKLGMPQF--------- 290
Cdd:cd14089  154 TTKKSLqTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKKRIRNGQYefpnpewsn 232
                        250       260
                 ....*....|....*....|.
gi 768032625 291 LSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14089  233 VSEEAKDLIRGLLKTDPSERL 253
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
72-281 1.24e-32

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: 126.95  E-value: 1.24e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14193   10 EILGGGRFGQVHkCEEKSSG----LKLAAKIIKARSQKEKEEV--KNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL--DEEGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd14193   84 DGGELFDRIIDEnYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKPREKLRVN 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 228 FcGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIL 281
Cdd:cd14193  164 F-GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNIL 216
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
434-696 1.29e-32

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: 128.97  E-value: 1.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI------EILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVahtvteSRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 587
Cdd:cd05595   83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLM-LDKDGH---IKITDFGLCKEGITDGATMKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILArIGSGKFSlsggywNSVSDTAKDLVSKMLH 667
Cdd:cd05595  159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELIL-MEEIRFP------RTLSPEAKSLLAGLLK 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 668 VDPHQRL-----TAALVLRHPWI--VHWDQLPQYQL 696
Cdd:cd05595  232 KDPKQRLgggpsDAKEVMEHRFFlsINWQDVVQKKL 267
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
72-310 1.45e-32

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: 127.35  E-value: 1.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKatlkvRDRVRtKMERDILVEV-------NHPFIVKLHYAFQTEGKLY 144
Cdd:cd14198   14 KELGRGKFA---VVRQCISKSTGQEYAAKFLKK-----RRRGQ-DCRAEILHEIavlelakSNPRVVNLHEVYETTSEII 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEV--MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---EGHIKLTDFGLSKEsI 219
Cdd:cd14198   85 LILEYAAGGEIFNLCVPDLaeMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSiypLGDIKIVDFGMSRK-I 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ----FLSPEA 295
Cdd:cd14198  164 GHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsSVSQLA 243
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd14198  244 TDFIQKLLVKNPEKR 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
68-308 1.63e-32

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 128.80  E-value: 1.63e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkkiSGSDAR--QLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQ-----TE 140
Cdd:cd07834    2 YELLKPIGSGAYGVVC-----SAYDKRtgRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRppspeEF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSID 220
Cdd:cd07834   77 NDVYIVTELMET-DLHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLAR-GVD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVE---YMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP------QF 290
Cdd:cd07834  155 PDEDKGFLTEYVVtrwYRAPELLlSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEV-LGTPseedlkFI 233
                        250
                 ....*....|....*...
gi 768032625 291 LSPEAQSLLRMLFKRNPA 308
Cdd:cd07834  234 SSEKARNYLKSLPKKPKK 251
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
71-316 1.74e-32

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: 126.39  E-value: 1.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd08221    5 VRVLGRGAFGEAVLYRKTEDN---SLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEV--MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSF 228
Cdd:cd08221   82 NGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGM--PQFlSPEAQSLLRMLFKRN 306
Cdd:cd08221  162 VGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDidEQY-SEEIIQLVHDCLHQD 240
                        250
                 ....*....|....*.
gi 768032625 307 PANR------LVNPFL 316
Cdd:cd08221  241 PEDRptaeelLERPLL 256
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
434-691 1.74e-32

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: 128.24  E-value: 1.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE------ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDEVAhtltenRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 587
Cdd:cd05571   83 FFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLL-LDKDGH---IKITDFGLCKEEISYGATTKTFCGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTP-EEILAriGSGKFSlsggywNSVSDTAKDLVSKML 666
Cdd:cd05571  159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLfELILM--EEVRFP------STLSPEAKSLLAGLL 230
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 667 HVDPHQRL-----TAALVLRHPWI--VHWDQL 691
Cdd:cd05571  231 KKDPKKRLgggprDAKEIMEHPFFasINWDDL 262
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
426-691 2.23e-32

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: 128.12  E-value: 2.23e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSemlEKEQVAHVRAerdILAEADNPWVVKLYYSFQDEENLYLIM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASavlFTITKTV---EYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRa 576
Cdd:cd05599   81 EFLPGGDMMTLLMKKDTLTEEETR---FYIAETVlaiESIHKLGYIHRDIKPDNLL-LDARGH---IKLSDFGLCTGLK- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILArigsgkfslsggyWNS-- 653
Cdd:cd05599  153 KSHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFcSDDPQETCRKIMN-------------WREtl 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 654 -------VSDTAKDLVSKMLhVDPHQRLTA---ALVLRHPWI--VHWDQL 691
Cdd:cd05599  220 vfppevpISPEAKDLIERLL-CDAEHRLGAngvEEIKSHPFFkgVDWDHI 268
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
427-624 2.33e-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: 126.31  E-value: 2.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS-----------KRDPTEEIEILLRYGQHPNIITLKDVYDDGKYV 495
Cdd:cd13993    1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgndfqKLPQLREIDLHRRVSRHPNIITLHDVFETEVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKILRQKFFSEREASA--VLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRICDFGFAkq 573
Cdd:cd13993   81 YIVLEYCPNGDLFEAITENRIYVGKTELIknVFLQLIDAVKHCHSLGIYHRDIKPENILL---SQDEGTVKLCDFGLA-- 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 574 lraengllMTPCYTANF-------VAPEVL-----KRQGYD-AACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd13993  156 --------TTEKISMDFgvgsefyMAPECFdevgrSLKGYPcAAGDIWSLGIILLNLTFGRNPW 211
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
427-680 2.38e-32

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: 126.23  E-value: 2.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-------KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemmdaKARQDCLKEIDLLQQL-NHPNIIKYLASFIENNELNIVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKI----LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGnpeSIRICDFG----FA 571
Cdd:cd08224   80 ELADAGDLSRLIkhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANV-FITANG---VVKLGDLGlgrfFS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLRAENGLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTPEEILARIGSGKFS-LSGgy 650
Cdd:cd08224  156 SKTTAAHSLVGTPYY----MSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFY-GEKMNLYSLCKKIEKCEYPpLPA-- 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 651 wNSVSDTAKDLVSKMLHVDPHQRLTAALVL 680
Cdd:cd08224  229 -DLYSQELRDLVAACIQPDPEKRPDISYVL 257
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
428-683 3.62e-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: 126.46  E-value: 3.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYgQHPNIITLKDVY------DDGKYVYVVTEL 501
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQIMRRL-KHPNIVKLKYFFyssgekKDEVYLNLVMEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MkgGELLDKILRQKFFSEREASAV---LFT--ITKTVEYLHAQGVVHRDLKPSNILYVDESGNpesIRICDFGFAKQLRA 576
Cdd:cd14137   85 M--PETLYRVIRHYSKNKQTIPIIyvkLYSyqLFRGLAYLHSLGICHRDIKPQNLLVDPETGV---LKLCDFGSAKRLVP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 eNGLLMTpcY--TANFVAPE-VLKRQGYDAACDIWSLGVLLYTMLTGYTPFA--NGPD-----------DTPEEILA--- 637
Cdd:cd14137  160 -GEPNVS--YicSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPgeSSVDqlveiikvlgtPTREQIKAmnp 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 638 RIGSGKFSLSGGY-WNSV-----SDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14137  237 NYTEFKFPQIKPHpWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
428-685 4.29e-32

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: 127.42  E-value: 4.29e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKiidksKRDPTE----------EIEILLRYgQHPNIITLKDV-----YDDG 492
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIK-----KISPFEhqtyclrtlrEIKILLRF-KHENIIGILDIqrpptFESF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 493 KYVYVVTELMKGGelLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK 572
Cdd:cd07849   81 KDVYIVQELMETD--LYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLL-LNTNCD---LKICDFGLAR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 --QLRAENGLLMTPcYTAN--FVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGyTPFANGPD------------DTP-EE 634
Cdd:cd07849  155 iaDPEHDHTGFLTE-YVATrwYRAPEImLNSKGYTKAIDIWSVGCILAEMLSN-RPLFPGKDylhqlnlilgilGTPsQE 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 635 ILARIGSGKF-----SL---SGGYWNS----VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07849  233 DLNCIISLKArnyikSLpfkPKVPWNKlfpnADPKALDLLDKMLTFNPHKRITVEEALAHPYL 295
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
431-644 4.47e-32

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 125.35  E-value: 4.47e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   431 KEDIGVGSYSVCKRCIHKATNMEF----AVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:smart00221   4 GKKLGEGAFGEVYKGTLKGKGDGKevevAVKTLkedasEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMIVMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   502 MKGGELLD--KILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQL----- 574
Cdd:smart00221  83 MPGGDLLDylRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV----GENLVVKISDFGLSRDLydddy 158
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625   575 -RAENGLL----MtpcytanfvAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSGKF 644
Cdd:smart00221 159 yKVKGGKLpirwM---------APESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPY---PGMSNAEVLEYLKKGYR 222
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
74-311 5.64e-32

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: 125.12  E-value: 5.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd14191   10 LGSGKFGQVFrLVEKKTK----KVWAGKFFKAYSAKEKENIRQEIS--IMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEG-HIKLTDFGLSKEsIDHEKKAYSFC 229
Cdd:cd14191   84 GELFERIIDEdFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARR-LENAGSLKVLF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRMLFKR 305
Cdd:cd14191  163 GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLLKK 242

                 ....*.
gi 768032625 306 NPANRL 311
Cdd:cd14191  243 DMKARL 248
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
434-691 6.54e-32

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: 126.62  E-value: 6.54e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS----KRDPTE---EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtilkKKEQNHimaERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENIL-LDCQGH---VVLTDFGLCKEGMEPEETTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYwnsvSDTAKDLVSKML 666
Cdd:cd05603  159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYS---RDVSQMYDNILHKPLHLPGGK----TVAACDLLQGLL 231
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 667 HVDPHQRLTAAL----VLRHPWI--VHWDQL 691
Cdd:cd05603  232 HKDQRRRLGAKAdfleIKNHVFFspINWDDL 262
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
434-684 6.62e-32

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: 125.20  E-value: 6.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYS----VCKRCIHKATNMeFAVKIIDKS----KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd05583    2 LGTGAYGkvflVRKVGGHDAGKL-YAMKVLKKAtivqKAKTAEhtmtERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRA-ENGL 580
Cdd:cd05583   81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSEGH---VVLTDFGLSKEFLPgENDR 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKR--QGYDAACDIWSLGVLLYTMLTGYTPFA-NGPDDTPEEILARIGSGKFSLSggywNSVSDT 657
Cdd:cd05583  157 AYSFCGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTvDGERNSQSEISKRILKSHPPIP----KTFSAE 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 658 AKDLVSKMLHVDPHQRLTAAL-----VLRHPW 684
Cdd:cd05583  233 AKDFILKLLEKDPKKRLGAGPrgaheIKEHPF 264
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
426-685 6.89e-32

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: 125.36  E-value: 6.89e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK--RDPTE-----EIEILLRYgQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14117    6 DDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQieKEGVEhqlrrEIEIQSHL-RHPNILRLYNYFHDRKRIYLI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGF---AKQLR 575
Cdd:cd14117   85 LEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLM----GYKGELKIADFGWsvhAPSLR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AEngllmTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpddTPEEILARIgsGKFSLSggYWNSVS 655
Cdd:cd14117  161 RR-----TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESA---SHTETYRRI--VKVDLK--FPPFLS 228
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14117  229 DGSRDLISKLLRYHPSERLPLKGVMEHPWV 258
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
62-316 7.35e-32

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: 124.86  E-value: 7.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADP-SQFELLKVLGQGSFGKVFLVKKISgsDARQLyamkVLKKATLKVRDRvRTKM--ERDILVEVNHPFIVKLHYAFQ 138
Cdd:cd06648    2 PGDPrSDLDNFVKIGEGSTGIVCIATDKS--TGRQV----AVKKMDLRKQQR-RELLfnEVVIMRDYQHPNIVEMYSSYL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd06648   75 VGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI---LKAKLGMPQFLSPEA 295
Cdd:cd06648  154 SKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIrdnEPPKLKNLHKVSPRL 233
                        250       260
                 ....*....|....*....|....*..
gi 768032625 296 QSLLRMLFKRNPANR------LVNPFL 316
Cdd:cd06648  234 RSFLDRMLVRDPAQRataaelLNHPFL 260
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
68-260 8.00e-32

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: 125.23  E-value: 8.00e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARqlYAMKVLKKATLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQTEGKLY 144
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERVPTGKV--YAVKKLKPNYAGAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEED---VKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS-----K 216
Cdd:cd14052   80 IQTELCENGSLDVFLSELGLLGRLDefrVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwplI 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 217 ESIDHEkkaysfcGTVEYMAPEVVNRRGHTQSADWWSFGVLMFE 260
Cdd:cd14052  160 RGIERE-------GDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
428-691 1.01e-31

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: 125.50  E-value: 1.01e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYS----VCKRCIHKATNMeFAVKIIDKS----KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYV 495
Cdd:cd05613    2 FELLKVLGTGAYGkvflVRKVSGHDAGKL-YAMKVLKKAtivqKAKTAEhtrtERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQ-L 574
Cdd:cd05613   81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSSGH---VVLTDFGLSKEfL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGLLMTPCYTANFVAPEVLK--RQGYDAACDIWSLGVLLYTMLTGYTPFA-NGPDDTPEEILARIgsgkFSLSGGYW 651
Cdd:cd05613  157 LDENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRI----LKSEPPYP 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRL-----TAALVLRHPWI--VHWDQL 691
Cdd:cd05613  233 QEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFqkINWDDL 279
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
72-316 1.11e-31

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: 124.42  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRT-----KMERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRADSRQKTvvdalKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID--HEKK 224
Cdd:cd06629   87 LEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDiyGNNG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVV--NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSL 298
Cdd:cd06629  167 ATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPvpedVNLSPEALDF 246
                        250       260
                 ....*....|....*....|....
gi 768032625 299 LRMLFKRNPANR------LVNPFL 316
Cdd:cd06629  247 LNACFAIDPRDRptaaelLSHPFL 270
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
425-685 1.21e-31

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: 124.72  E-value: 1.21e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDkSKRDPTEEIE----ILLRYGQHPNIIT------LKDVYDDGKY 494
Cdd:cd06608    5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD-IIEDEEEEIKleinILRKFSNHPNIATfygafiKKDPPGGDDQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLD--KILRQKFFSEREA--SAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpesIRICDFGF 570
Cdd:cd06608   84 LWLVMEYCGGGSVTDlvKGLRKKGKRLKEEwiAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE----VKLVDFGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLRAENGLLMTPCYTANFVAPEVLK-----RQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFS 645
Cdd:cd06608  160 SAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLC---DMHPMRALFKIPRNPPP 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 646 --LSGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06608  237 tlKSPEKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
74-311 1.58e-31

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: 124.75  E-value: 1.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGkvfLVKKISGSDARQLYAMKVLKKATlkvRDRVRtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd14175    9 IGVGSYS---VCKRCVHKATNMEYAVKVIDKSK---RDPSE---EIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEGH---IKLTDFGLSKESIDHEKKAYSF 228
Cdd:cd14175   80 GELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQ---GKDRKETMTMILKAKL----GMPQFLSPEAQSLLRM 301
Cdd:cd14175  160 CYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFAngpSDTPEEILTRIGSGKFtlsgGNWNTVSDAAKDLVSK 239
                        250
                 ....*....|
gi 768032625 302 LFKRNPANRL 311
Cdd:cd14175  240 MLHVDPHQRL 249
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
434-682 1.70e-31

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: 123.50  E-value: 1.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK------RDP-TEEIEiLLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRvakphqREKiVNEIE-LHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESgnpESIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd14189   88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN-FFINEN---MELKVGDFGLAARLEPPEQRKKTICG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpddTPEEILARIGSGKFSLSGgywnSVSDTAKDLVSKML 666
Cdd:cd14189  164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETL---DLKETYRCIKQVKYTLPA----SLSLPARHLLAGIL 236
                        250
                 ....*....|....*.
gi 768032625 667 HVDPHQRLTAALVLRH 682
Cdd:cd14189  237 KRNPGDRLTLDQILEH 252
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
67-333 2.39e-31

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: 123.12  E-value: 2.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGsdaRQLYAMKVLKKATLK----VRDRVRTKMERDILVEVN---HPFIVKLHYAFQT 139
Cdd:cd14005    1 QYEVGDLLGKGGFGTVYSGVRIRD---GLPVAVKFVPKSRVTewamINGPVPVPLEIALLLKASkpgVPGVIRLLDWYER 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGG-DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EEGHIKLTDFG---L 214
Cdd:cd14005   78 PDGFLLIMERPEPCqDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGcgaL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESidhekkAYS-FCGTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGTLPFqgkdrkETMTMILKAKLGMPQFLS 292
Cdd:cd14005  158 LKDS------VYTdFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPF------ENDEQILRGNVLFRPRLS 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 293 PEAQSLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:cd14005  226 KECCDLISRCLQFDPSKRP-----------SLEQILSHPWF 255
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
68-347 4.17e-31

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: 123.59  E-value: 4.17e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATlkvRDrvrTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14178    5 YEIKEDIGIGSYS---VCKRCVHKATSTEYAVKIIDKSK---RD---PSEEIEILLRYgQHPNIITLKDVYDDGKFVYLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEGH---IKLTDFGLSKESIDHE 222
Cdd:cd14178   76 MELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAEN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF-QGKDrkETMTMILkAKLGMPQF---------LS 292
Cdd:cd14178  156 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFaNGPD--DTPEEIL-ARIGSGKYalsggnwdsIS 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANRLVNPfligagpdgveEIKRHSFFSTIDW---NKLYRREIH 347
Cdd:cd14178  233 DAAKDIVSKMLHVDPHQRLTAP-----------QVLRHPWIVNREYlsqNQLSRQDVH 279
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
431-644 4.49e-31

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 122.25  E-value: 4.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   431 KEDIGVGSY-SVCK---RCIHKATNMEFAVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:smart00219   4 GKKLGEGAFgEVYKgklKGKGGKKKVEVAVKTLkedasEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPLYIVMEY 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   502 MKGGELLDkILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQL----- 574
Cdd:smart00219  83 MEGGDLLS-YLRKNrpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV----GENLVVKISDFGLSRDLydddy 157
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625   575 -RAENGLL----MtpcytanfvAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSGKF 644
Cdd:smart00219 158 yRKRGGKLpirwM---------APESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPY---PGMSNEEVLEYLKNGYR 221
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
68-310 4.63e-31

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: 122.53  E-value: 4.63e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRK---DDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLS--KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI-KLTDFGLSKEsIDHEKK 224
Cdd:cd08220   79 EYAPGGTLFEYIQqrKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKI-LSSKSK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG-MPQFLSPEAQSLLRMLF 303
Cdd:cd08220  158 AYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSML 237

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd08220  238 HLDPNKR 244
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
67-310 4.64e-31

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: 122.41  E-value: 4.64e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDarqLYAMKVLKkatLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGE---LAAVKVIK---LEPGDDFEIiQQEISMLKECRHPNIVAYFGSYLRRDKLWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGG---DLFTRLSKevmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHE 222
Cdd:cd06613   75 VMEYCGGGslqDIYQVTGP---LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQ-LTAT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 -KKAYSFCGTVEYMAPEV--VNRR-GHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF-----LSP 293
Cdd:cd06613  151 iAKRKSFIGTPYWMAPEVaaVERKgGYDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDPPKLkdkekWSP 230
                        250
                 ....*....|....*..
gi 768032625 294 EAQSLLRMLFKRNPANR 310
Cdd:cd06613  231 DFHDFIKKCLTKNPKKR 247
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
68-311 4.70e-31

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: 123.44  E-value: 4.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKvlkkatlkvrdRVRTKMERD-----------ILVEVNHPFIVKLH-- 134
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNK---KTGELVALK-----------KIRMENEKEgfpitaireikLLQKLDHPNVVRLKei 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 ----YAFQTEGKLYLILDFLRGgDLfTRL--SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIK 208
Cdd:cd07840   67 vtskGSAKYKGSIYMVFEYMDH-DL-TGLldNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSKESIDHEKKAY-SFCGTVEYMAPEVVnrRGHTQSA---DWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAk 284
Cdd:cd07840  145 LADFGLARPYTKENNADYtNRVITLWYRPPELL--LGATRYGpevDMWSVGCILAELFTGKPIFQGKTELEQLEKIFEL- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 285 LGMP--------------------------------QFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd07840  222 CGSPteenwpgvsdlpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRI 280
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
118-311 4.97e-31

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 122.23  E-value: 4.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 118 ERDILVEVNHPFIVKLHYAFQTEGK-LYLILDFLRGGDLFTR--LSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDL 194
Cdd:cd14109   46 EVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLASTIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDL 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 195 KPENILLDEEgHIKLTDFGLSKESIDHeKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK 274
Cdd:cd14109  126 RPEDILLQDD-KLKLADFGQSRRLLRG-KLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDR 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768032625 275 ETMTMILKAKLGMP----QFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14109  204 ETLTNVRSGKWSFDssplGNISDDARDFIKKLLVYIPESRL 244
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
434-685 4.99e-31

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: 122.64  E-value: 4.99e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII---------DKSKRDPTE----EIEiLLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd06628    8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsaenKDRKKSMLDalqrEIA-LLRELQHENIVQYLGSSSDANHLNIFLE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAeNGL 580
Cdd:cd06628   87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANIL-VDNKG---GIKISDFGISKKLEA-NSL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMT-----PCYTAN--FVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSgkfSLSGGYWNS 653
Cdd:cd06628  162 STKnngarPSLQGSvfWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF---PDCTQMQAIFKIGE---NASPTIPSN 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06628  236 ISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
72-311 5.73e-31

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: 123.21  E-value: 5.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVRTKMErdILVEVN-HPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14173    8 EVLGEGAYARVQTCINLITN---KEYAVKIIEKRPGHSRSRVFREVE--MLYQCQgHRNVLELIEFFEEEDKFYLVFEKM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI---KLTDFGL-------SKESID 220
Cdd:cd14173   83 RGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLgsgiklnSDCSPI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQS-----ADWWSFGVLMFEMLTGTLPFQGK-------DRKET--------MTMI 280
Cdd:cd14173  163 STPELLTPCGSAEYMAPEVVEAFNEEASiydkrCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEAcpacqnmlFESI 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 281 LKAKLGMPQ----FLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14173  243 QEGKYEFPEkdwaHISCAAKDLISKLLVRDAKQRL 277
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
428-683 6.77e-31

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: 121.56  E-value: 6.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVckrcIHKATNMEFAVKIIDKSKR------DPT-------EEIEILLRYGQHPNIITLKDVYDDGKY 494
Cdd:cd14019    3 YRIIEKIGEGTFSS----VYKAEDKLHDLYDRNKGRLvalkhiYPTsspsrilNELECLERLGGSNNVSGLITAFRNEDQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDkILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPESIR--ICDFGFA- 571
Cdd:cd14019   79 VVAVLPYIEHDDFRD-FYRK--MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY-----NRETGKgvLVDFGLAq 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 -----KQLRAengllmtPCY-TANFVAPEVLKR---QGydAACDIWSLGVLLYTMLTGYTPFANGPDDtpEEILARIGSg 642
Cdd:cd14019  151 reedrPEQRA-------PRAgTRGFRAPEVLFKcphQT--TAIDIWSAGVILLSILSGRFPFFFSSDD--IDALAEIAT- 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 643 kfsLSGgywnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14019  219 ---IFG------SDEAYDLLDKLLELDPSKRITAEEALKHP 250
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
423-687 7.38e-31

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 122.27  E-value: 7.38e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGV--GSY---SVCKrciHKATNMEFAVKIIDKSKRDPteeIEILLRY--GQHPNIITLKDVYDDGKYV 495
Cdd:PHA03390  11 QFLKNCEIVKKLKLidGKFgkvSVLK---HKPTQKLFVQKIIKAKNFNA---IEPMVHQlmKDNPNFIKLYYSVTTLKGH 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpesIRICDFGFAKQLR 575
Cdd:PHA03390  85 VLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDR---IYLCDYGLCKIIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AENgllmtpCY--TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDD--TPEEILARIgSGKFSLSggyw 651
Cdd:PHA03390 162 TPS------CYdgTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEelDLESLLKRQ-QKKLPFI---- 230
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRLTA-ALVLRHPWIVH 687
Cdd:PHA03390 231 KNVSKNANDFVQSMLKYNINYRLTNyNEIIKHPFLKI 267
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
434-734 7.49e-31

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: 123.45  E-value: 7.49e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVK------IIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKtirkahIVSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 587
Cdd:cd05585   82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENIL-LDYTGH---IALCDFGLCKLNMKDDDKTNTFCGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGywnsVSDTAKDLVSKMLH 667
Cdd:cd05585  158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFY---DENTNEMYRKILQEPLRFPDG----FDRDAKDLLIGLLN 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 668 VDPHQRL---TAALVLRHPWI--VHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQ 734
Cdd:cd05585  231 RDPTKRLgynGAQEIKNHPFFdqIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSVVDDSHLSE 302
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
67-310 7.85e-31

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: 123.07  E-value: 7.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKV------RDRVRtkmERDILVEVNHPFIVKLHYAFQT 139
Cdd:cd07841    1 RYEKGKKLGEGTYAVVYKARdKETG----RIVAIKKIKLGERKEakdginFTALR---EIKLLQELKHPNIIGLLDVFGH 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLrGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd07841   74 KSNINLVFEFM-ETDLEKVIkDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARSF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP--------- 288
Cdd:cd07841  153 GSPNRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEA-LGTPteenwpgvt 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 289 ------QF--------------LSPEAQSLLRMLFKRNPANR 310
Cdd:cd07841  232 slpdyvEFkpfpptplkqifpaASDDALDLLQRLLTLNPNKR 273
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
434-685 1.20e-30

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: 121.26  E-value: 1.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtikeiaDEMKVLEGL-DHPNLVRYYGVEVHREEVYIFMEYCQEGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQKFFsEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAE-------- 577
Cdd:cd06626   87 EE-LLRHGRI-LDEAVIRVYTlqLLEGLAYLHENGIVHRDIKPANIF-LDSNG---LIKLGDFGSAVKLKNNtttmapge 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 -NGLLMTPCYTanfvAPEVLKRQ---GYDAACDIWSLGVLLYTMLTGYTPFANGpdDTPEEILARIGSG-KFSLSGGywN 652
Cdd:cd06626  161 vNSLVGTPAYM----APEVITGNkgeGHGRAADIWSLGCVVLEMATGKRPWSEL--DNEWAIMYHVGMGhKPPIPDS--L 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06626  233 QLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
434-687 1.27e-30

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: 122.40  E-value: 1.27e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCkrCI--HKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd06659   29 IGEGSTGVV--CIarEKHSGRQVAVKMMDLRKQQRREllfnEVVIMRDY-QHPNVVEMYKSYLVGEELWVLMEYLQGGAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAE----NGLLMT 583
Cdd:cd06659  106 TD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG----RVKLSDFGFCAQISKDvpkrKSLVGT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARI-GSGKFSLSGGYwnSVSDTAKDLV 662
Cdd:cd06659  181 PYW----MAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFS---DSPVQAMKRLrDSPPPKLKNSH--KASPVLRDFL 251
                        250       260
                 ....*....|....*....|....*
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPWIVH 687
Cdd:cd06659  252 ERMLVRDPQERATAQELLDHPFLLQ 276
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
434-684 1.45e-30

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: 120.89  E-value: 1.45e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK---RDPTEEIEILLRYGQHPNIITLKDVY--DDGKYVYVvTELMKGGELL 508
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStklKDFLREYNISLELSVHPHIIKTYDVAfeTEDYYVFA-QEYAPYGDLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgNPESIRICDFGFAkqlRAENGLLMTPCYTA 588
Cdd:cd13987   80 SIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDK--DCRRVKLCDFGLT---RRVGSTVKRVSGTI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 589 NFVAPEVL---KRQGY--DAACDIWSLGVLLYTMLTGYTPF--ANGpDDTPEEILARIGSGKFSLSGGYWNSVSDTAKDL 661
Cdd:cd13987  155 PYTAPEVCeakKNEGFvvDPSIDVWAFGVLLFCCLTGNFPWekADS-DDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRM 233
                        250       260
                 ....*....|....*....|....*.
gi 768032625 662 VSKMLHVDPHQRLTAALVLR---HPW 684
Cdd:cd13987  234 FKKLLAPEPERRCSIKEVFKylgDRW 259
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
68-310 1.54e-30

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: 120.73  E-value: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVflvkKISGSdarQLYAMKVlkkaTLKVRDRVRTK---------MERDILVEVNHPFIVKLHYAFQ 138
Cdd:cd14164    2 YTLGTTIGEGSFSKV----KLATS---QKYCCKV----AIKIVDRRRASpdfvqkflpRELSILRRVNHPNIVQMFECIE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 -TEGKLYLILDfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG-HIKLTDFGLSK 216
Cdd:cd14164   71 vANGRLYIVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFAR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ESIDHEKKAYSFCGTVEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGTLPFQGkdrkETMTMILKAKLGM--PQFLSP 293
Cdd:cd14164  150 FVEDYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDE----TNVRRLRLQQRGVlyPSGVAL 225
                        250
                 ....*....|....*....
gi 768032625 294 E--AQSLLRMLFKRNPANR 310
Cdd:cd14164  226 EepCRALIRTLLQFNPSTR 244
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
434-705 1.75e-30

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: 122.68  E-value: 1.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDK----SKRDPTEEI---EILLR--YGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKkvivAKKEVAHTIgerNILVRtaLDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENIL-LDANGH---IALCDFGLSKADLTDNKTTNTF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFAngPDDTpEEILARIGSGKFSLSGgywNSVSDTAKDLVS 663
Cdd:cd05586  157 CGTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFY--AEDT-QQMYRNIAFGKVRFPK---DVLSDEGRSFVK 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 664 KMLHVDPHQRLTA---ALVLR-HPWI--VHWDQLPQYQLNRQDAPHLV 705
Cdd:cd05586  231 GLLNRNPKHRLGAhddAVELKeHPFFadIDWDLLSKKKITPPFKPIVD 278
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
434-691 1.93e-30

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: 122.12  E-value: 1.93e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYS----VCKRCIHKATNMeFAVKIIDKSK---RD---PTEEIEILLRYGqHPNIITLKDVYD-DGKyVYVVTELM 502
Cdd:cd05582    3 LGQGSFGkvflVRKITGPDAGTL-YAMKVLKKATlkvRDrvrTKMERDILADVN-HPFIVKLHYAFQtEGK-LYLILDFL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLM 582
Cdd:cd05582   80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEDGH---IKLTDFGLSKESIDHEKKAY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPD--DTPEEIL-ARIGSGKFslsggywnsVSDTAK 659
Cdd:cd05582  156 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPF-QGKDrkETMTMILkAKLGMPQF---------LSPEAQ 225
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 660 DLVSKMLHVDPHQRLTAAL-----VLRHPWIVH--WDQL 691
Cdd:cd05582  226 SLLRALFKRNPANRLGAGPdgveeIKRHPFFATidWNKL 264
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
66-311 2.06e-30

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: 121.04  E-value: 2.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVLkkaTLKVRDRVRTKMERDI-----LVEVNHPFIVKLHYAFQTE 140
Cdd:cd06917    1 SLYRRLELVGRGSYGAVYRGYHVK---TGRVVALKVL---NLDTDDDDVSDIQKEVallsqLKLGQPKNIIKYYGSYLKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTrLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06917   75 PSLWIIMDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNR-RGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKlgmPQFL-----SPE 294
Cdd:cd06917  154 NSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSK---PPRLegngySPL 230
                        250
                 ....*....|....*..
gi 768032625 295 AQSLLRMLFKRNPANRL 311
Cdd:cd06917  231 LKEFVAACLDEEPKDRL 247
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
428-685 2.47e-30

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: 120.49  E-value: 2.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdksKRDPTEEIEIL------LRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd06613    2 YELIQRIGSGTYGDVYKARNIATGELAAVKVI---KLEPGDDFEIIqqeismLKECRHPNIVAYFGSYLRRDKLWIVMEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRA----E 577
Cdd:cd06613   79 CGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANIL-LTEDGD---VKLADFGVSAQLTAtiakR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPCYtanfVAPEVL---KRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKF---SLSG-GY 650
Cdd:cd06613  155 KSFIGTPYW----MAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMF---DLHPMRALFLIPKSNFdppKLKDkEK 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 651 WnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06613  228 W---SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
426-695 2.55e-30

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: 122.43  E-value: 2.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYS----VCKrcihKATNMEFAVKIIDKS---KRDPTE----EIEILLRyGQHPNIITLKDVYDDGKY 494
Cdd:cd05598    1 SMFEKIKTIGVGAFGevslVRK----KDTNALYAMKTLRKKdvlKRNQVAhvkaERDILAE-ADNEWVVKLYYSFQDKEN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL 574
Cdd:cd05598   76 LYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNIL-IDRDGH---IKLTDFGLCTGF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 R--------AENGLLMTPcytaNFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSL 646
Cdd:cd05598  152 RwthdskyyLAHSLVGTP----NYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFL---AQTPAETQLKVINWRTTL 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 647 SGGYWNSVSDTAKDLVSKMLhVDPHQRL---TAALVLRHPWI--VHWDQLPQYQ 695
Cdd:cd05598  225 KIPHEANLSPEAKDLILRLC-CDAEDRLgrnGADEIKAHPFFagIDWEKLRKQK 277
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
447-689 3.73e-30

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: 120.59  E-value: 3.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 447 HKATNMEFAVKIIDKSK---RDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE---LLDKI------ 511
Cdd:cd05609   21 HRETRQRFAMKKINKQNlilRNQIQQVFVerdILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatLLKNIgplpvd 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 512 LRQKFFSEreasAVLftitkTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQlraenGLL-MTP------ 584
Cdd:cd05609  101 MARMYFAE----TVL-----ALEYLHSYGIVHRDLKPDNLL-ITSMGH---IKLTDFGLSKI-----GLMsLTTnlyegh 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 -------------CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYw 651
Cdd:cd05609  163 iekdtrefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFG---DTPEELFGQVISDEIEWPEGD- 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRL---TAALVLRHPWIVHWD 689
Cdd:cd05609  239 DALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDLD 279
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
72-311 4.29e-30

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: 120.09  E-value: 4.29e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFlvkkisgsdarQLYAMKVLKKATLKV-RDRVRTKMERDILVEVNH-PFIVKLHYAFQT--EGK--LYL 145
Cdd:cd14172   10 QVLGLGVNGKVL-----------ECFHRRTGQKCALKLlYDSPKARREVEHHWRASGgPHIVHILDVYENmhHGKrcLLI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKESID 220
Cdd:cd14172   79 IMECMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HeKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgKDRKETMTMILKAKLGMPQF---------L 291
Cdd:cd14172  159 Q-NALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFY-SNTGQAISPGMKRRIRMGQYgfpnpewaeV 236
                        250       260
                 ....*....|....*....|
gi 768032625 292 SPEAQSLLRMLFKRNPANRL 311
Cdd:cd14172  237 SEEAKQLIRHLLKTDPTERM 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
74-310 7.14e-30

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: 119.31  E-value: 7.14e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKvRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14113   15 LGRGRFS---VVKKCDQRGTKRAVATKFVNKKLMK-RDQV--THELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE---EGHIKLTDFGLSKEsIDHEKKAYSFCG 230
Cdd:cd14113   89 RLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQslsKPTIKLADFGDAVQ-LNTTYYIHQLLG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP----QFLSPEAQSLLRMLFKRN 306
Cdd:cd14113  168 SPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQMD 247

                 ....
gi 768032625 307 PANR 310
Cdd:cd14113  248 PAKR 251
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
434-704 7.70e-30

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: 120.84  E-value: 7.70e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS-------KRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilnrkeQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05604   84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENIL-LDSQGH---IVLTDFGLCKEGISNSDTTTTFCG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTpEEILARIGSGKFSLSGGywnsVSDTAKDLVSKML 666
Cdd:cd05604  160 TPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYC--RDT-AEMYENILHKPLVLRPG----ISLTAWSILEELL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 667 HVDPHQRLTAA----LVLRHPWI--VHWDQLPQYQLNRQDAPHL 704
Cdd:cd05604  233 EKDRQLRLGAKedflEIKNHPFFesINWTDLVQKKIPPPFNPNV 276
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
68-311 8.44e-30

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 120.90  E-value: 8.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATlkvRDRVRtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14176   21 YEVKEDIGVGSYS---VCKRCIHKATNMEFAVKIIDKSK---RDPTE---EIEILLRYgQHPNIITLKDVYDDGKYVYVV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEGH---IKLTDFGLSKESIDHE 222
Cdd:cd14176   92 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFqGKDRKETMTMILkAKLGMPQF---------LSP 293
Cdd:cd14176  172 GLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEIL-ARIGSGKFslsggywnsVSD 249
                        250
                 ....*....|....*...
gi 768032625 294 EAQSLLRMLFKRNPANRL 311
Cdd:cd14176  250 TAKDLVSKMLHVDPHQRL 267
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
428-685 1.04e-29

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: 119.83  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIinEILvMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd06655  101 GSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL----GMDGSVKLTDFGFCAQITPEQSKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGS-GKFSLSGGywNSVSDTAKDLVS 663
Cdd:cd06655  176 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIATnGTPELQNP--EKLSPIFRDFLN 250
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06655  251 RCLEMDVEKRGSAKELLQHPFL 272
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
68-270 1.05e-29

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: 118.53  E-value: 1.05e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFL-----------VKKIsgsdarQLYAMKVLKKatlkvrdRVRTKMERDILVEVNHPFIVKLHYA 136
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRarclldgrlvaLKKV------QIFEMMDAKA-------RQDCLKEIDLLQQLNHPNIIKYLAS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 137 FQTEGKLYLILDFLRGGDLfTRLSKE-----VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTD 211
Cdd:cd08224   69 FIENNELNIVLELADAGDL-SRLIKHfkkqkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 212 FGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd08224  148 LGLGRFFSSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYG 206
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
434-682 1.12e-29

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 118.58  E-value: 1.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSK------RDPTE-EIEiLLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd14188    9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRvskphqREKIDkEIE-LHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESgnpESIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd14188   88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN-FFINEN---MELKVGDFGLAARLEPLEHRRRTICG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKML 666
Cdd:cd14188  164 TPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFET---TNLKETYRCIREARYSLP----SSLLAPAKHLIASML 236
                        250
                 ....*....|....*.
gi 768032625 667 HVDPHQRLTAALVLRH 682
Cdd:cd14188  237 SKNPEDRPSLDEIIRH 252
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
428-685 1.25e-29

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: 119.44  E-value: 1.25e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd06656  101 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTM 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGS-GKFSLSGGywNSVSDTAKDLVS 663
Cdd:cd06656  176 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLN---ENPLRALYLIATnGTPELQNP--ERLSAVFRDFLN 250
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06656  251 RCLEMDVDRRGSAKELLQHPFL 272
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
448-733 1.71e-29

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: 119.80  E-value: 1.71e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 448 KATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSER 520
Cdd:cd05592   17 KGTNQYFAIKALKKDvvlEDDDVEctmiERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNGGDLMFHIQQSGRFDED 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 521 EASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQG 600
Cdd:cd05592   97 RARFYGAEIICGLQFLHSRGIIYRDLKLDNVL-LDREGH---IKIADFGMCKENIYGENKASTFCGTPDYIAPEILKGQK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 601 YDAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGKFSlsggYWNSVSDTAKDLVSKMLHVDPHQRL-----T 675
Cdd:cd05592  173 YNQSVDWWSFGVLLYEMLIGQSPF-HGEDE--DELFWSICNDTPH----YPRWLTKEAASCLSLLLERNPEKRLgvpecP 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 676 AALVLRHPWI--VHWDQLPQYQLNRQDAPHlVKGAMAATY-SALNRNQSPVLEPVGRSTLA 733
Cdd:cd05592  246 AGDIRDHPFFktIDWDKLERREIDPPFKPK-VKSANDVSNfDPDFTMEKPVLTPVDKKLLA 305
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
434-685 2.01e-29

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: 117.84  E-value: 2.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKI--IDKSKRDPTEEI-----EI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEVkalecEIqLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESGNpesIRICDFGFAKQLRA--ENGLLMT 583
Cdd:cd06625   88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILR-DSNGN---VKLGDFGASKRLQTicSSTGMKS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSG--KFSLSggywNSVSDTAKDL 661
Cdd:cd06625  164 VTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWA---EFEPMAAIFKIATQptNPQLP----PHVSEDARDF 236
                        250       260
                 ....*....|....*....|....
gi 768032625 662 VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06625  237 LSLIFVRNKKQRPSAEELLSHSFV 260
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
423-685 2.52e-29

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: 119.21  E-value: 2.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEiLLRYGQHPNIITLKDVY-DDGKYV 495
Cdd:cd07856    7 EITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVlakrtyRELK-LLKHLRHENIISLSDIFiSPLEDI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMkgGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAkqlR 575
Cdd:cd07856   86 YFVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNIL-VNENCD---LKICDFGLA---R 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AENGLLMTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGyTPFANGPD-------------DTPEEILARIGS 641
Cdd:cd07856  157 IQDPQMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEG-KPLFPGKDhvnqfsiitellgTPPDDVINTICS 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 642 -------------GKFSLSGGYWNSVSDtAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07856  236 entlrfvqslpkrERVPFSEKFKNADPD-AIDLLEKMLVFDPKKRISAAEALAHPYL 291
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
434-732 3.01e-29

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


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 118.86  E-value: 3.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVLKKDvilQDDDVEctmtEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05590   83 LMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVL-LDHEGH---CKLADFGMCKEGIFNGKTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILarigsgKFSLSGGYWnsVSDTAKDLVSKM 665
Cdd:cd05590  159 TPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFeAENEDDLFEAIL------NDEVVYPTW--LSQDAVDILKAF 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 666 LHVDPHQRLTA------ALVLRHPWI--VHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTL 732
Cdd:cd05590  231 MTKNPTMRLGSltlggeEAILRHPFFkeLDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEDPVLTPIEESLL 305
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
428-683 3.22e-29

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: 117.13  E-value: 3.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID------KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDisrmsrKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKGKLNIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNpesIRICDFGFAKQLRAENG 579
Cdd:cd08529   81 AENGDLHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNI-FLDKGDN---VKIGDLGVAKILSDTTN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFS-LSGGYwnsvSDTA 658
Cdd:cd08529  157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEA---QNQGALILKIVRGKYPpISASY----SQDL 229
                        250       260
                 ....*....|....*....|....*
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd08529  230 SQLIDSCLTKDYRQRPDTTELLRNP 254
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
428-728 3.73e-29

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: 118.87  E-value: 3.73e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYS----VCKRCIHKATNMeFAVKIIDKS---KRDPTEE-----IEILLRYGQHPNIITLKDVYDDGKYV 495
Cdd:cd05614    2 FELLKVLGTGAYGkvflVRKVSGHDANKL-YAMKVLRKAalvQKAKTVEhtrteRNVLEHVRQSPFLVTLHYAFQTDAKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQ-L 574
Cdd:cd05614   81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENIL-LDSEGH---VVLTDFGLSKEfL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGLLMTPCYTANFVAPEVLKRQ-GYDAACDIWSLGVLLYTMLTGYTPFA-NGPDDTPEEILARIgsgkFSLSGGYWN 652
Cdd:cd05614  157 TEEKERTYSFCGTIEYMAPEIIRGKsGHGKAVDWWSLGILMFELLTGASPFTlEGEKNTQSEVSRRI----LKCDPPFPS 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTAAL-----VLRHPWI--VHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLE 725
Cdd:cd05614  233 FIGPVARDLLQKLLCKDPKKRLGAGPqgaqeIKEHPFFkgLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYS 312

                 ...
gi 768032625 726 PVG 728
Cdd:cd05614  313 PAG 315
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
426-685 3.99e-29

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: 117.71  E-value: 3.99e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD---PT---EEIEILLRyGQHPNIITLKDVY--DDGKYVYV 497
Cdd:cd07843    5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKegfPItslREINILLK-LQHPNIVTVKEVVvgSNLDKIYM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELM----KGgeLLDKILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQ 573
Cdd:cd07843   84 VMEYVehdlKS--LMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLL----NNRGILKICDFGLARE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 ----LRAengllmtpcYTANFV-----APEVLKRQG-YDAACDIWSLGVLLYTMLTGyTPFANGPD--DTPEEILARIGS 641
Cdd:cd07843  156 ygspLKP---------YTQLVVtlwyrAPELLLGAKeYSTAIDMWSVGCIFAELLTK-KPLFPGKSeiDQLNKIFKLLGT 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 642 -------GKFSLSGG---------YWN--------SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07843  226 ptekiwpGFSELPGAkkktftkypYNQlrkkfpalSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
64-332 4.13e-29

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: 117.40  E-value: 4.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPS-QFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKkatlkvrdrVRTKMERDILVEVN-------HPFIVKLHY 135
Cdd:cd06608    3 DPAgIFELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMD---------IIEDEEEEIKLEINilrkfsnHPNIATFYG 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AFQT------EGKLYLILDFLRGGDLfTRLSKEVM-----FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd06608   71 AFIKkdppggDDQLWLVMEYCGGGSV-TDLVKGLRkkgkrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVN-----RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTM 279
Cdd:cd06608  150 AEVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFK 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 280 ILK---AKLGMPQFLSPEAQSLLRMLFKRNPANRlvnPFligagpdgVEEIKRHSF 332
Cdd:cd06608  230 IPRnppPTLKSPEKWSKEFNDFISECLIKNYEQR---PF--------TEELLEHPF 274
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
71-310 4.15e-29

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: 117.05  E-value: 4.15e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKISGSdarQLYAMKVLkkaTLKVRDRVRT-KMERDILVEV-NHPFIVKL--HYAFQTEG-KLYL 145
Cdd:cd13985    5 TKQLGEGGFSYVYLAHDVNTG---RRYALKRM---YFNDEEQLRVaIKEIEIMKRLcGHPNIVQYydSAILSSEGrKEVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLDEEGHIKLTDFGlSKESIDH 221
Cdd:cd13985   79 LLMEYCPGSLVDILEKSPPspLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG-SATTEHY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVE----------YMAPEVVN---RRGHTQSADWWSFGVLMFEMLTGTLPFQGkdrkETMTMILKAKLGMP 288
Cdd:cd13985  158 PLERAEEVNIIEeeiqknttpmYRAPEMIDlysKKPIGEKADIWALGCLLYKLCFFKLPFDE----SSKLAIVAGKYSIP 233
                        250       260
                 ....*....|....*....|....
gi 768032625 289 QF--LSPEAQSLLRMLFKRNPANR 310
Cdd:cd13985  234 EQprYSPELHDLIRHMLTPDPAER 257
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
64-272 4.16e-29

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: 117.54  E-value: 4.16e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKISGSdarqlyamKVLKKATLKV--RDRVRTKM--ERDILVEVNHPFIVKLHYAFQT 139
Cdd:cd06620    3 KNQDLETLKDLGAGNGGSVSKVLHIPTG--------TIMAKKVIHIdaKSSVRKQIlrELQILHECHSPYIVSFYGAFLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 E-GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKfylaELALA----LDHLHS-LGIIYRDLKPENILLDEEGHIKLTDFG 213
Cdd:cd06620   75 EnNNIIICMEYMDCGSLDKILKKKGPFPEEVLG----KIAVAvlegLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 214 LSKESIDheKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKD 272
Cdd:cd06620  151 VSGELIN--SIADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSN 207
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
428-684 4.74e-29

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: 117.67  E-value: 4.74e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR-------DPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkeakdgiNFTALREIkLLQELKHPNIIGLLDVFGHKSNINLVF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGelLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAE 577
Cdd:cd07841   82 EFMETD--LEKVIKDKsiVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLL-IASDG---VLKLADFGLARSFGSP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPCYTANFVAPEVL--KRQgYDAACDIWSLGVLLYTMLTGyTPFANGPDD------------TPEE-----ILAR 638
Cdd:cd07841  156 NRKMTHQVVTRWYRAPELLfgARH-YGVGVDMWSVGCIFAELLLR-VPFLPGDSDidqlgkifealgTPTEenwpgVTSL 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 639 IGSGKFSLSGG-----YWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07841  234 PDYVEFKPFPPtplkqIFPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
511-682 5.11e-29

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 117.51  E-value: 5.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 511 ILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpESIRICDFGFAKQLRAENGLLM----TPCY 586
Cdd:cd13974  123 VIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRT---RKITITNFCLGKHLVSEDDLLKdqrgSPAY 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 tanfVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSL-SGGywnSVSDTAKDLVSK 664
Cdd:cd13974  200 ----ISPDVLSGKPYLGkPSDMWALGVVLFTMLYGQFPFY---DSIPQELFRKIKAAEYTIpEDG---RVSENTVCLIRK 269
                        170
                 ....*....|....*...
gi 768032625 665 MLHVDPHQRLTAALVLRH 682
Cdd:cd13974  270 LLVLNPQKRLTASEVLDS 287
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
434-734 5.45e-29

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: 118.36  E-value: 5.45e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDvilQDDDVDctmtEKRILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05591   83 LMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNIL-LDAEGH---CKLADFGMCKEGILNGKTTTTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARigsgkfSLSGGYWnsVSDTAKDLVSKM 665
Cdd:cd05591  159 TPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFeADNEDDLFESILHD------DVLYPVW--LSKEAVSILKAF 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 666 LHVDPHQRL-------TAALVLRHPWI--VHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQSPVLEPVGRSTLAQ 734
Cdd:cd05591  231 MTKNPAKRLgcvasqgGEDAIRQHPFFreIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQ 308
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
74-310 6.01e-29

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: 115.67  E-value: 6.01e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLvkkisGSDARQLYAMKvlkkatlKVRDRVRTKMERdiLVEVNHPFIVKLHyAFQTEGKLYLIL-DFLRG 152
Cdd:cd14059    1 LGSGAQGAVFL-----GKFRGEEVAVK-------KVRDEKETDIKH--LRKLNHPNIIKFK-GVCTQAPCYCILmEYCPY 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAySFCGTV 232
Cdd:cd14059   66 GQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKM-SFAGTV 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 233 EYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLS-PEA-QSLLRMLFKRNPANR 310
Cdd:cd14059  145 AWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLQLPVPSTcPDGfKLLMKQCWNSKPRNR 224
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
66-321 6.37e-29

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 118.77  E-value: 6.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATlkvRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 143
Cdd:PLN00034  74 SELERVNRIGSGAGGTVYKVIHRPTG---RLYALKVIYGNH---EDTVRRQICREIeiLRDVNHPNVVKCHDMFDHNGEI 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDL-FTRLSKEVmfteedvkfYLAELAL----ALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-- 216
Cdd:PLN00034 148 QVLLEFMDGGSLeGTHIADEQ---------FLADVARqilsGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRil 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 -ESIDhekKAYSFCGTVEYMAPEVVNR-----RGHTQSADWWSFGVLMFEMLTGTLPF----QGkDRKETMTMI-LKAKL 285
Cdd:PLN00034 219 aQTMD---PCNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQG-DWASLMCAIcMSQPP 294
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 286 GMPQFLSPEAQSLLRMLFKRNPANR------LVNPFLIGAGP 321
Cdd:PLN00034 295 EAPATASREFRHFISCCLQREPAKRwsamqlLQHPFILRAQP 336
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
434-676 6.58e-29

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: 118.58  E-value: 6.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDK-------SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05602   15 IGKGSFGKVLLARHKSDEKFYAVKVLQKkailkkkEEKHIMSERNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05602   95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENIL-LDSQGH---IVLTDFGLCKENIEPNGTTSTFCG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKML 666
Cdd:cd05602  171 TPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYS---RNTAEMYDNILNKPLQLK----PNITNSARHLLEGLL 243
                        250
                 ....*....|
gi 768032625 667 HVDPHQRLTA 676
Cdd:cd05602  244 QKDRTKRLGA 253
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
427-688 6.92e-29

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: 118.28  E-value: 6.92e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYS-VCK-RCIHKATNMEFAVK----IIDKS---KRdPTEEIEILLRYGQHPNIITL--KDVYDDGKY- 494
Cdd:cd07857    1 RYELIKELGQGAYGiVCSaRNAETSEEETVAIKkitnVFSKKilaKR-ALRELKLLRHFRGHKNITCLydMDIVFPGNFn 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 -VYVVTELMKGGelLDKILRQ-KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAK 572
Cdd:cd07857   80 eLYLYEELMEAD--LHQIIRSgQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLL-VNADC---ELKICDFGLAR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRA---ENGLLMTPcYTAN--FVAPEV-LKRQGYDAACDIWSLGVLLYTMLtGYTPFANGPD------------DTP-E 633
Cdd:cd07857  154 GFSEnpgENAGFMTE-YVATrwYRAPEImLSFQSYTKAIDVWSVGCILAELL-GRKPVFKGKDyvdqlnqilqvlGTPdE 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 634 EILARIGSGK-----FSLS-------GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHW 688
Cdd:cd07857  232 ETLSRIGSPKaqnyiRSLPnipkkpfESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIW 298
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
428-685 7.19e-29

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: 117.13  E-value: 7.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI--EIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd06654  102 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTM 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGS-GKFSLSGGywNSVSDTAKDLVS 663
Cdd:cd06654  177 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLN---ENPLRALYLIATnGTPELQNP--EKLSAIFRDFLN 251
                        250       260
                 ....*....|....*....|..
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06654  252 RCLEMDVEKRGSAKELLQHQFL 273
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-311 7.46e-29

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: 116.79  E-value: 7.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISgsdARQLYAMKVL---KKATLKVRDRVRTKmerdilvevNHPFIVKLHYAFQTE---------- 140
Cdd:cd14171   14 LGTGISGPVRVCVKKS---TGERFALKILldrPKARTEVRLHMMCS---------GHPNIVQIYDVYANSvqfpgesspr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGLSKE 217
Cdd:cd14171   82 ARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SiDHEKKAYSFcgTVEYMAPEVV--------NRRGHTQ---------SADWWSFGVLMFEMLTGTLPFQGKDRKETMT-- 278
Cdd:cd14171  162 D-QGDLMTPQF--TPYYVAPQVLeaqrrhrkERSGIPTsptpytydkSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITkd 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 279 ---MILKAKLGMPQ----FLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14171  239 mkrKIMTGSYEFPEeewsQISEMAKDIVRKLLCVDPEERM 278
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
428-685 7.50e-29

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: 116.21  E-value: 7.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSY---------SVCKRCIHKATNMEfavKIIDKSKRDPTEEIeILLRYGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd08225    2 YEIIKKIGEGSFgkiylakakSDSEHCVIKEIDLT---KMPVKEKEASKKEV-ILLAKMKHPNIVTFFASFQENGRLFIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRICDFGFAKQLRA 576
Cdd:cd08225   78 MEYCDGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFL---SKNGMVAKLGDFGIARQLND 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFS-LSGGYwnsvS 655
Cdd:cd08225  155 SMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEG---NNLHQLVLKICQGYFApISPNF----S 227
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 656 DTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08225  228 RDLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
72-311 9.03e-29

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: 116.67  E-value: 9.03e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKV-FLVKKISGSDarqlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPfIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd14174    8 ELLGEGAYAKVqGCVSLQNGKE----YAVKIIEKNAGHSRSRVFREVETLYQCQGNKN-ILELIEFFEDDTRFYLVFEKL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---DEEGHIKLTDFGL-------SKESID 220
Cdd:cd14174   83 RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLgsgvklnSACTPI 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVV-----NRRGHTQSADWWSFGVLMFEMLTGTLPFQGK-------DRKET--------MTMI 280
Cdd:cd14174  163 TTPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwDRGEVcrvcqnklFESI 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 281 LKAKLGMPQ----FLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14174  243 QEGKYEFPDkdwsHISSEAKDLISKLLVRDAKERL 277
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
68-268 1.11e-28

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: 116.37  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGsdaRQLYAMKVLKKATlkvrdrvRTKMERDILVEVN------HPFIVKLHYAF--QT 139
Cdd:cd06621    3 IVELSSLGEGAGGSVTKCRLRNT---KTIFALKTITTDP-------NPDVQKQILRELEinkscaSPYIVKYYGAFldEQ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDL---FTRLSKEVMFTEEDVKFYLAELAL-ALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd06621   73 DSSIGIAMEYCEGGSLdsiYKKVKKKGGRIGEKVLGKIAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 216 KESIdhEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd06621  153 GELV--NSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF 203
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
434-686 1.32e-28

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 118.00  E-value: 1.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVRRQICREIEIL-RDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DKilrqKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEngllMTPCY-- 586
Cdd:PLN00034 161 GT----HIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLL-INSAKN---VKIADFGVSRILAQT----MDPCNss 228
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 --TANFVAPEV----LKRQGYDA-ACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGsgkFSLSGGYWNSVSDTAK 659
Cdd:PLN00034 229 vgTIAYMSPERintdLNHGAYDGyAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAIC---MSQPPEAPATASREFR 305
                        250       260
                 ....*....|....*....|....*..
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:PLN00034 306 HFISCCLQREPAKRWSAMQLLQHPFIL 332
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
64-316 1.37e-28

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: 115.41  E-value: 1.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPS-QFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVrdrvrtkMERDILV--EVNHPFIVKLHYAFQTE 140
Cdd:cd06647    4 DPKkKYTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKEL-------IINEILVmrENKNPNIVNYLDSYLVG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06647   77 DELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIlkAKLGMPQFLSPEAQSLLR 300
Cdd:cd06647  156 EQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI--ATNGTPELQNPEKLSAIF 233
                        250       260
                 ....*....|....*....|....*..
gi 768032625 301 MLF----------KRNPANRLV-NPFL 316
Cdd:cd06647  234 RDFlnrclemdveKRGSAKELLqHPFL 260
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
68-343 1.65e-28

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: 116.27  E-value: 1.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATlkvRDrvrTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14177    6 YELKEDIGVGSYS---VCKRCIHRATNMEFAVKIIDKSK---RD---PSEEIEILMRYgQHPNIITLKDVYDDGRYVYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEEGH---IKLTDFGLSKESIDHE 222
Cdd:cd14177   77 TELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGEN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILkaKLGMPQF---------LSP 293
Cdd:cd14177  157 GLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILL--RIGSGKFslsggnwdtVSD 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 294 EAQSLLRMLFKRNPANRLVnpfligagpdgVEEIKRHSFFSTIDWNKLYR 343
Cdd:cd14177  235 AAKDLLSHMLHVDPHQRYT-----------AEQVLKHSWIACRDQLPHYQ 273
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
425-685 1.87e-28

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: 115.61  E-value: 1.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVY-DDGKyVYVVT 499
Cdd:cd06611    4 NDIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEdfmvEIDILSEC-KHPNIVGLYEAYfYENK-LWILI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILR-QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpesIRICDFGFAKQLRAEN 578
Cdd:cd06611   82 EFCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD----VKLADFGVSAKNKSTL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVL-----KRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSG---KFSLSGGY 650
Cdd:cd06611  158 QKRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHH---ELNPMRVLLKILKSeppTLDQPSKW 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 651 WNSVsdtaKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06611  235 SSSF----NDFLKSCLVKDPDDRPTAAELLKHPFV 265
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
428-681 1.90e-28

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: 115.12  E-value: 1.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEILLRYGQHPNIITLKD--VYDDG--KYVYVVT 499
Cdd:cd13985    2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMyfndEEQLRVAIKEIEIMKRLCGHPNIVQYYDsaILSSEgrKEVLLLM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMkGGELLDKILR--QKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYvdesGNPESIRICDFGFA---- 571
Cdd:cd13985   82 EYC-PGSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILF----SNTGRFKLCDFGSAtteh 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 -KQLRAEN--------GLLMTPCYTAnfvaPEVLKRQGYDAAC---DIWSLGVLLYTMLTGYTPFangpddTPEEILaRI 639
Cdd:cd13985  157 yPLERAEEvniieeeiQKNTTPMYRA----PEMIDLYSKKPIGekaDIWALGCLLYKLCFFKLPF------DESSKL-AI 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 640 GSGKFSLSGGywNSVSDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd13985  226 VAGKYSIPEQ--PRYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
434-685 2.13e-28

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: 115.20  E-value: 2.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEiEILL-RYGQHPNIITLKDVYDDGKYVYVVTELMKGGELlD 509
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIperDSREVQPLHE-EIALhSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSL-S 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILRQKF--FSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDESGnpeSIRICDFGFAKQLRAENGLLMTPC 585
Cdd:cd06624   94 ALLRSKWgpLKDNENTIGYYTkqILEGLKYLHDNKIVHRDIKGDNVLVNTYSG---VVKISDFGTSKRLAGINPCTETFT 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKR--QGYDAACDIWSLGVLLYTMLTGYTPFAN-GPddtPEEILARIGSgkFSLSGGYWNSVSDTAKDLV 662
Cdd:cd06624  171 GTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIElGE---PQAAMFKVGM--FKIHPEIPESLSEEAKSFI 245
                        250       260
                 ....*....|....*....|...
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06624  246 LRCFEPDPDKRATASDLLQDPFL 268
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
64-311 2.28e-28

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: 115.13  E-value: 2.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVF--LVKKISGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd05032    4 PREKITLIRELGQGSFGMVYegLAKGVVKGEPETRVAIKTVNENA-SMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLFTRLsKEVMFTEEDVKFY-----------LAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLT 210
Cdd:cd05032   83 PTLVVMELMAKGDLKSYL-RSRRPEAENNPGLgpptlqkfiqmAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 211 DFGLSKESIDHE--KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAKL-- 285
Cdd:cd05032  162 DFGMTRDIYETDyyRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLKFVIDGGHld 241
                        250       260
                 ....*....|....*....|....*....
gi 768032625 286 ---GMPQFLspeaQSLLRMLFKRNPANRL 311
Cdd:cd05032  242 lpeNCPDKL----LELMRMCWQYNPKMRP 266
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
434-685 2.32e-28

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: 115.52  E-value: 2.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRREllfnEVVIMRDY-HHENVVDMYNSYLVGDELWVVMEFLEGGALTD 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 kILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTPCYTAN 589
Cdd:cd06658  109 -IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDG----RIKLSDFGFCAQVSKEVPKRKSLVGTPY 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 590 FVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIgsgKFSLSGGYWNS--VSDTAKDLVSKMLH 667
Cdd:cd06658  184 WMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEP---PLQAMRRI---RDNLPPRVKDShkVSSVLRGFLDLMLV 257
                        250
                 ....*....|....*...
gi 768032625 668 VDPHQRLTAALVLRHPWI 685
Cdd:cd06658  258 REPSQRATAQELLQHPFL 275
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
432-643 2.49e-28

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: 114.52  E-value: 2.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  432 EDIGVGSY-SVCK---RCIHKATNMEFAVKIIDKSKRDPT-----EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:pfam07714   5 EKLGEGAFgEVYKgtlKGEGENTKIKVAVKTLKEGADEEEredflEEASIMKKL-DHPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  503 KGGELLDKiLRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL------ 574
Cdd:pfam07714  84 PGGDLLDF-LRKHKRKLTLKDLLSMAlqIAKGMEYLESKNFVHRDLAARNCL-VSENLV---VKISDFGLSRDIydddyy 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  575 RAENGLLMTPCYTanfvAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSGK 643
Cdd:pfam07714 159 RKRGGGKLPIKWM----APESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY---PGMSNEEVLEFLEDGY 221
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
68-310 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: 114.33  E-value: 2.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKkiSGSDArQLYAMKvlkkatlKVRDRVRTKMER-DILVEVN-------HPFIVKLHYAFQT 139
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVR--SREDG-KLYAVK-------RSRSRFRGEKDRkRKLEEVErheklgeHPNCVRFIKAWEE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsI 219
Cdd:cd14050   73 KGILYIQTE-LCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-L 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNrrGH-TQSADWWSFGVLMFEMLTGT-LPFQGKDRKETMTMILKAKLGMPqfLSPEAQS 297
Cdd:cd14050  151 DKEDIHDAQEGDPRYMAPELLQ--GSfTKAADIFSLGITILELACNLeLPSGGDGWHQLRQGYLPEEFTAG--LSPELRS 226
                        250
                 ....*....|...
gi 768032625 298 LLRMLFKRNPANR 310
Cdd:cd14050  227 IIKLMMDPDPERR 239
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
75-310 3.24e-28

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: 114.15  E-value: 3.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  75 GQGSFGKVFLVKkisGSDARQLYAMKVLKkatLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 154
Cdd:cd14111   12 ARGRFGVIRRCR---ENATGKNFPAKIVP---YQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 155 LFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG-------LSKESIDHekkays 227
Cdd:cd14111   86 LLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGsaqsfnpLSLRQLGR------ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLRMLFK 304
Cdd:cd14111  160 RTGTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKLypnVSQSASLFLKKVLS 239

                 ....*.
gi 768032625 305 RNPANR 310
Cdd:cd14111  240 SYPWSR 245
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
428-673 3.27e-28

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: 114.52  E-value: 3.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSY-SVCKRCIHKATNMEFAVKII--------------DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDG 492
Cdd:cd08528    2 YAVLELLGSGAFgCVYKVRKKSNGQTLLALKEInmtnpafgrteqerDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 493 KYVYVVTELMKGGELLDKI--LRQK--FFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILYvdesGNPESIRICD 567
Cdd:cd08528   82 DRLYIVMELIEGAPLGEHFssLKEKneHFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIML----GEDDKVTITD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFS-L 646
Cdd:cd08528  158 FGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYS---TNMLTLATKIVEAEYEpL 234
                        250       260
                 ....*....|....*....|....*..
gi 768032625 647 SGGYWnsvSDTAKDLVSKMLHVDPHQR 673
Cdd:cd08528  235 PEGMY---SDDITFVIRSCLTPDPEAR 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
61-320 4.60e-28

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: 114.70  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  61 EKADPSQF-ELLKVLGQGSFGKVFLVK-KISGsdaRQLyAMKVLKkatlkVRDRVRTKM---ERDILVEVNHPFIVKLHY 135
Cdd:cd06659   15 DQGDPRQLlENYVKIGEGSTGVVCIAReKHSG---RQV-AVKMMD-----LRKQQRRELlfnEVVIMRDYQHPNVVEMYK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AFQTEGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd06659   86 SYLVGEELWVLMEYLQGGAL-TDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFC 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 KESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA---KLGMPQFLS 292
Cdd:cd06659  165 AQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKAS 244
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 293 PEAQSLLRMLFKRNPANR------LVNPFLIGAG 320
Cdd:cd06659  245 PVLRDFLERMLVRDPQERataqelLDHPFLLQTG 278
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
67-334 4.85e-28

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: 114.28  E-value: 4.85e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVR--------------------------DRVRTKMErd 120
Cdd:cd14200    1 QYKLQSEIGKGSYG---VVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplaplERVYQEIA-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 121 ILVEVNHPFIVKLHYAFQ--TEGKLYLILDFLRGGDLFtRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPEN 198
Cdd:cd14200   76 ILKKLDHVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 199 ILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSA---DWWSFGVLMFEMLTGTLPFQGkdrKE 275
Cdd:cd14200  155 LLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYGKCPFID---EF 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 276 TMTMILKAKLGMPQF-----LSPEAQSLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSFFS 334
Cdd:cd14200  232 ILALHNKIKNKPVEFpeepeISEELKDLILKMLDKNPETRI-----------TVPEIKVHPWVT 284
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-279 4.94e-28

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: 115.23  E-value: 4.94e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKkatLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd06615    3 FEKLGELGAGNGGVVTKVLhRPSG----LIMARKLIH---LEIKPAIRNQIIRElkVLHECNSPYIVGFYGAFYSDGEIS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEdvkfYLAELALA-LDHLHSL----GIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd06615   76 ICMEHMDGGSLDQVLKKAGRIPEN----ILGKISIAvLRGLTYLrekhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLI 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DheKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTM 279
Cdd:cd06615  152 D--SMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAM 209
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
68-334 5.37e-28

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: 114.44  E-value: 5.37e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKkATLKVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLI 146
Cdd:cd06617    3 LEVIEELGRGAYG---VVDKMRHVPTGTIMAVKRIR-ATVNSQEQKRLLMDLDISMRSVDcPYTVTFYGALFREGDVWIC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGG--DLFTRLSKEVMFTEEDVkfyLAELAL----ALDHLHS-LGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd06617   79 MEVMDTSldKFYKKVYDKGLTIPEDI---LGKIAVsivkALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSfCGTVEYMAPEVVN----RRGHTQSADWWSFGVLMFEMLTGTLPF-QGKDRKETMTMILKA---KLGMPQFl 291
Cdd:cd06617  156 DSVAKTID-AGCKPYMAPERINpelnQKGYDVKSDVWSLGITMIELATGRFPYdSWKTPFQQLKQVVEEpspQLPAEKF- 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 292 SPEAQSLLRMLFKRNPANRLVNPfligagpdgveEIKRHSFFS 334
Cdd:cd06617  234 SPEFQDFVNKCLKKNYKERPNYP-----------ELLQHPFFE 265
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
411-691 6.72e-28

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: 115.55  E-value: 6.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 411 HSIVQQLHRNSIQFTDgYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPT----EEIEILlrygQHPN-- 481
Cdd:cd05596   12 EKPVNEITKLRMNAED-FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFemiKRSDSaffwEERDIM----AHANse 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 482 -IITLKDVYDDGKYVYVVTELMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNp 560
Cdd:cd05596   87 wIVQLHYAFQDDKYLYMVMDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNML-LDASGH- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 561 esIRICDFGFAKQLrAENGLLM--TPCYTANFVAPEVLKRQG----YDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEE 634
Cdd:cd05596  164 --LKLADFGTCMKM-DKDGLVRsdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVG 237
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 635 ILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLhVDPHQRLTA---ALVLRHPWIVH----WDQL 691
Cdd:cd05596  238 TYGKIMNHKNSLQFPDDVEISKDAKSLICAFL-TDREVRLGRngiEEIKAHPFFKNdqwtWDNI 300
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
415-688 7.57e-28

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: 115.52  E-value: 7.57e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 415 QQLHRNSIQFTDGYEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDK-------SKRDPTEEIeiLLRYGQHPNIITLK 486
Cdd:cd07877    6 QELNKTIWEVPERYQNLSPVGSGAYgSVCA-AFDTKTGLRVAVKKLSRpfqsiihAKRTYRELR--LLKHMKHENVIGLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 487 DVYDDGKY------VYVVTELMkgGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESGnp 560
Cdd:cd07877   83 DVFTPARSleefndVYLVTHLM--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN-LAVNEDC-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 561 eSIRICDFGFAKQLRAE-NGLLMTPCYTanfvAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDD-------- 630
Cdd:cd07877  158 -ELKILDFGLARHTDDEmTGYVATRWYR----APEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFP-GTDHidqlklil 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 631 ----TPE-EILARIGSGKfslSGGYWNSVSDTAK---------------DLVSKMLHVDPHQRLTAALVLRHPWIVHW 688
Cdd:cd07877  232 rlvgTPGaELLKKISSES---ARNYIQSLTQMPKmnfanvfiganplavDLLEKMLVLDSDKRITAAQALAHAYFAQY 306
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
64-267 7.74e-28

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: 113.63  E-value: 7.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFlvkkiSGSDAR--QLYAMKV--LKKATLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQ 138
Cdd:cd06641    1 DPEElFTKLEKIGKGSFGEVF-----KGIDNRtqKVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLSKEVMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd06641   73 KDTKLWIIMEYLGGGSALDLLEPGPL-DETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLP 267
Cdd:cd06641  152 TDTQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
66-332 8.70e-28

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 113.91  E-value: 8.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLkVRD--------------------RVRTKMER-----D 120
Cdd:cd14199    2 NQYKLKDEIGKGSYG---VVKLAYNEDDNTYYAMKVLSKKKL-MRQagfprrppprgaraapegctQPRGPIERvyqeiA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 121 ILVEVNHPFIVKLHYAFQ--TEGKLYLILDFLRGGDLFtRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPEN 198
Cdd:cd14199   78 ILKKLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 199 ILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVN--RRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKE 275
Cdd:cd14199  157 LLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSetRKIFSgKALDVWAMGVTLYCFVFGQCPFMDERILS 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 276 TMTMILKAKLGMPQF--LSPEAQSLLRMLFKRNPANRLVNPfligagpdgveEIKRHSF 332
Cdd:cd14199  237 LHSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRISVP-----------EIKLHPW 284
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
74-284 8.79e-28

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: 114.51  E-value: 8.79e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFL-VKKISGsdarQLYAMKVLKKAT----LKVRDRvrtkmERDILVEVNHPFIVKLhYAFQTE----GKLy 144
Cdd:cd13988    1 LGQGATANVFRgRHKKTG----DLYAVKVFNNLSfmrpLDVQMR-----EFEVLKKLNHKNIVKL-FAIEEElttrHKV- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRL---SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL--LDEEGH--IKLTDFGLSKE 217
Cdd:cd13988   70 LVMELCPCGSLYTVLeepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARE 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 218 SIDHEKKAySFCGTVEYMAPEVVNR---RGHTQ-----SADWWSFGVLMFEMLTGTLPFQ----GKDRKETMTMILKAK 284
Cdd:cd13988  150 LEDDEQFV-SLYGTEEYLHPDMYERavlRKDHQkkygaTVDLWSIGVTFYHAATGSLPFRpfegPRRNKEVMYKIITGK 227
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
426-666 9.71e-28

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: 116.26  E-value: 9.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK---SKRDPT----EEIEILlRYGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd05622   73 EDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSaffwEERDIM-AFANSPWVVQLFYAFQDDRYLYMV 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN 578
Cdd:cd05622  152 MEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKEG 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 gllMTPCYTA----NFVAPEVLKRQG----YDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGY 650
Cdd:cd05622  227 ---MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYA---DSLVGTYSKIMNHKNSLTFPD 300
                        250
                 ....*....|....*.
gi 768032625 651 WNSVSDTAKDLVSKML 666
Cdd:cd05622  301 DNDISKEAKNLICAFL 316
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
68-330 9.71e-28

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: 112.78  E-value: 9.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVflvkkisgsdaRQLYAMKVLKKATLKVRDR-------VRTKMERD--ILVEVNHPFIVKLHYAFQ 138
Cdd:cd14163    2 YQLGKTIGEGTYSKV-----------KEAFSKKHQRKVAIKIIDKsggpeefIQRFLPRElqIVERLDHKNIIHVYEMLE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 -TEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLdEEGHIKLTDFGLSKE 217
Cdd:cd14163   71 sADGKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 -SIDHEKKAYSFCGTVEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPQFL--SP 293
Cdd:cd14163  150 lPKGGRELSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG-VSLPGHLgvSR 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 294 EAQSLLRmlfkrnpanRLVNPFLIgAGPDgVEEIKRH 330
Cdd:cd14163  229 TCQDLLK---------RLLEPDMV-LRPS-IEEVSWH 254
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
74-268 9.86e-28

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: 113.90  E-value: 9.86e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgSDARQLYAMKVLKKAtLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL------YLIL 147
Cdd:cd14038    2 LGTGGFGNVLRWIN---QETGEQVAIKQCRQE-LSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDL---FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EEGHI-KLTDFGLSKEsIDH 221
Cdd:cd14038   78 EYCQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQqgEQRLIhKIIDLGYAKE-LDQ 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14038  157 GSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
428-683 1.07e-27

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: 113.08  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVckrcIHKATNME---FAVKIIDKSKRDPTE------EIEILLRYGQHPNIITLKD--VYDDGKYVY 496
Cdd:cd14131    3 YEILKQLGKGGSSK----VYKVLNPKkkiYALKRVDLEGADEQTlqsyknEIELLKKLKGSDRIIQLYDyeVTDEDDYLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELmkgGEL-LDKILRQKFFSEREASAVLFTIT---KTVEYLHAQGVVHRDLKPSNILYVDesGNpesIRICDFGFAK 572
Cdd:cd14131   79 MVMEC---GEIdLATILKKKRPKPIDPNFIRYYWKqmlEAVHTIHEEGIVHSDLKPANFLLVK--GR---LKLIDFGIAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGLLM--TPCYTANFVAPEVLKRQGYDA----------ACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIG 640
Cdd:cd14131  151 AIQNDTTSIVrdSQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQH--ITNPIAKLQAII 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 641 SGKFSLSggyWNSVSDT-AKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14131  229 DPNHEIE---FPDIPNPdLIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
460-685 1.11e-27

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: 112.52  E-value: 1.11e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 460 DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLH 537
Cdd:cd08221   40 EKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 538 AQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTM 617
Cdd:cd08221  119 KAGILHRDIKTLNIFLT----KADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYEL 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 618 LTGYTPF-ANGPDDTPEEILArigsgkfslsgGYWNSV----SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08221  195 LTLKRTFdATNPLRLAVKIVQ-----------GEYEDIdeqySEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
64-267 1.14e-27

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: 113.22  E-value: 1.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFlvkkiSGSDAR--QLYAMKV--LKKATLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQ 138
Cdd:cd06640    1 DPEElFTKLERIGKGSFGEVF-----KGIDNRtqQVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLsKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd06640   73 KGTKLWIIMEYLGGGSALDLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLP 267
Cdd:cd06640  152 TDTQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
74-284 1.42e-27

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: 113.03  E-value: 1.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISgsdARQLYAMKVLKkatLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14104    8 LGRGQFGIVHRCVETS---SKKTYMAKFVK---VKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLS-KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE--GHIKLTDFGLSKESIDHEKKAYSFCg 230
Cdd:cd14104   82 DIFERITtARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSRQLKPGDKFRLQYT- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK 284
Cdd:cd14104  161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAE 214
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
434-685 1.54e-27

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: 113.19  E-value: 1.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREllfnEVVIMRDY-QHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 kILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTPCYTAN 589
Cdd:cd06657  107 -IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEVPRRKSLVGTPY 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 590 FVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIgsgKFSLSGGYWN--SVSDTAKDLVSKMLH 667
Cdd:cd06657  182 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMI---RDNLPPKLKNlhKVSPSLKGFLDRLLV 255
                        250
                 ....*....|....*...
gi 768032625 668 VDPHQRLTAALVLRHPWI 685
Cdd:cd06657  256 RDPAQRATAAELLKHPFL 273
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
429-689 1.55e-27

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: 113.24  E-value: 1.55e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 429 EVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSkrDPTEE-------IEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd06618   18 ENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRS--GNKEEnkrilmdLDVVLKSHDCPYIVKCYGYFITDSDVFICMEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MkgGELLDKILR--QKFFSEREASAVLFTITKTVEYL-HAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL---R 575
Cdd:cd06618   96 M--STCLDKLLKriQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNIL-LDESGN---VKLCDFGISGRLvdsK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AENGLLMTPCYtanfVAPEVL---KRQGYDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARI-GSGKFSLSGGyw 651
Cdd:cd06618  170 AKTRSAGCAAY----MAPERIdppDNPKYDIRADVWSLGISLVELATGQFPYRN--CKTEFEVLTKIlNEEPPSLPPN-- 241
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWD 689
Cdd:cd06618  242 EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYE 279
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
426-687 1.82e-27

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: 112.90  E-value: 1.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdksKRDPTEEI--EIL-----LRYGQHPNIITLKDVYDDGK--YVY 496
Cdd:cd06621    1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTI---TTDPNPDVqkQILreleiNKSCASPYIVKYYGAFLDEQdsSIG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELlDKIL-----RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFA 571
Cdd:cd06621   78 IAMEYCEGGSL-DSIYkkvkkKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNIL-LTRKGQ---VKLCDFGVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLraENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANG-PDDTPEEILARIGSGKFSL--- 646
Cdd:cd06621  153 GEL--VNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFpPEGePPLGPIELLSYIVNMPNPElkd 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 647 ---SGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVH 687
Cdd:cd06621  231 epeNGIKW---SESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKA 271
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
66-270 1.85e-27

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: 112.43  E-value: 1.85e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd08228    2 ANFQIEKKIGRGQFSEVY--RATCLLDRKPVALKKVQIFEMMDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRL----SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd08228   80 VLELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSK 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 222 EKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd08228  160 TTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG 208
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-685 1.86e-27

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: 112.13  E-value: 1.86e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKI---IDKSKRDPTEEIEI-----LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVlkeISVGELQPDETVDAnreakLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKI----LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpesIRICDFGFAKQLR 575
Cdd:cd08222   82 EYCEGGDLDDKIseykKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-----IKVGDFGISRILM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKF-SLSGGYwnsv 654
Cdd:cd08222  157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDG---QNLLSVMYKIVEGETpSLPDKY---- 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 655 SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08222  230 SKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
74-321 2.30e-27

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: 112.81  E-value: 2.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVK-KISGsdarQLYAMKvlkkaTLKVRDRVRTKM---ERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd06657   28 IGEGSTGIVCIATvKSSG----KLVAVK-----KMDLRKQQRRELlfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFC 229
Cdd:cd06657   99 LEGGAL-TDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI---LKAKLGMPQFLSPEAQSLLRMLFKRN 306
Cdd:cd06657  178 GTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVRD 257
                        250       260
                 ....*....|....*....|.
gi 768032625 307 PANR------LVNPFLIGAGP 321
Cdd:cd06657  258 PAQRataaelLKHPFLAKAGP 278
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
455-643 2.74e-27

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: 111.48  E-value: 2.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYGqHPNIITLKDVYDDGKYVYVVTELMKGGELLDKiLRQK----------FFSE 519
Cdd:cd00192   27 AVKTLkedasESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYLVMEYMEGGDLLDF-LRKSrpvfpspepsTLSL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 520 REASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPC------YTAnfvaP 593
Cdd:cd00192  105 KDLLSFAIQIAKGMEYLASKKFVHRDLAARNCL-VGEDLV---VKISDFGLSRDIYDDDYYRKKTGgklpirWMA----P 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 594 EVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSGK 643
Cdd:cd00192  177 ESLKDGIFTSKSDVWSFGVLLWEIFTlGATPY---PGLSNEEVLEYLRKGY 224
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
444-685 2.97e-27

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 110.98  E-value: 2.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 444 RCIHKATNMEFAVKIIDKSkrDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTElMKGGELLDKILRQKFFSEREAS 523
Cdd:cd13976   11 RCVDIHTGEELVCKVVPVP--ECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFE-RDHGDLHSYVRSRKRLREPEAA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 AVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQG-YD 602
Cdd:cd13976   88 RLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERT--KLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEILNSGAtYS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 603 A-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGywnsVSDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd13976  166 GkAADVWSLGVILYTMLVGRYPFH---DSEPASLFAKIRRGQFAIPET----LSPRARCLIRSLLRREPSERLTAEDILL 238

                 ....
gi 768032625 682 HPWI 685
Cdd:cd13976  239 HPWL 242
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
63-321 3.51e-27

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: 112.12  E-value: 3.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  63 ADPSQ-FELLKVLGQGSFGKVFLVKKISgsdarqLYAMKVLKKATLKVRDRvRTKMERDILV--EVNHPFIVKLHYAFQT 139
Cdd:cd06655   15 GDPKKkYTRYEKIGQGASGTVFTAIDVA------TGQEVAIKQINLQKQPK-KELIINEILVmkELKNPNIVNFLDSFLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd06655   88 GDELFVVMEYLAGGSL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQIT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIlkAKLGMPQFLSPEAQSLL 299
Cdd:cd06655  167 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI--ATNGTPELQNPEKLSPI 244
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 300 RMLF----------KRNPANRLV-NPFLIGAGP 321
Cdd:cd06655  245 FRDFlnrclemdveKRGSAKELLqHPFLKLAKP 277
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-685 3.62e-27

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: 111.06  E-value: 3.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEreesrkEVAVLSKM-KHPNIVQYQESFEENGNLYIVMDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGnpeSIRICDFGFAKQLRAENG 579
Cdd:cd08218   81 CDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNI-FLTKDG---IIKLGDFGIARVLNSTVE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpddTPEEILARIGSGKF-SLSGGYwnsvSDTA 658
Cdd:cd08218  157 LARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAG---NMKNLVLKIIRGSYpPVPSRY----SYDL 229
                        250       260
                 ....*....|....*....|....*..
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08218  230 RSLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-680 3.72e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 111.22  E-value: 3.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlpkSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNpesIRICDFGFAKQLRAENGLL 581
Cdd:cd08219   82 GGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNI-FLTQNGK---VKLGDFGSARLLTSPGAYA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpddTPEEILARIGSGKFS-LSGGYwnsvSDTAKD 660
Cdd:cd08219  158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQGSYKpLPSHY----SYELRS 230
                        250       260
                 ....*....|....*....|
gi 768032625 661 LVSKMLHVDPHQRLTAALVL 680
Cdd:cd08219  231 LIKQMFKRNPRSRPSATTIL 250
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
428-685 3.75e-27

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: 110.98  E-value: 3.75e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTE-EIEILLRYgQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmTKEERQAALnEVKVLSML-HHPNIIEYYESFLEDKALMIVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpESIRICDFGFAKQLRAE-- 577
Cdd:cd08220   81 APGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKR---TVVKIGDFGISKILSSKsk 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 -NGLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF--ANGPddtpeEILARIGSGKFSLSGGYWnsv 654
Cdd:cd08220  158 aYTVVGTPCY----ISPELCEGKPYNQKSDIWALGCVLYELASLKRAFeaANLP-----ALVLKIMRGTFAPISDRY--- 225
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 655 SDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08220  226 SEELRHLILSMLHLDPNKRPTLSEIMAQPII 256
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
64-314 4.42e-27

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: 112.25  E-value: 4.42e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKatlkVRDRvRTKMERDILVEVN-HPFIVKLHYAFQTEGK 142
Cdd:cd14132   16 SQDDYEIIRKIGRGKYSEVFEGINI---GNNEKVVIKVLKP----VKKK-KIKREIKILQNLRgGPNIVKLLDVVKDPQS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LY--LILDFLRGGDLFTRLSKevmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH-IKLTDFGLSkesi 219
Cdd:cd14132   88 KTpsLIFEYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA---- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 D--HEKKAYSF-CGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLP-FQGKDRKEtmtMILK-AK-LGMPQF-- 290
Cdd:cd14132  161 EfyHPGQEYNVrVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYD---QLVKiAKvLGTDDLya 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 291 --------LSPEAQSLLRMlFKRNPANRLVNP 314
Cdd:cd14132  238 yldkygieLPPRLNDILGR-HSKKPWERFVNS 268
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
428-684 5.72e-27

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: 110.40  E-value: 5.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-------RDPTE---EIEILLR--YGQHPNIITLKDVYD--DGk 493
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewamiNGPVPvplEIALLLKasKPGVPGVIRLLDWYErpDG- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 YVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpeSIRICDFGFAKQ 573
Cdd:cd14005   81 FLLIMERPEPCQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTG---EVKLIDFGCGAL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 LRAENglLMTPCYTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILarigsgkfslsggYWN 652
Cdd:cd14005  158 LKDSV--YTDFDGTRVYSPPEWIRHGRYHGrPATVWSLGILLYDMLCGDIPFENDEQILRGNVL-------------FRP 222
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 653 SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14005  223 RLSKECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
434-696 6.33e-27

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: 113.20  E-value: 6.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE-------ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05618   28 IGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDwvqtekhVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGD 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05618  108 LMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVL-LDSEGH---IKLTDYGMCKEGLRPGDTTSTFCG 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-----ANGPDDTPEEILARIGSGKfslSGGYWNSVSDTAKDL 661
Cdd:cd05618  184 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgsSDNPDQNTEDYLFQVILEK---QIRIPRSLSVKAASV 260
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 662 VSKMLHVDPHQRLTA------ALVLRHPWI--VHWDQLPQYQL 696
Cdd:cd05618  261 LKSFLNKDPKERLGChpqtgfADIQGHPFFrnVDWDLMEQKQV 303
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
434-685 6.50e-27

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: 112.46  E-value: 6.50e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDK-------SKRDpTEEIEiLLRYGQHPNIITLKDVY-----DDGKYVYVVTEL 501
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIANafdnridAKRT-LREIK-LLRHLDHENVIAIKDIMppphrEAFNDVYIVYEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGelLDKILRQ-KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd07858   91 MDTD--LHQIIRSsQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLL-LNANCD---LKICDFGLARTTSEKGDF 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFA---------------NGPDDTPEEILARIGSGKF 644
Cdd:cd07858  165 MTEYVVTRWYRAPELlLNCSEYTTAIDVWSVGCIFAELLGRKPLFPgkdyvhqlklitellGSPSEEDLGFIRNEKARRY 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 645 SLSGGY---------WNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07858  245 IRSLPYtprqsfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
427-685 7.15e-27

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: 110.22  E-value: 7.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-----KSKRDPTEEIEILLRYGQHPNIITLKDVYDDGK-YVYVVTE 500
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNlknasKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAEN 578
Cdd:cd08223   81 FCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLT----KSNIIKVGDLGIARVLESSS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDdtPEEILARIGSGKF-SLSGGYwnsvSDT 657
Cdd:cd08223  157 DMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAF-NAKD--MNSLVYKILEGKLpPMPKQY----SPE 229
                        250       260
                 ....*....|....*....|....*...
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd08223  230 LGELIKAMLHQDPEKRPSVKRILRQPYI 257
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
66-306 8.41e-27

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: 111.89  E-value: 8.41e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsgsDARQLYAMKVLKKATlKVRDRvrTKMERDILVEVNH------PFIVKLHYAFQT 139
Cdd:cd14134   12 NRYKILRLLGEGTFGKVLECWDR---KRKRYVAVKIIRNVE-KYREA--AKIEIDVLETLAEkdpngkSHCVQLRDWFDY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLrGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL----------DEEGH- 206
Cdd:cd14134   86 RGHMCIVFELL-GPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynPKKKRq 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 207 --------IKLTDFGLSkeSIDHEKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT 278
Cdd:cd14134  165 irvpkstdIKLIDFGSA--TFDDEYHS-SIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLA 241
                        250       260
                 ....*....|....*....|....*....
gi 768032625 279 MILKAkLG-MPQFLSPEAQSLLRMLFKRN 306
Cdd:cd14134  242 MMERI-LGpLPKRMIRRAKKGAKYFYFYH 269
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
56-321 8.74e-27

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: 111.35  E-value: 8.74e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  56 VKEGHEKADPSQFEllkVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVrdrvrtkMERDILV--EVNHPFIVKL 133
Cdd:cd06656   12 VSVGDPKKKYTRFE---KIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEL-------IINEILVmrENKNPNIVNY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 HYAFQTEGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG 213
Cdd:cd06656   82 LDSYLVGDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIlkAKLGMPQFLSP 293
Cdd:cd06656  161 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLI--ATNGTPELQNP 238
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 294 EAQSLLRMLF----------KRNPANRLV-NPFLIGAGP 321
Cdd:cd06656  239 ERLSAVFRDFlnrclemdvdRRGSAKELLqHPFLKLAKP 277
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
428-684 1.31e-26

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: 110.20  E-value: 1.31e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEiLLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMvkkiamREIK-MLKQLRHENLVNLIEVFRRKKRWYLVFEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGgELLDKIlrQKF---FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAEN 578
Cdd:cd07846   82 VDH-TVLDDL--EKYpngLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL-VSQSG---VVKLCDFGFARTLAAPG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWN----- 652
Cdd:cd07846  155 EVYTDYVATRWYRAPELLvGDTKYGKAVDVWAVGCLVTEMLTGEPLF---PGDSDIDQLYHIIKCLGNLIPRHQElfqkn 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 653 ----------------------SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07846  232 plfagvrlpevkeveplerrypKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
428-683 1.38e-26

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: 109.40  E-value: 1.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE------EIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd13997    2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKEraralrEVEAHAALGQHPNIVRYYSSWEEGGHLYIQMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGEL---LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNpesIRICDFGFAKQLRA-- 576
Cdd:cd13997   82 CENGSLqdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNI-FISNKGT---CKIGDFGLATRLETsg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 --ENGllmtpcyTANFVAPEVLK-RQGYDAACDIWSLGVLLYTMLTGYTPFANGPDdtpeeiLARIGSGKFSLSGGywNS 653
Cdd:cd13997  158 dvEEG-------DSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLPRNGQQ------WQQLRQGKLPLPPG--LV 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd13997  223 LSQELTRLLKVMLDPDPTRRPTADQLLAHD 252
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
441-684 1.42e-26

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: 110.14  E-value: 1.42e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 441 VCKrCIHKATNMEFAVKIIDKS--KRDPTE-----EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKI-- 511
Cdd:cd05605   16 VCA-CQVRATGKMYACKKLEKKriKKRKGEamalnEKQILEKV-NSRFVVSLAYAYETKDALCLVLTIMNGGDLKFHIyn 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 512 LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaENGLLMTPCYTANFV 591
Cdd:cd05605   94 MGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENIL-LDDHGH---VRISDLGLAVEIP-EGETIRGRVGTVGYM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 592 APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKMLHVDP 670
Cdd:cd05605  169 APEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrARKEKVKREEVDRRVKEDQEEYS----EKFSEEAKSICSQLLQKDP 244
                        250
                 ....*....|....*....
gi 768032625 671 HQRL-----TAALVLRHPW 684
Cdd:cd05605  245 KTRLgcrgeGAEDVKSHPF 263
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
415-688 1.63e-26

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: 111.29  E-value: 1.63e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 415 QQLHRNSIQFTDGYEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDKS------KRDPTEEIEiLLRYGQHPNIITLKD 487
Cdd:cd07878    4 QELNKTVWEVPERYQNLTPVGSGAYgSVCS-AYDTRLRQKVAVKKLSRPfqslihARRTYRELR-LLKHMKHENVIGLLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 488 VY------DDGKYVYVVTELMkgGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESGnpe 561
Cdd:cd07878   82 VFtpatsiENFNEVYLVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSN-VAVNEDC--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 562 SIRICDFGFAKQLRAE-NGLLMTPCYTanfvAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPD---------- 629
Cdd:cd07878  156 ELRILDFGLARQADDEmTGYVATRWYR----APEImLNWMHYNQTVDIWSVGCIMAELLKGKALFP-GNDyidqlkrime 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 630 --DTPE-EILARIGSG---KFSLS---------GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHW 688
Cdd:cd07878  231 vvGTPSpEVLKKISSEharKYIQSlphmpqqdlKKIFRGANPLAIDLLEKMLVLDSDKRISASEALAHPYFSQY 304
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
67-310 1.88e-26

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: 109.17  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGsdaRQLYAMKVLKKATL----KVRDRVRTKMERDILVEV----NHPFIVKLHYAFQ 138
Cdd:cd14101    1 QYTMGNLLGKGGFGTVYAGHRISD---GLQVAIKQISRNRVqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDF-LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EEGHIKLTDFGlsK 216
Cdd:cd14101   78 IPEGFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFG--S 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ESIDHEKKAYSFCGTVEYMAPEVVNRRG-HTQSADWWSFGVLMFEMLTGTLPFqgkdrkETMTMILKAKLGMPQFLSPEA 295
Cdd:cd14101  156 GATLKDSMYTDFDGTRVYSPPEWILYHQyHALPATVWSLGILLYDMVCGDIPF------ERDTDILKAKPSFNKRVSNDC 229
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd14101  230 RSLIRSCLAYNPSDR 244
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
61-321 2.14e-26

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: 109.74  E-value: 2.14e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  61 EKADPSQF--ELLKVlGQGSFGKVFLvkkisgsdARQLYAMKVLKKATLKVRDRVRTKM---ERDILVEVNHPFIVKLHY 135
Cdd:cd06658   16 SPGDPREYldSFIKI-GEGSTGIVCI--------ATEKHTGKQVAVKKMDLRKQQRRELlfnEVVIMRDYHHENVVDMYN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AFQTEGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd06658   87 SYLVGDELWVVMEFLEGGAL-TDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 KESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI---LKAKLGMPQFLS 292
Cdd:cd06658  166 AQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIrdnLPPRVKDSHKVS 245
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 293 PEAQSLLRMLFKRNPANR------LVNPFLIGAGP 321
Cdd:cd06658  246 SVLRGFLDLMLVREPSQRataqelLQHPFLKLAGP 280
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
65-305 2.35e-26

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: 110.85  E-value: 2.35e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVflvkkISGSDAR--QLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd07851   14 PDRYQNLSPVGSGAYGQV-----CSAFDTKtgRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 L------YLILDFLrGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07851   89 LedfqdvYLVTHLM-GADL-NNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 eSIDHEKKAYsfCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPQ--FL-- 291
Cdd:cd07851  167 -HTDDEMTGY--VATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNL-VGTPDeeLLkk 242
                        250
                 ....*....|....*.
gi 768032625 292 --SPEAQSLLRMLFKR 305
Cdd:cd07851  243 isSESARNYIQSLPQM 258
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-310 2.46e-26

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: 110.53  E-value: 2.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKkatLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd06650    7 FEKISELGAGNGGVVF---KVSHKPSGLVMARKLIH---LEIKPAIRNQIIRElqVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEdvkfYLAELALA----LDHLHSL-GIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06650   81 CMEHMDGGSLDQVLKKAGRIPEQ----ILGKVSIAvikgLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 heKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLR 300
Cdd:cd06650  157 --SMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPRTPGR 234
                        250
                 ....*....|
gi 768032625 301 MLFKRNPANR 310
Cdd:cd06650  235 PLSSYGMDSR 244
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
74-310 2.49e-26

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: 108.51  E-value: 2.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGkvfLVKKISGSDARQLYAMKVLKKatlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14115    1 IGRGRFS---IVKKCLHKATRKDVAVKFVSK---KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD---EEGHIKLTDFGLSKESIDHeKKAYSFCG 230
Cdd:cd14115   75 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQISGH-RHVHHLLG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQ--F--LSPEAQSLLRMLFKRN 306
Cdd:cd14115  154 NPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDeyFgdVSQAARDFINVILQED 233

                 ....
gi 768032625 307 PANR 310
Cdd:cd14115  234 PRRR 237
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
424-681 2.56e-26

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: 108.92  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI----LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd13996    4 YLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASEKVLrevkALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGEL---LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpesIRICDFGFAK---- 572
Cdd:cd13996   84 ELCEGGTLrdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLQ---VKIGDFGLATsign 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGLLMTP----------CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLtgyTPFangpdDTPEE---ILARI 639
Cdd:cd13996  161 QKRELNNLNNNNngntsnnsvgIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPF-----KTAMErstILTDL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 640 GSGKFSLSGGYWNsvsDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd13996  233 RNGILPESFKAKH---PKEADLIQSLLSKNPEERPSAEQLLR 271
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
72-311 2.67e-26

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: 109.74  E-value: 2.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVF-LVKKISGSDarqlYAMKVLKKATlKVRDRVRTKMERDilvevNHPFIVKL----HYAFQTEGKLYLI 146
Cdd:cd14170    8 QVLGLGINGKVLqIFNKRTQEK----FALKMLQDCP-KARREVELHWRAS-----QCPHIVRIvdvyENLYAGRKCLLIV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE---GHIKLTDFGLSKESIDH 221
Cdd:cd14170   78 MECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgKDRKETMTMILKAKLGMPQF---------LS 292
Cdd:cd14170  158 NSLT-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKTRIRMGQYefpnpewseVS 235
                        250
                 ....*....|....*....
gi 768032625 293 PEAQSLLRMLFKRNPANRL 311
Cdd:cd14170  236 EEVKMLIRNLLKTEPTQRM 254
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
73-272 3.01e-26

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 108.63  E-value: 3.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFlvkkiSGSDARQLYAMKVLK----KATLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd14061    1 VIGVGGFGKVY-----RGIWRGEEVAVKAARqdpdEDISVTLENVRQ--EARLFWMLRHPNIIALRGVCLQPPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSK-----EVMFTeedvkfYLAELALALDHLHSLG---IIYRDLKPENILLDE--EGH------IKLTDF 212
Cdd:cd14061   74 YARGGALNRVLAGrkippHVLVD------WAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaiENEdlenktLKITDF 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 213 GLSKESidHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKD 272
Cdd:cd14061  148 GLAREW--HKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGID 205
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
434-696 3.05e-26

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: 110.94  E-value: 3.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI------EILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05593   23 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 587
Cdd:cd05593  103 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILArIGSGKFSlsggywNSVSDTAKDLVSKMLH 667
Cdd:cd05593  179 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFP------RTLSADAKSLLSGLLI 251
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 668 VDPHQRL-----TAALVLRHPWI--VHWDQLPQYQL 696
Cdd:cd05593  252 KDPNKRLgggpdDAKEIMRHSFFtgVNWQDVYDKKL 287
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
67-288 3.65e-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: 109.56  E-value: 3.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkisgsD--ARQLYAMKVLKKatlkvrdrvRTKMERDILVEV--------NHP----FIVK 132
Cdd:cd14210   14 RYEVLSVLGKGSFGQVVKCL-----DhkTGQLVAIKIIRN---------KKRFHQQALVEVkilkhlndNDPddkhNIVR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 133 LHYAFQTEGKLYLILDFLrGGDL--------FTRLSKEVmfteedVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd14210   80 YKDSFIFRGHLCIVFELL-SINLyellksnnFQGLSLSL------IRKFAKQILQALQFLHKLNIIHCDLKPENILLKQP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GH--IKLTDFGLSkeSIDHEKKaYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK 282
Cdd:cd14210  153 SKssIKVIDFGSS--CFEGEKV-YTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIME 229

                 ....*.
gi 768032625 283 AkLGMP 288
Cdd:cd14210  230 V-LGVP 234
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
64-268 3.70e-26

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: 108.99  E-value: 3.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKV--LKKATLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd06642    1 DPEElFTKLERIGKGSFGEVY---KGIDNRTKEVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYITRYYGSYLKG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTRLsKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd06642   75 TKLWIIMEYLGGGSALDLL-KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd06642  154 TQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
428-684 4.08e-26

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 108.81  E-value: 4.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVK-IIDKSKRD--PTEEI-EI-LLRYGQHPNIITLKDVY------DDGKYVY 496
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkIRMENEKEgfPITAIrEIkLLQKLDHPNVVRLKEIVtskgsaKYKGSIY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGelLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL 574
Cdd:cd07840   81 MVFEYMDHD--LTGLLDNPEvkFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNIL-INNDGV---LKLADFGLARPY 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENgllmTPCYTANFV-----APEVL---KRqgYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSL 646
Cdd:cd07840  155 TKEN----NADYTNRVItlwyrPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIF---QGKTELEQLEKI----FEL 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 647 SGG----YWNSVSD---------------------------TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07840  222 CGSpteeNWPGVSDlpwfenlkpkkpykrrlrevfknvidpSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
67-288 4.20e-26

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: 108.31  E-value: 4.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLkvrdRVRTKMERDILVEVN-HPFIVKLHYAFQTEGKLYL 145
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTG---EEVAIKIEKKDSK----HPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLrgG----DLFTRLSKevMFTEEDVkFYLAELALA-LDHLHSLGIIYRDLKPENILLDEEGHIK---LTDFGLSKE 217
Cdd:cd14016   74 VMDLL--GpsleDLFNKCGR--KFSLKTV-LMLADQMISrLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SID-----H--EKKAYSFCGTVEYMApevVNR-RGHTQSA--DWWSFG-VLMFeMLTGTLPFQG---KDRKETMTMILKA 283
Cdd:cd14016  149 YRDprtgkHipYREGKSLTGTARYAS---INAhLGIEQSRrdDLESLGyVLIY-FLKGSLPWQGlkaQSKKEKYEKIGEK 224

                 ....*
gi 768032625 284 KLGMP 288
Cdd:cd14016  225 KMNTS 229
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
65-329 4.26e-26

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: 110.13  E-value: 4.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVflvkkISGSDARQLY--AMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd07877   16 PERYQNLSPVGSGAYGSV-----CAAFDTKTGLrvAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 L------YLILDfLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07877   91 LeefndvYLVTH-LMGADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ESiDHEKKAYsfCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP-----QF 290
Cdd:cd07877  169 HT-DDEMTGY--VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRL-VGTPgaellKK 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 291 LSPEA-----QSLLRMLfKRNPANrlvnpFLIGAGPDGVEEIKR 329
Cdd:cd07877  245 ISSESarnyiQSLTQMP-KMNFAN-----VFIGANPLAVDLLEK 282
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
434-726 4.62e-26

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: 109.70  E-value: 4.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05616    8 LGKGSFGKVMLAERKGTDELYAVKILKKDvviQDDDVEctmvEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05616   88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVM-LDSEGH---IKIADFGMCKENIWDGVTTKTFCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGKFSlsggYWNSVSDTAKDLVSKML 666
Cdd:cd05616  164 TPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF-EGEDE--DELFQSIMEHNVA----YPKSMSKEAVAICKGLM 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 667 HVDPHQRLTAAL-----VLRHPWI--VHWDQLPQYQLNRQDAPHlVKGAMAATYSALNRNQSPVLEP 726
Cdd:cd05616  237 TKHPGKRLGCGPegerdIKEHAFFryIDWEKLERKEIQPPYKPK-ACGRNAENFDRFFTRHPPVLTP 302
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
434-683 4.69e-26

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: 108.29  E-value: 4.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd06630    8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEqeevveaireEIRMMARL-NHPNIVRMLGATQHKSHFNIFVEWMA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpESIRICDFGFAKQLRAEN----- 578
Cdd:cd06630   87 GGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLL-VDSTG--QRLRIADFGAAARLASKGtgage 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 --GLLMTpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSggYWNSVSD 656
Cdd:cd06630  164 fqGQLLG---TIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPP--IPEHLSP 238
                        250       260
                 ....*....|....*....|....*..
gi 768032625 657 TAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd06630  239 GLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
56-299 4.71e-26

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: 109.04  E-value: 4.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  56 VKEGHEKADPSQFEllkVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVrdrvrtkMERDILV--EVNHPFIVKL 133
Cdd:cd06654   13 VSVGDPKKKYTRFE---KIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEL-------IINEILVmrENKNPNIVNY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 HYAFQTEGKLYLILDFLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG 213
Cdd:cd06654   83 LDSYLVGDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMIlkAKLGMPQFLSP 293
Cdd:cd06654  162 FCAQITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLI--ATNGTPELQNP 239

                 ....*.
gi 768032625 294 EAQSLL 299
Cdd:cd06654  240 EKLSAI 245
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
66-351 6.12e-26

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 109.76  E-value: 6.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVF-LVKKISGsdarQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL- 143
Cdd:cd07855    5 DRYEPIETIGSGAYGVVCsAIDTKSG----QKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYa 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 -----YLILDfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG----L 214
Cdd:cd07855   81 dfkdvYVVLD-LMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGmargL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP--QFL 291
Cdd:cd07855  160 CTSPEEHKYFMTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTV-LGTPsqAVI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 292 SPEAQSLLRMLFKrNPANRLVNPF---LIGAGPDG-----------------VEEIKRHSFFSTidwnklYRREI----- 346
Cdd:cd07855  239 NAIGADRVRRYIQ-NLPNKQPVPWetlYPKADQQAldllsqmlrfdpseritVAEALQHPFLAK------YHDPDdepdc 311

                 ....*
gi 768032625 347 HPPFK 351
Cdd:cd07855  312 APPFD 316
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
73-332 6.36e-26

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: 107.91  E-value: 6.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFLVKKISGsdarQLYAmkvLKKATLKVRDRVRTKM-------ERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd06631    8 VLGKGAYGTVYCGLTSTG----QLIA---VKQVELDTSDKEKAEKeyeklqeEVDLLKTLKHVNIVGYLGTCLEDNVVSI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE------SI 219
Cdd:cd06631   81 FMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRlcinlsSG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQ 296
Cdd:cd06631  161 SQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLpdkFSPEAR 240
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 297 SLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSF 332
Cdd:cd06631  241 DFVHACLTRDQDERP-----------SAEQLLKHPF 265
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
426-686 6.60e-26

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: 108.40  E-value: 6.60e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII----DKSK-RDPTEEIEILLRyGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd06622    1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrlelDESKfNQIIMELDILHK-AVSPYIVDFYGAFFIEGAVYMCME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELlDKILRQKFFSEREASAVLFTITKTV----EYLHAQ-GVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLR 575
Cdd:cd06622   80 YMDAGSL-DKLYAGGVATEGIPEDVLRRITYAVvkglKFLKEEhNIIHRDVKPTNVL-VNGNG---QVKLCDFGVSGNLV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AEngLLMTPCYTANFVAPEVLKRQG------YDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGG 649
Cdd:cd06622  155 AS--LAKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPY---PPETYANIFAQLSAIVDGDPPT 229
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 650 YWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd06622  230 LPSGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
74-268 8.02e-26

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


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 108.08  E-value: 8.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgsdaRQLYAMKVLK--KATLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKLYLI 146
Cdd:cd14039    1 LGTGGFGNVCLYQN------QETGEKIAIKscRLELSVKNKDRWCHEIQIMKKLNHPNVVKAcdvpeEMNFLVNDVPLLA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKE---VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG----HiKLTDFGLSKEsI 219
Cdd:cd14039   75 MEYCSGGDLRKLLNKPencCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivH-KIIDLGYAKD-L 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14039  153 DQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
73-316 9.27e-26

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: 107.49  E-value: 9.27e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFlvkkiSGSDARQLYAMKVlKKATLKVRDRVRTKMERDIL-VEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd06624   15 VLGKGTFGVVY-----AARDLSTQVRIAI-KEIPERDSREVQPLHEEIALhSRLSHKNIVQYLGSVSEDGFFKIFMEQVP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRL-SK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE-EGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd06624   89 GGSLSALLrSKwgPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTSKRLAGINPCTET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNR--RGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETmTMIlkaKLGM-------PQFLSPEAQSL 298
Cdd:cd06624  169 FTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQA-AMF---KVGMfkihpeiPESLSEEAKSF 244
                        250       260
                 ....*....|....*....|....
gi 768032625 299 LRMLFKRNPANR------LVNPFL 316
Cdd:cd06624  245 ILRCFEPDPDKRatasdlLQDPFL 268
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
444-685 1.07e-25

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 106.50  E-value: 1.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 444 RCIHKATNMEFAVKIIdkSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTElMKGGELLDKILRQKFFSEREAs 523
Cdd:cd14024   11 RAEHYQTEKEYTCKVL--SLRSYQECLAPYDRLGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLSEDEA- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 AVLFT-ITKTVEYLHAQGVVHRDLKpsnilyvdesgnpesirICDFGFAKQLRAENGLL-MTPCYTAN------------ 589
Cdd:cd14024   87 RGLFTqMARAVAHCHQHGVILRDLK-----------------LRRFVFTDELRTKLVLVnLEDSCPLNgdddsltdkhgc 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 590 --FVAPEVLK-RQGYDA-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGywnsVSDTAKDLVSKM 665
Cdd:cd14024  150 paYVGPEILSsRRSYSGkAADVWSLGVCLYTMLLGRYPFQ---DTEPAALFAKIRRGAFSLPAW----LSPGARCLVSCM 222
                        250       260
                 ....*....|....*....|
gi 768032625 666 LHVDPHQRLTAALVLRHPWI 685
Cdd:cd14024  223 LRRSPAERLKASEILLHPWL 242
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
68-310 1.14e-25

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: 107.79  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKAtlKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd07833    3 YEVLGVVGEGAYGVVL---KCRNKATGEIVAIKKFKES--EDDEDVKKTALREVkvLRQLRHENIVNLKEAFRRKGRLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGG--DLFTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd07833   78 VFEYVERTllELLEASPGGL--PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARPA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAY-SFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMpqfLSPEAQSllrm 301
Cdd:cd07833  156 SPLtDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKC-LGP---LPPSHQE---- 227

                 ....*....
gi 768032625 302 LFKRNPANR 310
Cdd:cd07833  228 LFSSNPRFA 236
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
434-696 1.16e-25

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: 108.86  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05619   13 LGKGSFGKVFLAELKGTNQFFAIKALKKDvvlMDDDVEctmvEKRVLSLAWEHPFLTHLFCTFQTKENLFFVMEYLNGGD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05619   93 LMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNIL-LDKDGH---IKIADFGMCKENMLGDAKTSTFCG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGkfslSGGYWNSVSDTAKDLVSKML 666
Cdd:cd05619  169 TPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPF-HGQDE--EELFQSIRMD----NPFYPRWLEKEAKDILVKLF 241
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 667 HVDPHQRLTAALVLR-HPWIVH--WDQLPQYQL 696
Cdd:cd05619  242 VREPERRLGVRGDIRqHPFFREinWEALEEREI 274
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
428-684 1.19e-25

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: 107.36  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-----EIEILLRYGQHPNIITLKDVYDDGKY--VYVVTE 500
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQvnnlrEIQALRRLSPHPNILRLIEVLFDRKTgrLALVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGG--ELLDKilRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesgnpESIRICDFGFAKqlraen 578
Cdd:cd07831   81 LMDMNlyELIKG--RKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-----DILKLADFGSCR------ 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTAN-----FVAPEVLKRQG-YDAACDIWSLGVLLYTMLTGYTPF--ANGPDD---------TP-EEILARIG 640
Cdd:cd07831  148 GIYSKPPYTEYistrwYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLFPLFpgTNELDQiakihdvlgTPdAEVLKKFR 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 641 SG-----KFSLSGGYW-----NSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07831  228 KSrhmnyNFPSKKGTGlrkllPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
67-316 1.23e-25

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: 107.74  E-value: 1.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVF--LVKKISGSDARQLYAMKVLKKATLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05045    1 NLVLGKTLGEGEFGKVVkaTAFRLKGRAGYTTVAVKMLKENASSSELRDLLS-EFNLLKQVNHPHVIKLYGACSQDGPLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDL--FTRLSKEV----------------------MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL 200
Cdd:cd05045   80 LIVEYAKYGSLrsFLRESRKVgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 201 LDEEGHIKLTDFGLSKESIDHEKKAYSFCG--TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKdRKETM 277
Cdd:cd05045  160 VAEGRKMKISDFGLSRDVYEEDSYVKRSKGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI-APERL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 278 TMILKAKLGM--PQFLSPEAQSLLRMLFKRNPANRLVNPFL 316
Cdd:cd05045  239 FNLLKTGYRMerPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
61-288 1.59e-25

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: 106.67  E-value: 1.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  61 EKADPSQFELLKVLGQGSFGKVFlvKKISGSDARQLYAMKVLKKATL-KVRDRVRtkMERDILVEVNHPFIVKLHYAFQT 139
Cdd:cd14145    1 LEIDFSELVLEEIIGIGGFGKVY--RAIWIGDEVAVKAARHDPDEDIsQTIENVR--QEAKLFAMLKHPNIIALRGVCLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKfYLAELALALDHLHSLGI---IYRDLKPENILLDEEGH--------IK 208
Cdd:cd14145   77 EPNLCLVMEFARGGPLNRVLSGKRIPPDILVN-WAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKVEngdlsnkiLK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSKESidHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP 288
Cdd:cd14145  156 ITDFGLAREW--HRTTKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP 233
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
426-683 1.63e-25

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: 107.63  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRdpteEIEILLRYGQHPNIITLKDV--YDDGKYVYVV 498
Cdd:cd14132   18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkpvkkKKIKR----EIKILQNLRGGPNIVKLLDVvkDPQSKTPSLI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELldKILRQKFfSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPE--SIRICDFGFAKqlra 576
Cdd:cd14132   94 FEYVNNTDF--KTLYPTL-TDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI-----DHEkrKLRLIDWGLAE---- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 engllmtpCYTAN-----------FVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDtpEEILARIGS--- 641
Cdd:cd14132  162 --------FYHPGqeynvrvasryYKGPELLvDYQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDN--YDQLVKIAKvlg 231
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 642 --------GKFSLS---------GGY----WNS---------VSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14132  232 tddlyaylDKYGIElpprlndilGRHskkpWERfvnsenqhlVTPEALDLLDKLLRYDHQERITAKEAMQHP 303
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
68-333 1.63e-25

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: 106.15  E-value: 1.63e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVN-HPFIVKLHYAFQTEGKLYLI 146
Cdd:cd14019    3 YRIIEKIGEGTFSSVYKAEDKLHDLYDRNKGRLVALKHIYPTSSPSRILNELECLERLGgSNNVSGLITAFRNEDQVVAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKevmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EEGHIKLTDFGLSK-ESIDHEKK 224
Cdd:cd14019   83 LPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQrEEDRPEQR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AySFCGTVEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGTLP-FQGKDRKETMTMIlkaklgMPQFLSPEAQSLLRML 302
Cdd:cd14019  160 A-PRAGTRGFRAPEVLFKCPHqTTAIDIWSAGVILLSILSGRFPfFFSSDDIDALAEI------ATIFGSDEAYDLLDKL 232
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 303 FKRNPANRlvnpflIGAgpdgvEEIKRHSFF 333
Cdd:cd14019  233 LELDPSKR------ITA-----EEALKHPFF 252
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
415-684 1.80e-25

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 108.45  E-value: 1.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 415 QQLHRNSIQFTDGYEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDK-------SKRDPTEEIeiLLRYGQHPNIITLK 486
Cdd:cd07879    4 EEVNKTVWELPERYTSLKQVGSGAYgSVCS-AIDKRTGEKVAIKKLSRpfqseifAKRAYRELT--LLKHMQHENVIGLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 487 DV------YDDGKYVYVVTELMKGGelLDKILRQKFfSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESGnp 560
Cdd:cd07879   81 DVftsavsGDEFQDFYLVMPYMQTD--LQKIMGHPL-SEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN-LAVNEDC-- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 561 eSIRICDFGFAKQLRAE-NGLLMTPCYTanfvAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFAN------------ 626
Cdd:cd07879  155 -ELKILDFGLARHADAEmTGYVVTRWYR----APEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGkdyldqltqilk 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 627 -----GPDDTPE----------EILARIGSGKFSLsggYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07879  230 vtgvpGPEFVQKledkaaksyiKSLPKYPRKDFST---LFPKASPQAVDLLEKMLELDVDKRLTATEALEHPY 299
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
72-310 1.90e-25

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: 105.86  E-value: 1.90e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFlvkKISGSDARQLyAMKVLKKaTLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05085    2 ELLGKGNFGEVY---KGTLKDKTPV-AVKTCKE-DLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDL--FTRLSKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhekKAYSFC 229
Cdd:cd05085   77 GGDFlsFLRKKKDELKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDD---GVYSSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 G----TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRMLF 303
Cdd:cd05085  153 GlkqiPIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCW 232

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd05085  233 DYNPENR 239
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
434-704 1.91e-25

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: 107.89  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE-------ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDwvqtekhVFETASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05588   83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVL-LDSEGH---IKLTDYGMCKEGLRPGDTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-----ANGPDDTPEEIL--------ARIGsgkfslsggywNS 653
Cdd:cd05588  159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdivgsSDNPDQNTEDYLfqvilekpIRIP-----------RS 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 654 VSDTAKDLVSKMLHVDPHQRLTAAL------VLRHPWI--VHWDQLPQYQLNRQDAPHL 704
Cdd:cd05588  228 LSVKAASVLKGFLNKNPAERLGCHPqtgfadIQSHPFFrtIDWEQLEQKQVTPPYKPRI 286
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
65-307 2.28e-25

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: 106.26  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVFLVkkISGSDARQLYAMKVLKKATLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQ--TE 140
Cdd:cd06653    1 PVNWRLGKLLGRGAFGEVYLC--YDADTGRELAVKQVPFDPDSQETSKEVNALECEIqlLKNLRHDRIVQYYGCLRdpEE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ES 218
Cdd:cd06653   79 KKLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriQT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHEKKAY-SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgkdRKETMTMILK-----AKLGMPQFLS 292
Cdd:cd06653  159 ICMSGTGIkSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKiatqpTKPQLPDGVS 235
                        250
                 ....*....|....*...
gi 768032625 293 PEAQSLLRMLF---KRNP 307
Cdd:cd06653  236 DACRDFLRQIFveeKRRP 253
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
434-724 2.28e-25

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: 107.34  E-value: 2.28e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVK-------IIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05620    3 LGKGSFGKVLLAELKGKGEYFAVKalkkdvvLIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05620   83 LMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVM-LDRDGH---IKIADFGMCKENVFGDNRASTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGkfslSGGYWNSVSDTAKDLVSKML 666
Cdd:cd05620  159 TPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPF-HGDDE--DELFESIRVD----TPHYPRWITKESKDILEKLF 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 667 HVDPHQRLTAALVLR-HPWI--VHWDQLPQYQLnrqDAPHLVKGAMAATYSALNR---NQSPVL 724
Cdd:cd05620  232 ERDPTRRLGVVGNIRgHPFFktINWTALEKREL---DPPFKPKVKSPSDYSNFDReflSEKPRL 292
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
65-288 2.54e-25

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 107.78  E-value: 2.54e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVFL-----------VKKISGSDaRQLYAMkvlkkatlkvrdrvRTKMERDILVEVNHPFIVKL 133
Cdd:cd07849    4 GPRYQNLSYIGEGAYGMVCSavhkptgqkvaIKKISPFE-HQTYCL--------------RTLREIKILLRFKHENIIGI 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 H-----YAFQTEGKLYLILDFLRGgDLFtRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIK 208
Cdd:cd07849   69 LdiqrpPTFESFKDVYIVQELMET-DLY-KLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSK---ESIDHEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAk 284
Cdd:cd07849  147 ICDFGLARiadPEHDHTGFLTEYVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGI- 225

                 ....
gi 768032625 285 LGMP 288
Cdd:cd07849  226 LGTP 229
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
415-684 2.68e-25

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 107.73  E-value: 2.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 415 QQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK-------SKRdPTEEIEiLLRYGQHPNIITLKD 487
Cdd:cd07880    4 QEVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfqselfAKR-AYRELR-LLKHMKHENVIGLLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 488 VY------DDGKYVYVVTELMkgGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNiLYVDESGnpe 561
Cdd:cd07880   82 VFtpdlslDRFHDFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGN-LAVNEDC--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 562 SIRICDFGFAKQLRAE-NGLLMTPCYTanfvAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPD--DTPEEILA 637
Cdd:cd07880  156 ELKILDFGLARQTDSEmTGYVVTRWYR----APEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLF-KGHDhlDQLMEIMK 230
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 638 RIG--SGKFSLS---------------------GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07880  231 VTGtpSKEFVQKlqsedaknyvkklprfrkkdfRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPY 300
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
66-270 2.86e-25

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 106.65  E-value: 2.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVR-DRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd08229   24 ANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLMDAKARaDCIK---EIDLLKQLNHPNVIKYYASFIEDNELN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRL----SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd08229  101 IVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSS 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd08229  181 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYG 230
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
432-685 3.00e-25

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: 105.39  E-value: 3.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFA---VKIIDKSKRDPT---EEIEILLRYgQHPNIITLKDVYDDGKYVYVV--TELMK 503
Cdd:cd13983    7 EVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERQrfkQEIEILKSL-KHPNIIKFYDSWESKSKKEVIfiTELMT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNIlYVDesGNPESIRICDFGFAKQLRAE--NG 579
Cdd:cd13983   86 SGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNI-FIN--GNTGEVKIGDLGLATLLRQSfaKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPcytaNFVAPEVLKrQGYDAACDIWSLGVLLYTMLTGYTPFANGpdDTPEEILARIGSGKF--SLSggywNSVSDT 657
Cdd:cd13983  163 VIGTP----EFMAPEMYE-EHYDEKVDIYAFGMCLLEMATGEYPYSEC--TNAAQIYKKVTSGIKpeSLS----KVKDPE 231
                        250       260
                 ....*....|....*....|....*...
gi 768032625 658 AKDLVSKMLhVDPHQRLTAALVLRHPWI 685
Cdd:cd13983  232 LKDFIEKCL-KPPDERPSARELLEHPFF 258
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
74-282 3.01e-25

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: 105.82  E-value: 3.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISGSDarqlYAMKVLK-KATLKVRDRVRTKMErdILVEVNHPFIVKLhYAFQTEGKLY-LILDFLR 151
Cdd:cd14066    1 IGSGGFGTVYKGVLENGTV----VAVKRLNeMNCAASKKEFLTELE--MLGRLRHPNLVRL-LGYCLESDEKlLVYEYMP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRL----SKEVMFTEEDVKFYLaELALALDHLHS---LGIIYRDLKPENILLDEEGHIKLTDFGLSKEsIDHEKK 224
Cdd:cd14066   74 NGSLEDRLhchkGSPPLPWPQRLKIAK-GIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARL-IPPSES 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 225 AYS---FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgKDRKETMTMILK 282
Cdd:cd14066  152 VSKtsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVD-ENRENASRKDLV 211
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
428-674 3.23e-25

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: 107.81  E-value: 3.23e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI------EILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd05594   27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd05594  107 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IKITDFGLCKEGIKDGAT 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILArIGSGKFSlsggywNSVSDTAKD 660
Cdd:cd05594  183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRFP------RTLSPEAKS 255
                        250
                 ....*....|....
gi 768032625 661 LVSKMLHVDPHQRL 674
Cdd:cd05594  256 LLSGLLKKDPKQRL 269
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
424-684 3.33e-25

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: 107.27  E-value: 3.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEIEILLRYGQH-----PNIITLKDVYDDGKYV 495
Cdd:cd14134   10 LTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrnvEKYREAAKIEIDVLETLAEKdpngkSHCVQLRDWFDYRGHM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMkGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDES----GNPES------- 562
Cdd:cd14134   90 CIVFELL-GPSLYDFLKKNNYgpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvYNPKKkrqirvp 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 563 ----IRICDFGFAkqlraengllmtpCY----------TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF---- 624
Cdd:cd14134  169 kstdIKLIDFGSA-------------TFddeyhssivsTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqthd 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 625 ----------ANGPddTPEEIL--ARIGSGKFSLSGGY--WNSVSDTAK------------------------DLVSKML 666
Cdd:cd14134  236 nlehlammerILGP--LPKRMIrrAKKGAKYFYFYHGRldWPEGSSSGRsikrvckplkrlmllvdpehrllfDLIRKML 313
                        330
                 ....*....|....*...
gi 768032625 667 HVDPHQRLTAALVLRHPW 684
Cdd:cd14134  314 EYDPSKRITAKEALKHPF 331
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
472-688 3.62e-25

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: 107.50  E-value: 3.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 472 ILLRYGQHPNIITLKDVY------DDGKYVYVVTELMKGGelLDKILRQKFFSEReASAVLFTITKTVEYLHAQGVVHRD 545
Cdd:cd07850   51 VLMKLVNHKNIIGLLNVFtpqkslEEFQDVYLVMELMDAN--LCQVIQMDLDHER-MSYLLYQMLCGIKHLHSAGIIHRD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 546 LKPSNILYVDESgnpeSIRICDFGFAKQlrAENGLLMTP-CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd07850  128 LKPSNIVVKSDC----TLKILDFGLART--AGTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLF 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 625 AnGPD------------DTP-EEILARIGS---------GKFSlsgGY--------WNSVSDT----------AKDLVSK 664
Cdd:cd07850  202 P-GTDhidqwnkiieqlGTPsDEFMSRLQPtvrnyvenrPKYA---GYsfeelfpdVLFPPDSeehnklkasqARDLLSK 277
                        250       260
                 ....*....|....*....|....
gi 768032625 665 MLHVDPHQRLTAALVLRHPWIVHW 688
Cdd:cd07850  278 MLVIDPEKRISVDDALQHPYINVW 301
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
426-686 4.09e-25

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: 105.97  E-value: 4.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdKSKRDPTE------EIEILLRYGQHPNIITLKD-VYDDGKyVYVV 498
Cdd:cd06617    1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEqkrllmDLDISMRSVDCPYTVTFYGaLFREGD-VWIC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGelLDKILRQKF-----FSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAK 572
Cdd:cd06617   79 MEVMDTS--LDKFYKKVYdkgltIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVL-INRNGQ---VKLCDFGISG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLraENGLLMTP---CytANFVAPE----VLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpdDTPEEILA-------- 637
Cdd:cd06617  153 YL--VDSVAKTIdagC--KPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPYDSW--KTPFQQLKqvveepsp 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 638 RIGSGKFSLSggywnsvsdtAKDLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd06617  227 QLPAEKFSPE----------FQDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
426-691 4.44e-25

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: 107.05  E-value: 4.44e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPT----EEIEILLRyGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd05597    1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWemlKRAETacfrEERDVLVN-GDRRWITKLHYAFQDENYLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLdkILRQKFFSEREASAVLFTITKTV---EYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR 575
Cdd:cd05597   80 MDYYCGGDLL--TLLSKFEDRLPEEMARFYLAEMVlaiDSIHQLGYVHRDIKPDNVL-LDRNGH---IRLADFGSCLKLR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 aENGLLM--TPCYTANFVAPEVLK-----RQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARigSGKFSLS 647
Cdd:cd05597  154 -EDGTVQssVAVGTPDYISPEILQamedgKGRYGPECDWWSLGVCMYEMLYGETPFyAESLVETYGKIMNH--KEHFSFP 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 648 gGYWNSVSDTAKDLVSKMLhVDPHQRLTAALV---LRHPWI--VHWDQL 691
Cdd:cd05597  231 -DDEDDVSEEAKDLIRRLI-CSRERRLGQNGIddfKKHPFFegIDWDNI 277
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
68-288 4.55e-25

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: 105.66  E-value: 4.55e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLkkatlkvrdRVRTKME-------RDI--LVEVNHPFIVKLHYAF 137
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARnKLTG----EVVALKKI---------RLDTETEgvpstaiREIslLKELNHPNIVKLLDVI 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDFLRGgDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd07860   69 HTENKLYLVFEFLHQ-DLkkFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 K------ESIDHEkkaysfCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07860  148 RafgvpvRTYTHE------VVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRT-LGTP 220
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
67-268 5.03e-25

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: 105.11  E-value: 5.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMK-VLKKATLKVRDRvrTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd14088    2 RYDLGQVIKTEEFCEIFRAKdKTTG----KLYTCKkFLKRDGRKVRKA--AKNEINILKMVKHPNILQLVDVFETRKEYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD---EEGHIKLTDFGLSKESIDH 221
Cdd:cd14088   76 IFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKLENGL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 222 EKKAysfCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14088  156 IKEP---CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPF 199
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
68-289 5.25e-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: 105.82  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKvlkkatlKVR-----DRVRTKMERDI-----LVEVNHPFIVKLH-- 134
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARdLQDG----RFVALK-------KVRvplseEGIPLSTIREIallkqLESFEHPNVVRLLdv 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 ---YAFQTEGKLYLILDFLRGgDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd07838   70 chgPRTDRELKLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 210 TDFGLSKeSIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMPQ 289
Cdd:cd07838  149 ADFGLAR-IYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFD-VIGLPS 226
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
64-310 5.86e-25

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: 104.84  E-value: 5.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKISGSDArqlyAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05059    2 DPSELTFLKELGSGQFGVVHLGKWRGKIDV----AIKMIKEGSMSEDDFIE---EAKVMMKLSHPKLVQLYGVCTKQRPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDL--FTRLSKEVMFTEedvkfYLAELAL----ALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE 217
Cdd:cd05059   75 FIVTEYMANGCLlnYLRERRGKFQTE-----QLLEMCKdvceAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARY 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SIDHEKKAySFcGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLS 292
Cdd:cd05059  150 VLDDEYTS-SV-GTkfpVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGyRLYRPHLAP 227
                        250
                 ....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANR 310
Cdd:cd05059  228 TEVYTIMYSCWHEKPEER 245
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
68-311 6.02e-25

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: 105.45  E-value: 6.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkkisgsDARQLYAMKV--LKKATLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd07835    1 YQKLEKIGEGTYGVVY--------KARDKLTGEIvaLKKIRLETEDEgVPSTAIREIslLKELNHPNIVRLLDVVHSENK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLrggDL----FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-- 216
Cdd:cd07835   73 LYLVFEFL---DLdlkkYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARaf 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ----ESIDHEkkaysfCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLG----- 286
Cdd:cd07835  150 gvpvRTYTHE------VVTLWYRAPEIlLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRT-LGtpded 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 287 -------MPQF------------------LSPEAQSLLRMLFKRNPANRL 311
Cdd:cd07835  223 vwpgvtsLPDYkptfpkwarqdlskvvpsLDEDGLDLLSQMLVYDPAKRI 272
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
434-685 6.87e-25

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: 104.77  E-value: 6.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII---------DKSKRDPT-----EEIEiLLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVelpktssdrADSRQKTVvdalkSEID-TLKDLDHPNIVQYLGFEETEDYFSIFL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKqlRAEN- 578
Cdd:cd06629   88 EYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNIL-VDLEGI---CKISDFGISK--KSDDi 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 -----GLLMTPcyTANFVAPEVL--KRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYW 651
Cdd:cd06629  162 ygnngATSMQG--SVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFKLGNKRSAPPVPED 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06629  237 VNLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
428-684 8.31e-25

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: 105.06  E-value: 8.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD---PTEEI-EI-LLRYGQHPNIITLKDVYDDGKYVYVVTE-- 500
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDegvPSTAIrEIsLLKELNHPNIVRLLDVVHSENKLYLVFEfl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 ---LMKggeLLDKILRQKFfSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAkqlRAE 577
Cdd:cd07835   81 dldLKK---YMDSSPLTGL-DPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLL-IDTEGA---LKLADFGLA---RAF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTpcYTANFV-----APEVL--KRQgYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSLSG-- 648
Cdd:cd07835  150 GVPVRT--YTHEVVtlwyrAPEILlgSKH-YSTPVDIWSVGCIFAEMVTRRPLF---PGDSEIDQLFRI----FRTLGtp 219
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 649 ------------GYWNS---------------VSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07835  220 dedvwpgvtslpDYKPTfpkwarqdlskvvpsLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
422-685 9.86e-25

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: 104.44  E-value: 9.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 422 IQFTDGyevkEDIGVGSY-SVCkrCIHKATNMEFAVKIIDKSKRDPT----------EEIEiLLRYGQHPNIITLKDVYD 490
Cdd:cd06631    1 IQWKKG----NVLGKGAYgTVY--CGLTSTGQLIAVKQVELDTSDKEkaekeyeklqEEVD-LLKTLKHVNIVGYLGTCL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGGELlDKILRQkFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVdesgnPES-IRICD 567
Cdd:cd06631   74 EDNVVSIFMEFVPGGSI-ASILAR-FGALEEPVFCRYTkqILEGVAYLHNNNVIHRDIKGNNIMLM-----PNGvIKLID 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLrAENGLLMTPCY-------TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIG 640
Cdd:cd06631  147 FGCAKRL-CINLSSGSQSQllksmrgTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMN---PMAAIFAIG 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 641 SGKfSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06631  223 SGR-KPVPRLPDKFSPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
432-690 1.19e-24

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: 104.37  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIID-KSKRDPTEEIE---ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd06642   10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDlEEAEDEIEDIQqeiTVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR----AENGLLMT 583
Cdd:cd06642   90 LD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVL-LSEQGD---VKLADFGVAGQLTdtqiKRNTFVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARI-GSGKFSLSGGYwnsvSDTAKDLV 662
Cdd:cd06642  165 PFW----MAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNS---DLHPMRVLFLIpKNSPPTLEGQH----SKPFKEFV 233
                        250       260
                 ....*....|....*....|....*...
gi 768032625 663 SKMLHVDPHQRLTAALVLRHPWIVHWDQ 690
Cdd:cd06642  234 EACLNKDPRFRPTAKELLKHKFITRYTK 261
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
469-683 1.19e-24

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: 104.28  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 469 EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG--ELLDKILRQKFF--SEREASAVLFTITKTVEYLHAQGVVHR 544
Cdd:cd13982   44 EVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAASlqDLVESPRESKLFlrPGLEPVRLLRQIASGLAHLHSLNIVHR 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 545 DLKPSNILY-VDESGNPESIRICDFGFAKQL---RAENGLLMTPCYTANFVAPEVL---KRQGYDAACDIWSLGVLLYTM 617
Cdd:cd13982  124 DLKPQNILIsTPNAHGNVRAMISDFGLCKKLdvgRSSFSRRSGVAGTSGWIAPEMLsgsTKRRQTRAVDIFSLGCVFYYV 203
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 618 LT-GYTPFAngpDDTPEEilARIGSGKFSLSggywNSVSDT-----AKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd13982  204 LSgGSHPFG---DKLERE--ANILKGKYSLD----KLLSLGehgpeAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
447-705 1.35e-24

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: 105.46  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 447 HKATNMEFAVKIIDKSKRDPTEEIEILL---------RYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKIlRQKFF 517
Cdd:cd05589   20 YKPTGELFAIKALKKGDIIARDEVESLMcekrifetvNSARHPFLVNLFACFQTPEHVCFVMEYAAGGDLMMHI-HEDVF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLK 597
Cdd:cd05589   99 SEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLL-LDTEG---YVKIADFGLCKEGMGFGDRTSTFCGTPEFLAPEVLT 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 598 RQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSlsggYWNSVSDTAKDLVSKMLHVDPHQRL--- 674
Cdd:cd05589  175 DTSYTRAVDWWGLGVLIYEMLVGESPF---PGDDEEEVFDSIVNDEVR----YPRFLSTEAISIMRRLLRKNPERRLgas 247
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 675 --TAALVLRHPWI--VHWDQLpqyqLNRQDAPHLV 705
Cdd:cd05589  248 erDAEDVKKQPFFrnIDWEAL----LARKIKPPFV 278
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
428-704 1.47e-24

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: 105.87  E-value: 1.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE-------ILLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05617   17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDwvqtekhVFEQASSNPFLVGLHSCFQTTSRLFLVIE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGL 580
Cdd:cd05617   97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVL-LDADGH---IKLTDYGMCKEGLGPGDT 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF---ANGPDDTPEEILARIGSGKfslSGGYWNSVSDT 657
Cdd:cd05617  173 TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQVILEK---PIRIPRFLSVK 249
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 658 AKDLVSKMLHVDPHQRLTAAL------VLRHPWI--VHWDQLPQYQLNRQDAPHL 704
Cdd:cd05617  250 ASHVLKGFLNKDPKERLGCQPqtgfsdIKSHTFFrsIDWDLLEKKQVTPPFKPQI 304
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
65-294 1.50e-24

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: 105.52  E-value: 1.50e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVflvkkISGSDA--RQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAF----- 137
Cdd:cd07878   14 PERYQNLTPVGSGAYGSV-----CSAYDTrlRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFtpats 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 -QTEGKLYLILDfLRGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07878   89 iENFNEVYLVTN-LMGADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 217 ESiDHEKKAYsfCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPqflSPE 294
Cdd:cd07878  167 QA-DDEMTGY--VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEV-VGTP---SPE 238
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
73-288 1.57e-24

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: 103.96  E-value: 1.57e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFL----VKKISGSDARQLYAMKVLKKAtlkvrDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd14146    1 IIGVGGFGKVYRatwkGQEVAVKAARQDPDEDIKATA-----ESVR--QEAKLFSMLRHPNIIKLEGVCLEEPNLCLVME 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFTEED---------VKFYLAELALALDHLHS---LGIIYRDLKPENILLDEE--------GHIK 208
Cdd:cd14146   74 FARGGTLNRALAAANAAPGPRrarripphiLVNWAVQIARGMLYLHEeavVPILHRDLKSSNILLLEKiehddicnKTLK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSKESidHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP 288
Cdd:cd14146  154 ITDFGLAREW--HRTTKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLP 231
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
428-624 1.67e-24

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: 106.24  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPT----EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05621   54 YDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFemiKRSDSaffwEERDIM-AFANSPWVVQLFCAFQDDKYLYMVME 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLraeNGL 580
Cdd:cd05621  133 YMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNML-LDKYGH---LKLADFGTCMKM---DET 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 581 LMTPCYTA----NFVAPEVLKRQG----YDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd05621  205 GMVHCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
428-681 1.92e-24

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: 103.57  E-value: 1.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-------KSKRDPTEEIEiLLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd08228    4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemmdaKARQDCVKEID-LLKQLNHPNVIKYLDSFIEDNELNIVLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKIL----RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGnpeSIRICDFG----FAK 572
Cdd:cd08228   83 LADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANV-FITATG---VVKLGDLGlgrfFSS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTPEEILARIGSGKF-SLSGGYW 651
Cdd:cd08228  159 KTTAAHSLVGTPYY----MSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFY-GDKMNLFSLCQKIEQCDYpPLPTEHY 233
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 652 nsvSDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd08228  234 ---SEKLRELVSMCIYPDPDQRPDIGYVHQ 260
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
64-270 1.97e-24

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: 103.23  E-value: 1.97e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFlvkkisgsdaRQLY-----AMKVLKKATLKVRDRVRTKMERDILvEVNHPFIVKLHYAFQ 138
Cdd:cd13979    1 DWEPLRLQEPLGSGGFGSVY----------KATYkgetvAVKIVRRRRKNRASRQSFWAELNAA-RLRHENIVRVLAAET 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYL---ILDFLRGGDLFTRL--SKEVMFTEEDVKfYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG 213
Cdd:cd13979   70 GTDFASLgliIMEYCGNGTLQQLIyeGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LS---KESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd13979  149 CSvklGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG 208
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
72-310 2.11e-24

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: 103.28  E-value: 2.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKI-SGSdarqLYAMKVLK--KATLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:cd06630    6 PLLGTGAFSSCYQARDVkTGT----LMAVKQVSfcRNSSSEQEEVVEAIREEIrmMARLNHPNIVRMLGATQHKSHFNIF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG-HIKLTDFGLSKESIDHEKKA 225
Cdd:cd06630   82 VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTGA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSF----CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGM-----PQFLSPEAQ 296
Cdd:cd06630  162 GEFqgqlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATtpppiPEHLSPGLR 241
                        250
                 ....*....|....
gi 768032625 297 SLLRMLFKRNPANR 310
Cdd:cd06630  242 DVTLRCLELQPEDR 255
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
68-320 2.21e-24

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: 103.51  E-value: 2.21e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKI-SGsdarQLYAMKVLKKatlkvrdRVRTKMERDILVEVN-------HPFIVKLHYAF-- 137
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRkTG----KYYAIKCMKK-------HFKSLEQVNNLREIQalrrlspHPNILRLIEVLfd 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDfLRGGDLFtrlskEVM------FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEgHIKLTD 211
Cdd:cd07831   70 RKTGRLALVFE-LMDMNLY-----ELIkgrkrpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLAD 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 212 FGlSKESIdHEKKAYS-FCGTVEYMAPEVVNRRG-HTQSADWWSFGVLMFEMLTgTLP-FQGKDRKETMTMILKAkLGMP 288
Cdd:cd07831  143 FG-SCRGI-YSKPPYTeYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILS-LFPlFPGTNELDQIAKIHDV-LGTP 218
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 289 qflspeAQSLLRMlFKRNPANRLVNPFLIGAG 320
Cdd:cd07831  219 ------DAEVLKK-FRKSRHMNYNFPSKKGTG 243
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
74-310 2.91e-24

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: 102.52  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISgsdarQLYAMKVLKKATLKVRDRVrtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14058    1 VGRGSFGVVCKARWRN-----QIVAVKIIESESEKKAFEV----EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRL-SKEV--MFTEEDVKFYLAELALALDHLHSLG---IIYRDLKPENILLDEEGH-IKLTDFGLSkesIDHEKKAY 226
Cdd:cd14058   72 SLYNVLhGKEPkpIYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTA---CDISTHMT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 227 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLS--PEA-QSLLRMLF 303
Cdd:cd14058  149 NNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAVHNGERPPLIKncPKPiESLMTRCW 228

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd14058  229 SKDPEKR 235
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
425-685 4.36e-24

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: 103.17  E-value: 4.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSkRDPTEEIE----ILLRYGQHPNIITLKDVY-----DDGKYV 495
Cdd:cd06638   17 SDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPI-HDIDEEIEaeynILKALSDHPNVVKFYGMYykkdvKNGDQL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELLDKIL----RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpesIRICDFGFA 571
Cdd:cd06638   96 WLVLELCNGGSVTDLVKgflkRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGG----VKLVDFGVS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLRAENGLLMTPCYTANFVAPEVL--KRQ---GYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSL 646
Cdd:cd06638  172 AQLTSTRLRRNTSVGTPFWMAPEVIacEQQldsTYDARCDVWSLGITAIELGDGDPPLA---DLHPMRALFKIPRNPPPT 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 647 --SGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06638  249 lhQPELW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
80-316 5.22e-24

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: 101.92  E-value: 5.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  80 GKVFLVKKISGSDARQLYAMKVLKkatLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRL 159
Cdd:cd14110   14 GRFSVVRQCEEKRSGQMLAAKIIP---YKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 160 SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlSKESIDHEKKAYS--FCGTVEYMAP 237
Cdd:cd14110   91 AERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG-NAQPFNQGKVLMTdkKGDYVETMAP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 238 EVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLRMLFKRNPANR---- 310
Cdd:cd14110  170 ELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGAVNFLKSTLCAKPWGRptas 249

                 ....*...
gi 768032625 311 --LVNPFL 316
Cdd:cd14110  250 ecLQNPWL 257
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
432-686 6.69e-24

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: 102.05  E-value: 6.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIID-KSKRDPTEEIE---ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd06640   10 ERIGKGSFGEVFKGIDNRTQQVVAIKIIDlEEAEDEIEDIQqeiTVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCYT 587
Cdd:cd06640   90 LD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVL-LSEQGD---VKLADFGVAGQLTDTQIKRNTFVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPfanGPDDTPEEILARIGSGKF-SLSGGYwnsvSDTAKDLVSKML 666
Cdd:cd06640  165 PFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP---NSDMHPMRVLFLIPKNNPpTLVGDF----SKPFKEFIDACL 237
                        250       260
                 ....*....|....*....|
gi 768032625 667 HVDPHQRLTAALVLRHPWIV 686
Cdd:cd06640  238 NKDPSFRPTAKELLKHKFIV 257
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
65-297 7.08e-24

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: 103.49  E-value: 7.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVflvkkISGSDARQ--LYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd07880   14 PDRYRDLKQVGSGAYGTV-----CSALDRRTgaKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 L------YLILDFLrGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07880   89 LdrfhdfYLVMPFM-GTDL-GKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLAR 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ESiDHEKKAYSFcgTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEA 295
Cdd:cd07880  167 QT-DSEMTGYVV--TRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKL 243

                 ..
gi 768032625 296 QS 297
Cdd:cd07880  244 QS 245
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
64-316 7.27e-24

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: 102.40  E-value: 7.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFLV-KKISGSdarqlyamkvlkKATLKVRDRVRtKMERDILVEVN-------HPFIVKLH 134
Cdd:cd06638   15 DPSDtWEIIETIGKGTYGKVFKVlNKKNGS------------KAAVKILDPIH-DIDEEIEAEYNilkalsdHPNVVKFY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAF-----QTEGKLYLILDFLRGGDLfTRLSKEVM-----FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd06638   82 GMYykkdvKNGDQLWLVLELCNGGSV-TDLVKGFLkrgerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSA-----DWWSFGVLMFEMLTGTLPFQGkdrketmtm 279
Cdd:cd06638  161 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIACEQQLDSTydarcDVWSLGITAIELGDGDPPLAD--------- 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 280 ilkaklgmpqfLSPeaqslLRMLFK--RNPANRLVNPFL 316
Cdd:cd06638  232 -----------LHP-----MRALFKipRNPPPTLHQPEL 254
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
65-332 7.82e-24

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: 101.66  E-value: 7.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVFLVkkISGSDARQLYAMKV-LKKATLKVRDRVRT-KMERDILVEVNHPFIVKlHYAF---QT 139
Cdd:cd06652    1 PTNWRLGKLLGQGAFGRVYLC--YDADTGRELAVKQVqFDPESPETSKEVNAlECEIQLLKNLLHERIVQ-YYGClrdPQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--E 217
Cdd:cd06652   78 ERTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SIDHEKKAY-SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgkdRKETMTMILK--AKLGMPQfLSPE 294
Cdd:cd06652  158 TICLSGTGMkSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKiaTQPTNPQ-LPAH 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 295 AQSLLRMLFKRNPANRLVNPFligagpdgVEEIKRHSF 332
Cdd:cd06652  234 VSDHCRDFLKRIFVEAKLRPS--------ADELLRHTF 263
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
434-674 7.89e-24

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: 102.86  E-value: 7.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELYAIKILKKDviiQDDDVEctmvEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKIlrQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd05587   84 LMYHI--QQVGKFKEPVAVFYAaeIAVGLFFLHSKGIIYRDLKLDNVM-LDAEGH---IKIADFGMCKEGIFGGKTTRTF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGKFSlsggYWNSVSDTAKDLVSK 664
Cdd:cd05587  158 CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPF-DGEDE--DELFQSIMEHNVS----YPKSLSKEAVSICKG 230
                        250
                 ....*....|
gi 768032625 665 MLHVDPHQRL 674
Cdd:cd05587  231 LLTKHPAKRL 240
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
454-682 8.19e-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: 101.99  E-value: 8.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 454 FAVK-IIDKSKRDPTE---EIEILLRYgQHPNIITLKD-----VYDDGKYVYVVTELMKGGELLDKILRQK----FFSER 520
Cdd:cd13986   28 YALKkILCHSKEDVKEamrEIENYRLF-NHPNILRLLDsqivkEAGGKKEVYLLLPYYKRGSLQDEIERRLvkgtFFPED 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 521 EASAVLFTITKTVEYLHAQ---GVVHRDLKPSNILyVDESGNPesiRICDFGFAKQLRAE---NGLLMT-------PCyT 587
Cdd:cd13986  107 RILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVL-LSEDDEP---ILMDLGSMNPARIEiegRREALAlqdwaaeHC-T 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 588 ANFVAPE---VLKRQGYDAACDIWSLGVLLYTMLTGYTPFangpddtpEEILARIGSGKFSLSGGYW-----NSVSDTAK 659
Cdd:cd13986  182 MPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF--------ERIFQKGDSLALAVLSGNYsfpdnSRYSEELH 253
                        250       260
                 ....*....|....*....|...
gi 768032625 660 DLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd13986  254 QLVKSMLVVNPAERPSIDDLLSR 276
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
425-685 8.76e-24

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: 102.38  E-value: 8.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKrDPTEEIE----ILLRYGQHPNIITLKDV-YDDGKYV---- 495
Cdd:cd06639   21 SDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPIS-DVDEEIEaeynILRSLPNHPNVVKFYGMfYKADQYVggql 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGG---ELLDKILRQ-KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpesIRICDFGFA 571
Cdd:cd06639  100 WLVLELCNGGsvtELVKGLLKCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVS 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLRAENGLLMTPCYTANFVAPEVL--KRQ---GYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARI--GSGKF 644
Cdd:cd06639  176 AQLTSARLRRNTSVGTPFWMAPEVIacEQQydySYDARCDVWSLGITAIELADGDPPLF---DMHPVKALFKIprNPPPT 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 645 SLSGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06639  253 LLNPEKW---CRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
66-317 8.78e-24

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: 102.23  E-value: 8.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvkKISGSDARQLYAMK----VLKKATLKvrdrvRTKMERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd06622    1 DEIEVLDELGKGNYGSVY---KVLHRPTGVTMAMKeirlELDESKFN-----QIIMELDILHKAVSPYIVDFYGAFFIEG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGG--DLFTRLSKEVMFTEEDVkfyLAELALALDH-LHSL----GIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd06622   73 AVYMCMEYMDAGslDKLYAGGVATEGIPEDV---LRRITYAVVKgLKFLkeehNIIHRDVKPTNVLVNGNGQVKLCDFGV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYSFCGTveYMAPEVVNRRG------HTQSADWWSFGVLMFEMLTGTLPFQgkdrKETMTMILkAKL--- 285
Cdd:cd06622  150 SGNLVASLAKTNIGCQS--YMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPYP----PETYANIF-AQLsai 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 768032625 286 ------GMPQFLSPEAQSLLRMLFKRNPANR------LVNPFLI 317
Cdd:cd06622  223 vdgdppTLPSGYSDDAQDFVAKCLNKIPNRRptyaqlLEHPWLV 266
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
66-310 8.99e-24

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: 102.11  E-value: 8.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKIsGSDARQLYAMKVlkkATLKVRDRVRTKMERDILVEVN-------HPFIVKLHYAFQ 138
Cdd:cd05053   12 DRLTLGKPLGEGAFGQVVKAEAV-GLDNKPNEVVTV---AVKMLKDDATEKDLSDLVSEMEmmkmigkHKNIINLLGACT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDL--FTRLSKEVM--------------FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD 202
Cdd:cd05053   88 QDGPLYVVVEYASKGNLreFLRARRPPGeeaspddprvpeeqLTQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 203 EEGHIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKEtMTM 279
Cdd:cd05053  168 EDNVMKIADFGLARDihHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE-LFK 246
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 280 ILKA--KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05053  247 LLKEghRMEKPQNCTQELYMLMRDCWHEVPSQR 279
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
66-310 9.22e-24

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: 101.36  E-value: 9.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvkkiSG--SDARQLyAMKVLKKA-TLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGK 142
Cdd:cd05148    6 EEFTLERKLGSGYFGEVW-----EGlwKNRVRV-AIKILKSDdLLKQQDFQK---EVQALKRLRHKHLISLF-AVCSVGE 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 -LYLILDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS---K 216
Cdd:cd05148   76 pVYIITELMEKGSLlaFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ESI--DHEKKAysfcgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLS 292
Cdd:cd05148  156 EDVylSSDKKI-----PYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAGyRMPCPAKCP 230
                        250
                 ....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANR 310
Cdd:cd05148  231 QEIYKIMLECWAAEPEDR 248
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
455-691 9.95e-24

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: 103.96  E-value: 9.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIDKS---KRDPTEEI----EILLRyGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLF 527
Cdd:cd05600   40 ALKIMKKKvlfKLNEVNHVlterDILTT-TNSPWLVKLLYAFQDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 528 TITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK---------QLRA---ENGLLMTPCYTANF----- 590
Cdd:cd05600  119 EMFAAISSLHQLGYIHRDLKPENFL-IDSSGH---IKLTDFGLASgtlspkkieSMKIrleEVKNTAFLELTAKErrniy 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 591 --------------------VAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGY 650
Cdd:cd05600  195 ramrkedqnyansvvgspdyMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFSG---STPNETWANLYHWKKTLQRPV 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 651 WN------SVSDTAKDLVSKMLhVDPHQRLTAAL-VLRHPWI--VHWDQL 691
Cdd:cd05600  272 YTdpdlefNLSDEAWDLITKLI-TDPQDRLQSPEqIKNHPFFknIDWDRL 320
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
434-624 1.06e-23

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: 100.97  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVckrcIHKAT--NMEFAVKIIDKS--KRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd14058    1 VGRGSFGV----VCKARwrNQIVAVKIIESEseKKAFEVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILRQKFFSEREASAVL---FTITKTVEYLHA---QGVVHRDLKPSNILYVDesgNPESIRICDFGFAKQLRAEngllMT 583
Cdd:cd14058   76 VLHGKEPKPIYTAAHAMswaLQCAKGVAYLHSmkpKALIHRDLKPPNLLLTN---GGTVLKICDFGTACDISTH----MT 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768032625 584 PCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd14058  149 NNKgSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPF 190
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
434-674 1.10e-23

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: 101.45  E-value: 1.10e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDPTEEI----EILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKriKKKKGETMalneKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAE---NGLLM 582
Cdd:cd05577   81 KYHIYNVGTRGFSEARAIFYAaeIICGLEHLHNRFIVYRDLKPENIL-LDDHGH---VRISDLGLAVEFKGGkkiKGRVG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYtanfVAPEVLKRQ-GYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIgsgkFSLSGGYWNSVSDTAKD 660
Cdd:cd05577  157 THGY----MAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrQRKEKVDKEELKRRT----LEMAVEYPDSFSPEARS 228
                        250
                 ....*....|....
gi 768032625 661 LVSKMLHVDPHQRL 674
Cdd:cd05577  229 LCEGLLQKDPERRL 242
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
63-316 1.28e-23

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: 101.61  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  63 ADPS-QFELLKVLGQGSFGKVFLV-KKISGSDArqlyAMKVLKKATlKVRDRVRTkmERDILVEV-NHPFIVKLHYAFQT 139
Cdd:cd06639   18 ADPSdTWDIIETIGKGTYGKVYKVtNKKDGSLA----AVKILDPIS-DVDEEIEA--EYNILRSLpNHPNVVKFYGMFYK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 E-----GKLYLILDFLRGGDLfTRLSKEVM-----FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd06639   91 AdqyvgGQLWLVLELCNGGSV-TELVKGLLkcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKL 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 210 TDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSA-----DWWSFGVLMFEMLTGTLPFqgKDRKETMTMILKAK 284
Cdd:cd06639  170 VDFGVSAQLTSARLRRNTSVGTPFWMAPEVIACEQQYDYSydarcDVWSLGITAIELADGDPPL--FDMHPVKALFKIPR 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 285 LGMPQFLSPE----------AQSLLRMLFKRNPANRLV-NPFL 316
Cdd:cd06639  248 NPPPTLLNPEkwcrgfshfiSQCLIKDFEKRPSVTHLLeHPFI 290
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
457-689 1.31e-23

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 102.75  E-value: 1.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 457 KIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYL 536
Cdd:PTZ00426  68 KIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYL 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 537 HAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENgllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYT 616
Cdd:PTZ00426 148 QSLNIVYRDLKPENLL-LDKDG---FIKMTDFGFAKVVDTRT---YTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYE 220
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 617 MLTGYTPF-ANGPDDTPEEILARIgsgkfslsgGYWNSVSDT-AKDLVSKMLHVDPHQRL-----TAALVLRHPWIVHWD 689
Cdd:PTZ00426 221 ILVGCPPFyANEPLLIYQKILEGI---------IYFPKFLDNnCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
74-312 1.34e-23

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 101.58  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVK--KISGSDARQLYAMKVLKKATLKVRDRVrtKMERDILVEVNHPFIVKLhYAFQTEGK-LYLILDFL 150
Cdd:cd05092   13 LGEGAFGKVFLAEchNLLPEQDKMLVAVKALKEATESARQDF--QREAELLTVLQHQHIVRF-YGVCTEGEpLIMVFEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDL--FTRL---SKEVMFTEEDVKF----------YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd05092   90 RHGDLnrFLRShgpDAKILDGGEGQAPgqltlgqmlqIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 KE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFL 291
Cdd:cd05092  170 RDiySTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGReLERPRTC 249
                        250       260
                 ....*....|....*....|.
gi 768032625 292 SPEAQSLLRMLFKRNPANRLV 312
Cdd:cd05092  250 PPEVYAIMQGCWQREPQQRHS 270
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
416-666 1.39e-23

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: 103.94  E-value: 1.39e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 416 QLHRnsiqftDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK---SKRDPT----EEIEILLRyGQHPNIITLKDV 488
Cdd:cd05624   68 QLHR------DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKwemLKRAETacfrEERNVLVN-GDCQWITTLHYA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 489 YDDGKYVYVVTELMKGGELLdkILRQKFFSEREASAVLFTITKTV---EYLHAQGVVHRDLKPSNILyVDESGNpesIRI 565
Cdd:cd05624  141 FQDENYLYLVMDYYVGGDLL--TLLSKFEDKLPEDMARFYIGEMVlaiHSIHQLHYVHRDIKPDNVL-LDMNGH---IRL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 566 CDFGFAKQLrAENGLLMTPCY--TANFVAPEVLKRQ-----GYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILA 637
Cdd:cd05624  215 ADFGSCLKM-NDDGTVQSSVAvgTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFyAESLVETYGKIMN 293
                        250       260
                 ....*....|....*....|....*....
gi 768032625 638 RIGSGKFSlsgGYWNSVSDTAKDLVSKML 666
Cdd:cd05624  294 HEERFQFP---SHVTDVSEEAKDLIQRLI 319
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
70-312 1.61e-23

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: 101.00  E-value: 1.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVFLVK--KISGSDARQLYAMKVLKKATLkvrDRVRTKMERD--ILVEVNHPFIVKLhYAFQTEGK-LY 144
Cdd:cd05049    9 LKRELGEGAFGKVFLGEcyNLEPEQDKMLVAVKTLKDASS---PDARKDFEREaeLLTNLQHENIVKF-YGVCTEGDpLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDL--FTRL------------SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLT 210
Cdd:cd05049   85 MVFEYMEHGDLnkFLRShgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIG 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 211 DFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LG 286
Cdd:cd05049  165 DFGMSRDiySTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEVIECITQGRlLQ 244
                        250       260
                 ....*....|....*....|....*.
gi 768032625 287 MPQFLSPEAQSLLRMLFKRNPANRLV 312
Cdd:cd05049  245 RPRTCPSEVYAVMLGCWKREPQQRLN 270
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
65-288 1.78e-23

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: 102.29  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKV-----------FLVKKISGSDARQLYAMKVLKKATLkvrdrvrtkmerdiLVEVNHPFIVKL 133
Cdd:cd07879   14 PERYTSLKQVGSGAYGSVcsaidkrtgekVAIKKLSRPFQSEIFAKRAYRELTL--------------LKHMQHENVIGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 HYAFQTEGKL------YLILDFLrggdlFTRLSKeVM---FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd07879   80 LDVFTSAVSGdefqdfYLVMPYM-----QTDLQK-IMghpLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNED 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GHIKLTDFGLSKESiDHEKKAYSFcgTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKA 283
Cdd:cd07879  154 CELKILDFGLARHA-DAEMTGYVV--TRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKV 230

                 ....*
gi 768032625 284 KlGMP 288
Cdd:cd07879  231 T-GVP 234
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
428-702 1.79e-23

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 102.80  E-value: 1.79e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE-----ILLRYGQHPNIITLKDVYDDGKY------VY 496
Cdd:cd07876   23 YQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRayrelVLLKCVNHKNIISLLNVFTPQKSleefqdVY 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGelLDKILRQKFFSEReASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQlrA 576
Cdd:cd07876  103 LVMELMDAN--LCQVIHMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC----TLKILDFGLART--A 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTP-CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPD--DTPEEILARIGSGKFSLSGGY--- 650
Cdd:cd07876  174 CTNFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIF-QGTDhiDQWNKVIEQLGTPSAEFMNRLqpt 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 651 ----------------------WNSVSDT---------AKDLVSKMLHVDPHQRLTAALVLRHPWIVHWdqlpqYQLNRQ 699
Cdd:cd07876  253 vrnyvenrpqypgisfeelfpdWIFPSESerdklktsqARDLLSKMLVIDPDKRISVDEALRHPYITVW-----YDPAEA 327

                 ...
gi 768032625 700 DAP 702
Cdd:cd07876  328 EAP 330
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
62-317 1.92e-23

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: 101.30  E-value: 1.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADPSQFELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRvRTKMERDILVEVNH-PFIVKLHYAFQTE 140
Cdd:cd06618   11 KADLNDLENLGEIGSGTCGQVYKMRHKKTG---HVMAVKQMRRSGNKEENK-RILMDLDVVLKSHDcPYIVKCYGYFITD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLrgGDLFTRLSKEVM-FTEEDVkfyLAELAL----ALDHL---HslGIIYRDLKPENILLDEEGHIKLTDF 212
Cdd:cd06618   87 SDVFICMELM--STCLDKLLKRIQgPIPEDI---LGKMTVsivkALHYLkekH--GVIHRDVKPSNILLDESGNVKLCDF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 213 GLSKESIDHEKKAYSfCGTVEYMAPEVVNRRGHTQ---SADWWSFGVLMFEMLTGTLPFQGKDRK-ETMTMILK---AKL 285
Cdd:cd06618  160 GISGRLVDSKAKTRS-AGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNeepPSL 238
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 286 GMPQFLSPEAQSLLRMLFKRNPANR------LVNPFLI 317
Cdd:cd06618  239 PPNEGFSPDFCSFVDLCLTKDHRYRpkyrelLQHPFIR 276
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
74-310 1.99e-23

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: 100.21  E-value: 1.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkKISGSDARQLYAMKVLKkATLKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEgKLYLILDFLRG 152
Cdd:cd05041    3 IGRGNFGDVY---RGVLKPDNTEVAVKTCR-ETLPPDLKRKFLQEARILKQYDHPNIVKLiGVCVQKQ-PIMIVMELVPG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDL--FTRLSKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCG 230
Cdd:cd05041   78 GSLltFLRKKGARLTVKQLLQMCL-DAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDGLK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 T--VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQfLSPEAQSLLRML-FKR 305
Cdd:cd05041  157 QipIKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQIESGyRMPAPE-LCPEAVYRLMLQcWAY 235

                 ....*
gi 768032625 306 NPANR 310
Cdd:cd05041  236 DPENR 240
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
444-684 2.02e-23

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: 99.73  E-value: 2.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 444 RCIHKATNMEFAVKIIDKSKRDptEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTElMKGGELLDKILRQKFFSEREAS 523
Cdd:cd14022   11 RAVHLHSGEELVCKVFDIGCYQ--ESLAPCFCLPAHSNINQITEIILGETKAYVFFE-RSYGDMHSFVRTCKKLREEEAA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 AVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQG-YD 602
Cdd:cd14022   88 RLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERT--RVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGsYS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 603 A-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd14022  166 GkAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEILD 238

                 ...
gi 768032625 682 HPW 684
Cdd:cd14022  239 HPW 241
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
432-684 2.34e-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: 100.66  E-value: 2.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTEEI-EI-LLRYGQHPNIITLKDVYDDGKYVYVVTELMKggE 506
Cdd:cd07860    6 EKIGEGTYGVVYKARNKLTGEVVALKKIrldTETEGVPSTAIrEIsLLKELNHPNIVKLLDVIHTENKLYLVFEFLH--Q 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAV---LFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAkqlRAENGLLMT 583
Cdd:cd07860   84 DLKKFMDASALTGIPLPLIksyLFQLLQGLAFCHSHRVLHRDLKPQNLL-INTEG---AIKLADFGLA---RAFGVPVRT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 pcYTANFV-----APEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWNSVSD- 656
Cdd:cd07860  157 --YTHEVVtlwyrAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALF---PGDSEIDQLFRIFRTLGTPDEVVWPGVTSm 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 657 ------------------------TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07860  232 pdykpsfpkwarqdfskvvppldeDGRDLLSQMLHYDPNKRISAKAALAHPF 283
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
67-268 2.38e-23

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: 100.72  E-value: 2.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGsdaRQLYAMKVLK-KATLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd06619    2 DIQYQEILGHGNGGTVYKAYHLLT---RRILAVKVIPlDITVELQKQIMSELE--ILYKCDSPYIIGFYGAFFVENRISI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGG--DLFTRLSKEVmfteedvkfyLAELALA----LDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd06619   77 CTEFMDGGslDVYRKIPEHV----------LGRIAVAvvkgLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 220 DHEKKAYsfCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd06619  147 NSIAKTY--VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPY 193
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
434-681 2.53e-23

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: 100.16  E-value: 2.53e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKatNMEFAVKIidkSKRDPTEEIEI----------LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14061    2 IGVGGFGKVYRGIWR--GEEVAVKA---ARQDPDEDISVtlenvrqearLFWMLRHPNIIALRGVCLQPPNLCLVMEYAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELlDKILRQKffseREASAVLFT----ITKTVEYLHAQG---VVHRDLKPSNILyVDESGNPESI-----RICDFGFA 571
Cdd:cd14061   77 GGAL-NRVLAGR----KIPPHVLVDwaiqIARGMNYLHNEApvpIIHRDLKSSNIL-ILEAIENEDLenktlKITDFGLA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 KQLraENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDdtPEEILARIGSGKFSLSggYW 651
Cdd:cd14061  151 REW--HKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPY-KGID--GLAVAYGVAVNKLTLP--IP 223
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd14061  224 STCPEPFAQLMKDCWQPDPHDRPSFADILK 253
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
428-684 2.62e-23

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: 100.81  E-value: 2.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVckrcIHKATNME----FAVKIIdkskRDPTE----------EIEIL--LRYGQHPNIITLKDV--- 488
Cdd:cd07838    1 YEEVAEIGEGAYGT----VYKARDLQdgrfVALKKV----RVPLSeegiplstirEIALLkqLESFEHPNVVRLLDVchg 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 489 --YDDGKYVYVVTELMKG--GELLDKiLRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIR 564
Cdd:cd07838   73 prTDRELKLTLVFEHVDQdlATYLDK-CPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNIL-VTSDG---QVK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 565 ICDFGFAKQLraENGLLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTM---------------------LTGyT 622
Cdd:cd07838  148 LADFGLARIY--SFEMALTSVVvTLWYRAPEVLLQSSYATPVDMWSVGCIFAELfnrrplfrgsseadqlgkifdVIG-L 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 623 PfanGPDDTPEEILARIGSGKFSLSGGYWNSV---SDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07838  225 P---SEEEWPRNSALPRSSFPSYTPRPFKSFVpeiDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
68-299 2.62e-23

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 99.98  E-value: 2.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLkkaTLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd14108    4 YDIHKEIGRGAFS---YLRRVKEKSSDLSFAAKFI---PVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG--HIKLTDFGLSKESIDHEKKa 225
Cdd:cd14108   78 E-LCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQ- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLG----MPQFLSPEAQSLL 299
Cdd:cd14108  156 YCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAfeesMFKDLCREAKGFI 233
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
67-310 2.67e-23

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: 99.66  E-value: 2.67e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDArqlYAMKVLKKatlkvrDRV----------RTKMERDILVEVNHPF--IVKLH 134
Cdd:cd14100    1 QYQVGPLLGSGGFGSVYSGIRVADGAP---VAIKHVEK------DRVsewgelpngtRVPMEIVLLKKVGSGFrgVIRLL 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGKLYLILDFLRG-GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EEGHIKLTDF 212
Cdd:cd14100   72 DWFERPDSFVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 213 G---LSKESIdhekkaYS-FCGTVEYMAPEVVN-RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRketmtmILKAKLGM 287
Cdd:cd14100  152 GsgaLLKDTV------YTdFDGTRVYSPPEWIRfHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFF 219
                        250       260
                 ....*....|....*....|...
gi 768032625 288 PQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14100  220 RQRVSSECQHLIKWCLALRPSDR 242
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
74-310 2.71e-23

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: 99.73  E-value: 2.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDR--VRtkmERDILVEVNHPFIVKLHYAFQTEGkLYLILDFLR 151
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKefLR---EASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKKAYSFCGT 231
Cdd:cd05060   79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSR-ALGAGSDYYRATTA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 232 ----VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd05060  158 grwpLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGErLPRPEECPQEIYSIMLSCWKY 237

                 ....*
gi 768032625 306 NPANR 310
Cdd:cd05060  238 RPEDR 242
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
473-685 2.94e-23

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 102.51  E-value: 2.94e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 473 LLRYGQHPNIITLKDV-----YDDGKYVYVVTELMKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLK 547
Cdd:cd07853   52 MLCFFKHDNVLSALDIlqpphIDPFEEIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIK 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 548 PSNILYvdesGNPESIRICDFGFAKQLRAENGLLMT-PCYTANFVAPEVLK-RQGYDAACDIWSLGVLLYTMLTGYTPF- 624
Cdd:cd07853  131 PGNLLV----NSNCVLKICDFGLARVEEPDESKHMTqEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRRILFq 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 625 ANGPDDTPEEIL-------------ARIGSGKFSLSGG---------YWNSVSDT--AKDLVSKMLHVDPHQRLTAALVL 680
Cdd:cd07853  207 AQSPIQQLDLITdllgtpsleamrsACEGARAHILRGPhkppslpvlYTLSSQATheAVHLLCRMLVFDPDKRISAADAL 286

                 ....*
gi 768032625 681 RHPWI 685
Cdd:cd07853  287 AHPYL 291
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
74-270 3.24e-23

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: 100.52  E-value: 3.24e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVflvKKISGSDARQLYAMKVLKkATLKVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd06616   14 IGRGAFGTV---NKMLHKPSGTIMAVKRIR-STVDEKEQKRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWICMELMDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 G-DLFTRL---SKEVMFTEEdvkfYLAELAL----ALDHL-HSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhek 223
Cdd:cd06616   90 SlDKFYKYvyeVLDSVIPEE----ILGKIAVatvkALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD--- 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 224 kaySFCGTVE-----YMAPEVVN----RRGHTQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd06616  163 ---SIAKTRDagcrpYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPK 215
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
73-288 3.31e-23

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: 99.68  E-value: 3.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFlvKKISGSDARQLYAMKVLKKATLKVR-DRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd14148    1 IIGVGGFGKVY--KGLWRGEEVAVKAARQDPDEDIAVTaENVR--QEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKfYLAELALALDHLHS---LGIIYRDLKPENILLDE--EGH------IKLTDFGLSKESid 220
Cdd:cd14148   77 GGALNRALAGKKVPPHVLVN-WAVQIARGMNYLHNeaiVPIIHRDLKSSNILILEpiENDdlsgktLKITDFGLAREW-- 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP 288
Cdd:cd14148  154 HKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLP 221
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
434-726 3.34e-23

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: 101.61  E-value: 3.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTE----EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05615   18 LGKGSFGKVMLAERKGSDELYAIKILKKDvviQDDDVEctmvEKRVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENGLLMTPCY 586
Cdd:cd05615   98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVM-LDSEGH---IKIADFGMCKEHMVEGVTTRTFCG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDtpEEILARIGSGKFSlsggYWNSVSDTAKDLVSKML 666
Cdd:cd05615  174 TPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPF-DGEDE--DELFQSIMEHNVS----YPKSLSKEAVSICKGLM 246
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 667 HVDPHQRLTAAL-----VLRHPWI--VHWDQLPQYQLNRQDAPHlVKGAMAATYSALNRNQSPVLEP 726
Cdd:cd05615  247 TKHPAKRLGCGPegerdIREHAFFrrIDWDKLENREIQPPFKPK-VCGKGAENFDKFFTRGQPVLTP 312
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
68-293 3.88e-23

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: 101.28  E-value: 3.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKkatLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd06649    7 FERISELGAGNGG---VVTKVQHKPSGLIMARKLIH---LEIKPAIRNQIIRElqVLHECNSPYIVGFYGAFYSDGEISI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDV-KFYLAEL-ALA-LDHLHSlgIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhe 222
Cdd:cd06649   81 CMEHMDGGSLDQVLKEAKRIPEEILgKVSIAVLrGLAyLREKHQ--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLID-- 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 223 KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTM----ILKAKLGMPQFLSP 293
Cdd:cd06649  157 SMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKELEAIfgrpVVDGEEGEPHSISP 231
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
67-310 4.81e-23

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: 99.70  E-value: 4.81e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVF----LVK-KISGSDARQLYA-MKVLKKATLkVRDRVRtkmERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd13990    1 RYLLLNLLGKGGFSEVYkafdLVEqRYVACKIHQLNKdWSEEKKQNY-IKHALR---EYEIHKSLDHPRIVKLYDVFEID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 -GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSL--GIIYRDLKPENILLDEE---GHIKLTDFGL 214
Cdd:cd13990   77 tDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIkpPIIHYDLKPGNILLHSGnvsGEIKITDFGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYS------FCGTVEYMAPE--VVNRRGHTQSA--DWWSFGVLMFEMLTGTLPF---QGKDRKETMTMIL 281
Cdd:cd13990  157 SKIMDDESYNSDGmeltsqGAGTYWYLPPEcfVVGKTPPKISSkvDVWSVGVIFYQMLYGRKPFghnQSQEAILEENTIL 236
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 282 KAKLGmpQF-----LSPEAQSLLRMLFKRNPANR 310
Cdd:cd13990  237 KATEV--EFpskpvVSSEAKDFIRRCLTYRKEDR 268
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
435-691 4.85e-23

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 99.96  E-value: 4.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 435 GVGSYSVCKRcihKATNMEFAVKIIDKS---KRDPTE----EIEILLRYgqHPN-IITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05608   13 GFGEVSACQM---RATGKLYACKKLNKKrlkKRKGYEgamvEKRILAKV--HSRfIVSLAYAFQTKTDLCLVMTIMNGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILR----QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAenGLLM 582
Cdd:cd05608   88 LRYHIYNvdeeNPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVL-LDDDGN---VRISDLGLAVELKD--GQTK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCY--TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILARIgsgkFSLSGGYWNSVSDTAK 659
Cdd:cd05608  162 TKGYagTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFrARGEKVENKELKQRI----LNDSVTYSEKFSPASK 237
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 660 DLVSKMLHVDPHQRL-----TAALVLRHPWI--VHWDQL 691
Cdd:cd05608  238 SICEALLAKDPEKRLgfrdgNCDGLRTHPFFrdINWRKL 276
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
64-288 5.51e-23

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: 99.33  E-value: 5.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFlvkkiSGSDARQLYAMKVLKK---ATLKVRDRvRTKMERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd14147    1 SFQELRLEEVIGIGGFGKVY-----RGSWRGELVAVKAARQdpdEDISVTAE-SVRQEARLFAMLAHPNIIALKAVCLEE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKfYLAELALALDHLHS---LGIIYRDLKPENILLDEEGH--------IKL 209
Cdd:cd14147   75 PNLCLVMEYAAGGPLSRALAGRRVPPHVLVN-WAVQIARGMHYLHCealVPVIHRDLKSNNILLLQPIEnddmehktLKI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 210 TDFGLSKESidHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMP 288
Cdd:cd14147  154 TDFGLAREW--HKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLP 230
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
74-310 5.74e-23

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: 98.85  E-value: 5.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkkiSG---SDaRQLYAMKVLKKaTLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd05084    4 IGRGNFGEVF-----SGrlrAD-NTPVAVKSCRE-TLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEVMFTEEDVKFYLAELALA-LDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhekKAYSFC 229
Cdd:cd05084   77 QGGDFLTFLRTEGPRLKVKELIRMVENAAAgMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEED---GVYAAT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 G-----TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRML 302
Cdd:cd05084  154 GgmkqiPVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQGvRLPCPENCPDEVYRLMEQC 233

                 ....*...
gi 768032625 303 FKRNPANR 310
Cdd:cd05084  234 WEYDPRKR 241
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
69-310 7.07e-23

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: 99.03  E-value: 7.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  69 ELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKK-ATLKVRDRVRTkmERDILVEVNHPFIVKLhYAFQTEGKLYLIL 147
Cdd:cd05056    9 TLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNcTSPSVREKFLQ--EAYIMRQFDHPHIVKL-IGVITENPVWIVM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTE-EDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE-KKA 225
Cdd:cd05056   86 ELAPLGELRSYLQVNKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESyYKA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRMLF 303
Cdd:cd05056  166 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCW 245

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd05056  246 AYDPSKR 252
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
429-686 8.22e-23

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: 99.05  E-value: 8.22e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 429 EVKEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSK--RDPTEEIEILlRYGQHPNIITLKDVY-DDGKYVYVVTELM 502
Cdd:cd06620    8 ETLKDLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSvrKQILRELQIL-HECHSPYIVSFYGAFlNENNNIIICMEYM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELlDKILRQK-FFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaeNGL 580
Cdd:cd06620   87 DCGSL-DKILKKKgPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNIL-VNSKGQ---IKLCDFGVSGELI--NSI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDD-----TPEEI---LARI---GSGKFSLSGG 649
Cdd:cd06620  160 ADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDDddgynGPMGIldlLQRIvnePPPRLPKDRI 239
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 650 YwnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd06620  240 F----PKDLRDFVDRCLLKDPRERPSPQLLLDHDPFI 272
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
68-329 1.03e-22

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: 99.79  E-value: 1.03e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVL----KKATLKvrdrvRTKMERDILVEV-NHPFIVKLH-------Y 135
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITnvfsKKILAK-----RALRELKLLRHFrGHKNITCLYdmdivfpG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AFQtegKLYLILDfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS 215
Cdd:cd07857   77 NFN---ELYLYEE-LMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 KE-SIDHEKKA---YSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP-- 288
Cdd:cd07857  153 RGfSENPGENAgfmTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQV-LGTPde 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 289 ----QFLSPEAQSLLRMLfkRNPANRLVNPFLIGAGPDGVEEIKR 329
Cdd:cd07857  232 etlsRIGSPKAQNYIRSL--PNIPKKPFESIFPNANPLALDLLEK 274
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
67-288 1.27e-22

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: 98.71  E-value: 1.27e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKkatLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd07836    1 NFKQLEKLGEGTYATVY---KGRNRTTGEIVALKEIH---LDAEEGTPSTAIREIslMKELKHENIVRLHDVIHTENKLM 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGgDLftrlsKEVMFTEED--------VKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07836   75 LVFEYMDK-DL-----KKYMDTHGVrgaldpntVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLAR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 217 ESIDHEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07836  149 AFGIPVNTFSNEVVTLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRI-MGTP 220
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
434-691 1.33e-22

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 99.28  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDPTEEIEI----LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05632   10 LGKGGFGEVCACQVRATGKMYACKRLEKKriKKRKGESMALnekqILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKI--LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLrAENGLLMTPC 585
Cdd:cd05632   90 KFHIynMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENIL-LDDYGH---IRISDLGLAVKI-PEGESIRGRV 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTP-EEILARIGSGKFSLSGGYwnsvSDTAKDLVSK 664
Cdd:cd05632  165 GTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKrEEVDRRVLETEEVYSAKF----SEEAKSICKM 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 665 MLHVDPHQRL-----TAALVLRHPWI--VHWDQL 691
Cdd:cd05632  241 LLTKDPKQRLgcqeeGAGEVKRHPFFrnMNFKRL 274
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
64-310 1.33e-22

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: 98.01  E-value: 1.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKkisgSDARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05114    2 NPSELTFMKELGSGLFGVVRLGK----WRAQYKVAIKAIREGAMSEEDFIE---EAKVMMKLTHPKLVQLYGVCTQQKPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLA-ELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd05114   75 YIVTEFMENGCLLNYLRQRRGKLSRDMLLSMCqDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKaySFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQS 297
Cdd:cd05114  155 YT--SSSGAkfpVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGhRLYRPKLASKSVYE 232
                        250
                 ....*....|...
gi 768032625 298 LLRMLFKRNPANR 310
Cdd:cd05114  233 VMYSCWHEKPEGR 245
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
67-314 1.58e-22

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 98.22  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGSDARQLYAMKVLKKATlkvRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGK- 142
Cdd:cd05038    5 HLKFIKQLGEGHFGSVELCRyDPLGDNTGEQVAVKSLQPSG---EEQHMSDFKReiEILRTLDHEYIVKYKGVCESPGRr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 -LYLILDFLRGGDL--FTRLSKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKesI 219
Cdd:cd05038   82 sLRLIMEYLPSGSLrdYLQRHRDQIDLKRLLLFAS-QICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK--V 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGT-----VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRkETMTMILKAKLGMPQFlspe 294
Cdd:cd05038  159 LPEDKEYYYVKEpgespIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPA-LFLRMIGIAQGQMIVT---- 233
                        250       260
                 ....*....|....*....|
gi 768032625 295 aqSLLRMLfKRNPanRLVNP 314
Cdd:cd05038  234 --RLLELL-KSGE--RLPRP 248
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
434-683 1.65e-22

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: 98.17  E-value: 1.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDPTE-----EIEILLRYGQHpNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05630    8 LGKGGFGEVCACQVRATGKMYACKKLEKKriKKRKGEamalnEKQILEKVNSR-FVVSLAYAYETKDALCLVLTLMNGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKI--LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLrAENGLLMTP 584
Cdd:cd05630   87 LKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENIL-LDDHGH---IRISDLGLAVHV-PEGQTIKGR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSgkfSLSGGYWNSVSDTAKDLVSK 664
Cdd:cd05630  162 VGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVK---EVPEEYSEKFSPQARSLCSM 238
                        250       260
                 ....*....|....*....|....
gi 768032625 665 MLHVDPHQRL-----TAALVLRHP 683
Cdd:cd05630  239 LLCKDPAERLgcrggGAREVKEHP 262
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
426-684 1.72e-22

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: 98.21  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEiLLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd07847    1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVikkialREIR-MLKQLKHPNLVNLIEVFRRKRKLHLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGEL--LDKilRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAE 577
Cdd:cd07847   80 EYCDHTVLneLEK--NPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQG----QIKLCDFGFARILTGP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPCYTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGyTPFANGPDDTPEEILARIGSGK--------FSLSG 648
Cdd:cd07847  154 GDDYTDYVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLTG-QPLWPGKSDVDQLYLIRKTLGDliprhqqiFSTNQ 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 649 ---GYWNSVSDTAKDLVSKM--------------LHVDPHQRLTAALVLRHPW 684
Cdd:cd07847  233 ffkGLSIPEPETREPLESKFpnisspalsflkgcLQMDPTERLSCEELLEHPY 285
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
72-310 1.81e-22

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: 97.35  E-value: 1.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDArqlyAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGK-LYLILDFL 150
Cdd:cd05034    1 KKLGAGQFGEVWMGVWNGTTKV----AVKTLKPGTMSPEAFLQ---EAQIMKKLRHDKLVQL-YAVCSDEEpIYIVTELM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSf 228
Cdd:cd05034   73 SKGSLldYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTARE- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 cGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRMLF 303
Cdd:cd05034  152 -GAkfpIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERGyRMPKPPGCPDELYDIMLQCW 230

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd05034  231 KKEPEER 237
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
427-684 1.84e-22

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: 98.90  E-value: 1.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 427 GYEVKEDIGVGSYSVckrcIHKA------TNMEFAVKIIDKSKRDPT-------EEIeILLRYGQHPNIITLKDVYDDG- 492
Cdd:cd07842    1 KYEIEGCIGRGTYGR----VYKAkrkngkDGKEYAIKKFKGDKEQYTgisqsacREI-ALLRELKHENVVSLVEVFLEHa 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 493 -KYVYVVTELMKGgELLDKIlrqKFFSEREASAV--------LFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESI 563
Cdd:cd07842   76 dKSVYLLFDYAEH-DLWQII---KFHRQAKRVSIppsmvkslLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERGVV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 564 RICDFGFA-------KQLRAENGLLMTPCYTanfvAPEVL--KRQgYDAACDIWSLGVLLYTMLTGYTPFANGPDD---- 630
Cdd:cd07842  152 KIGDLGLArlfnaplKPLADLDPVVVTIWYR----APELLlgARH-YTKAIDIWAIGCIFAELLTLEPIFKGREAKikks 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 631 TP------EEILARIGS------------------GKFSLSGGYWNS-----------VSDTAKDLVSKMLHVDPHQRLT 675
Cdd:cd07842  227 NPfqrdqlERIFEVLGTptekdwpdikkmpeydtlKSDTKASTYPNSllakwmhkhkkPDSQGFDLLRKLLEYDPTKRIT 306

                 ....*....
gi 768032625 676 AALVLRHPW 684
Cdd:cd07842  307 AEEALEHPY 315
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
434-683 1.90e-22

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: 98.14  E-value: 1.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS--KRDPTEEIEI----LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05631    8 LGKGGFGEVCACQVRATGKMYACKKLEKKriKKRKGEAMALnekrILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKI--LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLrAENGLLMTPC 585
Cdd:cd05631   88 KFHIynMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENIL-LDDRGH---IRISDLGLAVQI-PEGETVRGRV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTP-EEILARIGSGKFSlsggYWNSVSDTAKDLVSK 664
Cdd:cd05631  163 GTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKrEEVDRRVKEDQEE----YSEKFSEDAKSICRM 238
                        250       260
                 ....*....|....*....|....
gi 768032625 665 MLHVDPHQRL-----TAALVLRHP 683
Cdd:cd05631  239 LLTKNPKERLgcrgnGAAGVKQHP 262
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
66-310 2.21e-22

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: 97.77  E-value: 2.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05090    5 SAVRFMEELGECAFGKIYKGHlYLPGMDHAQLVAIKTLKDYN-NPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRL------SKEVMFTEED--VKFYL---------AELALALDHLHSLGIIYRDLKPENILLDEEGHI 207
Cdd:cd05090   84 MLFEFMNQGDLHEFLimrsphSDVGCSSDEDgtVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 208 KLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK 284
Cdd:cd05090  164 KISDLGLSREiySSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQ 243
                        250       260
                 ....*....|....*....|....*..
gi 768032625 285 -LGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05090  244 lLPCSEDCPPRMYSLMTECWQEIPSRR 270
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
67-316 2.30e-22

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: 97.67  E-value: 2.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkisgSDARQLYAMKV--LKKATLKVRDRVrtKMERDILVEVNH-PFIVKL--HYAFQTEG 141
Cdd:cd14131    2 PYEILKQLGKGGSSKVYKVL----NPKKKIYALKRvdLEGADEQTLQSY--KNEIELLKKLKGsDRIIQLydYEVTDEDD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFlRGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLdEEGHIKLTDFGLSKE-- 217
Cdd:cd14131   76 YLYMVMEC-GEIDLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL-VKGRLKLIDFGIAKAiq 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 ----SIDHEkkaySFCGTVEYMAPEVVNRRGHTQ----------SADWWSFGVLMFEMLTGTLPFQgkdrkETMTMIlkA 283
Cdd:cd14131  154 ndttSIVRD----SQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQ-----HITNPI--A 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 284 KLG----------MPQFLSPEAQSLLRMLFKRNPANR------LVNPFL 316
Cdd:cd14131  223 KLQaiidpnheieFPDIPNPDLIDVMKRCLQRDPKKRpsipelLNHPFL 271
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
426-680 2.32e-22

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: 97.45  E-value: 2.32e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVK--EDIGVGSYSVCKRCIHKATNMefAVKIIDKSK----RDPTEEIEILLRYGQHPNII---TLKDVYDDGKYVY 496
Cdd:cd13979    1 DWEPLRlqEPLGSGGFGSVYKATYKGETV--AVKIVRRRRknraSRQSFWAELNAARLRHENIVrvlAAETGTDFASLGL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKI--LRQKFFSEReasAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFAK 572
Cdd:cd13979   79 IIMEYCGNGTLQQLIyeGSEPLPLAH---RILISldIARALRFCHSHGIVHLDVKPANIL-ISEQGVC---KLCDFGCSV 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGLLMTPCY---TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSG-KFSLSG 648
Cdd:cd13979  152 KLGEGNEVGTPRSHiggTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG---LRQHVLYAVVAKDlRPDLSG 228
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 649 GYWNSVSDTAKDLVSKMLHVDPHQRLTAALVL 680
Cdd:cd13979  229 LEDSEFGQRLRSLISRCWSAQPAERPNADESL 260
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
434-624 2.35e-22

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: 97.90  E-value: 2.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVK-------IIDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYV------YVVTE 500
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqelsPSDKNRERWCLEVQIMKKL-NHPNVVSARDVPPELEKLspndlpLLAME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELlDKILRQKF----FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAKQLra 576
Cdd:cd13989   80 YCSGGDL-RKVLNQPEnccgLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIV-LQQGGGRVIYKLIDLGYAKEL-- 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 577 ENGLLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd13989  156 DQGSLCTSFVgTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
67-274 2.43e-22

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 99.92  E-value: 2.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARqlyamKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 146
Cdd:PHA03207  93 QYNILSSLTPGSEGEVFVCTKHGDEQRK-----KVIVKAVTGGKTPGR---EIDILKTISHRAIINLIHAYRWKSTVCMV 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH--EKK 224
Cdd:PHA03207 165 MPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHpdTPQ 243
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK 274
Cdd:PHA03207 244 CYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGKQVK 293
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
68-316 2.60e-22

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: 96.95  E-value: 2.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVR---DRVR--TKMERDIlvEVNHPFIVKLHYAFQTEGK 142
Cdd:cd14133    1 YEVLEVLGKGTFGQVV---KCYDLLTGEEVALKIIKNNKDYLDqslDEIRllELLNKKD--KADKYHIVRLKDVFYFKNH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLrGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL--DEEGHIKLTDFGLSKES 218
Cdd:cd14133   76 LCIVFELL-SQNLyeFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCFL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHekkAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT------------MILKAKLG 286
Cdd:cd14133  155 TQR---LYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLAriigtigippahMLDQGKAD 231
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 287 MPQFLspeaqSLLRMLFKRNPANR------LVNPFL 316
Cdd:cd14133  232 DELFV-----DFLKKLLEIDPKERptasqaLSHPWL 262
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
428-684 2.82e-22

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: 97.49  E-value: 2.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD---PTEEI-EI-LLRYGQHPNIITLKDVYDDGKYVYVVTEL- 501
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEegvPSTAIrEIsLLKELQHPNIVCLEDVLMQENRLYLVFEFl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 -MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQ----LRA 576
Cdd:cd07861   82 sMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLL-IDNKGV---IKLADFGLARAfgipVRV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTPCYTanfvAPEVL-KRQGYDAACDIWSLGVLLYTMLTGyTPFANGPDD------------TP-EEILARIGS- 641
Cdd:cd07861  158 YTHEVVTLWYR----APEVLlGSPRYSTPVDIWSIGTIFAEMATK-KPLFHGDSEidqlfrifrilgTPtEDIWPGVTSl 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 642 ----------GKFSLSGGYWNsVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07861  233 pdykntfpkwKKGSLRTAVKN-LDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
69-310 3.00e-22

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 97.42  E-value: 3.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  69 ELLKVLGQGSFGKVFLVKKISGSDArqlyAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd05072   10 KLVKKLGAGQFGEVWMGYYNNSTKV----AVKTLKPGTMSVQAFLE---EANLMKTLQHDKLVRLYAVVTKEEPIYIITE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSkevmfTEEDVKFYL-------AELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd05072   83 YMAKGSLLDFLK-----SDEGGKVLLpklidfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDN 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCG-TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSL 298
Cdd:cd05072  158 EYTAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGyRMPRMENCPDELYDI 237
                        250
                 ....*....|..
gi 768032625 299 LRMLFKRNPANR 310
Cdd:cd05072  238 MKTCWKEKAEER 249
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
432-686 3.59e-22

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: 97.07  E-value: 3.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIID-KSKRDPTEEIE---ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd06641   10 EKIGKGSFGEVFKGIDNRTQKVVAIKIIDlEEAEDEIEDIQqeiTVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLR----AENGLLMT 583
Cdd:cd06641   90 LD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVL-LSEHG---EVKLADFGVAGQLTdtqiKRN*FVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSGGYWnsvSDTAKDLVS 663
Cdd:cd06641  165 PFW----MAPEVIKQSAYDSKADIWSLGITAIELARGEPPHS---ELHPMKVLFLIPKNNPPTLEGNY---SKPLKEFVE 234
                        250       260
                 ....*....|....*....|...
gi 768032625 664 KMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd06641  235 ACLNKEPSFRPTAKELLKHKFIL 257
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
453-646 3.62e-22

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


Pssm-ID: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 96.02  E-value: 3.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 453 EFAVKIIDKSKrdpteEIEIL-LRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQkffsEREASAVLFT--- 528
Cdd:cd14059   18 EVAVKKVRDEK-----ETDIKhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYE-VLRA----GREITPSLLVdws 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 --ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRaENGLLMTPCYTANFVAPEVLKRQGYDAACD 606
Cdd:cd14059   88 kqIASGMNYLHLHKIIHRDLKSPNVLV----TYNDVLKISDFGTSKELS-EKSTKMSFAGTVAWMAPEVIRNEPCSEKVD 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 768032625 607 IWSLGVLLYTMLTGYTPFANGPDDTpeeILARIGSGKFSL 646
Cdd:cd14059  163 IWSFGVVLWELLTGEIPYKDVDSSA---IIWGVGSNSLQL 199
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
66-288 4.42e-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: 97.44  E-value: 4.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvkKISGSDARQLYAMKvlkkatlkvrdRVRTKMERD-----------ILVEVNHPFIVKLH 134
Cdd:cd07845    7 TEFEKLNRIGEGTYGIVY---RARDTTSGEIVALK-----------KVRMDNERDgipisslreitLLLNLRHPNIVELK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQteGK----LYLILDFLRGgDLfTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIK 208
Cdd:cd07845   73 EVVV--GKhldsIFLVMEYCEQ-DL-ASLLDNMPtpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSKESIDHEKKAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILkAKLGM 287
Cdd:cd07845  149 IADFGLARTYGLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLII-QLLGT 227

                 .
gi 768032625 288 P 288
Cdd:cd07845  228 P 228
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
68-307 4.42e-22

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: 98.01  E-value: 4.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFG-----------KVFLVKKISgsDARQlyamkvlkKATlkvrDRVRTKMERDILVEVN-HPFIVKLHY 135
Cdd:cd07852    9 YEILKKLGKGAYGivwkaidkktgEVVALKKIF--DAFR--------NAT----DAQRTFREIMFLQELNdHPNIIKLLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AFQTE-GK-LYLILDFLRGgDLFTRLSKEVMfteEDV--KFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTD 211
Cdd:cd07852   75 VIRAEnDKdIYLVFEYMET-DLHAVIRANIL---EDIhkQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLAD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 212 FGLSKeSIDHEKKAYSFCGTVEYMA------PEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGkdrkeTMTM----- 279
Cdd:cd07852  151 FGLAR-SLSQLEEDDENPVLTDYVAtrwyraPEIlLGSTRYTKGVDMWSVGCILGEMLLGKPLFPG-----TSTLnqlek 224
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 280 ILKAkLGMP------QFLSPEAQSLLRMLFKRNP 307
Cdd:cd07852  225 IIEV-IGRPsaedieSIQSPFAATMLESLPPSRP 257
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
68-316 5.80e-22

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: 96.27  E-value: 5.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKKATLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd06645   13 FELIQRIGSGTYGDVYKARNVNTG---ELAAIKVIKLEPGEDFAVV--QQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd06645   88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEV--VNRR-GHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF-----LSPEAQSLL 299
Cdd:cd06645  168 FIGTPYWMAPEVaaVERKgGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLkdkmkWSNSFHHFV 247
                        250       260
                 ....*....|....*....|...
gi 768032625 300 RMLFKRNPANR------LVNPFL 316
Cdd:cd06645  248 KMALTKNPKKRptaeklLQHPFV 270
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
419-685 5.84e-22

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: 97.02  E-value: 5.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 419 RNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE----EIEILLRYgQHPNIITLKDV-YDDGK 493
Cdd:cd06644    5 RRDLDPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEdymvEIEILATC-NHPYIVKLLGAfYWDGK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 yVYVVTELMKGGELlDKILRQ--KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFA 571
Cdd:cd06644   84 -LWIMIEFCPGGAV-DAIMLEldRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDG----DIKLADFGVS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 ----KQLRAENGLLMTPCYTA-NFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFS- 645
Cdd:cd06644  158 aknvKTLQRRDSFIGTPYWMApEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHH---ELNPMRVLLKIAKSEPPt 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 646 -LSGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06644  235 lSQPSKW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFV 272
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
426-731 6.40e-22

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


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 98.21  E-value: 6.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI-------EILLRyGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd05627    2 DDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVahiraerDILVE-ADGAWVVKMFYSFQDKRNLYLI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN 578
Cdd:cd05627   81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLL-LDAKGH---VKLSDFGLCTGLKKAH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 -----------------------------------GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTP 623
Cdd:cd05627  157 rtefyrnlthnppsdfsfqnmnskrkaetwkknrrQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 624 FANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLhVDPHQRLTAALVLR---HPWI--VHWDQLPQyqlnR 698
Cdd:cd05627  237 FCS---ETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFC-TDAENRIGSNGVEEiksHPFFegVDWEHIRE----R 308
                        330       340       350
                 ....*....|....*....|....*....|...
gi 768032625 699 QDAPHLVKGAMAATYSALNRNQSPVLEPVGRST 731
Cdd:cd05627  309 PAAIPIEIKSIDDTSNFDDFPESDILQPAPNTT 341
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
428-683 6.90e-22

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: 96.34  E-value: 6.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYS-VCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEIL--LRYGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14052    2 FANVELIGSGEFSqVYKVSERVPTGKVYAVKKLKPNYAGAKdrlrrlEEVSILreLTLDGHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGEL---LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR 575
Cdd:cd14052   82 TELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVL-ITFEGT---LKIGDFGMATVWP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AENGLLMTPcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGP----------DDTPEEILARIGSGKFS 645
Cdd:cd14052  158 LIRGIEREG--DREYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNGDawqklrsgdlSDAPRLSSTDLHSASSP 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 646 LSGGYWNSVSDTA-----KDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14052  236 SSNPPPDPPNMPIlsgslDRVVRWMLSPEPDRRPTADDVLATP 278
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
489-680 7.77e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 99.71  E-value: 7.77e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 489 YDDGKY---VYVVTELMKGGELlDKILRQKF-----FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgnP 560
Cdd:PTZ00267 131 FDDFKSddkLLLIMEYGSGGDL-NKQIKQRLkehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM-----P 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 561 ESI-RICDFGFAKQLRAENGLLMTP--CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPddTPEEILA 637
Cdd:PTZ00267 205 TGIiKLGDFGFSKQYSDSVSLDVASsfCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF-KGP--SQREIMQ 281
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 638 RIGSGKFSlsgGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVL 680
Cdd:PTZ00267 282 QVLYGKYD---PFPCPVSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
434-624 7.99e-22

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


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 95.82  E-value: 7.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATnmEFAVKiidKSKRDPTEEIEI----------LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14148    2 IGVGGFGKVYKGLWRGE--EVAVK---AARQDPDEDIAVtaenvrqearLFWMLQHPNIIALRGVCLNPPHLCLVMEYAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELlDKILRQKFFSEREASAVLFTITKTVEYLHAQGVV---HRDLKPSNILYVDESGNPE----SIRICDFGFAKQLRA 576
Cdd:cd14148   77 GGAL-NRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEPIENDDlsgkTLKITDFGLAREWHK 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 577 ENGllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd14148  156 TTK--MSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
74-268 9.16e-22

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: 95.29  E-value: 9.16e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkkiSGSDARQLYAMKVLKKATLKVRDRVrtKM---ERDILVEVNHPFIVKLHYA-FQTEGKLYLILDF 149
Cdd:cd14064    1 IGSGSFGKVY-----KGRCRNKIVAIKRYRANTYCSKSDV--DMfcrEVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLA-ELALALDHLHSLG--IIYRDLKPENILLDEEGHIKLTDFGLSK--ESIDHEKK 224
Cdd:cd14064   74 VSGGSLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRflQSLDEDNM 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 225 AYSfCGTVEYMAPEVVNRRG-HTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14064  154 TKQ-PGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
74-310 9.36e-22

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 95.41  E-value: 9.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKV----FLVKKisgsdARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGkLYLILDF 149
Cdd:cd05116    3 LGSGNFGTVkkgyYQMKK-----VVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKKAYSFC 229
Cdd:cd05116   77 AELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSK-ALRADENYYKAQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 230 GT----VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQSLLRMLF 303
Cdd:cd05116  156 THgkwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCW 235

                 ....*..
gi 768032625 304 KRNPANR 310
Cdd:cd05116  236 TYDVDER 242
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
428-683 1.50e-21

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: 94.68  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII------DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSrsrfrgEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MkGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLL 581
Cdd:cd14050   83 C-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL----SKDGVCKLGDFGLVVELDKEDIHD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MT---PCYtanfVAPEVLkrQG-YDAACDIWSLGVllyTML------------TGYTPFANGpdDTPEEILarigsgkfs 645
Cdd:cd14050  158 AQegdPRY----MAPELL--QGsFTKAADIFSLGI---TILelacnlelpsggDGWHQLRQG--YLPEEFT--------- 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 646 lsggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14050  218 ------AGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
445-684 1.56e-21

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 94.34  E-value: 1.56e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 445 CIHKATNMEFAVKIIDKSKrdptEEIEILLRYGQHPNIITLKDVY--DDGKYVYVVTELmkgGELLDKILRQKFFSEREA 522
Cdd:cd14023   14 QLHSGAELQCKVFPLKHYQ----DKIRPYIQLPSHRNITGIVEVIlgDTKAYVFFEKDF---GDMHSYVRSCKRLREEEA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 523 SAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQG-Y 601
Cdd:cd14023   87 ARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERT--QLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTGtY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 602 DA-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKMLHVDPHQRLTAALVL 680
Cdd:cd14023  165 SGkSADVWSLGVMLYTLLVGRYPFH---DSDPSALFSKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEIL 237

                 ....
gi 768032625 681 RHPW 684
Cdd:cd14023  238 LHPW 241
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
68-310 1.65e-21

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: 94.64  E-value: 1.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkkisgSDARQLYAMKVLKKATLKVR-------DRVRTKMERDILVEVNHPF--IVKLHYAFQ 138
Cdd:cd14102    2 YQVGSVLGSGGFGTVY-------AGSRIADGLPVAVKHVVKERvtewgtlNGVMVPLEIVLLKKVGSGFrgVIKLLDWYE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLR-GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-EEGHIKLTDFG--- 213
Cdd:cd14102   75 RPDGFLIVMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGsga 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LSKESIdhekkaYS-FCGTVEYMAPEVVN-RRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRketmtmILKAKLGMPQFL 291
Cdd:cd14102  155 LLKDTV------YTdFDGTRVYSPPEWIRyHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEE------ILRGRLYFRRRV 222
                        250
                 ....*....|....*....
gi 768032625 292 SPEAQSLLRMLFKRNPANR 310
Cdd:cd14102  223 SPECQQLIKWCLSLRPSDR 241
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
66-289 1.70e-21

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: 95.17  E-value: 1.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFL-VKKISGSDARQLYAMKVLKKATLKVRDRVRTKmERDILVEVNHPFIVKLhYAFQTEGKLY 144
Cdd:cd05057    7 TELEKGKVLGSGAFGTVYKgVWIPEGEKVKIPVAIKVLREETGPKANEEILD-EAYVMASVDHPHLVRL-LGICLSSQVQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLF-------TRLSKEVMFTeedvkfYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKe 217
Cdd:cd05057   85 LITQLMPLGCLLdyvrnhrDNIGSQLLLN------WCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAK- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 218 SIDHEKKAYSFCG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQ 289
Cdd:cd05057  158 LLDVDEKEYHAEGgkvPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGeRLPQPP 234
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
432-635 1.76e-21

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: 94.43  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVK-----IIDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKtcretLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQ-----LRAENGL 580
Cdd:cd05041   80 LLTFLRKKGaRLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENN----VLKISDFGMSREeedgeYTVSDGL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 581 LMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAN-----------------GPDDTPEEI 635
Cdd:cd05041  156 KQIP---IKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGmsnqqtreqiesgyrmpAPELCPEAV 225
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
67-310 1.94e-21

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: 95.85  E-value: 1.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKIsGSDARQ-----LYAMKVLK-KATLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTE 140
Cdd:cd05101   25 KLTLGKPLGEGCFGQVVMAEAV-GIDKDKpkeavTVAVKMLKdDATEKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDL-----------------FTRLSKEVMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDE 203
Cdd:cd05101  103 GPLYVIVEYASKGNLreylrarrppgmeysydINRVPEEQM-TFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTE 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 204 EGHIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI 280
Cdd:cd05101  182 NNVMKIADFGLARDinNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKLL 261
                        250       260       270
                 ....*....|....*....|....*....|.
gi 768032625 281 LKA-KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05101  262 KEGhRMDKPANCTNELYMMMRDCWHAVPSQR 292
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
431-694 2.00e-21

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: 95.12  E-value: 2.00e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKD-VYDDGKyVYVVTELMKG 504
Cdd:cd06616   11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRIrstvdEKEQKRLLMDLDVVMRSSDCPYIVKFYGaLFREGD-CWICMELMDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GelLDKILR------QKFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLraE 577
Cdd:cd06616   90 S--LDKFYKyvyevlDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNIL-LDRNGN---IKLCDFGISGQL--V 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMT------PcytanFVAPEVL----KRQGYDAACDIWSLGVLLYTMLTGYTPFANGpdDTPEEILARIGSGKFS-L 646
Cdd:cd06616  162 DSIAKTrdagcrP-----YMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPYPKW--NSVFDQLTQVVKGDPPiL 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 647 SGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQY 694
Cdd:cd06616  235 SNSEEREFSPSFVNFVNLCLIKDESKRPKYKELLKHPFIKMYEERNVD 282
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
72-303 2.25e-21

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: 94.76  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISgsDARQLYAMKVLKKATLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGK--LYLIL 147
Cdd:cd06651   13 KLLGQGAFGRVYLCYDVD--TGRELAAKQVQFDPESPETSKEVSALECEIqlLKNLQHERIVQYYGCLRDRAEktLTIFM 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--ESIDHEKKA 225
Cdd:cd06651   91 EYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTICMSGTG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 Y-SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQgkdRKETMTMILK-----AKLGMPQFLSPEAQSLL 299
Cdd:cd06651  171 IrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiatqpTNPQLPSHISEHARDFL 247

                 ....
gi 768032625 300 RMLF 303
Cdd:cd06651  248 GCIF 251
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
64-280 2.47e-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: 95.51  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKISgsdARQLYAMKvlkkatlKVRDRVRTK-------MERDILVEVNHPFIVKLHYA 136
Cdd:cd07865   10 EVSKYEKLAKIGQGTFGEVFKARHRK---TGQIVALK-------KVLMENEKEgfpitalREIKILQLLKHENVVNLIEI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 137 FQTE--------GKLYLILDFLRGgDLFTRLS-KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI 207
Cdd:cd07865   80 CRTKatpynrykGSIYLVFEFCEH-DLAGLLSnKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVL 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 208 KLTDFGLSKE-SIDHEKKAYSFCG---TVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI 280
Cdd:cd07865  159 KLADFGLARAfSLAKNSQPNRYTNrvvTLWYRPPELlLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLI 236
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
64-316 2.55e-21

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: 94.69  E-value: 2.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKkatlkvrdrVRTKMERDILVEVN-------HPFIVKLHY 135
Cdd:cd06636   13 DPAGiFELVEVVGNGTYGQVYKGRHVKTG---QLAAIKVMD---------VTEDEEEEIKLEINmlkkyshHRNIATYYG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AF------QTEGKLYLILDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI 207
Cdd:cd06636   81 AFikksppGHDDQLWLVMEFCGAGSVtdLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 208 KLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQS-----ADWWSFGVLMFEMLTGTLPFQGKDRKETMTMI-- 280
Cdd:cd06636  161 KLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDAtydyrSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIpr 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 281 -----LKAKLGMPQFLSPEAQSLLRMLFKRNPANRLV-NPFL 316
Cdd:cd06636  241 npppkLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLkHPFI 282
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
68-316 2.61e-21

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 94.18  E-value: 2.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLvkkiSGSDARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGKLYLIL 147
Cdd:cd05067    9 LKLVERLGAGQFGEVWM----GYYNGHTKVAIKSLKQGSMSPDAFLA---EANLMKQLQHQRLVRLY-AVVTQEPIYIIT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSkevmfTEEDVKFYL-------AELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd05067   81 EYMENGSLVDFLK-----TPSGIKLTInklldmaAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCG-TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQS 297
Cdd:cd05067  156 NEYTAREGAKfPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQNLERGyRMPRPDNCPEELYQ 235
                        250
                 ....*....|....*....
gi 768032625 298 LLRMLFKRNPANRLVNPFL 316
Cdd:cd05067  236 LMRLCWKERPEDRPTFEYL 254
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
430-673 2.90e-21

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: 94.34  E-value: 2.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKEDIGVGSYSVCKRCIHKATnmEFAVKiidKSKRDPTEEIE----------ILLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14145   10 LEEIIGIGGFGKVYRAIWIGD--EVAVK---AARHDPDEDISqtienvrqeaKLFAMLKHPNIIALRGVCLKEPNLCLVM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELlDKILRQKFFSEREASAVLFTITKTVEYLHAQGVV---HRDLKPSNILYVDESGNPE----SIRICDFGFAK 572
Cdd:cd14145   85 EFARGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKVENGDlsnkILKITDFGLAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDTPeeILARIGSGKFSLsggywn 652
Cdd:cd14145  164 EWHRTTK--MSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF-RGIDGLA--VAYGVAMNKLSL------ 232
                        250       260
                 ....*....|....*....|....*
gi 768032625 653 SVSDTAKDLVSKML----HVDPHQR 673
Cdd:cd14145  233 PIPSTCPEPFARLMedcwNPDPHSR 257
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
426-684 2.99e-21

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 94.88  E-value: 2.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRD---PTEEI-EI-LLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDegvPSTAIrEIsLLKEMQHGNIVRLQDVVHSEKRLYLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LmkggelLDKILRQKFFS-------EREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpeSIRICDFGFAKQ 573
Cdd:PLN00009  82 Y------LDLDLKKHMDSspdfaknPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLL-IDRRTN--ALKLADFGLARA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 LRAENGLLMTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSLSG---- 648
Cdd:PLN00009 153 FGIPVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLF---PGDSEIDELFKI----FRILGtpne 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 649 GYWNSVS---------------DTAK----------DLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:PLN00009 226 ETWPGVTslpdyksafpkwppkDLATvvptlepagvDLLSKMLRLDPSKRITARAALEHEY 286
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
416-691 3.05e-21

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: 97.01  E-value: 3.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 416 QLHRnsiqftDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDK---SKRDPT----EEIEILLRyGQHPNIITLKDV 488
Cdd:cd05623   68 RLHK------EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKwemLKRAETacfrEERDVLVN-GDSQWITTLHYA 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 489 YDDGKYVYVVTELMKGGELLdkILRQKF---FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRI 565
Cdd:cd05623  141 FQDDNNLYLVMDYYVGGDLL--TLLSKFedrLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNIL-MDMNGH---IRL 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 566 CDFGFAKQLrAENGLLMTPCY--TANFVAPEVLK-----RQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEEILA 637
Cdd:cd05623  215 ADFGSCLKL-MEDGTVQSSVAvgTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFyAESLVETYGKIMN 293
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 638 RIGSGKFSLSggyWNSVSDTAKDLVSKMLHVDPHQRLTAAL--VLRHPWI--VHWDQL 691
Cdd:cd05623  294 HKERFQFPTQ---VTDVSENAKDLIRRLICSREHRLGQNGIedFKNHPFFvgIDWDNI 348
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
126-270 3.16e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 98.33  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 126 NHPFIVKLhYAFQTEGKL-YLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:NF033483  65 SHPNIVSV-YDVGEDGGIpYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKD 143
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 205 GHIKLTDFG----LSKESIDHEKkaySFCGTVEYMAPE-----VVNRRghtqsADWWSFGVLMFEMLTGTLPFQG 270
Cdd:NF033483 144 GRVKVTDFGiaraLSSTTMTQTN---SVLGTVHYLSPEqarggTVDAR-----SDIYSLGIVLYEMLTGRPPFDG 210
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
426-685 3.16e-21

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: 94.71  E-value: 3.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEE--IEI-LLRYGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd06643    5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDymVEIdILASCDHPNIVKLLDAFYYENNLWILIEFC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILR-QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFA----KQLRAE 577
Cdd:cd06643   85 AGGAVDAVMLElERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG----DIKLADFGVSakntRTLQRR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NGLLMTPCYtanfVAPEVL-----KRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIG-SGKFSLSG-GY 650
Cdd:cd06643  161 DSFIGTPYW----MAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHH---ELNPMRVLLKIAkSEPPTLAQpSR 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 651 WnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06643  234 W---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
64-310 3.36e-21

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: 93.86  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGkvfLVKKISGSDARQLyAMKVLKKATLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05112    2 DPSELTFVQEIGSGQFG---LVHLGYWLNKDKV-AIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLEQAPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd05112   75 CLVFEFMEHGCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQ 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKaySFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQS 297
Cdd:cd05112  155 YT--SSTGTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGfRLYKPRLASTHVYE 232
                        250
                 ....*....|...
gi 768032625 298 LLRMLFKRNPANR 310
Cdd:cd05112  233 IMNHCWKERPEDR 245
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
434-624 3.54e-21

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: 94.64  E-value: 3.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVK-----IIDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYV------YVVTELM 502
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKqcrqeLSPKNRERWCLEIQIMKRL-NHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELlDKILRQ--KFFSEREAS--AVLFTITKTVEYLHAQGVVHRDLKPSNIlyVDESGNPESI-RICDFGFAKQLraE 577
Cdd:cd14038   81 QGGDL-RKYLNQfeNCCGLREGAilTLLSDISSALRYLHENRIIHRDLKPENI--VLQQGEQRLIhKIIDLGYAKEL--D 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 578 NGLLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd14038  156 QGSLCTSFVgTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
73-268 3.83e-21

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 93.44  E-value: 3.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFL-VKKISGSDArqlyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL--DF 149
Cdd:cd13983    8 VLGRGSFKTVYRaFDTEEGIEV----AWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLD-EEGHIKLTDFGLSKESIDHekKAY 226
Cdd:cd13983   84 MTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQS--FAK 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768032625 227 SFCGTVEYMAPEVVNRrGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd13983  162 SVIGTPEFMAPEMYEE-HYDEKVDIYAFGMCLLEMATGEYPY 202
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
66-310 4.01e-21

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: 94.17  E-value: 4.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKISGSDArqlYAmkvLKKATLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAF------ 137
Cdd:cd14048    6 TDFEPIQCLGRGGFGVVFEAKNKVDDCN---YA---VKRIRLPNNELAREKVLREVraLAKLDHPGIVRYFNAWlerppe 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 -----QTEGKLYLILDFLRGGDLFTRLSKEVMFTEED---VKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd14048   80 gwqekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 210 TDFGLS------------KESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLtgtLPFQGK-DRKET 276
Cdd:cd14048  160 GDFGLVtamdqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFSTQmERIRT 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 277 MTMILKAKLGmPQFLS--PEAQSLLRMLFKRNPANR 310
Cdd:cd14048  237 LTDVRKLKFP-ALFTNkyPEERDMVQQMLSPSPSER 271
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
434-682 4.09e-21

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 93.95  E-value: 4.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKAtnMEFAVKiidKSKRDPTEEIEI----------LLRYGQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14146    2 IGVGGFGKVYRATWKG--QEVAVK---AARQDPDEDIKAtaesvrqeakLFSMLRHPNIIKLEGVCLEEPNLCLVMEFAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELlDKIL------RQKFFSEREASAVLFT----ITKTVEYLHAQGVV---HRDLKPSNILYV-----DESGNpESIRI 565
Cdd:cd14146   77 GGTL-NRALaaanaaPGPRRARRIPPHILVNwavqIARGMLYLHEEAVVpilHRDLKSSNILLLekiehDDICN-KTLKI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 566 CDFGFAKQLRAENGllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDDTPeeILARIGSGKFS 645
Cdd:cd14146  155 TDFGLAREWHRTTK--MSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY-RGIDGLA--VAYGVAVNKLT 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 768032625 646 LsggywnSVSDTAKDLVSKML----HVDPHQRLTAALVLRH 682
Cdd:cd14146  230 L------PIPSTCPEPFAKLMkecwEQDPHIRPSFALILEQ 264
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
74-299 4.19e-21

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: 93.86  E-value: 4.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVflVKKISGSDARQL-YAMKVLKKATLK-VRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGkLYLILDFLR 151
Cdd:cd05115   12 LGSGNFGCV--KKGVYKMRKKQIdVAIKVLKQGNEKaVRDEMMR--EAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMAS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLS-KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE--SIDHEKKAYSF 228
Cdd:cd05115   87 GGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAlgADDSYYKARSA 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 229 CG-TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQSLL 299
Cdd:cd05115  167 GKwPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFIEQGKrMDCPAECPPEMYALM 240
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
479-684 4.46e-21

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: 93.92  E-value: 4.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYDDGKYVYV-VTELMKGGELlDKILRQ-KFFSEREASAVLFTITKTVEYL--HAQGVVHRDLKPSNILYv 554
Cdd:cd13990   63 HPRIVKLYDVFEIDTDSFCtVLEYCDGNDL-DFYLKQhKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILL- 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 555 DESGNPESIRICDFGFAKQLRAENGLLMTPCYTANFVA------PEVLKRQG----YDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd13990  141 HSGNVSGEIKITDFGLSKIMDDESYNSDGMELTSQGAGtywylpPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPF 220
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 625 anGPDDTPEEIL-------ARIGSGKFSlsggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd13990  221 --GHNQSQEAILeentilkATEVEFPSK------PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
434-713 4.48e-21

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: 94.74  E-value: 4.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII--DKSKR----DPTEEIEILLRYgQHPNIITLKDVYDdGKY---VYVVTELMKG 504
Cdd:cd07845   15 IGEGTYGIVYRARDTTSGEIVALKKVrmDNERDgipiSSLREITLLLNL-RHPNIVELKEVVV-GKHldsIFLVMEYCEQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 --GELLDKILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGlLM 582
Cdd:cd07845   93 dlASLLDNMPTP--FSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKG----CLKIADFGLARTYGLPAK-PM 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPC-YTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGyTPFANGPDD------------TPEE-----ILARIGSGK 643
Cdd:cd07845  166 TPKvVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAH-KPLLPGKSEieqldliiqllgTPNEsiwpgFSDLPLVGK 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 644 FSLSGGYWNS-------VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIvhwdqlpqyqlnrQDAPHLVKGAMAATY 713
Cdd:cd07845  245 FTLPKQPYNNlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSYF-------------KEKPLPCEPEMMPTF 308
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
66-310 5.35e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 98.66  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625   66 SQFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAF--QTEGKL 143
Cdd:PTZ00266   13 NEYEVIKKIGNGRFGEVFLVKH---KRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  144 YLILDFLRGGDLFTRLSK-EVMF---TEEDVKFYLAELALALDHLHSLG-------IIYRDLKPENILLDEE-GHI---- 207
Cdd:PTZ00266   90 YILMEFCDAGDLSRNIQKcYKMFgkiEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLSTGiRHIgkit 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  208 ------------KLTDFGLSKeSIDHEKKAYSFCGTVEYMAPEVV--NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR 273
Cdd:PTZ00266  170 aqannlngrpiaKIGDFGLSK-NIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFHKANN 248
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 768032625  274 KETMTMILKAKLGMP-QFLSPEAQSLLRMLFKRNPANR 310
Cdd:PTZ00266  249 FSQLISELKRGPDLPiKGKSKELNILIKNLLNLSAKER 286
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
498-691 6.10e-21

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: 93.66  E-value: 6.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFA-----K 572
Cdd:cd05606   76 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANIL-LDEHGH---VRISDLGLAcdfskK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGllmtpcyTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSggyw 651
Cdd:cd05606  152 KPHASVG-------THGYMAPEVLqKGVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELP---- 220
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRL-----TAALVLRHPWI--VHWDQL 691
Cdd:cd05606  221 DSFSPELKSLLEGLLQRDVSKRLgclgrGATEVKEHPFFkgVDWQQV 267
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
71-310 6.29e-21

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: 93.30  E-value: 6.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKkISGSDARQLYAMkVLKKATLKVRDRVRT---KMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05046   10 ITTLGRGEFGEVFLAK-AKGIEEEGGETL-VLVKALQKTKDENLQsefRRELDMFRKLSHKNVVRLLGLCREAEPHYMIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDL--FTRLSKEVMFTEE----DVKFYLA---ELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd05046   88 EYTDLGDLkqFLRATKSKDEKLKppplSTKQKVAlctQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDV 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 IDHEkkAYSFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAKLGMPQflsPE 294
Cdd:cd05046  168 YNSE--YYKLRNAlipLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELPV---PE 242
                        250       260
                 ....*....|....*....|.
gi 768032625 295 A-QSLLRMLFKR----NPANR 310
Cdd:cd05046  243 GcPSRLYKLMTRcwavNPKDR 263
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
425-633 7.35e-21

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: 92.98  E-value: 7.35e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 425 TDGYEVKEDIGVGSYSVCKRCIHKATNME--FAVKIIDKSKRDPTEEIEI-LLRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14112    2 TGRFSFGSEIFRGRFSVIVKAVDSTTETDahCAVKIFEVSDEASEAVREFeSLRTLQHENVQRLIAAFKPSNFAYLVMEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdeSGNPESIRICDFGFAKQLraeNGLL 581
Cdd:cd14112   82 LQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQ--SVRSWQVKLVDFGRAQKV---SKLG 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 582 MTP-CYTANFVAPEVLK-RQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPE 633
Cdd:cd14112  156 KVPvDGDTDWASPEFHNpETPITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEE 209
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
423-684 9.08e-21

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: 93.92  E-value: 9.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDgYEVKEDIGVGSYSVCKRCIHKATNMEFAVK-IIDKSKRD-----PTEEIEILLRYgQHPNIITLKD-VYDDGK-- 493
Cdd:cd07866    6 KLRD-YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDgfpitALREIKILKKL-KHPNVVPLIDmAVERPDks 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 -----YVYVVTELMK---GGELLDKILRqkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRI 565
Cdd:cd07866   84 krkrgSVYMVTPYMDhdlSGLLENPSVK---LTESQIKCYMLQLLEGINYLHENHILHRDIKAANIL-IDNQGI---LKI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 566 CDFGFAKQLRAENGLLMTPC------YTANFV-----APE-VLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPD-DTP 632
Cdd:cd07866  157 ADFGLARPYDGPPPNPKGGGgggtrkYTNLVVtrwyrPPElLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDiDQL 236
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 633 EEILARIGS-------GKFSLSGG----------------YWNSVSDTAkDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07866  237 HLIFKLCGTpteetwpGWRSLPGCegvhsftnyprtleerFGKLGPEGL-DLLSKLLSLDPYKRLTASDALEHPY 310
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
64-310 1.02e-20

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: 92.47  E-value: 1.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFlvkkisgsdaRQLY------AMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLhYAF 137
Cdd:cd05068    6 DRKSLKLLRKLGSGQFGEVW----------EGLWnnttpvAVKTLKPGTMDPEDFLR---EAQIMKKLRHPKLIQL-YAV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QT-EGKLYLILDFLRGGDLFTRLSKE--VMFTEEDVKFyLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05068   72 CTlEEPIYIITELMKHGSLLEYLQGKgrSLQLPQLIDM-AAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKeSIDHEKKAYSFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMiLKAKLGMPQF 290
Cdd:cd05068  151 AR-VIKVEDEYEAREGAkfpIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQ-VERGYRMPCP 228
                        250       260
                 ....*....|....*....|..
gi 768032625 291 LSPEAQSLLRML--FKRNPANR 310
Cdd:cd05068  229 PNCPPQLYDIMLecWKADPMER 250
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
70-275 1.16e-20

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: 92.76  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVflvkkISGSDARQLYAMKVLKKaTLKVRDRVRTKMErDILVEV------NHPFIVKL-HYAFQ-TEG 141
Cdd:cd05075    4 LGKTLGEGEFGSV-----MEGQLNQDDSVLKVAVK-TMKIAICTRSEME-DFLSEAvcmkefDHPNVMRLiGVCLQnTES 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLY----LILDFLRGGDL-----FTRLSKEVMF--TEEDVKFyLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLT 210
Cdd:cd05075   77 EGYpspvVILPFMKHGDLhsfllYSRLGDCPVYlpTQMLVKF-MTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVA 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 211 DFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKE 275
Cdd:cd05075  156 DFGLSKKiyNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSE 223
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
74-262 1.23e-20

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: 92.17  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgsdaRQLYAMKVLKKATLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14065    1 LGKGFFGEVYKVTH------RETGKVMVMKELKRFDEQRSFLK-EVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLA-ELALALDHLHSLGIIYRDLKPENILLDEEGHIK---LTDFGLSKESIDH------EK 223
Cdd:cd14065   74 TLEELLKSMDEQLPWSQRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDEktkkpdRK 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14065  154 KRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
66-307 1.27e-20

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: 92.75  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 145
Cdd:cd07848    1 NKFEVLGVVGEGAYG---VVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGG--DLFTRLSKEVMftEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd07848   78 VFEYVEKNmlELLEEMPNGVP--PEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYS-FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPqflsPEAQSllrmL 302
Cdd:cd07848  156 ANYTeYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLP----AEQMK----L 227

                 ....*
gi 768032625 303 FKRNP 307
Cdd:cd07848  228 FYSNP 232
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
70-310 1.47e-20

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: 93.15  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVFLVKKIsGSDARQ-----LYAMKVLKK-ATLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEGKL 143
Cdd:cd05098   17 LGKPLGEGCFGQVVLAEAI-GLDKDKpnrvtKVAVKMLKSdATEKDLSDLISEMEMMKMIG-KHKNIINLLGACTQDGPL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDL--FTRLSK--------------EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI 207
Cdd:cd05098   95 YVIVEYASKGNLreYLQARRppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVM 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 208 KLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA- 283
Cdd:cd05098  175 KIADFGLARDihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKLLKEGh 254
                        250       260
                 ....*....|....*....|....*..
gi 768032625 284 KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05098  255 RMDKPSNCTNELYMMMRDCWHAVPSQR 281
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
454-695 1.61e-20

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: 93.79  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 454 FAVKIIDKSK---RDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLF 527
Cdd:cd05610   32 YAVKVVKKADminKNMVHQVQAerdALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYIS 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 528 TITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK-QLRAE---NGLLMTPCY----------------- 586
Cdd:cd05610  112 EVALALDYLHRHGIIHRDLKPDNML-ISNEGH---IKLTDFGLSKvTLNRElnmMDILTTPSMakpkndysrtpgqvlsl 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 --------------------------------TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEE 634
Cdd:cd05610  188 isslgfntptpyrtpksvrrgaarvegerilgTPDYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFN---DETPQQ 264
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 635 ILARIGSGKFSLSGGYwNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI--VHWDQLpQYQ 695
Cdd:cd05610  265 VFQNILNRDIPWPEGE-EELSVNAQNAIEILLTMDPTKRAGLKELKQHPLFhgVDWENL-QNQ 325
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
426-662 1.68e-20

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 94.34  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI-------EILLRyGQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd05628    1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVghiraerDILVE-ADSLWVVKMFYSFQDKLNLYLI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQL---- 574
Cdd:cd05628   80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLL-LDSKGH---VKLSDFGLCTGLkkah 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 -------------------------------RAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTP 623
Cdd:cd05628  156 rtefyrnlnhslpsdftfqnmnskrkaetwkRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 624 FANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLV 662
Cdd:cd05628  236 FCS---ETPQETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
76-311 1.83e-20

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: 91.61  E-value: 1.83e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  76 QGSFGKVFLVKKISGSD--ARQLYAMKVLKKATLKVRDRVRtkmerdilvevnHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd13995   14 RGAFGKVYLAQDTKTKKrmACKLIPVEQFKPSDVEIQACFR------------HENIAELYGALLWEETVHLFMEAGEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIkLTDFGLSKESIDHEKKAYSFCGTVE 233
Cdd:cd13995   82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 234 YMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKET----MTMILKAK---LGMPQFLSPEAQSLLRMLFKRN 306
Cdd:cd13995  161 YMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQApplEDIAQDCSPAMRELLEAALERN 240

                 ....*
gi 768032625 307 PANRL 311
Cdd:cd13995  241 PNHRS 245
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
68-262 2.01e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 93.79  E-value: 2.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDarqlyamkvlkKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:PHA03209  68 YTVIKTLTPGSEGRVFVATKPGQPD-----------PVVLKIGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGgDLFTRLSKEVMFTEEDVKFYLAELAL-ALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDhEKKAY 226
Cdd:PHA03209 137 PHYSS-DLYTYLTKRSRPLPIDQALIIEKQILeGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVV-APAFL 214
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 768032625 227 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:PHA03209 215 GLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
72-333 2.01e-20

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: 91.95  E-value: 2.01e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDArqlyAMKVLKKATLKVRDRvrtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFL 150
Cdd:cd13982    7 KVLGYGSEGTIVFRGTFDGRPV----AVKRLLPEFFDFADR-----EVQLLRESdEHPNVIRYFCTEKDRQFLYIALELC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGG--DLFT--RLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD-----EEGHIKLTDFGLSKESidh 221
Cdd:cd13982   78 AASlqDLVEspRESKLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahGNVRAMISDFGLCKKL--- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSF------CGTVEYMAPEVVN---RRGHTQSADWWSFGVLMFEMLTGTL-PFQGKDRKEtmTMILKAKLGMPQFL 291
Cdd:cd13982  155 DVGRSSFsrrsgvAGTSGWIAPEMLSgstKRRQTRAVDIFSLGCVFYYVLSGGShPFGDKLERE--ANILKGKYSLDKLL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 292 S-----PEAQSLLRMLFKRNPANRlvnpfligagPDgVEEIKRHSFF 333
Cdd:cd13982  233 SlgehgPEAQDLIERMIDFDPEKR----------PS-AEEVLNHPFF 268
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
64-292 2.12e-20

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: 91.48  E-value: 2.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKISGSDArqlyAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05113    2 DPKDLTFLKELGTGQFGVVKYGKWRGQYDV----AIKMIKEGSMSEDEFIE---EAKVMMNLSHEKLVQLYGVCTKQRPI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd05113   75 FIITEYMANGCLLNYLrEMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 223 KKaySFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLS 292
Cdd:cd05113  155 YT--SSVGSkfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGlRLYRPHLAS 227
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
434-693 2.35e-20

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: 93.76  E-value: 2.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd05629    9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSemfKKDQLAHVKAerdVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDF----GFAKQ---------- 573
Cdd:cd05629   89 MTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNIL-IDRGGH---IKLSDFglstGFHKQhdsayyqkll 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 --------LRAENGLLM-------------------------TPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTG 620
Cdd:cd05629  165 qgksnknrIDNRNSVAVdsinltmsskdqiatwkknrrlmaySTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLIG 244
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 621 YTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLhVDPHQRL---TAALVLRHPWI--VHWDQLPQ 693
Cdd:cd05629  245 WPPFCS---ENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLI-TNAENRLgrgGAHEIKSHPFFrgVDWDTIRQ 318
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
434-684 2.46e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 92.90  E-value: 2.46e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFA---VKIIDKSKRDPTE---------------EIEILlRYGQHPNIITLKDVYDDGKYV 495
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDrqlvgmcgihfttlrELKIM-NEIKHENIMGLVDVYVEGDFI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGelLDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGnpeSIRICDFGFA--- 571
Cdd:PTZ00024  96 NLVMDIMASD--LKKVVDRKiRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANI-FINSKG---ICKIADFGLArry 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 ----------KQLRAENGLLMTP-CYTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARI 639
Cdd:PTZ00024 170 gyppysdtlsKDETMQRREEMTSkVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLF---PGENEIDQLGRI 246
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 640 gsgkFSLSG----------------------------GYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:PTZ00024 247 ----FELLGtpnednwpqakklplyteftprkpkdlkTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEY 315
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
455-685 2.81e-20

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: 92.92  E-value: 2.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDG--------------KYVYVVTELMKGGelLDKILRQKF 516
Cdd:cd07854   34 AVKKIvltdPQSVKHALREIKIIRRL-DHDNIVKVYEVLGPSgsdltedvgsltelNSVYIVQEYMETD--LANVLEQGP 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 517 FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPES--IRICDFGFAKQLRAE---NGLLMTPCYTANFV 591
Cdd:cd07854  111 LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFI-----NTEDlvLKIGDFGLARIVDPHyshKGYLSEGLVTKWYR 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 592 APE-VLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPD----------------DTPEEILARIGSgKFSLSGGYWN-- 652
Cdd:cd07854  186 SPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHEleqmqlilesvpvvreEDRNELLNVIPS-FVRNDGGEPRrp 264
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 653 ------SVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07854  265 lrdllpGVNPEALDFLEQILTFNPMDRLTAEEALMHPYM 303
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
428-685 3.11e-20

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 92.22  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCI-HKaTNMEFAVKIIDKSKRDPTE---EIEIL--LRYG---QHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14210   15 YEVLSVLGKGSFGQVVKCLdHK-TGQLVAIKIIRNKKRFHQQalvEVKILkhLNDNdpdDKHNIVRYKDSFIFRGHLCIV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMkGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgNPESIRICDFG---Fakq 573
Cdd:cd14210   94 FELL-SINLYELLKSNNFqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQP--SKSSIKVIDFGsscF--- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 lraENGLLmtpcYT---ANFV-APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARI---------- 639
Cdd:cd14210  168 ---EGEKV----YTyiqSRFYrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLF---PGENEEEQLACImevlgvppks 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 640 -------------GSGK---FSLSGG---YWNSVSDTAK---------DLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14210  238 lidkasrrkkffdSNGKprpTTNSKGkkrRPGSKSLAQVlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
70-310 3.38e-20

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: 92.33  E-value: 3.38e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVFLVKKISGSDARQ----LYAMKVLK-KATLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05099   16 LGKPLGEGCFGQVVRAEAYGIDKSRPdqtvTVAVKMLKdNATDKDLADLISEMELMKLIG-KHKNIINLLGVCTQEGPLY 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDL-----------------FTRLSKEVMfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHI 207
Cdd:cd05099   95 VIVEYAAKGNLreflrarrppgpdytfdITKVPEEQL-SFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVM 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 208 KLTDFGLSK--ESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA- 283
Cdd:cd05099  174 KIADFGLARgvHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFKLLREGh 253
                        250       260
                 ....*....|....*....|....*..
gi 768032625 284 KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05099  254 RMDKPSNCTHELYMLMRECWHAVPTQR 280
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
74-275 3.43e-20

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: 90.53  E-value: 3.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVF--------LVKKISGSD--ARQLYAMK----VLKKATlkvrdrvrtkmerdilvEVNhpfiVKLHYAFQT 139
Cdd:cd14062    1 IGSGSFGTVYkgrwhgdvAVKKLNVTDptPSQLQAFKnevaVLRKTR-----------------HVN----ILLFMGYMT 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLskEVMfteeDVKFYLAEL-------ALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDF 212
Cdd:cd14062   60 KPQLAIVTQWCEGSSLYKHL--HVL----ETKFEMLQLidiarqtAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDF 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 213 GL----SKESIDHEKKAYSfcGTVEYMAPEVVNRRG---HTQSADWWSFGVLMFEMLTGTLPFQGKDRKE 275
Cdd:cd14062  134 GLatvkTRWSGSQQFEQPT--GSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
428-688 3.57e-20

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 92.84  E-value: 3.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE-----ILLRYGQHPNIITLKDVYDDGKY------VY 496
Cdd:cd07874   19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRayrelVLMKCVNHKNIISLLNVFTPQKSleefqdVY 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGelLDKILRQKFFSEReASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQlrA 576
Cdd:cd07874   99 LVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC----TLKILDFGLART--A 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 ENGLLMTP-CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPD--DTPEEILARIGS------------ 641
Cdd:cd07874  170 GTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFP-GRDyiDQWNKVIEQLGTpcpefmkklqpt 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 642 ----------------------GKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHW 688
Cdd:cd07874  249 vrnyvenrpkyagltfpklfpdSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPYINVW 317
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
448-674 3.82e-20

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: 91.50  E-value: 3.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 448 KATNMEFAVKIIDKS--KRDPTEEIEIL----LRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRqkfFSER- 520
Cdd:cd05607   24 KNTGQMYACKKLDKKrlKKKSGEKMALLekeiLEKVNSPFIVSLAYAFETKTHLCLVMSLMNGGDLKYHIYN---VGERg 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 521 -EASAVLF---TITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRaENGLLMTPCYTANFVAPEVL 596
Cdd:cd05607  101 iEMERVIFysaQITCGILHLHSLKIVYRDMKPENVL-LDDNGN---CRLSDLGLAVEVK-EGKPITQRAGTNGYMAPEIL 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 597 KRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTP-EEILARIGSGKFSLSGgywNSVSDTAKDLVSKMLHVDPHQRL 674
Cdd:cd05607  176 KEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSkEELKRRTLEDEVKFEH---QNFTEEAKDICRLFLAKKPENRL 251
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
71-288 4.28e-20

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: 91.22  E-value: 4.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVK-KISGSdarqlyaMKVLKKATLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd07871   10 LDKLGEGTYATVFKGRsKLTEN-------LVALKEIRLEHEEGAPCTAIREVslLKNLKHANIVTLHDIIHTERCLTLVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGgDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAY 226
Cdd:cd07871   83 EYLDS-DLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYS 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 227 SFCGTVEYMAPEVVnrRGHTQSA---DWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07871  162 NEVVTLWYRPPDVL--LGSTEYStpiDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRL-LGTP 223
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
66-310 4.56e-20

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 91.62  E-value: 4.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVKKI-SGSDARQLYAMKVLKKATL-KVRDRVRTkmERDILVEVNHPFIVKLhYAFQTEGKL 143
Cdd:cd05108    7 TEFKKIKVLGSGAFGTVYKGLWIpEGEKVKIPVAIKELREATSpKANKEILD--EAYVMASVDNPHVCRL-LGICLTSTV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGGDL--FTRLSKEVMFTEEDVKfYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd05108   84 QLITQLMPFGCLldYVREHKDNIGSQYLLN-WCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTV--EYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQS 297
Cdd:cd05108  163 EKEYHAEGGKVpiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEISSILEKGeRLPQPPICTIDVYM 242
                        250
                 ....*....|...
gi 768032625 298 LLRMLFKRNPANR 310
Cdd:cd05108  243 IMVKCWMIDADSR 255
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
62-310 5.28e-20

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: 90.47  E-value: 5.28e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADPSQ-FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKkatLKVRDRVRTKMERDILV-EVNHPFIVKLHYAFQT 139
Cdd:cd06646    4 RRNPQHdYELIQRVGSGTYGDVYKARNLHTG---ELAAVKIIK---LEPGDDFSLIQQEIFMVkECKHCNIVAYFGSYLS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd06646   78 REKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKIT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVV---NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF-----L 291
Cdd:cd06646  158 ATIAKRKSFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPKLkdktkW 237
                        250
                 ....*....|....*....
gi 768032625 292 SPEAQSLLRMLFKRNPANR 310
Cdd:cd06646  238 SSTFHNFVKISLTKNPKKR 256
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
447-673 5.34e-20

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: 91.13  E-value: 5.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 447 HKATNMEFAVK-----IIDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYV-----YVVTELMKGGEL---LDKILR 513
Cdd:cd14039   14 NQETGEKIAIKscrleLSVKNKDRWCHEIQIMKKL-NHPNVVKACDVPEEMNFLvndvpLLAMEYCSGGDLrklLNKPEN 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 514 QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESiRICDFGFAKQLraENGLLMTPCY-TANFVA 592
Cdd:cd14039   93 CCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKIVH-KIIDLGYAKDL--DQGSLCTSFVgTLQYLA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 593 PEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANG----------PDDTPEEILA---RIGSGKFSLSGGYWNSVS---- 655
Cdd:cd14039  170 PELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNlqpftwhekiKKKDPKHIFAveeMNGEVRFSTHLPQPNNLCsliv 249
                        250
                 ....*....|....*...
gi 768032625 656 DTAKDLVSKMLHVDPHQR 673
Cdd:cd14039  250 EPMEGWLQLMLNWDPVQR 267
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
432-684 5.99e-20

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: 90.62  E-value: 5.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKII--DKSKRDPTEEI-EI-LLRYGQHPNIITLKDVyddgkyVYVVTELMKGGEL 507
Cdd:cd07836    6 EKLGEGTYATVYKGRNRTTGEIVALKEIhlDAEEGTPSTAIrEIsLMKELKHENIVRLHDV------IHTENKLMLVFEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAV--------LFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENG 579
Cdd:cd07836   80 MDKDLKKYMDTHGVRGALdpntvksfTYQLLKGIAFCHENRVLHRDLKPQNLL-INKRGE---LKLADFGLARAFGIPVN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDtpEEILARIgsgkFSLSG----GYWNSV 654
Cdd:cd07836  156 TFSNEVVTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMITGRPLFP-GTNN--EDQLLKI----FRIMGtpteSTWPGI 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 655 SD-------------------------TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07836  229 SQlpeykptfpryppqdlqqlfphadpLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
68-310 7.09e-20

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: 90.43  E-value: 7.09e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAmkvLKKATLKVRDRVRTKM-ERDILVEVNHPFIVKL-HYAFQTEGK--- 142
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLS---TGRLYA---LKKILCHSKEDVKEAMrEIENYRLFNHPNILRLlDSQIVKEAGgkk 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 -LYLILDFLRGG---DLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSL---GIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd13986   76 eVYLLLPYYKRGslqDEIERRLVKgTFFPEDRILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVLLSEDDEPILMDLGS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 ----------SKESIDHEKKAYSFCgTVEYMAPEVVNRRGH---TQSADWWSFGVLMFEMLTGTLPFQGK-DRKETMTM- 279
Cdd:cd13986  156 mnparieiegRREALALQDWAAEHC-TMPYRAPELFDVKSHctiDEKTDIWSLGCTLYALMYGESPFERIfQKGDSLALa 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 280 ILKAKLGMPQ--FLSPEAQSLLRMLFKRNPANR 310
Cdd:cd13986  235 VLSGNYSFPDnsRYSEELHQLVKSMLVVNPAER 267
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
67-310 7.12e-20

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: 90.42  E-value: 7.12e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVrdrvrTKMERDILVEV-NHPFIVKL--HYAFQTEGKL 143
Cdd:cd14037    4 HVTIEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNV-----CKREIEIMKRLsGHKNIVGYidSSANRSGNGV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 Y---LILDFLRGGDLF----TRLSkeVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd14037   79 YevlLLMEYCKGGGVIdlmnQRLQ--TGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESI------------DHEKKAYSfcgTVEYMAPEVVN---RRGHTQSADWWSFGVLMFEMLTGTLPFQgkdrkETMTM 279
Cdd:cd14037  157 ATTKIlppqtkqgvtyvEEDIKKYT---TLQYRAPEMIDlyrGKPITEKSDIWALGCLLYKLCFYTTPFE-----ESGQL 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 280 -ILKAKLGMPQF--LSPEAQSLLRMLFKRNPANR 310
Cdd:cd14037  229 aILNGNFTFPDNsrYSKRLHKLIRYMLEEDPEKR 262
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
479-632 7.23e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 94.09  E-value: 7.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDES 557
Cdd:NF033483  66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKD-YIREHGpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-ITKD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 558 GNpesIRICDFGFAkqlRAENGLLMTpcYTANFV------APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGpdDT 631
Cdd:NF033483 144 GR---VKVTDFGIA---RALSSTTMT--QTNSVLgtvhylSPEQARGGTVDARSDIYSLGIVLYEMLTGRPPF-DG--DS 212

                 .
gi 768032625 632 P 632
Cdd:NF033483 213 P 213
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
67-274 7.34e-20

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


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 91.19  E-value: 7.34e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARqLYAMKVLKkATLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAF--QTEGK 142
Cdd:cd07842    1 KYEIEGCIGRGTYGRVYKAKRKNGKDGK-EYAIKKFK-GDKEQYTGISQSACREIalLRELKHENVVSLVEVFleHADKS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGgDL-----FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFG 213
Cdd:cd07842   79 VYLLFDYAEH-DLwqiikFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLG 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 214 LSKESIDHEKKAYSFCG---TVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK 274
Cdd:cd07842  158 LARLFNAPLKPLADLDPvvvTIWYRAPELLlGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAK 222
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-690 7.51e-20

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: 90.96  E-value: 7.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-----KSKRDPTEEIEILlrygqH----PNIITLKDV-YDDGKyV 495
Cdd:cd06615    1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHleikpAIRNQIIRELKVL-----HecnsPYIVGFYGAfYSDGE-I 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMKGGELlDKILRQkffSEREASAVLFTITKTV----EYLHAQ-GVVHRDLKPSNILyVDESGNpesIRICDFGF 570
Cdd:cd06615   75 SICMEHMDGGSL-DQVLKK---AGRIPENILGKISIAVlrglTYLREKhKIMHRDVKPSNIL-VNSRGE---IKLCDFGV 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLRaeNGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTG----------------------------YT 622
Cdd:cd06615  147 SGQLI--DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrypipppdakeleamfgrpvsegeakesHR 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 623 PFANGPDDTPE-----EILARIGSGKF-SLSGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQ 690
Cdd:cd06615  225 PVSGHPPDSPRpmaifELLDYIVNEPPpKLPSGAF---SDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAEL 295
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
434-706 8.94e-20

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: 92.00  E-value: 8.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSY-SVCKRCiHKATNMEFAVKIIDKS---KRDPTEEIEI---LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05626    9 LGIGAFgEVCLAC-KVDTHALYAMKTLRKKdvlNRNQVAHVKAerdILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLR----------- 575
Cdd:cd05626   88 MMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNIL-IDLDGH---IKLTDFGLCTGFRwthnskyyqkg 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 ------------------------------------AENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05626  164 shirqdsmepsdlwddvsncrcgdrlktleqratkqHQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 620 GYTPFAnGPddTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQ--RLTAALVLRHPWIVHWDQlpQYQLN 697
Cdd:cd05626  244 GQPPFL-AP--TPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFSEVDF--SSDIR 318

                 ....*....
gi 768032625 698 RQDAPHLVK 706
Cdd:cd05626  319 TQPAPYVPK 327
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
74-310 9.25e-20

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 89.87  E-value: 9.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLV-KKISGsdarqLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 152
Cdd:cd14027    1 LDSGGFGKVSLCfHRTQG-----LVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKevMFTEEDVK-FYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG---------LSKESIDHE 222
Cdd:cd14027   76 GNLMHVLKK--VSVPLSVKgRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTKEEHNEQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFC----GTVEYMAPE---VVNRRGhTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAK-----LGMPQF 290
Cdd:cd14027  154 REVDGTAkknaGTLYYMAPEhlnDVNAKP-TEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGnrpdvDDITEY 232
                        250       260
                 ....*....|....*....|
gi 768032625 291 LSPEAQSLLRMLFKRNPANR 310
Cdd:cd14027  233 CPREIIDLMKLCWEANPEAR 252
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
434-630 1.02e-19

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: 89.64  E-value: 1.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSvckrCIHKAT---NMEFAVKIID-----KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd14066    1 IGSGGFG----TVYKGVlenGTVVAVKRLNemncaASKKEFLTELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEYMPNG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDkilrqkFFSEREASAVL---------FTITKTVEYLHAQG---VVHRDLKPSNILyVDESGNPesiRICDFGFAKQ 573
Cdd:cd14066   76 SLED------RLHCHKGSPPLpwpqrlkiaKGIARGLEYLHEECpppIIHGDIKSSNIL-LDEDFEP---KLTDFGLARL 145
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 574 LRAENGLLMT--PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDD 630
Cdd:cd14066  146 IPPSESVSKTsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENREN 204
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
66-280 1.08e-19

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: 90.13  E-value: 1.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVF---LVKKISGSDArQLYAMKVLKK-ATLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd05048    5 SAVRFLEELGEGAFGKVYkgeLLGPSSEESA-ISVAIKTLKEnASPKTQQDFRR--EAELMSDLQHPNIVCLLGVCTKEQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLFTRL-----SKEVMFTEEDVKF----------YLA-ELALALDHLHSLGIIYRDLKPENILLDEEG 205
Cdd:cd05048   82 PQCMLFEYMAHGDLHEFLvrhspHSDVGVSSDDDGTassldqsdflHIAiQIAAGMEYLSSHHYVHRDLAARNCLVGDGL 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 206 HIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI 280
Cdd:cd05048  162 TVKISDFGLSRDiySSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMI 239
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
424-682 1.13e-19

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: 89.47  E-value: 1.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSY-SVCKrCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDG---------- 492
Cdd:cd14047    4 FRQDFKEIELIGSGGFgQVFK-AKHRIDGKTYAIKRVKLNNEKAEREVKALAKL-DHPNIVRYNGCWDGFdydpetsssn 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 493 ------KYVYVVTELMKGGEL-----------LDKILRQKFFSEreasavlftITKTVEYLHAQGVVHRDLKPSNILYVD 555
Cdd:cd14047   82 ssrsktKCLFIQMEFCEKGTLeswiekrngekLDKVLALEIFEQ---------ITKGVEYIHSKKLIHRDLKPSNIFLVD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 556 ESgnpeSIRICDFGFAKQLRAENGLLMTPCyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYtpfangpDDTPE-- 633
Cdd:cd14047  153 TG----KVKIGDFGLVTSLKNDGKRTKSKG-TLSYMSPEQISSQDYGKEVDIYALGLILFELLHVC-------DSAFEks 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 634 EILARIGSGKFSLSggyWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd14047  221 KFWTDLRNGILPDI---FDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
69-317 1.17e-19

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: 90.24  E-value: 1.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  69 ELLKVLGQGSFGKVF--LVKKISGSDARQLYAMKVLKkATLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 145
Cdd:cd05055   38 SFGKTLGAGAFGKVVeaTAYGLSKSDAVMKVAVKMLK-PTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILV 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLdEEGHI-KLTDFGLSKEsIDHE 222
Cdd:cd05055  117 ITEYCCYGDLlnFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLL-THGKIvKICDFGLARD-IMND 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGT---VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAKLGM--PQFLSPEAQ 296
Cdd:cd05055  195 SNYVVKGNArlpVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMaqPEHAPAEIY 274
                        250       260
                 ....*....|....*....|.
gi 768032625 297 SLLRMLFKRNPANRLVNPFLI 317
Cdd:cd05055  275 DIMKTCWDADPLKRPTFKQIV 295
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
71-310 1.37e-19

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: 90.94  E-value: 1.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVflvkkISGSDA--RQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL----- 143
Cdd:cd07850    5 LKPIGSGAQGIV-----CAAYDTvtGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 -YLILDFLrGGDLFTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKesidhe 222
Cdd:cd07850   80 vYLVMELM-DANLCQVIQMDL--DHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR------ 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFCGTVE-----YMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMP--QFLSpEA 295
Cdd:cd07850  151 TAGTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIE-QLGTPsdEFMS-RL 228
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd07850  229 QPTVRNYVENRPKYA 243
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
517-683 1.42e-19

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 92.62  E-value: 1.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 517 FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRA--ENGLLMTPCYTANFVAPE 594
Cdd:PTZ00283 140 FREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNG----LVKLGDFGFSKMYAAtvSDDVGRTFCGTPYYVAPE 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 595 VLKRQGYDAACDIWSLGVLLYTMLTGYTPFaNGPDdtPEEILARIGSGKFSlsgGYWNSVSDTAKDLVSKMLHVDPHQRL 674
Cdd:PTZ00283 216 IWRRKPYSKKADMFSLGVLLYELLTLKRPF-DGEN--MEEVMHKTLAGRYD---PLPPSISPEMQEIVTALLSSDPKRRP 289

                 ....*....
gi 768032625 675 TAALVLRHP 683
Cdd:PTZ00283 290 SSSKLLNMP 298
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
67-313 1.61e-19

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: 89.71  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISgsDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVN---HPFIVKLHYAFQT---- 139
Cdd:cd07862    2 QYECVAEIGEGAYGKVFKARDLK--NGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVsrtd 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 -EGKLYLILDFLrGGDLFTRLSK--EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSk 216
Cdd:cd07862   80 rETKLTLVFEHV-DQDLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 esidhekKAYSF-------CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPQ 289
Cdd:cd07862  158 -------RIYSFqmaltsvVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDV-IGLPG 229
                        250       260
                 ....*....|....*....|....*
gi 768032625 290 FLS-PEAQSLLRMLFKRNPANRLVN 313
Cdd:cd07862  230 EEDwPRDVALPRQAFHSKSAQPIEK 254
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
67-288 1.78e-19

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 89.21  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKL---HYAFQTEGKL 143
Cdd:cd05074   10 QFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLigvSLRSRAKGRL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 ---YLILDFLRGGDLFT-----RLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05074   90 pipMVILPFMKHGDLHTfllmsRIGEEpFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 215 SKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMP 288
Cdd:cd05074  170 SKKiySGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLIKGnRLKQP 247
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
68-315 1.82e-19

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: 89.59  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKvlkkatlkvrdrvRTKMER-------------DILVEVNHPFIVKL 133
Cdd:cd07843    7 YEKLNRIEEGTYGVVYRARdKKTG----EIVALK-------------KLKMEKekegfpitslreiNILLKLQHPNIVTV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 HYAF--QTEGKLYLILDFLRGgDLFTRLskEVM---FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIK 208
Cdd:cd07843   70 KEVVvgSNLDKIYMVMEYVEH-DLKSLM--ETMkqpFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 209 LTDFGLSKESIDHEKKAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGM 287
Cdd:cd07843  147 ICDFGLAREYGSPLKPYTQLVVTLWYRAPELLlGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKL-LGT 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 288 PQFLS-PEAQSLL---RMLFKRNPANRLVNPF 315
Cdd:cd07843  226 PTEKIwPGFSELPgakKKTFTKYPYNQLRKKF 257
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
118-310 2.02e-19

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: 88.74  E-value: 2.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 118 ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPE 197
Cdd:cd14112   50 EFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 198 NILLD--EEGHIKLTDFGlSKESIDHEKKAYSfCGTVEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGTLPFQG--KD 272
Cdd:cd14112  129 NIMFQsvRSWQVKLVDFG-RAQKVSKLGKVPV-DGDTDWASPEFHNPETPiTVQSDIWGLGVLTFCLLSGFHPFTSeyDD 206
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768032625 273 RKETMTMILKAKLG---MPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14112  207 EEETKENVIFVKCRpnlIFVEATQEALRFATWALKKSPTRR 247
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
74-302 2.03e-19

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: 88.71  E-value: 2.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISgsdARQLYAMKVlkKATLKVRDRVRtkmeRDILVEVNHPFIVKLHYAFQTEG----KLYLILDF 149
Cdd:cd14025    4 VGSGGFGQVYKVRHKH---WKTWLAIKC--PPSLHVDDSER----MELLEEAKKMEMAKFRHILPVYGicsePVGLVMEY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTeeDVKFYLA-ELALALDHLHSLG--IIYRDLKPENILLDEEGHIKLTDFGLSK---ESIDHEK 223
Cdd:cd14025   75 METGSLEKLLASEPLPW--ELRFRIIhETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 224 KAYSFCGTVEYMAPEVV---NRRGHTQSaDWWSFGVLMFEMLTGTLPFQGKdrKETMTMILKAKLGMPQFLSP------- 293
Cdd:cd14025  153 SRDGLRGTIAYLPPERFkekNRCPDTKH-DVYSFAIVIWGILTQKKPFAGE--NNILHIMVKVVKGHRPSLSPiprqrps 229

                 ....*....
gi 768032625 294 EAQSLLRML 302
Cdd:cd14025  230 ECQQMICLM 238
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
67-298 2.35e-19

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 88.54  E-value: 2.35e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLvKKISGSdarqlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYLI 146
Cdd:cd14150    1 EVSMLKRIGTGSFGTVFR-GKWHGD-----VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAII 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRL----SKEVMFTEEDVKfylAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS--KESID 220
Cdd:cd14150   74 TQWCEGSSLYRHLhvteTRFDTMQLIDVA---RQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAtvKTRWS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSFCGTVEYMAPEVVNRRG---HTQSADWWSFGVLMFEMLTGTLPFQG-KDRKETMTMILKAklgmpqFLSPEAQ 296
Cdd:cd14150  151 GSQQVEQPSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSNiNNRDQIIFMVGRG------YLSPDLS 224

                 ..
gi 768032625 297 SL 298
Cdd:cd14150  225 KL 226
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
63-310 2.49e-19

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: 90.08  E-value: 2.49e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  63 ADP------SQFELLKVLGQGSFGKVFLVKKISGSDARQ----LYAMKVLKK-ATLKVRDRVRTKMERDILVEvNHPFIV 131
Cdd:cd05100    3 ADPkwelsrTRLTLGKPLGEGCFGQVVMAEAIGIDKDKPnkpvTVAVKMLKDdATDKDLSDLVSEMEMMKMIG-KHKNII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 132 KLHYAFQTEGKLYLILDFLRGGDL--FTRLSK--------------EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLK 195
Cdd:cd05100   82 NLLGACTQDGPLYVLVEYASKGNLreYLRARRppgmdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 196 PENILLDEEGHIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKD 272
Cdd:cd05100  162 ARNVLVTEDNVMKIADFGLARDvhNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 241
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 273 RKETMTMILKA-KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05100  242 VEELFKLLKEGhRMDKPANCTHELYMIMRECWHAVPSQR 280
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
433-685 2.66e-19

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: 89.33  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEIL------LRYGQHPNIITLKDVYDDGKYVYVVTE--LMKG 504
Cdd:cd06633   28 EIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEKWQDIikevkfLQQLKHPNTIEYKGCYLKDHTAWLVMEycLGSA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkiLRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesgnPESIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd06633  108 SDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE----PGQVKLADFGSASIASPANSFVGTP 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 CYtanfVAPEV---LKRQGYDAACDIWSLGVLLYTMLTGYTPFAN----------GPDDTPeeilarigsgkfSLSGGYW 651
Cdd:cd06633  182 YW----MAPEVilaMDEGQYDGKVDIWSLGITCIELAERKPPLFNmnamsalyhiAQNDSP------------TLQSNEW 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 652 nsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06633  246 ---TDSFRGFVDYCLQKIPQERPSSAELLRHDFV 276
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
68-288 2.71e-19

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: 89.02  E-value: 2.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKvlkKATLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd07861    2 YTKIEKIGEGTYGVVYKGRnKKTG----QIVAMK---KIRLESEEEgVPSTAIREIslLKELQHPNIVCLEDVLMQENRL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGgDL---FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSID 220
Cdd:cd07861   75 YLVFEFLSM-DLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLAR-AFG 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSF-CGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07861  153 IPVRVYTHeVVTLWYRAPEVlLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRI-LGTP 221
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
434-685 3.01e-19

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: 88.16  E-value: 3.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII-------DKSKRDPTEEIEI-LLRYGQHPNIIT----LKDvyDDGKYVYVVTEL 501
Cdd:cd06653   10 LGRGAFGEVYLCYDADTGRELAVKQVpfdpdsqETSKEVNALECEIqLLKNLRHDRIVQyygcLRD--PEEKKLSIFVEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESGNpesIRICDFGFAKQLRA--ENG 579
Cdd:cd06653   88 MPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILR-DSAGN---VKLGDFGASKRIQTicMSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCY-TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpddtpEEILARIgsgkFSLSGGYWN-----S 653
Cdd:cd06653  164 TGIKSVTgTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAE------YEAMAAI----FKIATQPTKpqlpdG 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 654 VSDTAKDLVsKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06653  234 VSDACRDFL-RQIFVEEKRRPTAEFLLRHPFV 264
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
67-376 3.12e-19

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: 89.09  E-value: 3.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAMKvlkkatlkvrdRVRTKMERD-----------ILVEVNHPFIVKLHY 135
Cdd:cd07864    8 KFDIIGIIGEGTYGQVY---KAKDKDTGELVALK-----------KVRLDNEKEgfpitaireikILRQLNHRSVVNLKE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AF----------QTEGKLYLILDFLrGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd07864   74 IVtdkqdaldfkKDKGAFYLVFEYM-DHDLMGLLeSGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GHIKLTDFGLSKESIDHEKKAYS-FCGTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK 282
Cdd:cd07864  153 GQIKLADFGLARLYNSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 283 AkLGMPqflspeaqsllrmlfkrNPANrlvnpfligaGPDgveeIKRHSFFSTIDWNKLYRREIHPPF----KPATGRPE 358
Cdd:cd07864  233 L-CGSP-----------------CPAV----------WPD----VIKLPYFNTMKPKKQYRRRLREEFsfipTPALDLLD 280
                        330       340
                 ....*....|....*....|
gi 768032625 359 DTFYFDPE--FTAKTPKDSP 376
Cdd:cd07864  281 HMLTLDPSkrCTAEQALNSP 300
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
428-684 3.56e-19

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: 89.46  E-value: 3.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEIL-----LRYGQHPNIITLKDVY-----DDGKYVYV 497
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILreiklLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGelLDKILR---------QKFFsereasavLFTITKTVEYLHAQGVVHRDLKPSNILyvdesGNPE-SIRICD 567
Cdd:cd07859   82 VFELMESD--LHQVIKanddltpehHQFF--------LYQLLRALKYIHTANVFHRDLKPKNIL-----ANADcKLKICD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGllmTPCYTANFV------APEVLKR--QGYDAACDIWSLGVLLYTMLTGyTPFANGPD---------- 629
Cdd:cd07859  147 FGLARVAFNDTP---TAIFWTDYVatrwyrAPELCGSffSKYTPAIDIWSIGCIFAEVLTG-KPLFPGKNvvhqldlitd 222
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 630 ---DTPEEILARIGSGKfslSGGYWNS---------------VSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07859  223 llgTPSPETISRVRNEK---ARRYLSSmrkkqpvpfsqkfpnADPLALRLLERLLAFDPKDRPTAEEALADPY 292
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
423-682 3.69e-19

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: 88.39  E-value: 3.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYD------- 490
Cdd:cd14048    3 RFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIrlpnnELAREKVLREVRALAKL-DHPGIVRYFNAWLerppegw 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 ----DGKYVYVVTELMKGGELLDKILRQKFFSEREASAVL---FTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESI 563
Cdd:cd14048   82 qekmDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVCLnifKQIASAVEYLHSKGLIHRDLKPSNVFFSLD----DVV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 564 RICDFGFAKQLRA----ENGLLMTPCY--------TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTpfangpddT 631
Cdd:cd14048  158 KVGDFGLVTAMDQgepeQTVLTPMPAYakhtgqvgTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFS--------T 229
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 632 PEE---ILARIGSGKFSLSggYWNSVSDTaKDLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd14048  230 QMErirTLTDVRKLKFPAL--FTNKYPEE-RDMVQQMLSPSPSERPEAHEVIEH 280
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
434-685 3.88e-19

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: 87.79  E-value: 3.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII-------DKSKRDPTEEIEI-LLRYGQHPNIIT----LKDVYDdgKYVYVVTEL 501
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQVqfdpespETSKEVNALECEIqLLKNLLHERIVQyygcLRDPQE--RTLSIFMEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESGNpesIRICDFGFAKQLRA---EN 578
Cdd:cd06652   88 MPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILR-DSVGN---VKLGDFGASKRLQTiclSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGpddtpeEILARIgsgkFSLSGGYWNS----- 653
Cdd:cd06652  164 TGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWAEF------EAMAAI----FKIATQPTNPqlpah 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 654 VSDTAKDLVsKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06652  234 VSDHCRDFL-KRIFVEAKLRPSADELLRHTFV 264
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
72-311 5.01e-19

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 87.86  E-value: 5.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVF--LVKKISG-SDARQLYAMKVLKK-ATlkVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05044    1 KFLGSGAFGEVFegTAKDILGdGSGETKVAVKTLRKgAT--DQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAEL-ALALD------HLHSLGIIYRDLKPENILLDEEGH----IKLTDFGLSK 216
Cdd:cd05044   79 ELMEGGDLLSYLRAARPTAFTPPLLTLKDLlSICVDvakgcvYLEDMHFVHRDLAARNCLVSSKDYrervVKIGDFGLAR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 E--SIDHEKKAYSFCGTVEYMAPE-VVNRRGHTQSaDWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILK-AKLGMPQFL 291
Cdd:cd05044  159 DiyKNDYYRKEGEGLLPVRWMAPEsLVDGVFTTQS-DVWAFGVLMWEILTlGQQPYPARNNLEVLHFVRAgGRLDQPDNC 237
                        250       260
                 ....*....|....*....|
gi 768032625 292 SPEAQSLLRMLFKRNPANRL 311
Cdd:cd05044  238 PDDLYELMLRCWSTDPEERP 257
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
64-268 6.39e-19

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: 87.85  E-value: 6.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQ-FELLKVLGQGSFGKVFLVKKISGSdarQLYAMKVLKkatLKVRDRVRTKMERDILVEVNHPFIVKLHY-AF---- 137
Cdd:cd06637    3 DPAGiFELVELVGNGTYGQVYKGRHVKTG---QLAAIKVMD---VTGDEEEEIKQEINMLKKYSHHRNIATYYgAFikkn 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 --QTEGKLYLILDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG 213
Cdd:cd06637   77 ppGMDDQLWLVMEFCGAGSVtdLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQS-----ADWWSFGVLMFEMLTGTLPF 268
Cdd:cd06637  157 VSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDAtydfkSDLWSLGITAIEMAEGAPPL 216
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
477-685 6.87e-19

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: 87.21  E-value: 6.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 477 GQHPNIITLKDVYDDGK-YVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVD 555
Cdd:cd14101   64 PGHRGVIRLLDWFEIPEgFLLVLERPQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 556 ESGNpesIRICDFGFAKQLRAE-----NGllmtpcyTANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFangpd 629
Cdd:cd14101  144 RTGD---IKLIDFGSGATLKDSmytdfDG-------TRVYSPPEWILYHQYHAlPATVWSLGILLYDMVCGDIPF----- 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 630 DTPEEILAriGSGKFSlsggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14101  209 ERDTDILK--AKPSFN------KRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
64-268 7.64e-19

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 87.23  E-value: 7.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVK-KISGSdaRQLY-AMKVLKkATLKVRDRVRTKMERDILVEVNHPFIVKLHyAFQTEG 141
Cdd:cd05066    2 DASCIKIEKVIGAGEFGEVCSGRlKLPGK--REIPvAIKTLK-AGYTEKQRRDFLSEASIMGQFDHPNIIHLE-GVVTRS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLIL-DFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd05066   78 KPVMIVtEYMENGSLDAFLRKhDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLE 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 220 DHEKKAYSFCG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPF 268
Cdd:cd05066  158 DDPEAAYTTRGgkiPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 210
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
72-310 7.71e-19

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: 87.93  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKK--ISGSDARQLYAMKVLKK-ATLKVRDRVRTKMErdILVEV-NHPFIVKLHYAFQT-EGKLYLI 146
Cdd:cd05054   13 KPLGRGAFGKVIQASAfgIDKSATCRTVAVKMLKEgATASEHKALMTELK--ILIHIgHHLNVVNLLGACTKpGGPLMVI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRL-SKEVMF-------------------------TEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL 200
Cdd:cd05054   91 VEFCKFGNLSNYLrSKREEFvpyrdkgardveeeedddelykeplTLEDLICYSFQVARGMEFLASRKCIHRDLAARNIL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 201 LDEEGHIKLTDFGLSKE---SIDHEKKAYSFCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKET 276
Cdd:cd05054  171 LSENNVVKICDFGLARDiykDPDYVRKGDARL-PLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQMDEE 249
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 768032625 277 MTMILK--AKLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05054  250 FCRRLKegTRMRAPEYTTPEIYQIMLDCWHGEPKER 285
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
67-333 7.99e-19

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: 87.49  E-value: 7.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAmkvLKKATLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd07839    1 KYEKLEKIGEGTYGTVF---KAKNRETHEIVA---LKRVRLDDDDEgVPSSALREIclLKELKHKNIVRLYDVLHSDKKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGgDL---FTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSID 220
Cdd:cd07839   75 TLVFEYCDQ-DLkkyFDSCNGDI--DPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR-AFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HEKKAYSF-CGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLP-FQGKDRKETMTMILKAkLGMPQF------- 290
Cdd:cd07839  151 IPVRCYSAeVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRL-LGTPTEeswpgvs 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 291 -----------------------LSPEAQSLLRMLFKRNPANRLvnpfligagpdGVEEIKRHSFF 333
Cdd:cd07839  230 klpdykpypmypattslvnvvpkLNSTGRDLLQNLLVCNPVQRI-----------SAEEALQHPYF 284
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
73-310 8.71e-19

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: 87.28  E-value: 8.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFlvkkiSGSDARQLYAMKVLKKATLKVRDRVRTKM-------------------ERDILVEVNHPFIVKL 133
Cdd:cd14000    1 LLGDGGFGSVY-----RASYKGEPVAVKIFNKHTSSNFANVPADTmlrhlratdamknfrllrqELTVLSHLHHPSIVYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 HYAfqTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELAL----ALDHLHSLGIIYRDLKPENILL-----DEE 204
Cdd:cd14000   76 LGI--GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GHIKLTDFGLSKESIdhEKKAYSFCGTVEYMAPEVVNRR-GHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKa 283
Cdd:cd14000  154 IIIKIADYGISRQCC--RMGAKGSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG- 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 284 klGMPQFLS-------PEAQSLLRMLFKRNPANR 310
Cdd:cd14000  231 --GLRPPLKqyecapwPEVEVLMKKCWKENPQQR 262
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
65-288 9.13e-19

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: 86.95  E-value: 9.13e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVFL-VKKISGSDARQLyAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd05063    4 PSHITKQKVIGAGEFGEVFRgILKMPGRKEVAV-AIKTLKPGYTE-KQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGG--DLFTRlSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd05063   82 MIITEYMENGalDKYLR-DHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDD 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 222 EKKAYSFCG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI-----LKAKLGMP 288
Cdd:cd05063  161 PEGTYTTSGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAIndgfrLPAPMDCP 236
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
469-682 9.76e-19

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: 86.95  E-value: 9.76e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 469 EIEILLRYGQHPNIITLKDVY-----DDGKYVYVVTELMKGGELLD---KILRQKFfSEREASAVLFTITKTVEYLHA-- 538
Cdd:cd14037   50 EIEIMKRLSGHKNIVGYIDSSanrsgNGVYEVLLLMEYCKGGGVIDlmnQRLQTGL-TESEILKIFCDVCEAVAAMHYlk 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 539 QGVVHRDLKPSNILYVDeSGNpesIRICDFGFA--KQLRAENGLLM-----------TPCYTAnfvaPEVL---KRQGYD 602
Cdd:cd14037  129 PPLIHRDLKVENVLISD-SGN---YKLCDFGSAttKILPPQTKQGVtyveedikkytTLQYRA----PEMIdlyRGKPIT 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 603 AACDIWSLGVLLYTMLTGYTPFANGPDdtpeeiLArIGSGKFSLSGgywNSV-SDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd14037  201 EKSDIWALGCLLYKLCFYTTPFEESGQ------LA-ILNGNFTFPD---NSRySKRLHKLIRYMLEEDPEKRPNIYQVSY 270

                 .
gi 768032625 682 H 682
Cdd:cd14037  271 E 271
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
428-685 1.06e-18

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: 87.33  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVckrcIHKATNMEFAVKIIDKSKRDPT----------EEIEILLRYGQ--HPNIITLKDV-----YD 490
Cdd:cd07863    2 YEPVAEIGVGAYGT----VYKARDPHSGHFVALKSVRVQTnedglplstvREVALLKRLEAfdHPNIVRLMDVcatsrTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTE---------LMKG---GELLDKI--LRQKFFSereasavlftitkTVEYLHAQGVVHRDLKPSNILyVDE 556
Cdd:cd07863   78 RETKVTLVFEhvdqdlrtyLDKVpppGLPAETIkdLMRQFLR-------------GLDFLHANCIVHRDLKPENIL-VTS 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 557 SGnpeSIRICDFGFAKQLRAEngLLMTP-CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF-ANGPDDTPEE 634
Cdd:cd07863  144 GG---QVKLADFGLARIYSCQ--MALTPvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFcGNSEADQLGK 218
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 635 ILARIG--------------SGKFSLSG-----GYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07863  219 IFDLIGlppeddwprdvtlpRGAFSPRGprpvqSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
472-688 1.07e-18

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: 88.56  E-value: 1.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 472 ILLRYGQHPNIITLKDVYDDGKY------VYVVTELMKGGelLDKILRQKFFSEReASAVLFTITKTVEYLHAQGVVHRD 545
Cdd:cd07875   75 VLMKCVNHKNIIGLLNVFTPQKSleefqdVYIVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRD 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 546 LKPSNILYVDESgnpeSIRICDFGFAKQlrAENGLLMTP-CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd07875  152 LKPSNIVVKSDC----TLKILDFGLART--AGTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLF 225
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 625 AnGPD--DTPEEILARIGS-----------------------GKFSLSGGYWNSV-----------SDTAKDLVSKMLHV 668
Cdd:cd07875  226 P-GTDhiDQWNKVIEQLGTpcpefmkklqptvrtyvenrpkyAGYSFEKLFPDVLfpadsehnklkASQARDLLSKMLVI 304
                        250       260
                 ....*....|....*....|
gi 768032625 669 DPHQRLTAALVLRHPWIVHW 688
Cdd:cd07875  305 DASKRISVDEALQHPYINVW 324
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
66-283 1.27e-18

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: 87.91  E-value: 1.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVF-----------LVKKISGSDARQLyamkvlKKATLKVRdrvrtkmerdILVEVNHPFIVKLH 134
Cdd:cd07854    5 SRYMDLRPLGCGSNGLVFsavdsdcdkrvAVKKIVLTDPQSV------KHALREIK----------IIRRLDHDNIVKVY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGK--------------LYLILDFLRGgDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL 200
Cdd:cd07854   69 EVLGPSGSdltedvgsltelnsVYIVQEYMET-DL-ANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 201 LDEEGHI-KLTDFGLSK-ESIDHEKKAYSFCGTVE--YMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKE 275
Cdd:cd07854  147 INTEDLVlKIGDFGLARiVDPHYSHKGYLSEGLVTkwYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELE 226

                 ....*...
gi 768032625 276 TMTMILKA 283
Cdd:cd07854  227 QMQLILES 234
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
433-686 1.43e-18

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: 85.96  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEI-EIL-----LRYGQHPNIITLKDVYDDGKYVYVVTELMKGG- 505
Cdd:cd06607    8 EIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEKWqDIIkevkfLRQLRHPNTIEYKGCYLREHTAWLVMEYCLGSa 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ----ELLDKILRqkffsEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesgnPESIRICDFGFAKQLRAENGLL 581
Cdd:cd06607   88 sdivEVHKKPLQ-----EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTE----PGTVKLADFGSASLVCPANSFV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 MTPcYtanFVAPEV---LKRQGYDAACDIWSLGVLLYTMLTGYTPFAN----------GPDDTPeeilarigsgkfSLSG 648
Cdd:cd06607  159 GTP-Y---WMAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNmnamsalyhiAQNDSP------------TLSS 222
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 649 GYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIV 686
Cdd:cd06607  223 GEW---SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
450-642 1.71e-18

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 85.95  E-value: 1.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 450 TNMEFAVKII---DKSK-RDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLdKILRQKFFSEREASAV 525
Cdd:cd05148   29 NRVRVAIKILksdDLLKqQDFQKEVQALKRL-RHKHLISLFAVCSVGEPVYIITELMEKGSLL-AFLRSPEGQVLPVASL 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 526 LFTITKTVE---YLHAQGVVHRDLKPSNILyVDESgnpESIRICDFGFAKqlraengLLMTPCYTAN-------FVAPEV 595
Cdd:cd05148  107 IDMACQVAEgmaYLEEQNSIHRDLAARNIL-VGED---LVCKVADFGLAR-------LIKEDVYLSSdkkipykWTAPEA 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 596 LKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05148  176 ASHGTFSTKSDVWSFGILLYEMFTyGQVPY---PGMNNHEVYDQITAG 220
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
68-261 1.88e-18

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: 85.58  E-value: 1.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISgsdARQLYAMKVL----KKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 143
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKR---TSEVVAIKKMsysgKQSTEKWQDIIK---EVKFLRQLRHPNTIEYKGCYLREHTA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRG--GDLFTRLSKEVMftEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlskeSIDH 221
Cdd:cd06607   77 WLVMEYCLGsaSDIVEVHKKPLQ--EVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG----SASL 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 222 EKKAYSFCGTVEYMAPEVV---NRRGHTQSADWWSFGVLMFEM 261
Cdd:cd06607  151 VCPANSFVGTPYWMAPEVIlamDEGQYDGKVDVWSLGITCIEL 193
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
64-280 2.03e-18

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 85.89  E-value: 2.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVLKK-ATLKVRDRVRTkmERDILVEVNHPFIVKLhYAFQTEGK 142
Cdd:cd05033    2 DASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSgYSDKQRLDFLT--EASIMGQFDHPNVIRL-EGVVTKSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 -LYLILDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsID 220
Cdd:cd05033   79 pVMIVTEYMENGSLDKFLREnDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRR-LE 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 221 HEKKAYSFCG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI 280
Cdd:cd05033  158 DSEATYTTKGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAV 221
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
153-333 2.08e-18

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: 85.09  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDL--FTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI--DHEKKAYSF 228
Cdd:cd14022   69 GDMhsFVRTCKKL--REEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYIlrGHDDSLSDK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 229 CGTVEYMAPEVVNRRGH--TQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRN 306
Cdd:cd14022  147 HGCPAYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRRE 226
                        170       180
                 ....*....|....*....|....*..
gi 768032625 307 PANRLVNpfligagpdgvEEIKRHSFF 333
Cdd:cd14022  227 PSERLTS-----------QEILDHPWF 242
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
11-288 2.50e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 88.17  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  11 QKMAVESPSDSAENGQQIMDEPMGEEEINpqteevsikeiaithhvkegheKADPSQFELLKVLGQGSFGKVFlvKKISG 90
Cdd:PTZ00036  33 KKLDEEERSHNNNAGEDEDEEKMIDNDIN----------------------RSPNKSYKLGNIIGNGSFGVVY--EAICI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  91 SDARQLYAMKVLKKATLKVRDRVrtkmerdILVEVNHPFIVKLHYAFQTEGK--------LYLILDFL-----RGGDLFT 157
Cdd:PTZ00036  89 DTSEKVAIKKVLQDPQYKNRELL-------IMKNLNHINIIFLKDYYYTECFkkneknifLNVVMEFIpqtvhKYMKHYA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 158 RLSKEV-MFTeedVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH-IKLTDFGLSKESIDHEKKAYSFCGTVeYM 235
Cdd:PTZ00036 162 RNNHALpLFL---VKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYICSRF-YR 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 236 APEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:PTZ00036 238 APELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQV-LGTP 290
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
67-307 2.64e-18

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: 85.94  E-value: 2.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKAtlKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd07846    2 KYENLGLVGEGSYG---MVMKCRHKETGQIVAIKKFLES--EDDKMVKKIAMREIkmLKQLRHENLVNLIEVFRRKKRWY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKK 224
Cdd:cd07846   77 LVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-TLAAPGE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYS-FCGTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMpqfLSPEAQSllrmL 302
Cdd:cd07846  156 VYTdYVATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIK-CLGN---LIPRHQE----L 227

                 ....*
gi 768032625 303 FKRNP 307
Cdd:cd07846  228 FQKNP 232
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
428-683 2.69e-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: 85.82  E-value: 2.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDptEEIE-------ILLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEEN--EEVKettlrelKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGG--ELLDKIlrQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNpESIRICDFGFAKQLRAEN 578
Cdd:cd07848   81 YVEKNmlELLEEM--PNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLI---SHN-DVLKLCDFGFARNLSEGS 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPcYTAN--FVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAN--------------GPdDTPEEILARIGSG 642
Cdd:cd07848  155 NANYTE-YVATrwYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGeseidqlftiqkvlGP-LPAEQMKLFYSNP 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 643 KF------------SLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd07848  233 RFhglrfpavnhpqSLERRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
428-684 2.91e-18

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 86.60  E-value: 2.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCI-HKATNMEFAVKII---DKSKRDPTEEIEILLRYGQHPN-----IITLKDVYDDGKYVYVV 498
Cdd:cd14214   15 YEIVGDLGEGTFGKVVECLdHARGKSQVALKIIrnvGKYREAARLEINVLKKIKEKDKenkflCVLMSDWFNFHGHMCIA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMkgGELLDKILRQKFFSEREASAV---LFTITKTVEYLHAQGVVHRDLKPSNILYVD--------ESGNPE------ 561
Cdd:cd14214   95 FELL--GKNTFEFLKENNFQPYPLPHIrhmAYQLCHALKFLHENQLTHTDLKPENILFVNsefdtlynESKSCEeksvkn 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 562 -SIRICDFGFAKqlrAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAN-------------- 626
Cdd:cd14214  173 tSIRVADFGSAT---FDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQThenrehlvmmekil 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 627 GPddTPEEILARIGSGKFSLSGGY-WNSVSDTAK------------------------DLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd14214  250 GP--IPSHMIHRTRKQKYFYKGSLvWDENSSDGRyvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRITLKEALL 327

                 ...
gi 768032625 682 HPW 684
Cdd:cd14214  328 HPF 330
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
74-310 2.97e-18

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: 85.75  E-value: 2.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVK-KISGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG--KLYLILDFL 150
Cdd:cd05079   12 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKLIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLSKEV-MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHEKKAYS-- 227
Cdd:cd05079   91 PSGSLKEYLPRNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEYYTvk 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 --FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT--------GTL------PFQGKDRKETMTMILK--AKLGMPQ 289
Cdd:cd05079  170 ddLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspMTLflkmigPTHGQMTVTRLVRVLEegKRLPRPP 249
                        250       260
                 ....*....|....*....|.
gi 768032625 290 FLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05079  250 NCPEEVYQLMRKCWEFQPSKR 270
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
336-395 3.15e-18

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 78.94  E-value: 3.15e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625   336 IDWNKLYRREIHPPFKPATGRPEDTFYFDPEFTAKTPKDSPGIPPSANAHQL--FRGFSFVA 395
Cdd:smart00133   3 IDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGIQQepFRGFSYVF 64
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
91-314 3.19e-18

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 84.71  E-value: 3.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  91 SDARQLYAMKVLKKATLKVRDRVRTKMERDI--LVEVnhpfivklhyaFQTEGKLYLIL--DFlrgGDLFTRLSKEVMFT 166
Cdd:cd14023   17 SGAELQCKVFPLKHYQDKIRPYIQLPSHRNItgIVEV-----------ILGDTKAYVFFekDF---GDMHSYVRSCKRLR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 167 EEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL-----TDFGLSKESIDHEKKAYsfcGTVEYMAPEVVN 241
Cdd:cd14023   83 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLrleslEDTHIMKGEDDALSDKH---GCPAYVSPEILN 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 242 RRG--HTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLVNP 314
Cdd:cd14023  160 TTGtySGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTAP 234
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
430-624 3.52e-18

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: 85.08  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKEDIGVGSYSVCKRCIHKATNMefAVKiidKSKRDPTEEIEI----------LLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd14147    7 LEEVIGIGGFGKVYRGSWRGELV--AVK---AARQDPDEDISVtaesvrqearLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELldkilRQKFFSEREASAVLFT----ITKTVEYLHAQG---VVHRDLKPSNILY----VDESGNPESIRICDF 568
Cdd:cd14147   82 EYAAGGPL-----SRALAGRRVPPHVLVNwavqIARGMHYLHCEAlvpVIHRDLKSNNILLlqpiENDDMEHKTLKITDF 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 569 GFAKQLRAENGllMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd14147  157 GLAREWHKTTQ--MSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
118-288 3.57e-18

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: 85.82  E-value: 3.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 118 ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLrGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKP 196
Cdd:cd07873   50 EVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL-DKDLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKP 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 197 ENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKE 275
Cdd:cd07873  129 QNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEE 208
                        170
                 ....*....|...
gi 768032625 276 TMTMILKAkLGMP 288
Cdd:cd07873  209 QLHFIFRI-LGTP 220
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
67-262 3.58e-18

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: 85.24  E-value: 3.58e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTkmerdiLVEVNHPFIVKLHYAFQTEGK--- 142
Cdd:cd14047    7 DFKEIELIGSGGFGQVFKAKhRIDG----KTYAIKRVKLNNEKAEREVKA------LAKLDHPNIVRYNGCWDGFDYdpe 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 -------------LYLILDFLRGGDLFTRLSK----EVMFTEEDVKFYlaELALALDHLHSLGIIYRDLKPENILLDEEG 205
Cdd:cd14047   77 tsssnssrsktkcLFIQMEFCEKGTLESWIEKrngeKLDKVLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTG 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 206 HIKLTDFGLSKESIDHEKKAYSFcGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14047  155 KVKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
70-351 4.17e-18

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


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 85.41  E-value: 4.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVF--LVKKISGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05061   10 LLRELGQGSFGMVYegNARDIIKGEAETRVAVKTVNESA-SLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSK----------EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE 217
Cdd:cd05061   89 ELMAHGDLKSYLRSlrpeaennpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRD 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 --SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILK-AKLGMPQFLSP 293
Cdd:cd05061  169 iyETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDgGYLDQPDNCPE 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 294 EAQSLLRMLFKRNPAnrlvnpfligagpdgveeiKRHSFFSTIDwnkLYRREIHPPFK 351
Cdd:cd05061  249 RVTDLMRMCWQFNPK-------------------MRPTFLEIVN---LLKDDLHPSFP 284
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
72-310 4.31e-18

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: 84.58  E-value: 4.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLvkkisGS-DARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLI---- 146
Cdd:cd14203    1 VKLGQGCFGEVWM-----GTwNGTTKVAIKTLKPGTMSPEAFLE---EAQIMKKLRHDKLVQL-YAVVSEEPIYIVtefm 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 -----LDFLRGGD-LFTRLSKEVMFTeedvkfylAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd14203   72 skgslLDFLKDGEgKYLKLPQLVDMA--------AQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 HE---KKAYSFcgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEA 295
Cdd:cd14203  144 NEytaRQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESL 221
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd14203  222 HELMCQCWRKDPEER 236
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
75-310 4.91e-18

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: 84.24  E-value: 4.91e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  75 GQGSFGKVFLVKKISGSdarQLYAMKVLKKatlkvrdrvrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 154
Cdd:cd14060    2 GGGSFGSVYRAIWVSQD---KEVAVKKLLK----------IEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGS 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 155 LF----TRLSKEVMFTEedVKFYLAELALALDHLHS---LGIIYRDLKPENILLDEEGHIKLTDFGLSKesIDHEKKAYS 227
Cdd:cd14060   69 LFdylnSNESEEMDMDQ--IMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASR--FHSHTTHMS 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK--AKLGMPQFLSPEAQSLLRMLFKR 305
Cdd:cd14060  145 LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEknERPTIPSSCPRSFAELMRRCWEA 224

                 ....*
gi 768032625 306 NPANR 310
Cdd:cd14060  225 DVKER 229
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
113-311 5.12e-18

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: 84.33  E-value: 5.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 113 VRTKMERdiLVEVNHPFIVKLhYAFQTE-------GKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLH 185
Cdd:cd14012   45 LEKELES--LKKLRHPNLVSY-LAFSIErrgrsdgWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 186 SLGIIYRDLKPENILLD---EEGHIKLTDFGLSKE--------SIDHEKKAYsfcgtveYMAPEVVN-RRGHTQSADWWS 253
Cdd:cd14012  122 RNGVVHKSLHAGNVLLDrdaGTGIVKLTDYSLGKTlldmcsrgSLDEFKQTY-------WLPPELAQgSKSPTRKTDVWD 194
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 254 FGVLMFEMLTGTLPFQgkdRKETMTMILkaklgMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14012  195 LGLLFLQMLFGLDVLE---KYTSPNPVL-----VSLDLSASLQDFLSKCLSLDPKKRP 244
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
432-626 5.23e-18

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: 84.42  E-value: 5.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKAtNMEFAVKIIDK---SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:cd05059   10 KELGSGQFGVVHLGKWRG-KIDVAIKMIKEgsmSEDDFIEEAKVMMKL-SHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DKILRQKffsEREASAVLFT----ITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKqlraengLLMTP 584
Cdd:cd05059   88 NYLRERR---GKFQTEQLLEmckdVCEAMEYLESNGFIHRDLAARNCL-VGEQN---VVKVSDFGLAR-------YVLDD 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 585 CYTANF--------VAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAN 626
Cdd:cd05059  154 EYTSSVgtkfpvkwSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYER 204
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
73-310 5.88e-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: 84.71  E-value: 5.88e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVfLVKKISGSDARQLYAMKVLKKATLKvRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05047    2 VIGEGNFGQV-LKARIKKDGLRMDAAIKRMKEYASK-DDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFtEEDVKF-----------------YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05047   80 HGNLLDFLRKSRVL-ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYSFCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLS 292
Cdd:cd05047  159 SRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPLNCD 237
                        250
                 ....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANR 310
Cdd:cd05047  238 DEVYDLMRQCWREKPYER 255
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
50-264 6.30e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 86.59  E-value: 6.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  50 IAITHHVKEGHEKADpsqFELLKVLGQGSFGKVFLVKKisgsdarqlyaMKVLKKATLKVRDRVRTKMERDILVEVNHPF 129
Cdd:PHA03212  79 LALCAEARAGIEKAG---FSILETFTPGAEGFAFACID-----------NKTCEHVVIKAGQRGGTATEAHILRAINHPS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 130 IVKLHYAFQTEGKLYLILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:PHA03212 145 IIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCL 223
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 210 TDFGLSKESID-HEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTG 264
Cdd:PHA03212 224 GDFGAACFPVDiNANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATC 279
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
69-310 7.72e-18

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: 7.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  69 ELLKVLGQGSFGKVFLvkkisGSDARQLYAMKVLKkatlkvrDRVRTK----MERDILVEVNHPFIVKLHYAFQTEGKLY 144
Cdd:cd05039    9 KLGELIGKGEFGDVML-----GDYRGQKVAVKCLK-------DDSTAAqaflAEASVMTTLRHPNLVQLLGVVLEGNGLY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESiDHE 222
Cdd:cd05039   77 IVTEYMAKGSLvdYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA-SSN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFcgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLR 300
Cdd:cd05039  156 QDGGKL--PIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPHVEKGyRMEAPEGCPPEVYKVMK 233
                        250
                 ....*....|
gi 768032625 301 MLFKRNPANR 310
Cdd:cd05039  234 NCWELDPAKR 243
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
64-284 7.87e-18

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: 84.43  E-value: 7.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVKKI-SGSDARQLYAMKVLKKATLKVRDRVRTkmERDILVEVNHPFIV----------- 131
Cdd:cd05043    4 SRERVTLSDLLQEGTFGRIFHGILRdEKGKEEEVLVKTVKDHASEIQVTMLLQ--ESSLLYGLSHQNLLpilhvciedge 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 132 --KLHYAFQTEGKLYLildFLRGGDLFTRLSKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd05043   82 kpMVLYPYMNWGNLKL---FLQQCRLSEANNPQALSTQQLVHMAL-QIACGMSYLHRRGVIHKDIAARNCVIDDELQVKI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 210 TDFGLSKESI--------DHEKKAysfcgtVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI 280
Cdd:cd05043  158 TDNALSRDLFpmdyhclgDNENRP------IKWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDPFEMAAYL 231

                 ....
gi 768032625 281 LKAK 284
Cdd:cd05043  232 KDGY 235
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
68-288 8.28e-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: 84.35  E-value: 8.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKkatLKVRD-----RVRtkmERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRsKLTG----QLVALKEIR---LEHEEgapftAIR---EASLLKDLKHANIVTLHDIIHTKK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGgDLFTRLSKEVMFTE-EDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-ESI 219
Cdd:cd07844   72 TLTLVFEYLDT-DLKQYMDDCGGGLSmHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARaKSV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 220 dhEKKAYSF-CGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQG-KDRKETMTMILKAkLGMP 288
Cdd:cd07844  151 --PSKTYSNeVVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRV-LGTP 219
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
428-694 8.38e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 86.63  E-value: 8.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIeILLRYGQHPNIITLKDVY--------DDGKYVYVVT 499
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNREL-LIMKNLNHINIIFLKDYYytecfkknEKNIFLNVVM 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKggELLDKILrqKFFSEREASAVLFTIT-------KTVEYLHAQGVVHRDLKPSNILyVDEsgNPESIRICDFGFAK 572
Cdd:PTZ00036 147 EFIP--QTVHKYM--KHYARNNHALPLFLVKlysyqlcRALAYIHSKFICHRDLKPQNLL-IDP--NTHTLKLCDFGSAK 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGLLMTPCyTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPD-----------DTPEEILARIG 640
Cdd:PTZ00036 220 NLLAGQRSVSYIC-SRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSvdqlvriiqvlGTPTEDQLKEM 298
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 641 SGKFS-----------LSGGYWNSVSDTAKDLVSKMLHVDPHQRLTA--ALV------LRHPWIvhwdQLPQY 694
Cdd:PTZ00036 299 NPNYAdikfpdvkpkdLKKVFPKGTPDDAINFISQFLKYEPLKRLNPieALAdpffddLRDPCI----KLPKY 367
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
448-684 8.93e-18

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 84.30  E-value: 8.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 448 KATNMEFAVKIIDK------SKRDPTEEIEIL---------LRygqHPNIITLKDVYDDGKY-VYVVTELMKG------G 505
Cdd:cd14011   18 KSTKQEVSVFVFEKkqleeySKRDREQILELLkrgvkqltrLR---HPRILTVQHPLEESREsLAFATEPVFAslanvlG 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKFFSEREASAV-----LFTITKTVEYLH-AQGVVHRDLKPSNIlYVDESGnpeSIRICDFGFA-KQLRAEN 578
Cdd:cd14011   95 ERDNMPSPPPELQDYKLYDVeikygLLQISEALSFLHnDVKLVHGNICPESV-VINSNG---EWKLAGFDFCiSSEQATD 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTA----------NFVAPEVLKRQGYDAACDIWSLGVLLYTML-TGYTPFANGPD-DTPEEILARIGSGKFSL 646
Cdd:cd14011  171 QFPYFREYDPnlpplaqpnlNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNlLSYKKNSNQLRQLSLSL 250
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 647 sggyWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14011  251 ----LEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
66-310 9.99e-18

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: 84.31  E-value: 9.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvKKI---SGSDARQLYAMKVLkkatlkvRDRVRTKMERDILVE------VNHPFIVKLhYA 136
Cdd:cd05109    7 TELKKVKVLGSGAFGTVY--KGIwipDGENVKIPVAIKVL-------RENTSPKANKEILDEayvmagVGSPYVCRL-LG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 137 FQTEGKLYLILDFLRGGDL--FTRLSKEVMFTEeDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05109   77 ICLTSTVQLVTQLMPYGCLldYVRENKDRIGSQ-DLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKeSIDHEKKAYSFCG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQ 289
Cdd:cd05109  156 AR-LLDIDETEYHADGgkvPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPAREIPDLLEKGeRLPQPP 234
                        250       260
                 ....*....|....*....|.
gi 768032625 290 FLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05109  235 ICTIDVYMIMVKCWMIDSECR 255
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
482-674 1.02e-17

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: 85.87  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 482 IITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIL--------- 552
Cdd:cd05625   63 VVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILidrdghikl 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 553 ------------------------------YVDESGNPESIRICDFGFAKQLRA----ENGLLMTPCYTANFVAPEVLKR 598
Cdd:cd05625  143 tdfglctgfrwthdskyyqsgdhlrqdsmdFSNEWGDPENCRCGDRLKPLERRAarqhQRCLAHSLVGTPNYIAPEVLLR 222
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 599 QGYDAACDIWSLGVLLYTMLTGYTPFANgpdDTPEEILARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHvDPHQRL 674
Cdd:cd05625  223 TGYTQLCDWWSVGVILFEMLVGQPPFLA---QTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRL 294
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
428-684 1.02e-17

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 84.90  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCI-HKATNMEFAVKII---DKSKRDPTEEIEILlrygQHPN---------IITLKDVYDDGKY 494
Cdd:cd14213   14 YEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIVknvDRYREAARSEIQVL----EHLNttdpnstfrCVQMLEWFDHHGH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMkGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVD----ESGNPE------- 561
Cdd:cd14213   90 VCIVFELL-GLSTYDFIKENSFlpFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQsdyvVKYNPKmkrdert 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 562 ----SIRICDFGFAKQLRAENGLLMTpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAN----------- 626
Cdd:cd14213  169 lknpDIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQThdskehlamme 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 627 ---GPddTPEEILARIGSGKF-----------SLSGGYWNSVSDTAK--------------DLVSKMLHVDPHQRLTAAL 678
Cdd:cd14213  246 rilGP--LPKHMIQKTRKRKYfhhdqldwdehSSAGRYVRRRCKPLKefmlsqdvdheqlfDLIQKMLEYDPAKRITLDE 323

                 ....*.
gi 768032625 679 VLRHPW 684
Cdd:cd14213  324 ALKHPF 329
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
428-674 1.04e-17

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: 85.11  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKsKRDPTEEIEIL----------LRYGQHPNIITLKDVYDDGKYVYV 497
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMKQGETLalnerimlslVSTGDCPFIVCMTYAFHTPDKLCF 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFA-----K 572
Cdd:cd05633   86 ILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHV---RISDLGLAcdfskK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGllmtpcyTANFVAPEVLKR-QGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSggyw 651
Cdd:cd05633  162 KPHASVG-------THGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP---- 230
                        250       260
                 ....*....|....*....|...
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRL 674
Cdd:cd05633  231 DSFSPELKSLLEGLLQRDVSKRL 253
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
67-264 1.04e-17

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: 84.35  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAMK---------VLKKATLKvrdrvrtkmERDILVEVNHPFIVKLHYAF 137
Cdd:cd07847    2 KYEKLSKIGEGSYGVVF---KCRNRETGQIVAIKkfveseddpVIKKIALR---------EIRMLKQLKHPNLVNLIEVF 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDFLRGgDLFTRLSKEVMFTEED-VKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07847   70 RRKRKLHLVFEYCDH-TVLNELEKNPRGVPEHlIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 217 ESIDHEKKAYSFCGTVEYMAPEVVnrRGHTQ---SADWWSFGVLMFEMLTG 264
Cdd:cd07847  149 ILTGPGDDYTDYVATRWYRAPELL--VGDTQygpPVDVWAIGCVFAELLTG 197
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
70-280 1.19e-17

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 83.98  E-value: 1.19e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVF--LVKKISGSDARQLYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEGKlYLI 146
Cdd:cd05036   10 LIRALGQGAFGEVYegTVSGMPGDPSPLQVAVKTLPELCSE-QDEMDFLMEALIMSKFNHPNIVRCiGVCFQRLPR-FIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDL--FTR-----LSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH---IKLTDFGLSK 216
Cdd:cd05036   88 LELMAGGDLksFLRenrprPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvAKIGDFGMAR 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 217 E--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI 280
Cdd:cd05036  168 DiyRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFV 234
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
70-311 1.24e-17

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 83.94  E-value: 1.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVFLVK--KISGSDARQLYAMKVLKKATLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05093    9 LKRELGEGAFGKVFLAEcyNLCPEQDKILVAVKTLKDASDNARKDFHR--EAELLTNLQHEHIVKFYGVCVEGDPLIMVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDL--FTRL-----------SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05093   87 EYMKHGDLnkFLRAhgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQF 290
Cdd:cd05093  167 SRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRvLQRPRT 246
                        250       260
                 ....*....|....*....|.
gi 768032625 291 LSPEAQSLLRMLFKRNPANRL 311
Cdd:cd05093  247 CPKEVYDLMLGCWQREPHMRL 267
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
127-314 1.29e-17

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 82.86  E-value: 1.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 127 HPFIVKLHYAFQTEGKLYLIL--DFlrgGDL--FTRLSKEVMFTEEDVKFYlaELALALDHLHSLGIIYRDLKPENILLD 202
Cdd:cd13976   44 HPNISGVHEVIAGETKAYVFFerDH---GDLhsYVRSRKRLREPEAARLFR--QIASAVAHCHRNGIVLRDLKLRKFVFA 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 203 EEGHIKLTDFGLSKESID-------HEKKaysfcGTVEYMAPEVVNRRGH--TQSADWWSFGVLMFEMLTGTLPFQGKDR 273
Cdd:cd13976  119 DEERTKLRLESLEDAVILegeddslSDKH-----GCPAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEP 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768032625 274 KETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRLVNP 314
Cdd:cd13976  194 ASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAE 234
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
66-298 1.30e-17

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: 84.29  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvKKISGSDARQlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAF-------- 137
Cdd:cd07866    8 RDYEILGKLGEGTFGEVY--KARQIKTGRV-VALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAverpdksk 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDFLrGGDLFTRLSKE-VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK 216
Cdd:cd07866   85 RKRGSVYMVTPYM-DHDLSGLLENPsVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLAR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 eSIDHEKKAYSFCGTVE------------YMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKa 283
Cdd:cd07866  164 -PYDGPPPNPKGGGGGGtrkytnlvvtrwYRPPELLlGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFK- 241
                        250
                 ....*....|....*.
gi 768032625 284 KLGMPQFLS-PEAQSL 298
Cdd:cd07866  242 LCGTPTEETwPGWRSL 257
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
56-309 1.43e-17

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: 84.68  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  56 VKEGHEKADpsQFELLKVLGQGSFGKVflVKKISGSDARQLyAMKVLKKatlKVRDRVRTKMERDILVEVNHP------F 129
Cdd:cd14226    5 VKNGEKWMD--RYEIDSLIGKGSFGQV--VKAYDHVEQEWV-AIKIIKN---KKAFLNQAQIEVRLLELMNKHdtenkyY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 130 IVKLHYAFQTEGKLYLIL--------DFLRGGDlFTRLSKEVmfteedVKFYLAELALALDHLHS--LGIIYRDLKPENI 199
Cdd:cd14226   77 IVRLKRHFMFRNHLCLVFellsynlyDLLRNTN-FRGVSLNL------TRKFAQQLCTALLFLSTpeLSIIHCDLKPENI 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 200 LL--DEEGHIKLTDFGLSKESidhEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETM 277
Cdd:cd14226  150 LLcnPKRSAIKIIDFGSSCQL---GQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQM 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 768032625 278 TMILkAKLGMPQFLSPEAQSLLRMLFKRNPAN 309
Cdd:cd14226  227 NKIV-EVLGMPPVHMLDQAPKARKFFEKLPDG 257
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
67-288 1.49e-17

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: 85.08  E-value: 1.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKV-----------FLVKKISGSDARQLYAMKVLKKATLkvrdrvrtkmerdiLVEVNHPFIVKLHY 135
Cdd:cd07876   22 RYQQLKPIGSGAQGIVcaafdtvlginVAVKKLSRPFQNQTHAKRAYRELVL--------------LKCVNHKNIISLLN 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 136 AFQTEGKL------YLILDfLRGGDLFTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKL 209
Cdd:cd07876   88 VFTPQKSLeefqdvYLVME-LMDANLCQVIHMEL--DHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKI 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 210 TDFGLSKESIDHEKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMP 288
Cdd:cd07876  165 LDFGLARTACTNFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIE-QLGTP 241
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
428-685 1.56e-17

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: 83.52  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE---EIEILLRYGQHPNIITLKDVY--------DDgkYVY 496
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEiklEINMLKKYSHHRNIATYYGAFikksppghDD--QLW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL 574
Cdd:cd06636   96 LVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGLLMTPCYTANFVAPEVLK-----RQGYDAACDIWSLGVLLYTMLTGYTPFANG---------PDDTPEEILARIG 640
Cdd:cd06636  172 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDMhpmralfliPRNPPPKLKSKKW 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 641 SGKFSlsggywnsvsdtakDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06636  252 SKKFI--------------DFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
65-317 1.56e-17

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


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 84.73  E-value: 1.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  65 PSQFELLKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK-- 142
Cdd:cd07858    4 DTKYVPIKPIGRGAYGIVCSAKN---SETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHRea 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 ---LYLILDfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd07858   81 fndVYIVYE-LMDTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPQ------FLS 292
Cdd:cd07858  160 EKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITEL-LGSPSeedlgfIRN 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 293 PEAQSLLRML--FKRNPANRL---VNPFLI 317
Cdd:cd07858  239 EKARRYIRSLpyTPRQSFARLfphANPLAI 268
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
72-298 1.64e-17

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 84.43  E-value: 1.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFL-VKKISGSDArQLYAMKVLKKATLKVRDRVRTKM---------ERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:PTZ00024  15 AHLGEGTYGKVEKaYDTLTGKIV-AIKKVKIIEISNDVTKDRQLVGMcgihfttlrELKIMNEIKHENIMGLVDVYVEGD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK----- 216
Cdd:PTZ00024  94 FINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLARrygyp 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 ---------ESIDHEKKAYSFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLG 286
Cdd:PTZ00024 173 pysdtlskdETMQRREEMTSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFEL-LG 251
                        250
                 ....*....|...
gi 768032625 287 MPQFLS-PEAQSL 298
Cdd:PTZ00024 252 TPNEDNwPQAKKL 264
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
453-642 1.81e-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: 82.72  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 453 EFAVKIIDKSKRDPT---EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkilrqkFFSEREASAVLFT- 528
Cdd:cd05034   21 KVAVKTLKPGTMSPEaflQEAQIMKKL-RHDKLVQLYAVCSDEEPIYIVTELMSKGSLLD------YLRTGEGRALRLPq 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 -------ITKTVEYLHAQGVVHRDLKPSNILyVDESgnpESIRICDFGFAKqlraengLLMTPCYTAN--------FVAP 593
Cdd:cd05034   94 lidmaaqIASGMAYLESRNYIHRDLAARNIL-VGEN---NVCKVADFGLAR-------LIEDDEYTARegakfpikWTAP 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 594 EVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05034  163 EAALYGRFTIKSDVWSFGILLYEIVTyGRVPY---PGMTNREVLEQVERG 209
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
428-674 2.03e-17

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: 83.94  E-value: 2.03e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKsKRDPTEEIEIL----------LRYGQHPNIITLKDVYDDGKYVYV 497
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMKQGETLalnerimlslVSTGDCPFIVCMSYAFHTPDKLSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFA-----K 572
Cdd:cd14223   81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANIL-LDEFGH---VRISDLGLAcdfskK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLRAENGllmtpcyTANFVAPEVLKRQ-GYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEilarIGSGKFSLSGGYW 651
Cdd:cd14223  157 KPHASVG-------THGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE----IDRMTLTMAVELP 225
                        250       260
                 ....*....|....*....|...
gi 768032625 652 NSVSDTAKDLVSKMLHVDPHQRL 674
Cdd:cd14223  226 DSFSPELRSLLEGLLQRDVNRRL 248
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
419-687 2.13e-17

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: 84.29  E-value: 2.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 419 RNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII--DKSKRDPTE-EIEILLRYGQHP-----NIITLKDVYD 490
Cdd:cd14226    6 KNGEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIknKKAFLNQAQiEVRLLELMNKHDtenkyYIVRLKRHFM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGgELLDKILRQKF----------FSEREASAVLFTITKTVEylhaqgVVHRDLKPSNILYVdesgNP 560
Cdd:cd14226   86 FRNHLCLVFELLSY-NLYDLLRNTNFrgvslnltrkFAQQLCTALLFLSTPELS------IIHCDLKPENILLC----NP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 561 E--SIRICDFGFAKQLraenGLLMTPCYTANFV-APEVLKRQGYDAACDIWSLGVLLYTMLTGyTPFANG---------- 627
Cdd:cd14226  155 KrsAIKIIDFGSSCQL----GQRIYQYIQSRFYrSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLFSGanevdqmnki 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 628 -------------------------PDDTPE-----EILARIGSGKFSLS-------GG--------YWNSVSDTAK--D 660
Cdd:cd14226  230 vevlgmppvhmldqapkarkffeklPDGTYYlkktkDGKKYKPPGSRKLHeilgvetGGpggrragePGHTVEDYLKfkD 309
                        330       340
                 ....*....|....*....|....*..
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWIVH 687
Cdd:cd14226  310 LILRMLDYDPKTRITPAEALQHSFFKR 336
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
71-263 2.76e-17

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 83.02  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKIS-GSDARQLYAMKVLKKATLK-VRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK--LYLI 146
Cdd:cd05081    9 ISQLGKGNFGSVELCRYDPlGDNTGALVAVKQLQHSGPDqQRDFQR---EIQILKALHSDFIVKYRGVSYGPGRrsLRLV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKesIDHEKKA 225
Cdd:cd05081   86 MEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAK--LLPLDKD 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 226 YSFC-----GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT 263
Cdd:cd05081  164 YYVVrepgqSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
67-300 3.05e-17

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: 83.68  E-value: 3.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGkvfLVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK---- 142
Cdd:cd07859    1 RYKIQEVIGKGSYG---VVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 -LYLILDfLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDH 221
Cdd:cd07859   78 dIYVVFE-LMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFND 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAY---SFCGTVEYMAPEVVNR--RGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMPqflSPEAQ 296
Cdd:cd07859  157 TPTAIfwtDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDL-LGTP---SPETI 232

                 ....
gi 768032625 297 SLLR 300
Cdd:cd07859  233 SRVR 236
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
433-682 3.30e-17

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: 82.36  E-value: 3.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFA-----VKIIDKSKRDP-TEEIEiLLRYGQHPNIITLKDVYDDG----KYVYVVTELM 502
Cdd:cd14033    8 EIGRGSFKTVYRGLDTETTVEVAwcelqTRKLSKGERQRfSEEVE-MLKGLQHPNIVRFYDSWKSTvrghKCIILVTELM 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESGnpeSIRICDFGFAKQLRAE--N 578
Cdd:cd14033   87 TSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGPTG---SVKIGDLGLATLKRASfaK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPcytaNFVAPEVLKRQgYDAACDIWSLGVLLYTMLTGYTPFANGPDdtPEEILARIGSGKFSLSggYWNSVSDTA 658
Cdd:cd14033  164 SVIGTP----EFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPYSECQN--AAQIYRKVTSGIKPDS--FYKVKVPEL 234
                        250       260
                 ....*....|....*....|....
gi 768032625 659 KDLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd14033  235 KEIIEGCIRTDKDERFTIQDLLEH 258
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
62-261 3.32e-17

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: 83.16  E-value: 3.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADPSQ-FELLKVLGQGSFGKVFLVkkiSGSDARQLYAMKVL----KKATLKVRDRVRtkmERDILVEVNHPFIVKLHYA 136
Cdd:cd06633   16 KDDPEEiFVDLHEIGHGSFGAVYFA---TNSHTNEVVAIKKMsysgKQTNEKWQDIIK---EVKFLQQLKHPNTIEYKGC 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 137 FQTEGKLYLILDFLRGG--DLFTRLSKEVMFTEEDVKFYLAELALAldHLHSLGIIYRDLKPENILLDEEGHIKLTDFGl 214
Cdd:cd06633   90 YLKDHTAWLVMEYCLGSasDLLEVHKKPLQEVEIAAITHGALQGLA--YLHSHNMIHRDIKAGNILLTEPGQVKLADFG- 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 skeSIDHEKKAYSFCGTVEYMAPEVVNRRGHTQ---SADWWSFGVLMFEM 261
Cdd:cd06633  167 ---SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDIWSLGITCIEL 213
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
71-269 3.62e-17

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 82.66  E-value: 3.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFLVKKisgSDARQLYAMKVLKKATLKV-RDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 149
Cdd:cd14026    2 LRYLSRGAFGTVSRARH---ADWRVTVAIKCLKLDSPVGdSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTeeDVKF-----YLAELALALDHLHSLG--IIYRDLKPENILLDEEGHIKLTDFGLSK-----E 217
Cdd:cd14026   79 MTNGSLNELLHEKDIYP--DVAWplrlrILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwrqlsI 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 218 SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSA---DWWSFGVLMFEMLTGTLPFQ 269
Cdd:cd14026  157 SQSRSSKSAPEGGTIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKIPFE 211
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
66-277 3.65e-17

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: 82.00  E-value: 3.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLvkkiSGSDARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGKLYL 145
Cdd:cd05073   11 ESLKLEKKLGAGQFGEVWM----ATYNKHTKVAVKTMKPGSMSVEAFLA---EANVMKTLQHDKLVKLH-AVVTKEPIYI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKF--YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEK 223
Cdd:cd05073   83 ITEFMAKGSLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEY 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 224 KAYSFCG-TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETM 277
Cdd:cd05073  163 TAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVI 218
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
67-310 3.81e-17

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 81.95  E-value: 3.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLvkkisGSDARQLYAMKVLKK-ATLKV---RDRVRTKMERDILVEVnhpfivkLHYAFQTEGK 142
Cdd:cd05082    7 ELKLLQTIGKGEFGDVML-----GDYRGNKVAVKCIKNdATAQAflaEASVMTQLRHSNLVQL-------LGVIVEEKGG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRL---SKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd05082   75 LYIVTEYMAKGSLVDYLrsrGRSVLGGDCLLKFSL-DVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEAS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSfcgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQS 297
Cdd:cd05082  154 STQDTGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPYPRIPLKDVVPRVEKGyKMDAPDGCPPAVYD 230
                        250
                 ....*....|...
gi 768032625 298 LLRMLFKRNPANR 310
Cdd:cd05082  231 VMKNCWHLDAAMR 243
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
433-619 4.09e-17

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: 82.43  E-value: 4.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHK----ATNMEFAVKII-----DKSKRDPTEEIEILlRYGQHPNIITLKDVYDD--GKYVYVVTEL 501
Cdd:cd05038   11 QLGEGHFGSVELCRYDplgdNTGEQVAVKSLqpsgeEQHMSDFKREIEIL-RTLDHEYIVKYKGVCESpgRRSLRLIMEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKFFSEReASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDesgNPESIRICDFGFAKQLRAENG 579
Cdd:cd05038   90 LPSGSLRDYLQRHRDQIDL-KRLLLFAsqICKGMEYLGSQRYIHRDLAARNIL-VE---SEDLVKISDFGLAKVLPEDKE 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 580 LlmtpcYTAN--------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05038  165 Y-----YYVKepgespifWYAPECLRESRFSSASDVWSFGVTLYELFT 207
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
66-312 4.12e-17

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: 82.39  E-value: 4.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlVKKISGSdarqlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYL 145
Cdd:cd14149   12 SEVMLSTRIGSGSFGTVY-KGKWHGD-----VAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRL----SKEVMFTEEDVKfylAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS--KESI 219
Cdd:cd14149   85 VTQWCEGSSLYKHLhvqeTKFQMFQLIDIA---RQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvKSRW 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQ---SADWWSFGVLMFEMLTGTLPF-QGKDRKETMTMILKAklgmpqFLSPEa 295
Cdd:cd14149  162 SGSQQVEQPTGSILWMAPEVIRMQDNNPfsfQSDVYSYGIVLYELMTGELPYsHINNRDQIIFMVGRG------YASPD- 234
                        250
                 ....*....|....*....
gi 768032625 296 qslLRMLFKRNPA--NRLV 312
Cdd:cd14149  235 ---LSKLYKNCPKamKRLV 250
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
67-342 4.46e-17

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: 81.92  E-value: 4.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGsdaRQLYAMKVLKKATlkvrDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 145
Cdd:cd14017    1 RWKVVKKIGGGGFGEIYKVRDVVD---GEEVAMKVESKSQ----PKQVLKMEVAVLKKLqGKPHFCRLIGCGRTERYNYI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDfLRGGDLftrlsKEVMFTEEDVKFYLA---ELAL----ALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFGL 214
Cdd:cd14017   74 VMT-LLGPNL-----AELRRSQPRGKFSVSttlRLGIqilkAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEK-------KAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQG-KDRKETMTMilKAKLG 286
Cdd:cd14017  148 ARQYTNKDGeverpprNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKlKDKEEVGKM--KEKID 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 287 MPQflspeaqsllrmLFKRNPANrlVNPFLigagpdgvEEIKRHSFFSTIDWNKLY 342
Cdd:cd14017  226 HEE------------LLKGLPKE--FFQIL--------KHIRSLSYFDTPDYKKLH 259
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
426-684 4.51e-17

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 82.82  E-value: 4.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI----LLRYGQHPNIITLKDVYDDGK-----YVY 496
Cdd:cd07869    5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIreasLLKGLKHANIVLLHDIIHTKEtltlvFEY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMK------GGELLDKIlrqKFFsereasavLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGF 570
Cdd:cd07869   85 VHTDLCQymdkhpGGLHPENV---KLF--------LFQLLRGLSYIHQRYILHRDLKPQNLLISDTG----ELKLADFGL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLRAENGLLMTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPD--DTPEEILARIGS------ 641
Cdd:cd07869  150 ARAKSVPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiqDQLERIFLVLGTpnedtw 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 642 -----------GKFSLSGG-----YWNSVS--DTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07869  230 pgvhslphfkpERFTLYSPknlrqAWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEY 290
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
74-310 4.58e-17

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: 82.04  E-value: 4.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLvkkiSGSDARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLILDFLRGG 153
Cdd:cd05069   20 LGQGCFGEVWM----GTWNGTTKVAIKTLKPGTMMPEAFLQ---EAQIMKKLRHDKLVPL-YAVVSEEPIYIVTEFMGKG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSkevmftEEDVKF--------YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd05069   92 SLLDFLK------EGDGKYlklpqlvdMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTA 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCG-TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRML 302
Cdd:cd05069  166 RQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKLC 245

                 ....*...
gi 768032625 303 FKRNPANR 310
Cdd:cd05069  246 WKKDPDER 253
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
428-647 5.24e-17

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: 81.73  E-value: 5.24e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT--EEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMkgG 505
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQleYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLL--G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQ--KFFSereasavlftiTKTV-----------EYLHAQGVVHRDLKPSNILyVDESGNPESIRICDFGFAK 572
Cdd:cd14016   80 PSLEDLFNKcgRKFS-----------LKTVlmladqmisrlEYLHSKGYIHRDIKPENFL-MGLGKNSNKVYLIDFGLAK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLR----------AEN-GLLMTPCYTAnfvapeVLKRQGY-----DaacDIWSLG-VLLYtMLTGYTPFANGPDDTPEEI 635
Cdd:cd14016  148 KYRdprtgkhipyREGkSLTGTARYAS------INAHLGIeqsrrD---DLESLGyVLIY-FLKGSLPWQGLKAQSKKEK 217
                        250
                 ....*....|..
gi 768032625 636 LARIGSGKFSLS 647
Cdd:cd14016  218 YEKIGEKKMNTS 229
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
66-288 5.68e-17

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: 82.62  E-value: 5.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVflvkkISGSDarQLYAMKVLKKATLK-----VRDRvRTKMERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd07856   10 TRYSDLQPVGMGAFGLV-----CSARD--QLTGQNVAVKKIMKpfstpVLAK-RTYRELKLLKHLRHENIISLSDIFISP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GK-LYLILDFLrGGDLfTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEsi 219
Cdd:cd07856   82 LEdIYFVTELL-GTDL-HRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI-- 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 dHEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07856  158 -QDPQMTGYVSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITEL-LGTP 225
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
431-689 6.20e-17

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: 81.85  E-value: 6.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSYSVCKRCIHKATNMEFAVKIID-----KSKRDPTEEIEILLRYGQhPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd06619    6 QEILGHGNGGTVYKAYHLLTRRILAVKVIPlditvELQKQIMSELEILYKCDS-PYIIGFYGAFFVENRISICTEFMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 EL--LDKILRQKFfsEREASAVLftitKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLraENGLLMT 583
Cdd:cd06619   85 SLdvYRKIPEHVL--GRIAVAVV----KGLTYLWSLKILHRDVKPSNML-VNTRGQ---VKLCDFGVSTQL--VNSIAKT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTP----FANGPDDTPEEIL--------ARIGSGKFslsggyw 651
Cdd:cd06619  153 YVGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPypqiQKNQGSLMPLQLLqcivdedpPVLPVGQF------- 225
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 768032625 652 nsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWD 689
Cdd:cd06619  226 ---SEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYN 260
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
68-310 6.77e-17

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 81.43  E-value: 6.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlVKKISGSDARQLY-AMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEGKLYL 145
Cdd:cd05035    1 LKLGKILGEGEFGSVM-EAQLKQDDGSQLKvAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLiGVCFTASDLNKP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 -----ILDFLRGGDLFTRL------SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05035   80 pspmvILPFMKHGDLHSYLlysrlgGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQF 290
Cdd:cd05035  160 SRKiySGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGnRLKQPED 239
                        250       260
                 ....*....|....*....|
gi 768032625 291 LSPEAQSLLRMLFKRNPANR 310
Cdd:cd05035  240 CLDEVYFLMYFCWTVDPKDR 259
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
18-274 6.82e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 84.36  E-value: 6.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  18 PSDSAENGQQIMDEPMGEEEINPQTEEV-----SIKEIAITHHVKEGHEKADPSQFELLKVLGQGSFGKVFL--VKKISG 90
Cdd:PHA03210  95 PRSNADLFASAGDGPSGAEDSDASHLDFdeappDAAGPVPLAQAKLKHDDEFLAHFRVIDDLPAGAFGKIFIcaLRASTE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  91 SDARQ---LYAMKVLKKATLKVRDRVR------TKMERDILV--EVNHPFIVKLHYAFQTEGKLYLI--------LDFLR 151
Cdd:PHA03210 175 EAEARrgvNSTNQGKPKCERLIAKRVKagsraaIQLENEILAlgRLNHENILKIEEILRSEANTYMItqkydfdlYSFMY 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKfylaELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlSKESIDHEKKA--YSFC 229
Cdd:PHA03210 255 DEAFDWKDRPLLKQTRAIMK----QLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFG-TAMPFEKEREAfdYGWV 329
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 230 GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTL-PFQGKDRK 274
Cdd:PHA03210 330 GTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDFcPIGDGGGK 375
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
424-682 7.56e-17

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: 81.65  E-value: 7.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDgYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVV 498
Cdd:cd14046    5 LTD-FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIklrseSKNNSRILREVMLLSRL-NHQHVVRYYQAWIERANLYIQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNpesIRICDFGFAKQLRAEN 578
Cdd:cd14046   83 MEYCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNI-FLDSNGN---VKIGDFGLATSNKLNV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCY------------------TANFVAPEVLKRQG--YDAACDIWSLGVLLYTMLtgYTPfangpdDTPEE---I 635
Cdd:cd14046  159 ELATQDINkstsaalgssgdltgnvgTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC--YPF------STGMErvqI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 636 LARIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd14046  231 LTALRSVSIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
424-685 7.74e-17

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: 82.24  E-value: 7.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 424 FTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdKSKRDPTE----EIEILLR-------YGQHPNIITLKDVYD-- 490
Cdd:cd14136    8 YNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVV-KSAQHYTEaaldEIKLLKCvreadpkDPGREHVVQLLDDFKht 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 --DGKYVYVVTELMkGGELLDKILRQKF------FSEREASAVLftitKTVEYLHAQ-GVVHRDLKPSNILYvdESGNPE 561
Cdd:cd14136   87 gpNGTHVCMVFEVL-GPNLLKLIKRYNYrgiplpLVKKIARQVL----QGLDYLHTKcGIIHTDIKPENVLL--CISKIE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 562 sIRICDFGFAkqlraengllmtpCYTAN----------FVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFA--NGPD 629
Cdd:cd14136  160 -VKIADLGNA-------------CWTDKhftediqtrqYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDphSGED 225
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 630 DTPE--------EILARI-----GSGKFSL----SGG---------YWnSVSDT-----------AKDLVS---KMLHVD 669
Cdd:cd14136  226 YSRDedhlaliiELLGRIprsiiLSGKYSReffnRKGelrhisklkPW-PLEDVlvekykwskeeAKEFASfllPMLEYD 304
                        330
                 ....*....|....*.
gi 768032625 670 PHQRLTAALVLRHPWI 685
Cdd:cd14136  305 PEKRATAAQCLQHPWL 320
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
67-311 8.06e-17

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 81.64  E-value: 8.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISgsdaRQLYAMKVLKKATLKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd14040    7 RYLLLHLLGRGGFSEVYKAFDLY----EQRYAAVKIHQLNKSWRDEKKENYhkhacrEYRIHKELDHPRIVKLYDYFSLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLY-LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLDEE---GHIKLTDFGL 214
Cdd:cd14040   83 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SK------ESIDHEKKAYSFCGTVEYMAPE--VVNRRGH--TQSADWWSFGVLMFEMLTGTLPFQGKDRKETM---TMIL 281
Cdd:cd14040  163 SKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqeNTIL 242
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 282 KA---KLGMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14040  243 KAtevQFPVKPVVSNEAKAFIRRCLAYRKEDRF 275
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
74-262 8.14e-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: 81.14  E-value: 8.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKvflvkkisgsdarqlyAMKVLKKATLKV---RDRVR--TKMERDILVEV------NHPFIVKLHYAFQTEGK 142
Cdd:cd14222    1 LGKGFFGQ----------------AIKVTHKATGKVmvmKELIRcdEETQKTFLTEVkvmrslDHPNVLKFIGVLYKDKR 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd14222   65 LNLLTEFIEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEK 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 --------------------KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14222  145 kkpppdkpttkkrtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
67-285 8.21e-17

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: 81.26  E-value: 8.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlVKKISGSdarqlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYLI 146
Cdd:cd14151    9 QITVGQRIGSGSFGTVY-KGKWHGD-----VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL----SKESIDH 221
Cdd:cd14151   82 TQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvkSRWSGSH 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 222 EKKAYSfcGTVEYMAPEVV---NRRGHTQSADWWSFGVLMFEMLTGTLPFQG-KDRKETMTMILKAKL 285
Cdd:cd14151  162 QFEQLS--GSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYL 227
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
67-311 8.27e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 82.03  E-value: 8.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISgsdaRQLYAMKVLKKATLKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd14041    7 RYLLLHLLGRGGFSEVYKAFDLT----EQRYVAVKIHQLNKNWRDEKKENYhkhacrEYRIHKELDHPRIVKLYDYFSLD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLY-LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLDEE---GHIKLTDFGL 214
Cdd:cd14041   83 TDSFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGtacGEIKITDFGL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SK-------ESIDHEKKAYSFCGTVEYMAPE--VVNRRGH--TQSADWWSFGVLMFEMLTGTLPFQGKDRKETM---TMI 280
Cdd:cd14041  163 SKimdddsyNSVDGMELTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIlqeNTI 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 281 LKA-KLGMP--QFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14041  243 LKAtEVQFPpkPVVTPEAKAFIRRCLAYRKEDRI 276
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
67-310 8.38e-17

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: 81.60  E-value: 8.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSD-ARQLYAMKVLKKATLK-VRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK-- 142
Cdd:cd14205    5 HLKFLQQLGKGNFGSVEMCRYDPLQDnTGEVVAVKKLQHSTEEhLRDFER---EIEILKSLQHDNIVKYKGVCYSAGRrn 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDH 221
Cdd:cd14205   82 LRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTK-VLPQ 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 222 EKKAYSFCGTVE----YMAPEVVNRRGHTQSADWWSFGVLMFEMLTGT----------LPFQGKDRKETMTM-----ILK 282
Cdd:cd14205  161 DKEYYKVKEPGEspifWYAPESLTESKFSVASDVWSFGVVLYELFTYIeksksppaefMRMIGNDKQGQMIVfhlieLLK 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 768032625 283 --AKLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14205  241 nnGRLPRPDGCPDEIYMIMTECWNNNVNQR 270
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
434-569 8.45e-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: 77.48  E-value: 8.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEILLRYGQH-PNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDdvnnEEGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 509 DKILRQKFFsEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESGNpesIRICDFG 569
Cdd:cd13968   81 AYTQEEELD-EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILL-SEDGN---VKLIDFG 136
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
447-629 8.82e-17

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: 81.96  E-value: 8.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 447 HKATNMEFAVKIID---KSKRDPT---EEIeILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQKF---F 517
Cdd:cd08216   21 HKPTNTLVAVKKINlesDSKEDLKflqQEI-LTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRD-LLKTHFpegL 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLLMTP-CYTANFV----- 591
Cdd:cd08216   99 PELAIAFILRDVLNALEYIHSKGYIHRSVKASHIL-ISGDG---KVVLSGLRYAYSMVKHGKRQRVVhDFPKSSEknlpw 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768032625 592 -APEVLKR--QGYDAACDIWSLGVLLYTMLTGYTPFANGPD 629
Cdd:cd08216  175 lSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPFSDMPA 215
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
74-262 8.98e-17

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: 81.16  E-value: 8.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkKISGSDARQLYAMKVLKkatlkvrdRVRTKMERDILVEV------NHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd14221    1 LGKGCFGQAI---KVTHRETGEVMVMKELI--------RFDEETQRTFLKEVkvmrclEHPNVLKFIGVLYKDKRLNFIT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLftRLSKEVMFTE----EDVKFyLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE- 222
Cdd:cd14221   70 EYIKGGTL--RGIIKSMDSHypwsQRVSF-AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKt 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 223 -------------KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14221  147 qpeglrslkkpdrKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
153-311 9.41e-17

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 80.31  E-value: 9.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 153 GDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI--DHEKKAYSFCG 230
Cdd:cd14024   69 GDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPlnGDDDSLTDKHG 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVN-RRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPA 308
Cdd:cd14024  149 CPAYVGPEILSsRRSYSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPA 228

                 ...
gi 768032625 309 NRL 311
Cdd:cd14024  229 ERL 231
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
426-685 9.49e-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: 81.77  E-value: 9.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII--DKSKR----DPTEEIEILlRYGQHPNIITLKDVYDDGKYV---- 495
Cdd:cd07864    7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrlDNEKEgfpiTAIREIKIL-RQLNHRSVVNLKEIVTDKQDAldfk 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 ------YVVTELMKGG--ELLDKILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICD 567
Cdd:cd07864   86 kdkgafYLVFEYMDHDlmGLLESGLVH--FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNIL-LNNKGQ---IKLAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGLLMT-PCYTANFVAPE-VLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARI-GSGKF 644
Cdd:cd07864  160 FGLARLYNSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLcGSPCP 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 645 S-----LSGGYWNS-----------------VSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd07864  240 AvwpdvIKLPYFNTmkpkkqyrrrlreefsfIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
432-626 1.09e-16

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 80.88  E-value: 1.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSY-SVCKRCIHKATNMEFAVKI-------IDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd05033   10 KVIGGGEFgEVCSGSLKLPGKKEIDVAIktlksgySDKQRLDFLTEASIMGQF-DHPNVIRLEGVVTKSRPVMIVTEYME 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGElLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESgnpESIRICDFGFAKQLRAENgll 581
Cdd:cd05033   89 NGS-LDKFLRENdgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNIL-VNSD---LVCKVSDFGLSRRLEDSE--- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 582 mtPCYTAN-------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAN 626
Cdd:cd05033  161 --ATYTTKggkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWD 211
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
62-288 1.10e-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: 81.66  E-value: 1.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADpsQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMKVLKKATLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd07869    3 KAD--SYEKLEKLGEGSYATVYKGKsKVNG----KLVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHTK 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGgDLFTRLSKEVM-FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESI 219
Cdd:cd07869   76 ETLTLVFEYVHT-DLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKS 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 220 DHEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQG-KDRKETMTMILKAkLGMP 288
Cdd:cd07869  155 VPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmKDIQDQLERIFLV-LGTP 224
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
66-310 1.16e-16

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: 81.01  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFLVK-KISGsdarQLYAMK--VLKKATlkVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd14049    6 NEFEEIARLGKGGYGKVYKVRnKLDG----QYYAIKkiLIKKVT--KRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYL----------ILDFLRGGDLFTRLS--KEVMFTEEDVKF---YLAELALALDHLHSLGIIYRDLKPENILLD-EEGH 206
Cdd:cd14049   80 LMLyiqmqlcelsLWDWIVERNKRPCEEefKSAPYTPVDVDVttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 207 IKLTDFGLSKESI-------DHEKKAYSF-----CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLtgtLPFQGK-DR 273
Cdd:cd14049  160 VRIGDFGLACPDIlqdgndsTTMSRLNGLthtsgVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---QPFGTEmER 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 768032625 274 KETMTMILKAKLgmPQFLS---PEAQSLLRMLFKRNPANR 310
Cdd:cd14049  237 AEVLTQLRNGQI--PKSLCkrwPVQAKYIKLLTSTEPSER 274
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
68-318 1.21e-16

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: 80.88  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLvkkiSGSDARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLIL 147
Cdd:cd05070   11 LQLIKRLGNGQFGEVWM----GTWNGNTKVAIKTLKPGTMSPESFLE---EAQIMKKLKHDKLVQL-YAVVSEEPIYIVT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKA 225
Cdd:cd05070   83 EYMSKGSLldFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 YSFCG-TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRML 302
Cdd:cd05070  163 RQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPQDCPISLHELMIHC 242
                        250
                 ....*....|....*.
gi 768032625 303 FKRNPANRLVNPFLIG 318
Cdd:cd05070  243 WKKDPEERPTFEYLQG 258
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
428-624 1.31e-16

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: 81.23  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID-------KSKRDPTEEIEiLLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd08229   26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQifdlmdaKARADCIKEID-LLKQLNHPNVIKYYASFIEDNELNIVLE 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDKIL----RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGnpeSIRICDFG----FAK 572
Cdd:cd08229  105 LADAGDLSRMIKhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANV-FITATG---VVKLGDLGlgrfFSS 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 573 QLRAENGLLMTPCYtanfVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd08229  181 KTTAAHSLVGTPYY----MSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 228
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
428-685 1.34e-16

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: 81.67  E-value: 1.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKR---DPTEEIEIL--LRY----GQHpNIITLKDVYDDGKYVYVV 498
Cdd:cd14225   45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRfhhQALVEVKILdaLRRkdrdNSH-NVIHMKEYFYFRNHLCIT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMkGGELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGfakqlra 576
Cdd:cd14225  124 FELL-GMNLYELIKKNNFqgFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQS--SIKVIDFG------- 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 577 engllmTPCYTANFV----------APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARI------- 639
Cdd:cd14225  194 ------SSCYEHQRVytyiqsrfyrSPEVILGLPYSMAIDMWSLGCILAELYTGYPLF---PGENEVEQLACImevlglp 264
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 640 -------GSGK--FSLSGGYWNSVSDT--------AKDL--------------VSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14225  265 ppelienAQRRrlFFDSKGNPRCITNSkgkkrrpnSKDLasalktsdplfldfIRRCLEWDPSKRMTPDEALQHEWI 341
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
70-311 1.58e-16

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 80.82  E-value: 1.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  70 LLKVLGQGSFGKVFLVK--KISGSDARQLYAMKVLKKATLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd05094    9 LKRELGEGAFGKVFLAEcyNLSPTKDKMLVAVKTLKDPTLAARKDF--QREAELLTNLQHDHIVKFYGVCGDGDPLIMVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDL--FTR--------------LSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTD 211
Cdd:cd05094   87 EYMKHGDLnkFLRahgpdamilvdgqpRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 212 FGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGM 287
Cdd:cd05094  167 FGMSRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIECITQGRvLER 246
                        250       260
                 ....*....|....*....|....
gi 768032625 288 PQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd05094  247 PRVCPKEVYDIMLGCWQREPQQRL 270
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
428-684 1.68e-16

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: 80.55  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVckrcIHKATNMEFA-------VKIIDKSKRDPTEEI-EI-LLRYGQHPNIITLKDVYDDGKyvyvv 498
Cdd:cd07839    2 YEKLEKIGEGTYGT----VFKAKNRETHeivalkrVRLDDDDEGVPSSALrEIcLLKELKHKNIVRLYDVLHSDK----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 tELMKGGELLDKILRQKFFS---EREASAV---LFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK 572
Cdd:cd07839   73 -KLTLVFEYCDQDLKKYFDScngDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQNLL-INKNGE---LKLADFGLAR 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QLraenGLLMTpCYTANFV-----APEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDdtPEEILARIgsgkFSL 646
Cdd:cd07839  148 AF----GIPVR-CYSAEVVtlwyrPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPLFPGND--VDDQLKRI----FRL 216
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 647 SGG----YWNSVSD-------------------------TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07839  217 LGTpteeSWPGVSKlpdykpypmypattslvnvvpklnsTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
434-645 1.68e-16

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: 81.00  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDK-SKRDPTE----EIEILLRYgQHPNIITLKDVYDD--GKYVYVVTELMKGGE 506
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDvqmrEFEVLKKL-NHKNIVKLFAIEEEltTRHKVLVMELCPCGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 L---LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYV-DESGnpESI-RICDFGFAKQLRaENGLL 581
Cdd:cd13988   80 LytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRViGEDG--QSVyKLTDFGAARELE-DDEQF 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 582 MTPCYTANFVAPEVLKR--------QGYDAACDIWSLGVLLYTMLTGYTPFAngPDDTP---EEILARIGSGKFS 645
Cdd:cd13988  157 VSLYGTEEYLHPDMYERavlrkdhqKKYGATVDLWSIGVTFYHAATGSLPFR--PFEGPrrnKEVMYKIITGKPS 229
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
68-274 1.69e-16

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 80.71  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSDAR-QLYAMKVLKkATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK--LY 144
Cdd:cd05080    6 LKKIRDLGEGHFGKVSLYCYDPTNDGTgEMVAVKALK-ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGksLQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 145 LILDFLRGGDLFTRLSKEvmfteedvKFYLAELAL-------ALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE 217
Cdd:cd05080   85 LIMEYVPLGSLRDYLPKH--------SIGLAQLLLfaqqiceGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 SID-HEKKAYSFCGT--VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRK 274
Cdd:cd05080  157 VPEgHEYYRVREDGDspVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQSPPTK 216
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
72-270 1.95e-16

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: 80.39  E-value: 1.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLvkkisGSDARQLYAMKVLKKatlkvRDRVRTKMERDI--LVEVNHP----FIVKLHYAFQTEGKLYL 145
Cdd:cd14056    1 KTIGKGRYGEVWL-----GKYRGEKVAVKIFSS-----RDEDSWFRETEIyqTVMLRHEnilgFIAADIKSTGSWTQLWL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMFTEEDVKFYLAeLALALDHLHS--------LGIIYRDLKPENILLDEEGHIKLTDFGLS-- 215
Cdd:cd14056   71 ITEYHEHGSLYDYLQRNTLDTEEALRLAYS-AASGLAHLHTeivgtqgkPAIAHRDLKSKNILVKRDGTCCIADLGLAvr 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 216 --------KESIDHEkkaysfCGTVEYMAPEVVNRRGHTQS------ADWWSFGVLMFEML-----TGT-----LPFQG 270
Cdd:cd14056  150 ydsdtntiDIPPNPR------VGTKRYMAPEVLDDSINPKSfesfkmADIYSFGLVLWEIArrceiGGIaeeyqLPYFG 222
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
72-290 2.01e-16

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 79.83  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEGKLYLILDFL 150
Cdd:cd05058    1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRIT-DIEEVEQFLKEGIIMKDFSHPNVLSLlGICLPSEGSPLVVLPYM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDL--FTRlSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID------HE 222
Cdd:cd05058   80 KHGDLrnFIR-SETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDkeyysvHN 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 223 KKAYSFcgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQF 290
Cdd:cd05058  159 HTGAKL--PVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLQGrRLLQPEY 226
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
428-676 2.27e-16

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: 80.68  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTEEIEILLR--------YGQHPNIITLKDV----------- 488
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPENVELALRefwalssiQRQHPNVIQLEECvlqrdglaqrm 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 489 -------------------------YDDGKYVYVVTELMKGGELLDKILRQKFfSEREASAVLFTITKTVEYLHAQGVVH 543
Cdd:cd13977   79 shgssksdlylllvetslkgercfdPRSACYLWFVMEFCDGGDMNEYLLSRRP-DRQTNTSFMLQLSSALAFLHRNQIVH 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 544 RDLKPSNILYVDESGNPeSIRICDFGFAKQLR--AENG---------LLMTPCYTANFVAPEVLKRQgYDAACDIWSLGV 612
Cdd:cd13977  158 RDLKPDNILISHKRGEP-ILKVADFGLSKVCSgsGLNPeepanvnkhFLSSACGSDFYMAPEVWEGH-YTAKADIFALGI 235
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 613 LLYTMLTGYTpFANGpdDTPEEIL---------------ARIGSGKFSLSGGYWN--SVSDTAKDLVSKMLHVDPHQRLT 675
Cdd:cd13977  236 IIWAMVERIT-FRDG--ETKKELLgtyiqqgkeivplgeALLENPKLELQIPLKKkkSMNDDMKQLLRDMLAANPQERPD 312

                 .
gi 768032625 676 A 676
Cdd:cd13977  313 A 313
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
429-681 2.27e-16

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: 80.09  E-value: 2.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 429 EVKEDIGVGSYSVckrcIHKAT-NMEFAVKIIDKSkRDPTEEIEIL------LRYGQHPNIITLKDVYDDGKYVYVVTEL 501
Cdd:cd14063    3 EIKEVIGKGRFGR----VHRGRwHGDVAIKLLNID-YLNEEQLEAFkeevaaYKNTRHDNLVLFMGACMDPPHLAIVTSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdESGNpesIRICDFGFAK-----QLR 575
Cdd:cd14063   78 CKGRTLYSLIHERKEkFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL--ENGR---VVITDFGLFSlsgllQPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 576 AENGLLMTPCYTANFVAPEVLK-------RQG---YDAACDIWSLGVLLYTMLTGYTPFANGPddtPEEILARIGSG-KF 644
Cdd:cd14063  153 RREDTLVIPNGWLCYLAPEIIRalspdldFEEslpFTKASDVYAFGTVWYELLAGRWPFKEQP---AESIIWQVGCGkKQ 229
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 645 SLSGgywNSVSDTAKDLVSKMLHVDPHQRLTAALVLR 681
Cdd:cd14063  230 SLSQ---LDIGREVKDILMQCWAYDPEKRPTFSDLLR 263
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
72-310 2.28e-16

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


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 80.36  E-value: 2.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVfLVKKISGSD-ARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKLYL 145
Cdd:cd14204   13 KVLGEGEFGSV-MEGELQQPDgTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLlgvclEVGSQRIPKPMV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 146 ILDFLRGGDLFTRLSKEVMftEEDVKF--------YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE 217
Cdd:cd14204   92 ILPFMKYGDLHSFLLRSRL--GSGPQHvplqtllkFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKK 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 218 --SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSP 293
Cdd:cd14204  170 iySGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLLHGhRLKQPEDCLD 249
                        250
                 ....*....|....*..
gi 768032625 294 EAQSLLRMLFKRNPANR 310
Cdd:cd14204  250 ELYDIMYSCWRSDPTDR 266
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
432-683 2.56e-16

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: 79.76  E-value: 2.56e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTEEI--EILLR-------YGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd14051    6 EKIGSGEFGSVYKCINRLDGCVYAIK---KSKKPVAGSVdeQNALNevyahavLGKHPHVVRYYSAWAEDDHMIIQNEYC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQK----FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGNPES---------------- 562
Cdd:cd14051   83 NGGSLADAISENEkageRFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI-FISRTPNPVSseeeeedfegeednpe 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 563 -----IRICDFGFA---KQLRAENGllmtpcyTANFVAPEVLkRQGYD--AACDIWSLGVLLYTMLTGYTPFANGPDDTp 632
Cdd:cd14051  162 snevtYKIGDLGHVtsiSNPQVEEG-------DCRFLANEIL-QENYShlPKADIFALALTVYEAAGGGPLPKNGDEWH- 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 768032625 633 eeilaRIGSGKFSlsggYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14051  233 -----EIRQGNLP----PLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
432-643 2.59e-16

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: 80.06  E-value: 2.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRC----IHKATNMEFAVKIIDKSK----RDPTEEIEILlRYGQHPNIITLKDV-YDDGKY-VYVVTEL 501
Cdd:cd14205   10 QQLGKGNFGSVEMCrydpLQDNTGEVVAVKKLQHSTeehlRDFEREIEIL-KSLQHDNIVKYKGVcYSAGRRnLRLIMEY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQKffsER--EASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL--R 575
Cdd:cd14205   89 LPYGSLRDYLQKHK---ERidHIKLLQYTsqICKGMEYLGTKRYIHRDLATRNILVENEN----RVKIGDFGLTKVLpqD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 576 AENGLLMTPCYTANF-VAPEVLKRQGYDAACDIWSLGVLLYTMLTgYTPFANGPddtPEEILARIGSGK 643
Cdd:cd14205  162 KEYYKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYELFT-YIEKSKSP---PAEFMRMIGNDK 226
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
468-624 2.68e-16

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: 79.28  E-value: 2.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 468 EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLdKILRQKFFSEREASAVLFTITKT--VEYLHAQGVVHRD 545
Cdd:cd05085   42 SEARILKQY-DHPNIVKLIGVCTQRQPIYIVMELVPGGDFL-SFLRKKKDELKTKQLVKFSLDAAagMAYLESKNCIHRD 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 546 LKPSNILYvdesGNPESIRICDFGFAKQ----LRAENGLLMTPCytaNFVAPEVLKRQGYDAACDIWSLGVLLY-TMLTG 620
Cdd:cd05085  120 LAARNCLV----GENNALKISDFGMSRQeddgVYSSSGLKQIPI---KWTAPEALNYGRYSSESDVWSFGILLWeTFSLG 192

                 ....
gi 768032625 621 YTPF 624
Cdd:cd05085  193 VCPY 196
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
426-687 2.79e-16

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: 79.70  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdksKRDPTEEIE------ILLRYGQHPNIITLKDVYDDGKYVYVVT 499
Cdd:cd06645   11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVI---KLEPGEDFAvvqqeiIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENG 579
Cdd:cd06645   88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNG----HVKLADFGVSAQITATIA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 LLMTPCYTANFVAPEVL---KRQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFS----LSGGYWn 652
Cdd:cd06645  164 KRKSFIGTPYWMAPEVAaveRKGGYNQLCDIWAVGITAIELAELQPPMF---DLHPMRALFLMTKSNFQppklKDKMKW- 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 768032625 653 svSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVH 687
Cdd:cd06645  240 --SNSFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
67-288 2.80e-16

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 81.33  E-value: 2.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVL---KKATLKVRDRVRT-----KMERDILVEVNHPFivkLHYAFQ 138
Cdd:cd14224   66 RYEVLKVIGKGSFGQVV---KAYDHKTHQHVALKMVrneKRFHRQAAEEIRIlehlkKQDKDNTMNVIHML---ESFTFR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRlSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH--IKLTDFGLSk 216
Cdd:cd14224  140 NHICMTFELLSMNLYELIKK-NKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSS- 217
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 217 eSIDHeKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd14224  218 -CYEH-QRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIEL-LGMP 286
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
66-263 3.10e-16

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 80.07  E-value: 3.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKV----------FLVKKISGSDAR---QLYAMKVLKKatlKVRDRVRTKMERD--ILVEVNHPFI 130
Cdd:cd05051    5 EKLEFVEKLGEGQFGEVhlceanglsdLTSDDFIGNDNKdepVLVAVKMLRP---DASKNAREDFLKEvkIMSQLKDPNI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 131 VKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVK-----------FYLA-ELALALDHLHSLGIIYRDLKPEN 198
Cdd:cd05051   82 VRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASAtnsktlsygtlLYMAtQIASGMKYLESLNFVHRDLATRN 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 199 ILLDEEGHIKLTDFGLSKE--SIDHekkaYSFCGTV----EYMAPEVVNRRGHTQSADWWSFGVLMFEMLT 263
Cdd:cd05051  162 CLVGPNYTIKIADFGMSRNlySGDY----YRIEGRAvlpiRWMAWESILLGKFTTKSDVWAFGVTLWEILT 228
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
67-288 3.35e-16

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: 80.52  E-value: 3.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVflVKKISgSDARQLYAMKVL--KK-------ATLKVRDRVRTKmERDILVEVNHpfiVKLHYAF 137
Cdd:cd14225   44 RYEILEVIGKGSFGQV--VKALD-HKTNEHVAIKIIrnKKrfhhqalVEVKILDALRRK-DRDNSHNVIH---MKEYFYF 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTegklYLILDF-LRGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH--IKLTDF 212
Cdd:cd14225  117 RN----HLCITFeLLGMNLYELIKKNNFqgFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVIDF 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 213 GlskESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd14225  193 G---SSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEV-LGLP 264
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
450-682 3.49e-16

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: 78.90  E-value: 3.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 450 TNMEFAVKIIDKSKRDPTEeIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTI 529
Cdd:cd13995   28 TKKRMACKLIPVEQFKPSD-VEIQACF-RHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHV 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 530 TKTVEYLHAQGVVHRDLKPSNILYVDESGnpesiRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWS 609
Cdd:cd13995  106 LKGLDFLHSKNIIHHDIKPSNIVFMSTKA-----VLVDFGLSVQMTEDVYVPKDLRGTEIYMSPEVILCRGHNTKADIYS 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 610 LGVLLYTMLTGYTPFANG-PDDTPEEILARIGSGKFSLSgGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd13995  181 LGATIIHMQTGSPPWVRRyPRSAYPSYLYIIHKQAPPLE-DIAQDCSPAMRELLEAALERNPNHRSSAAELLKH 253
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
67-282 3.76e-16

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 80.44  E-value: 3.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVflVKKISGSDARQLYAMKVLKKATlKVRDRVRtkMERDILVEV------NHPFIVKLHYAFQTE 140
Cdd:cd14214   14 RYEIVGDLGEGTFGKV--VECLDHARGKSQVALKIIRNVG-KYREAAR--LEINVLKKIkekdkeNKFLCVLMSDWFNFH 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLrGGDLFTRLsKEVMFTE---EDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--------------E 203
Cdd:cd14214   89 GHMCIAFELL-GKNTFEFL-KENNFQPyplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlyneskscE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 204 EGHIK-----LTDFGlsKESIDHEKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMT 278
Cdd:cd14214  167 EKSVKntsirVADFG--SATFDHEHHT-TIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENREHLV 243

                 ....
gi 768032625 279 MILK 282
Cdd:cd14214  244 MMEK 247
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
434-684 4.01e-16

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: 79.36  E-value: 4.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII-------DKSKRDPTEEIEI-LLRYGQHPNIITLKDVYDD--GKYVYVVTELMK 503
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVqfdpespETSKEVSALECEIqLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvDESGNpesIRICDFGFAKQLRA---ENGL 580
Cdd:cd06651   95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILR-DSAGN---VKLGDFGASKRLQTicmSGTG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 581 LMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANgpddtpEEILARIgsgkFSLSGGYWNS-----VS 655
Cdd:cd06651  171 IRSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAI----FKIATQPTNPqlpshIS 240
                        250       260
                 ....*....|....*....|....*....
gi 768032625 656 DTAKDLVSKMLhVDPHQRLTAALVLRHPW 684
Cdd:cd06651  241 EHARDFLGCIF-VEARHRPSAEELLRHPF 268
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
432-635 4.07e-16

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 78.82  E-value: 4.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKiidkSKRD--PTE-------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVK----SCREtlPPDlkakflqEARILKQY-SHPNIVRLIGVCTQKQPIYIVMELV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLdKILRQKffSEREASAVLFTITKTV----EYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQ----- 573
Cdd:cd05084   77 QGGDFL-TFLRTE--GPRLKVKELIRMVENAaagmEYLESKHCIHRDLAARNCLVTEKN----VLKISDFGMSREeedgv 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 LRAENGLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLY-TMLTGYTPFAN-----------------GPDDTPEEI 635
Cdd:cd05084  150 YAATGGMKQIP---VKWTAPEALNYGRYSSESDVWSFGILLWeTFSLGAVPYANlsnqqtreaveqgvrlpCPENCPDEV 226
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
62-261 4.30e-16

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: 80.09  E-value: 4.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADPSQ-FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVL-KKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQT 139
Cdd:cd06635   20 KEDPEKlFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSgKQSNEKWQDIIK---EVKFLQRIKHPNSIEYKGCYLR 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGG--DLFTRLSKEVMFTEEDVKFYLAELALAldHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlske 217
Cdd:cd06635   97 EHTAWLVMEYCLGSasDLLEVHKKPLQEIEIAAITHGALQGLA--YLHSHNMIHRDIKAGNILLTEPGQVKLADFG---- 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 218 SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQ---SADWWSFGVLMFEM 261
Cdd:cd06635  171 SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIEL 217
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
71-270 4.72e-16

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: 79.23  E-value: 4.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFL-VKKISGsdarQLYAMKVLkkaTLKVRDRV--RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd07870    5 LEKLGEGSYATVYKgISRING----QLVALKVI---SMKTEEGVpfTAIREASLLKGLKHANIVLLHDIIHTKETLTFVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGgDLFTRLSKEVM-FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAY 226
Cdd:cd07870   78 EYMHT-DLAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQTYS 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 227 SFCGTVEYMAPEVV-NRRGHTQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd07870  157 SEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
455-642 4.95e-16

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: 78.99  E-value: 4.95e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIDKSKRDPTE---EIEIL--LRygqHPNIITLKDVYDDGKYVYVVTELMKGGELLDkilrqkfFSEREASAVLFT- 528
Cdd:cd05068   36 AVKTLKPGTMDPEDflrEAQIMkkLR---HPKLIQLYAVCTLEEPIYIITELMKHGSLLE-------YLQGKGRSLQLPq 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 -------ITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENgllmtpCYTA--------NFVAP 593
Cdd:cd05068  106 lidmaaqVASGMAYLESQNYIHRDLAARNVL-VGENN---ICKVADFGLARVIKVED------EYEAregakfpiKWTAP 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 594 EVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05068  176 EAANYNRFSIKSDVWSFGILLTEIVTyGRIPY---PGMTNAEVLQQVERG 222
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
433-685 5.07e-16

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: 79.71  E-value: 5.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE-------EIEILLRYgQHPNIITLKDVYDDGKYVYVVTE--LMK 503
Cdd:cd06635   32 EIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEkwqdiikEVKFLQRI-KHPNSIEYKGCYLREHTAWLVMEycLGS 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDkiLRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDesgnPESIRICDFGFAKQLRAENGLLMT 583
Cdd:cd06635  111 ASDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE----PGQVKLADFGSASIASPANSFVGT 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 584 PCYtanfVAPEV---LKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGkfSLSGGYWnsvSDTAKD 660
Cdd:cd06635  185 PYW----MAPEVilaMDEGQYDGKVDVWSLGITCIELAERKPPLFNMNAMSALYHIAQNESP--TLQSNEW---SDYFRN 255
                        250       260
                 ....*....|....*....|....*
gi 768032625 661 LVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06635  256 FVDSCLQKIPQDRPTSEELLKHMFV 280
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
68-311 5.22e-16

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: 79.11  E-value: 5.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFLVKKISGSdarQLYAmkvLKKATLKVRDR-VRTKMERDI--LVEVNH-PFIVKLHYAFQTE--G 141
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTG---KLVA---LKKTRLEMEEEgVPSTALREVslLQMLSQsIYIVRLLDVEHVEenG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 K--LYLILDFLRGG-----DLFTRLSKEVMFTEEdVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE-GHIKLTDFG 213
Cdd:cd07837   77 KplLYLVFEYLDTDlkkfiDSYGRGPHNPLPAKT-IQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 LSK------ESIDHEkkaysfCGTVEYMAPEVVNRRGH-TQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLG 286
Cdd:cd07837  156 LGRaftipiKSYTHE------IVTLWYRAPEVLLGSTHySTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRL-LG 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 287 ------------------MPQF-----------LSPEAQSLLRMLFKRNPANRL 311
Cdd:cd07837  229 tpneevwpgvsklrdwheYPQWkpqdlsravpdLEPEGVDLLTKMLAYDPAKRI 282
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
433-684 5.88e-16

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: 78.99  E-value: 5.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFA------VKIIDKSKRDPTEEIEiLLRYGQHPNIITLKDVYDD----GKYVYVVTELM 502
Cdd:cd14031   17 ELGRGAFKTVYKGLDTETWVEVAwcelqdRKLTKAEQQRFKEEAE-MLKGLQHPNIVRFYDSWESvlkgKKCIVLVTELM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESGnpeSIRICDFGFAKQLRAE--N 578
Cdd:cd14031   96 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG---SVKIGDLGLATLMRTSfaK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPcytaNFVAPEVLKRQgYDAACDIWSLGVLLYTMLTGYTPFANGPDdtPEEILARIGSGkfsLSGGYWNSVSD-T 657
Cdd:cd14031  173 SVIGTP----EFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSECQN--AAQIYRKVTSG---IKPASFNKVTDpE 242
                        250       260
                 ....*....|....*....|....*..
gi 768032625 658 AKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd14031  243 VKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
428-685 6.24e-16

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 79.57  E-value: 6.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYS-VCKRCIHKATNMEFAVKII---DKSKRDPTEEIEILLRYGQHP-----NIITLKDVYDDGKYVYVV 498
Cdd:cd14135    2 YRVYGYLGKGVFSnVVRARDLARGNQEVAIKIIrnnELMHKAGLKELEILKKLNDADpddkkHCIRLLRHFEHKNHLCLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMKGG--ELLDKILRQKFFSereASAV------LFTITKtveYLHAQGVVHRDLKPSNILyVDESGNpeSIRICDFGF 570
Cdd:cd14135   82 FESLSMNlrEVLKKYGKNVGLN---IKAVrsyaqqLFLALK---HLKKCNILHADIKPDNIL-VNEKKN--TLKLCDFGS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQLrAENGLlmTPCYTANFV-APEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGS--GKFS-- 645
Cdd:cd14135  153 ASDI-GENEI--TPYLVSRFYrAPEIILGLPYDYPIDMWSVGCTLYELYTGKILF---PGKTNNHMLKLMMDlkGKFPkk 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 646 ----------------------------------------------LSGGYWNSVSDTAK------DLVSKMLHVDPHQR 673
Cdd:cd14135  227 mlrkgqfkdqhfdenlnfiyrevdkvtkkevrrvmsdikptkdlktLLIGKQRLPDEDRKkllqlkDLLDKCLMLDPEKR 306
                        330
                 ....*....|..
gi 768032625 674 LTAALVLRHPWI 685
Cdd:cd14135  307 ITPNEALQHPFI 318
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
430-684 7.44e-16

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: 78.89  E-value: 7.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKED-IGVGSYSVCKRCIHKATNMEFAVKII--DKSKRDPTEEI-EI-LLRYGQHPNIITLKDVYDDGKYVYVVTELmkg 504
Cdd:cd07873    5 IKLDkLGEGTYATVYKGRSKLTDNLVALKEIrlEHEEGAPCTAIrEVsLLKDLKHANIVTLHDIIHTEKSLTLVFEY--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 gelLDKILRQ------KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAEN 578
Cdd:cd07873   82 ---LDKDLKQylddcgNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLL-INERG---ELKLADFGLARAKSIPT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSLSGG----YWNS 653
Cdd:cd07873  155 KTYSNEVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLF---PGSTVEEQLHFI----FRILGTpteeTWPG 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 654 V---------------------------SDTAkDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07873  228 IlsneefksynypkyradalhnhaprldSDGA-DLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
67-310 7.76e-16

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: 79.75  E-value: 7.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVflvkkISGSDA--RQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL- 143
Cdd:cd07874   18 RYQNLKPIGSGAQGIV-----CAAYDAvlDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLe 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 -----YLILDfLRGGDLFTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd07874   93 efqdvYLVME-LMDANLCQVIQMEL--DHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 219 iDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMPqflSPEAQSL 298
Cdd:cd07874  170 -GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIE-QLGTP---CPEFMKK 244
                        250
                 ....*....|..
gi 768032625 299 LRMLFKRNPANR 310
Cdd:cd07874  245 LQPTVRNYVENR 256
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
428-684 7.85e-16

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 79.29  E-value: 7.85e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCI-HKATNMEFAVKII---DKSKRDPTEEIEILLRYGQH-PN----IITLKDVYDDGKYVYVV 498
Cdd:cd14215   14 YEIVSTLGEGTFGRVVQCIdHRRGGARVALKIIknvEKYKEAARLEINVLEKINEKdPEnknlCVQMFDWFDYHGHMCIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 TELMkGGELLDKILRQKFF--SEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYV---------------DESGNPE 561
Cdd:cd14215   94 FELL-GLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlekkrdERSVKST 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 562 SIRICDFGFAKQLRAENGLLMTpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAN--------------G 627
Cdd:cd14215  173 AIRVVDFGSATFDHEHHSTIVS---TRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQThdnrehlammerilG 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 628 PddTPEEILARIGSGKFSLSGGY-WNSVSDTAK------------------------DLVSKMLHVDPHQRLTAALVLRH 682
Cdd:cd14215  250 P--IPSRMIRKTRKQKYFYHGRLdWDENTSAGRyvrenckplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAALKH 327

                 ..
gi 768032625 683 PW 684
Cdd:cd14215  328 PF 329
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
67-288 7.89e-16

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: 78.85  E-value: 7.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQT---- 139
Cdd:cd07863    1 QYEPVAEIGVGAYGTVY---KARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLeafDHPNIVRLMDVCATsrtd 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 -EGKLYLILDFLrGGDLFTRLSKEVM--FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSk 216
Cdd:cd07863   78 rETKVTLVFEHV-DQDLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 217 esidhekKAYSF-------CGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILkAKLGMP 288
Cdd:cd07863  156 -------RIYSCqmaltpvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIF-DLIGLP 226
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
74-262 8.05e-16

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: 78.32  E-value: 8.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkKISGSDARQLYAMKVLKKATlkvrdrvrTKMERDILVEV------NHPFIVKLHYAFQTEGKLYLIL 147
Cdd:cd14154    1 LGKGFFGQAI---KVTHRETGEVMVMKELIRFD--------EEAQRNFLKEVkvmrslDHPNVLKFIGVLYKDKKLNLIT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDL--FTRLSKEVMFTEEDVKFyLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDHE--- 222
Cdd:cd14154   70 EYIPGGTLkdVLKDMARPLPWAQRVRF-AKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLAR-LIVEErlp 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 223 ------------------KKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14154  148 sgnmspsetlrhlkspdrKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
100-333 8.13e-16

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


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 78.52  E-value: 8.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 100 KVLKKATLKVRDRVRTKMERDI--LVEVNHPFIV---------KLHYAFQTE---GKLYLIL-DFLRGGDLFTRLSKEVM 164
Cdd:cd14011   32 KQLEEYSKRDREQILELLKRGVkqLTRLRHPRILtvqhpleesRESLAFATEpvfASLANVLgERDNMPSPPPELQDYKL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 165 FTEEdVKFYLAELALALDHLH-SLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCG-----------TV 232
Cdd:cd14011  112 YDVE-IKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpNL 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 233 EYMAPEVVNRRGHTQSADWWSFGVLMFEML-TGTLPFQGKDRKET----MTMILKAKLGMPQFLSPEAQSLLRMLFKRNP 307
Cdd:cd14011  191 NYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSykknSNQLRQLSLSLLEKVPEELRDHVKTLLNVTP 270
                        250       260
                 ....*....|....*....|....*.
gi 768032625 308 ANRlvnpfligagPDgVEEIKRHSFF 333
Cdd:cd14011  271 EVR----------PD-AEQLSKIPFF 285
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
469-683 8.18e-16

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: 77.79  E-value: 8.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 469 EIEILLRYgQHPNIITL------KDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVV 542
Cdd:cd14012   48 ELESLKKL-RHPNLVSYlafsieRRGRSDGWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHRNGVV 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 543 HRDLKPSNILyVDESGNPESIRICDFGFAKQLRAENG----LLMTPCYtanFVAPEVLKRQG-YDAACDIWSLGVLLYTM 617
Cdd:cd14012  127 HKSLHAGNVL-LDRDAGTGIVKLTDYSLGKTLLDMCSrgslDEFKQTY---WLPPELAQGSKsPTRKTDVWDLGLLFLQM 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 618 LTGytpfangpDDTPEeilarigsgKFSLSGGYWNSV--SDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14012  203 LFG--------LDVLE---------KYTSPNPVLVSLdlSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
428-704 8.46e-16

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: 78.61  E-value: 8.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTE---EIEILLRYGQHPNIITLKDVY--------DDgkYVY 496
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEikqEINMLKKYSHHRNIATYYGAFikknppgmDD--QLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 497 VVTELMKGGELLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL 574
Cdd:cd06637   86 LVMEFCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGLLMTPCYTANFVAPEVLK-----RQGYDAACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKF-SLSG 648
Cdd:cd06637  162 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLC---DMHPMRALFLIPRNPApRLKS 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 649 GYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVhwDQLPQYQLNRQDAPHL 704
Cdd:cd06637  239 KKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFIR--DQPNERQVRIQLKDHI 289
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
434-626 8.58e-16

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: 77.88  E-value: 8.58e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEIL-----LRYGQHPNIITLKDVYDDGKYVYVVTELMKGG--- 505
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLkeaekMERARHSYVLPLLGVCVERRSLGLVMEYMENGslk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKI-------LRQKFFSEreasavlftITKTVEYLH--AQGVVHRDLKPSNILyVDESGNpesIRICDFGFAK---- 572
Cdd:cd13978   81 SLLEREiqdvpwsLRFRIIHE---------IALGMNFLHnmDPPLLHHDLKPENIL-LDNHFH---VKISDFGLSKlgmk 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 573 -----QLRAENGLLMTPCYTanfvAPEVLKRQGY--DAACDIWSLGVLLYTMLTGYTPFAN 626
Cdd:cd13978  148 sisanRRRGTENLGGTPIYM----APEAFDDFNKkpTSKSDVYSFAIVIWAVLTRKEPFEN 204
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
429-624 8.76e-16

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: 77.99  E-value: 8.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 429 EVKEDIGVGSY-SVCKRCIHKATNMEFAVKI-------IDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05065    7 KIEEVIGAGEFgEVCRGRLKLPGKREIFVAIktlksgyTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRPVMIITE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGElLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPESI-RICDFGFAKQLRAE 577
Cdd:cd05065   86 FMENGA-LDSFLRQNdgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILV-----NSNLVcKVSDFGLSRFLEDD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 578 NGllmTPCYTAN--------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05065  160 TS---DPTYTSSlggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 212
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
432-635 1.17e-15

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: 77.38  E-value: 1.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATN---MEFAVKIIDKSK-------RDPTEEIEILLRYgQHPNIITLKDVYDDGKyVYVVTEL 501
Cdd:cd05040    1 EKLGDGSFGVVRRGEWTTPSgkvIQVAVKCLKSDVlsqpnamDDFLKEVNAMHSL-DHPNLIRLYGVVLSSP-LMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKiLRqkffsEREASAVLFT-------ITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQL 574
Cdd:cd05040   79 APLGSLLDR-LR-----KDQGHFLISTlcdyavqIANGMAYLESKRFIHRDLAARNILLA----SKDKVKIGDFGLMRAL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGllmtpCYTANF--------VAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFA--NG---------------- 627
Cdd:cd05040  149 PQNED-----HYVMQEhrkvpfawCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLglNGsqilekidkegerler 223

                 ....*...
gi 768032625 628 PDDTPEEI 635
Cdd:cd05040  224 PDDCPQDI 231
pknD PRK13184
serine/threonine-protein kinase PknD;
68-310 1.18e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 81.36  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFL-----------VKKISgsdaRQLYAMKVLKKATLKvrdrvrtkmERDILVEVNHPFIVKLhYA 136
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLaydpvcsrrvaLKKIR----EDLSENPLLKKRFLR---------EAKIAADLIHPGIVPV-YS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 137 FQTEGKL-YLILDFLRGGDLFTRL----SKEVMFTE----EDVKFYLA---ELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:PRK13184  70 ICSDGDPvYYTMPYIEGYTLKSLLksvwQKESLSKElaekTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLF 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GHIKLTDFG--LSKE---------SIDHEKKAYS-------FCGTVEYMAPEVVnrRGH--TQSADWWSFGVLMFEMLTG 264
Cdd:PRK13184 150 GEVVILDWGaaIFKKleeedlldiDVDERNICYSsmtipgkIVGTPDYMAPERL--LGVpaSESTDIYALGVILYQMLTL 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 265 TLPFQGKDRKEtmtMILKAKLGMPQFLSPE-------AQSLLRMLfKRNPANR 310
Cdd:PRK13184 228 SFPYRRKKGRK---ISYRDVILSPIEVAPYreippflSQIAMKAL-AVDPAER 276
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
466-634 1.21e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 79.15  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 466 PTEEIE-ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHR 544
Cdd:PHA03209 102 GTTLIEaMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 545 DLKPSNILYVDESgnpeSIRICDFGFAK-QLRAENGLLMTPCYTANfvAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTP 623
Cdd:PHA03209 182 DVKTENIFINDVD----QVCIGDLGAAQfPVVAPAFLGLAGTVETN--APEVLARDKYNSKADIWSAGIVLFEMLAYPST 255
                        170
                 ....*....|.
gi 768032625 624 FANGPDDTPEE 634
Cdd:PHA03209 256 IFEDPPSTPEE 266
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
73-310 1.23e-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: 78.12  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVflVKKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05089    9 VIGEGNFGQV--IKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYAP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFtEEDVKF-----------------YLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd05089   87 YGNLLDFLRKSRVL-ETDPAFakehgtastltsqqllqFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYSFCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLS 292
Cdd:cd05089  166 SRGEEVYVKKTMGRL-PVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRMEKPRNCD 244
                        250
                 ....*....|....*...
gi 768032625 293 PEAQSLLRMLFKRNPANR 310
Cdd:cd05089  245 DEVYELMRQCWRDRPYER 262
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
67-310 1.23e-15

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: 78.89  E-value: 1.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKV-----FLVKKisgSDARQLYAMKVLKK-ATLKVRDRVRTKMErdILVEVNHPF-IVKLHYA-FQ 138
Cdd:cd14207    8 RLKLGKSLGRGAFGKVvqasaFGIKK---SPTCRVVAVKMLKEgATASEYKALMTELK--ILIHIGHHLnVVNLLGAcTK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRL-SKEVMF---------------------------------------------------- 165
Cdd:cd14207   83 SGGPLMVIVEYCKYGNLSNYLkSKRDFFvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedkslsdv 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 166 ---------------TEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE---SIDHEKKAYS 227
Cdd:cd14207  163 eeeeedsgdfykrplTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDiykNPDYVRKGDA 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 FCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAKLGM--PQFLSPEAQSLLRMLFK 304
Cdd:cd14207  243 RL-PLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMraPEFATSEIYQIMLDCWQ 321

                 ....*.
gi 768032625 305 RNPANR 310
Cdd:cd14207  322 GDPNER 327
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
67-288 1.28e-15

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: 79.32  E-value: 1.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVflvkkISGSDA--RQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL- 143
Cdd:cd07875   25 RYQNLKPIGSGAQGIV-----CAAYDAilERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLe 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 -----YLILDfLRGGDLFTRLSKEVmfTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKES 218
Cdd:cd07875  100 efqdvYIVME-LMDANLCQVIQMEL--DHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTA 176
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 219 idhekkAYSFCGTVE-----YMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKaKLGMP 288
Cdd:cd07875  177 ------GTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIE-QLGTP 244
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
73-310 1.31e-15

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: 77.30  E-value: 1.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFlvkkiSGSDARQLYAMKVLKK-ATLKVrdrvrTKMERDILVEVNHPFIVKLhYAFQTEGKLyLILDFLR 151
Cdd:cd14068    1 LLGDGGFGSVY-----RAVYRGEDVAVKIFNKhTSFRL-----LRQELVVLSHLHHPSLVAL-LAAGTAPRM-LVMELAP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLA-ELALALDHLHSLGIIYRDLKPENILL-----DEEGHIKLTDFGLSKESIDHEKKa 225
Cdd:cd14068   69 KGSLDALLQQDNASLTRTLQHRIAlHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIK- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 226 ySFCGTVEYMAPEVVnrRG---HTQSADWWSFGVLMFEMLT-GTLPFQG-KDRKETMTMILKAKLGMPQFLS-----PEA 295
Cdd:cd14068  148 -TSEGTPGFRAPEVA--RGnviYNQQADVYSFGLLLYDILTcGERIVEGlKFPNEFDELAIQGKLPDPVKEYgcapwPGV 224
                        250
                 ....*....|....*
gi 768032625 296 QSLLRMLFKRNPANR 310
Cdd:cd14068  225 EALIKDCLKENPQCR 239
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
72-310 1.36e-15

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: 77.38  E-value: 1.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGkvfLVKK----ISGSDARQLyAMKVLKKATLKVRDRVRtkmerDILVEVN------HPFIVKLhYAFQTEG 141
Cdd:cd05040    1 EKLGDGSFG---VVRRgewtTPSGKVIQV-AVKCLKSDVLSQPNAMD-----DFLKEVNamhsldHPNLIRL-YGVVLSS 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLFTRLSKE----VMFTEEDvkfYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK- 216
Cdd:cd05040   71 PLMMVTELAPLGSLLDRLRKDqghfLISTLCD---YAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRa 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 --------ESIDHEKKAYSFCgtveymAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKdrkeTMTMILKA---- 283
Cdd:cd05040  148 lpqnedhyVMQEHRKVPFAWC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGL----NGSQILEKidke 217
                        250       260
                 ....*....|....*....|....*....
gi 768032625 284 --KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05040  218 geRLERPDDCPQDIYNVMLQCWAHKPADR 246
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
66-310 1.37e-15

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: 77.22  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvkkiSGSDARQLYAMKVLK-----KATLKvrdrvrtkmERDILVEVNHPFIVKLHYAFQTE 140
Cdd:cd05083    6 QKLTLGEIIGEGEFGAVL-----QGEYMGQKVAVKNIKcdvtaQAFLE---------ETAVMTKLQHKNLVRLLGVILHN 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GkLYLILDFLRGGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK-- 216
Cdd:cd05083   72 G-LYIVMELMSKGNLvnFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKvg 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 -ESIDHEKKAysfcgtVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSP 293
Cdd:cd05083  151 sMGVDNSRLP------VKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAVEKGyRMEPPEGCPP 224
                        250
                 ....*....|....*..
gi 768032625 294 EAQSLLRMLFKRNPANR 310
Cdd:cd05083  225 DVYSIMTSCWEAEPGKR 241
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
434-614 1.39e-15

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: 77.15  E-value: 1.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII--DKSKRDPTEEIEiLLRYGQHPNIITLKDV-YDDGKyVYVVTELMKGG---EL 507
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELkrFDEQRSFLKEVK-LMRRLSHPNILRFIGVcVKDNK-LNFITEYVNGGtleEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVlfTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIrICDFGFAKQL------RAENGLL 581
Cdd:cd14065   79 LKSMDEQLPWSQRVSLAK--DIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAV-VADFGLAREMpdektkKPDRKKR 155
                        170       180       190
                 ....*....|....*....|....*....|...
gi 768032625 582 MTPCYTANFVAPEVLKRQGYDAACDIWSLGVLL 614
Cdd:cd14065  156 LTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVL 188
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-633 1.42e-15

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 78.56  E-value: 1.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS-----KRDPTEEIEILlRYGQHPNIITLKDV-YDDGKyVYVVT 499
Cdd:cd06650    5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEikpaiRNQIIRELQVL-HECNSPYIVGFYGAfYSDGE-ISICM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELlDKILRQK-FFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRae 577
Cdd:cd06650   83 EHMDGGSL-DQVLKKAgRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNIL-VNSRG---EIKLCDFGVSGQLI-- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 578 NGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFAngPDDTPE 633
Cdd:cd06650  156 DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIP--PPDAKE 209
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
71-288 1.46e-15

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: 78.11  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  71 LKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKkatLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 148
Cdd:cd07872   11 LEKLGEGTYATVF---KGRSKLTENLVALKEIR---LEHEEGAPCTAIREVslLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLrGGDLftrlsKEVM------FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd07872   85 YL-DKDL-----KQYMddcgniMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPT 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 223 KKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07872  159 KTYSNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRL-LGTP 224
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
432-683 1.72e-15

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 77.28  E-value: 1.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTE---------EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd14139    6 EKIGVGEFGSVYKCIKRLDGCVYAIK---RSMRPFAGssneqlalhEVYAHAVLGHHPHVVRYYSAWAEDDHMIIQNEYC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQ----KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY----------VDESGNPES------ 562
Cdd:cd14139   83 NGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIchkmqsssgvGEEVSNEEDeflsan 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 563 --IRICDFGFAKQL---RAENGllmtpcyTANFVAPEVLKRQ-GYDAACDIWSLGvLLYTMLTGYTPFANGPDDtpeeiL 636
Cdd:cd14139  163 vvYKIGDLGHVTSInkpQVEEG-------DSRFLANEILQEDyRHLPKADIFALG-LTVALAAGAEPLPTNGAA-----W 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 637 ARIGSGKFSlsgGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14139  230 HHIRKGNFP---DVPQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
67-317 2.12e-15

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: 78.10  E-value: 2.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKK--ISGSDARQLYAMKVLKKATLKVRDRVRTKmERDILVEV-NHPFIVKLHYA-FQTEGK 142
Cdd:cd05102    8 RLRLGKVLGHGAFGKVVEASAfgIDKSSSCETVAVKMLKEGATASEHKALMS-ELKILIHIgNHLNVVNLLGAcTKPNGP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDL--FTRLSKEVM-------------------------------------------------------- 164
Cdd:cd05102   87 LMVIVEFCKYGNLsnFLRAKREGFspyrersprtrsqvrsmveavradrrsrqgsdrvasftestsstnqprqevddlwq 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 165 --FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE---SIDHEKKAYSFCgTVEYMAPEV 239
Cdd:cd05102  167 spLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDiykDPDYVRKGSARL-PLKWMAPES 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 240 VNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILK--AKLGMPQFLSPEAQSLLRMLFKRNPANRLVNPFL 316
Cdd:cd05102  246 IFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCQRLKdgTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDL 325

                 .
gi 768032625 317 I 317
Cdd:cd05102  326 V 326
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
64-310 2.37e-15

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: 77.35  E-value: 2.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVfLVKKISGSDARQLYAMKVLKKATLKvRDRVRTKMERDILVEVN-HPFIVKLHYAFQTEGK 142
Cdd:cd05088    5 EWNDIKFQDVIGEGNFGQV-LKARIKKDGLRMDAAIKRMKEYASK-DDHRDFAGELEVLCKLGhHPNIINLLGACEHRGY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFtEEDVKF-----------------YLAELALALDHLHSLGIIYRDLKPENILLDEEG 205
Cdd:cd05088   83 LYLAIEYAPHGNLLDFLRKSRVL-ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 206 HIKLTDFGLSKESIDHEKKAYSFCgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI-LKA 283
Cdd:cd05088  162 VAKIADFGLSRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpQGY 240
                        250       260
                 ....*....|....*....|....*..
gi 768032625 284 KLGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05088  241 RLEKPLNCDDEVYDLMRQCWREKPYER 267
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
435-624 2.45e-15

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: 76.15  E-value: 2.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 435 GVGSYSVCKRCIHKATNMEFAVKIIDKSKRdpteEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQ 514
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEK----EAEIL-SVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD-YLNS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 515 KFFSEREASAVL---FTITKTVEYLHAQG---VVHRDLKPSNILYVDESgnpeSIRICDFGfAKQLRAENgLLMTPCYTA 588
Cdd:cd14060   76 NESEEMDMDQIMtwaTDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADG----VLKICDFG-ASRFHSHT-THMSLVGTF 149
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 768032625 589 NFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd14060  150 PWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
433-673 2.87e-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: 76.56  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSY---SVCKRCI-HKATNMEFAVkiidkskrdpteEIEILLRYgQHPNIITLKDV-YDDGKYVYVVTELMKGGEL 507
Cdd:cd05082   21 DVMLGDYrgnKVAVKCIkNDATAQAFLA------------EASVMTQL-RHSNLVQLLGViVEEKGGLYIVTEYMAKGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDkILRQKFFSEREASAVL---FTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd05082   88 VD-YLRSRGRSVLGGDCLLkfsLDVCEAMEYLEGNNFVHRDLAARNVLVSEDN----VAKVSDFGLTKEASSTQDTGKLP 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 cytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG-KFSLSGGywnsVSDTAKDLV 662
Cdd:cd05082  163 ---VKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY---PRIPLKDVVPRVEKGyKMDAPDG----CPPAVYDVM 232
                        250
                 ....*....|.
gi 768032625 663 SKMLHVDPHQR 673
Cdd:cd05082  233 KNCWHLDAAMR 243
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
74-310 2.87e-15

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 76.61  E-value: 2.87e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVF--LVKKISGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05062   14 LGQGSFGMVYegIAKGVVKDEPETRVAIKTVNEAA-SMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYL----------AELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE--SI 219
Cdd:cd05062   93 RGDLKSYLRSLRPEMENNPVQAPpslkkmiqmaGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDiyET 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 220 DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAK-LGMPQFLSPEAQS 297
Cdd:cd05062  173 DYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVLRFVMEGGlLDKPDNCPDMLFE 252
                        250
                 ....*....|...
gi 768032625 298 LLRMLFKRNPANR 310
Cdd:cd05062  253 LMRMCWQYNPKMR 265
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
446-631 2.96e-15

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 77.14  E-value: 2.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 446 IHKATNMEFAVKIIdKSKRDPTE------EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQK--FF 517
Cdd:cd05055   60 SKSDAVMKVAVKML-KPTAHSSErealmsELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKResFL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAEN-----GLLMTPcytANFVA 592
Cdd:cd05055  139 TLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLT----HGKIVKICDFGLARDIMNDSnyvvkGNARLP---VKWMA 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 768032625 593 PEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDT 631
Cdd:cd05055  212 PESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDS 251
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
72-265 3.01e-15

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: 77.01  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKISGSDARQLYAMKVLKKA-------TLKVRDRVRtkmerdilvevNHPF---IVKLHYAFQTEG 141
Cdd:cd13981    6 KELGEGGYASVYLAKDDDEQSDGSLVALKVEKPPsiwefyiCDQLHSRLK-----------NSRLresISGAHSAHLFQD 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGGDLF-----TRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL------DEEGH---- 206
Cdd:cd13981   75 ESILVMDYSSQGTLLdvvnkMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicaDWPGEgeng 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 207 -----IKLTDFGlskESID----HEKKAY-SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGT 265
Cdd:cd13981  155 wlskgLKLIDFG---RSIDmslfPKNQSFkADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFGK 220
pknD PRK13184
serine/threonine-protein kinase PknD;
479-681 3.03e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.81  E-value: 3.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYDDGKYVYVVTELMKGgELLDKILR--------QKFFSEREASAVLF----TITKTVEYLHAQGVVHRDL 546
Cdd:PRK13184  61 HPGIVPVYSICSDGDPVYYTMPYIEG-YTLKSLLKsvwqkeslSKELAEKTSVGAFLsifhKICATIEYVHSKGVLHRDL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 547 KPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMT-------PCY-----------TANFVAPEVLKRQGYDAACDIW 608
Cdd:PRK13184 140 KPDNILL----GLFGEVVILDWGAAIFKKLEEEDLLDidvdernICYssmtipgkivgTPDYMAPERLLGVPASESTDIY 215
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 609 SLGVLLYTMLTGYTPFANG-----PDD----TPEEILArigsgkfslsggyWNSVSDTAKDLVSKMLHVDPHQRLTAALV 679
Cdd:PRK13184 216 ALGVILYQMLTLSFPYRRKkgrkiSYRdvilSPIEVAP-------------YREIPPFLSQIAMKALAVDPAERYSSVQE 282

                 ..
gi 768032625 680 LR 681
Cdd:PRK13184 283 LK 284
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
430-684 3.23e-15

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: 76.97  E-value: 3.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKED-IGVGSYSVCKRCIHKATNMEFAVKII--DKSKRDPTEEI-EI-LLRYGQHPNIITLKDVYDDGKYVYVVTELmkg 504
Cdd:cd07871    8 VKLDkLGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAIrEVsLLKNLKHANIVTLHDIIHTERCLTLVFEY--- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 gelLDKILRQ------KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAEN 578
Cdd:cd07871   85 ---LDSDLKQyldncgNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLL-INEKG---ELKLADFGLARAKSVPT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 579 GLLMTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIgsgkFSLSGG----YWNS 653
Cdd:cd07871  158 KTYSNEVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMF---PGSTVKEELHLI----FRLLGTpteeTWPG 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 654 VSDTAK--------------------------DLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07871  231 VTSNEEfrsylfpqyraqplinhaprldtdgiDLLSSLLLYETKSRISAEAALRHSY 287
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
67-288 3.42e-15

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 76.78  E-value: 3.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkkisgsDARQLYAMKV--LKKATLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEG 141
Cdd:PLN00009   3 QYEKVEKIGEGTYGVVY--------KARDRVTNETiaLKKIRLEQEDEgVPSTAIREIslLKEMQHGNIVRLQDVVHSEK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLrGGDLFTRLSKEVMFTEED--VKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH-IKLTDFGLSK-- 216
Cdd:PLN00009  75 RLYLVFEYL-DLDLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARaf 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 217 ----ESIDHEkkaysfCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:PLN00009 154 gipvRTFTHE------VVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRI-LGTP 223
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
432-642 4.47e-15

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: 75.76  E-value: 4.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVckrcIHKA---TNMEFAVKIIDK---SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd05112   10 QEIGSGQFGL----VHLGywlNKDKVAIKTIREgamSEEDFIEEAEVMMKL-SHPKLVQLYGVCLEQAPICLVFEFMEHG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESgnpESIRICDFGFAK-----QLRAENG 579
Cdd:cd05112   85 CLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCL-VGEN---QVVKVSDFGMTRfvlddQYTSSTG 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 580 llmtPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANgpdDTPEEILARIGSG 642
Cdd:cd05112  161 ----TKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYEN---RSNSEVVEDINAG 217
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
64-268 4.90e-15

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: 76.06  E-value: 4.90e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  64 DPSQFELLKVLGQGSFGKVFLVK-KISGSdaRQLY-AMKVLKkATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG 141
Cdd:cd05065    2 DVSCVKIEEVIGAGEFGEVCRGRlKLPGK--REIFvAIKTLK-SGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGG--DLFTRLsKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSK--- 216
Cdd:cd05065   79 PVMIITEFMENGalDSFLRQ-NDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfle 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 217 ESIDHEKKAYSFCGT--VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPF 268
Cdd:cd05065  158 DDTSDPTYTSSLGGKipIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 212
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
434-632 4.92e-15

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 75.63  E-value: 4.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKI----IDKSKRdpTEEIEILLRYgQHPNIIT-LKDVYDDGKyVYVVTELMKGGELL 508
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIykndVDQHKI--VREISLLQKL-SHPNIVRyLGICVKDEK-LHPILEYVSGGCLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DKILRQKF-FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIrICDFGFAKQL----RAENGLLMT 583
Cdd:cd14156   77 ELLAREELpLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAV-VTDFGLAREVgempANDPERKLS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 584 PCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTpfANgPDDTP 632
Cdd:cd14156  156 LVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIP--AD-PEVLP 201
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
74-268 4.95e-15

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: 76.01  E-value: 4.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVK-KISGsdarqlyamkvLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQtEGKLYLIL-DFLR 151
Cdd:cd13991   14 IGRGSFGEVHRMEdKQTG-----------FQCAVKKVRLEVFRAEELMACAGLTSPRVVPLYGAVR-EGPWVNIFmDLKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEG-HIKLTDFGLSkESIDHEKKAYS--- 227
Cdd:cd13991   82 GGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHA-ECLDPDGLGKSlft 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 228 ---FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd13991  161 gdyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
62-261 5.01e-15

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: 76.60  E-value: 5.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  62 KADPSQ-FELLKVLGQGSFGKVFLVKKISGSDARQLYAMKVL-KKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQT 139
Cdd:cd06634   10 KDDPEKlFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSgKQSNEKWQDIIK---EVKFLQKLRHPNTIEYRGCYLR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGG--DLFTRLSKEVMFTEEDVKFYLAELALAldHLHSLGIIYRDLKPENILLDEEGHIKLTDFGlske 217
Cdd:cd06634   87 EHTAWLVMEYCLGSasDLLEVHKKPLQEVEIAAITHGALQGLA--YLHSHNMIHRDVKAGNILLTEPGLVKLGDFG---- 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 768032625 218 SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQ---SADWWSFGVLMFEM 261
Cdd:cd06634  161 SASIMAPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIEL 207
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
428-612 5.72e-15

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: 75.84  E-value: 5.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE---ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQqeiFMVKECKHCNIVAYFGSYLSREKLWICMEYCGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd06646   91 GSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNG----DVKLADFGVAAKITATIAKRKSF 166
                        170       180       190
                 ....*....|....*....|....*....|.
gi 768032625 585 CYTANFVAPEVL---KRQGYDAACDIWSLGV 612
Cdd:cd06646  167 IGTPYWMAPEVAaveKNGGYNQLCDIWAVGI 197
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
432-683 5.95e-15

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 75.83  E-value: 5.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIIDK------SKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd14138   11 EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQNEYCNGG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKIL----RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIL--------------YVDESGNPESI-RIC 566
Cdd:cd14138   91 SLADAISenyrIMSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFisrtsipnaaseegDEDEWASNKVIfKIG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 567 DFGFAKQL---RAENGllmtpcyTANFVAPEVLKrQGYD--AACDIWSLGVLLYTMlTGYTPFANGPD---DTPEEILAR 638
Cdd:cd14138  171 DLGHVTRVsspQVEEG-------DSRFLANEVLQ-ENYThlPKADIFALALTVVCA-AGAEPLPTNGDqwhEIRQGKLPR 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 639 IGsgkfslsggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHP 683
Cdd:cd14138  242 IP-----------QVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
66-280 6.21e-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: 75.83  E-value: 6.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVF---LVKKISGsDARQLYAMKVLK-KATLKVRDRVRTK-MERDILvevNHPFIVKLHYAFQTE 140
Cdd:cd05091    6 SAVRFMEELGEDRFGKVYkghLFGTAPG-EQTQAVAIKTLKdKAEGPLREEFRHEaMLRSRL---QHPNIVCLLGVVTKE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDLFTRL--------------SKEVMFTEEDVKFY--LAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd05091   82 QPMSMIFSYCSHGDLHEFLvmrsphsdvgstddDKTVKSTLEPADFLhiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 205 GHIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMI 280
Cdd:cd05091  162 LNVKISDLGLFREvyAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMI 240
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
455-624 6.79e-15

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: 75.92  E-value: 6.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILRQKFFSEREASAVL--- 526
Cdd:cd05053   47 AVKMLkddatEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVVVEYASKGNLRE-FLRARRPPGEEASPDDprv 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 527 --------------FTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLR-------AENGLLmtpc 585
Cdd:cd05053  126 peeqltqkdlvsfaYQVARGMEYLASKKCIHRDLAARNVLVTED----NVMKIADFGLARDIHhidyyrkTTNGRL---- 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 768032625 586 yTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05053  198 -PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY 236
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
529-642 7.23e-15

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: 75.12  E-value: 7.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 ITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFA--KQLRAENGLLMTPCYTANFVAPEVLKRQG---YDA 603
Cdd:cd14062   98 TAQGMDYLHAKNIIHRDLKSNNIFLHEDL----TVKIGDFGLAtvKTRWSGSQQFEQPTGSILWMAPEVIRMQDenpYSF 173
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 768032625 604 ACDIWSLGVLLYTMLTGYTPFAN-GPDDtpeEILARIGSG 642
Cdd:cd14062  174 QSDVYAFGIVLYELLTGQLPYSHiNNRD---QILFMVGRG 210
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
426-684 7.50e-15

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: 76.03  E-value: 7.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKI----IDKSKRDPT--EEIEILLRYGQHPNIITLKDVY---DDGK-YV 495
Cdd:cd07837    1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKtrleMEEEGVPSTalREVSLLQMLSQSIYIVRLLDVEhveENGKpLL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELmkggelLDKILRQKFFSEREASA----------VLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGnpeSIRI 565
Cdd:cd07837   81 YLVFEY------LDTDLKKFIDSYGRGPHnplpaktiqsFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKG---LLKI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 566 CDFG----FAKQLRAENGLLMTPCYTanfvAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIg 640
Cdd:cd07837  152 ADLGlgraFTIPIKSYTHEIVTLWYR----APEVlLGSTHYSTPVDMWSVGCIFAEMSRKQPLF---PGDSELQQLLHI- 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 641 sgkFSLSGG----YWNSVS--------------DTAK----------DLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07837  224 ---FRLLGTpneeVWPGVSklrdwheypqwkpqDLSRavpdlepegvDLLTKMLAYDPAKRISAKAALQHPY 292
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
74-318 7.51e-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: 75.49  E-value: 7.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLvkkiSGSDARQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLILDFLRGG 153
Cdd:cd05071   17 LGQGCFGEVWM----GTWNGTTRVAIKTLKPGTMSPEAFLQ---EAQVMKKLRHEKLVQL-YAVVSEEPIYIVTEYMSKG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEV--MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYSFCG- 230
Cdd:cd05071   89 SLLDFLKGEMgkYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAKf 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 231 TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRMLFKRNPA 308
Cdd:cd05071  169 PIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGyRMPCPPECPESLHDLMCQCWRKEPE 248
                        250
                 ....*....|
gi 768032625 309 NRLVNPFLIG 318
Cdd:cd05071  249 ERPTFEYLQA 258
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
432-684 7.57e-15

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: 75.77  E-value: 7.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI----LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGEL 507
Cdd:cd07870    6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAIreasLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTDLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIL--YVDEsgnpesIRICDFGFAkqlRAENgllmTPC 585
Cdd:cd07870   86 QYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLisYLGE------LKLADFGLA---RAKS----IPS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 586 --YTANFVA-----PEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFAnGPDDTPEEiLARIGSGKFSLSGGYWNSVSD- 656
Cdd:cd07870  153 qtYSSEVVTlwyrpPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFP-GVSDVFEQ-LEKIWTVLGVPTEDTWPGVSKl 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 657 ---------------------------TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07870  231 pnykpewflpckpqqlrvvwkrlsrppKAEDLASQMLMMFPKDRISAQDALLHPY 285
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
68-288 8.36e-15

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


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 76.13  E-value: 8.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVRdrvRTKMERDILVEVNHPF-------IVKLHYAFQTE 140
Cdd:cd14212    1 YLVLDLLGQGTFGQVV---KCQDLKTNKLVAVKVLKNKPAYFR---QAMLEIAILTLLNTKYdpedkhhIVRLLDHFMHH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLrGGDLFtRLSKEVMF---TEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD--EEGHIKLTDFGls 215
Cdd:cd14212   75 GHLCIVFELL-GVNLY-ELLKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVnlDSPEIKLIDFG-- 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 216 keSIDHEKKA-YSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGtLP-FQGKDRKETMTMILKaKLGMP 288
Cdd:cd14212  151 --SACFENYTlYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPlFPGNSEYNQLSRIIE-MLGMP 221
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
455-680 8.68e-15

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 75.15  E-value: 8.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIDKSKRDpTEEIE-----ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLdKILRQKFFSEREAS------ 523
Cdd:cd05044   30 AVKTLRKGATD-QEKAEflkeaHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDLL-SYLRAARPTAFTPPlltlkd 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 --AVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQL------RAE-NGLLmtpcyTANFVAPE 594
Cdd:cd05044  108 llSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERVVKIGDFGLARDIykndyyRKEgEGLL-----PVRWMAPE 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 595 VLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILArigsgkFSLSGGYWNSVSDTAKDLVSKMLHV---DP 670
Cdd:cd05044  183 SLVDGVFTTQSDVWAFGVLMWEILTlGQQPY---PARNNLEVLH------FVRAGGRLDQPDNCPDDLYELMLRCwstDP 253
                        250
                 ....*....|
gi 768032625 671 HQRLTAALVL 680
Cdd:cd05044  254 EERPSFARIL 263
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
426-642 8.76e-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: 75.47  E-value: 8.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVckRCIHKATNMEFAVKI---------IDKSKRDPTEEIEILLRYGQHPNIITLKDVYDD----G 492
Cdd:cd14030   23 DGRFLKFDIEIGRGSF--KTVYKGLDTETTVEVawcelqdrkLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 493 KYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESGnpeSIRICDFGF 570
Cdd:cd14030  101 KCIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG---SVKIGDLGL 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 571 AKQLRAE--NGLLMTPcytaNFVAPEVLKRQgYDAACDIWSLGVLLYTMLTGYTPFANGPDdtPEEILARIGSG 642
Cdd:cd14030  178 ATLKRASfaKSVIGTP----EFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPYSECQN--AAQIYRRVTSG 244
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
165-299 9.55e-15

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: 76.17  E-value: 9.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 165 FTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKE---SIDHEKKAYSFCgTVEYMAPEVVN 241
Cdd:cd05103  176 LTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDiykDPDYVRKGDARL-PLKWMAPETIF 254
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 242 RRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILK--AKLGMPQFLSPEA-QSLL 299
Cdd:cd05103  255 DRVYTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKegTRMRAPDYTTPEMyQTML 316
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
434-624 1.01e-14

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 75.08  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSY-SVCKRCIHKATN-MEFAVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05047    3 IGEGNFgQVLKARIKKDGLrMDAAIKRMkeyasKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKF------FSEREASAVLFT----------ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGF 570
Cdd:cd05047   83 LLDFLRKSRVletdpaFAIANSTASTLSsqqllhfaadVARGMDYLSQKQFIHRDLAARNILV----GENYVAKIADFGL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 571 AK--QLRAENGLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05047  159 SRgqEVYVKKTMGRLP---VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 212
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
434-626 1.02e-14

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


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 74.90  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSY-SVCKRCIHKATNMEFAVKI-------IDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd05066   12 IGAGEFgEVCSGRLKLPGKREIPVAIktlkagyTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ElLDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesgNPESI-RICDFGFAKQLRAENgllm 582
Cdd:cd05066   91 S-LDAFLRKHdgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILV-----NSNLVcKVSDFGLSRVLEDDP---- 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 583 TPCYTAN-------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAN 626
Cdd:cd05066  161 EAAYTTRggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWE 212
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
428-684 1.02e-14

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: 75.11  E-value: 1.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEI----LLRYGQHPNIITLKDVyddgkyVYVVTELMK 503
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAIreasLLKDLKHANIVTLHDI------IHTKKTLTL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQ------KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAkqlRAE 577
Cdd:cd07844   76 VFEYLDTDLKQymddcgGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLL-ISERG---ELKLADFGLA---RAK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 578 NglLMTPCYTANFVA-----PEVL-KRQGYDAACDIWSLGVLLYTMLTGYTPFANGPD--DTPEEILARIGS-------- 641
Cdd:cd07844  149 S--VPSKTYSNEVVTlwyrpPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDveDQLHKIFRVLGTpteetwpg 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 642 -----GKFSLSGGY---------WNSVSDT--AKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07844  227 vssnpEFKPYSFPFypprplinhAPRLDRIphGEELALKFLQYEPKKRISAAEAMKHPY 285
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
411-621 1.10e-14

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: 76.28  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 411 HSIVQqlHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEIEILLRYGQHP----NII 483
Cdd:cd14227    2 YQLVQ--HEVLCSMTNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHpsyARQGQIEVSILARLSTESaddyNFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 484 TLKDVYDDGKYVYVVTELMKggELLDKILRQKFFSE---REASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNP 560
Cdd:cd14227   80 RAYECFQHKNHTCLVFEMLE--QNLYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 561 ESIRICDFGFAKQLraENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGY 621
Cdd:cd14227  158 YRVKVIDFGSASHV--SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGW 216
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
452-685 1.18e-14

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: 75.44  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 452 MEFAVKIIDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE--LMKGGELLDkiLRQKFFSEREASAVLFTI 529
Cdd:cd06634   48 MSYSGKQSNEKWQDIIKEVKFLQKL-RHPNTIEYRGCYLREHTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGA 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 530 TKTVEYLHAQGVVHRDLKPSNILYVDesgnPESIRICDFGFAKQLRAENGLLMTPCYtanfVAPEV---LKRQGYDAACD 606
Cdd:cd06634  125 LQGLAYLHSHNMIHRDVKAGNILLTE----PGLVKLGDFGSASIMAPANSFVGTPYW----MAPEVilaMDEGQYDGKVD 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 607 IWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGkfSLSGGYWnsvSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd06634  197 VWSLGITCIELAERKPPLFNMNAMSALYHIAQNESP--ALQSGHW---SEYFRNFVDSCLQKIPQDRPTSDVLLKHRFL 270
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
67-300 1.19e-14

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 75.82  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKKISGSDARqlYAMKVLKKATlKVRDRVRtkMERDILVEVNHP------FIVKLHYAFQTE 140
Cdd:cd14215   13 RYEIVSTLGEGTFGRVVQCIDHRRGGAR--VALKIIKNVE-KYKEAAR--LEINVLEKINEKdpenknLCVQMFDWFDYH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGGDL-FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL---------------DEE 204
Cdd:cd14215   88 GHMCISFELLGLSTFdFLKENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrDER 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 G----HIKLTDFGlsKESIDHEKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMi 280
Cdd:cd14215  168 SvkstAIRVVDFG--SATFDHEHHS-TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAM- 243
                        250       260
                 ....*....|....*....|
gi 768032625 281 lkaklgMPQFLSPEAQSLLR 300
Cdd:cd14215  244 ------MERILGPIPSRMIR 257
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
74-334 1.25e-14

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: 74.76  E-value: 1.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkkiSGSDARQLY--AMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQT--EGK--LYLIL 147
Cdd:cd14031   18 LGRGAFKTVY-----KGLDTETWVevAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKkcIVLVT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLD-EEGHIKLTDFGLSkeSIDHEKK 224
Cdd:cd14031   93 ELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLMRTSF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 225 AYSFCGTVEYMAPEVVNRRgHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKLGMPQF---LSPEAQSLLRM 301
Cdd:cd14031  171 AKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFnkvTDPEVKEIIEG 249
                        250       260       270
                 ....*....|....*....|....*....|...
gi 768032625 302 LFKRNPANRLvnpfligagpdGVEEIKRHSFFS 334
Cdd:cd14031  250 CIRQNKSERL-----------SIKDLLNHAFFA 271
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
66-289 1.52e-14

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: 75.10  E-value: 1.52e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVFlvKKI---SGSDARQLYAMKVLKKATlKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGK 142
Cdd:cd05110    7 TELKRVKVLGSGAFGTVY--KGIwvpEGETVKIPVAIKILNETT-GPKANVEFMDEALIMASMDHPHLVRL-LGVCLSPT 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSK-EVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKeSIDH 221
Cdd:cd05110   83 IQLVTQLMPHGCLLDYVHEhKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLAR-LLEG 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 222 EKKAYSFCG---TVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKAKLgMPQ 289
Cdd:cd05110  162 DEKEYNADGgkmPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLLEKGER-LPQ 232
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
434-679 1.54e-14

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: 74.22  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATnmEFAVKIIDK--SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVyvVTELMKGGELlDKI 511
Cdd:cd14068    2 LGDGGFGSVYRAVYRGE--DVAVKIFNKhtSFRLLRQELVVLSHL-HHPSLVALLAAGTAPRML--VMELAPKGSL-DAL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 512 LRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESI-RICDFGFAkQLRAENGlLMTPCYTA 588
Cdd:cd14068   76 LQQDnaSLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIaKIADYGIA-QYCCRMG-IKTSEGTP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 589 NFVAPEVLKRQ-GYDAACDIWSLGVLLYTMLTGYTPFANG---PDDTPE-EILARIGSGKFSLSGGYWNSVsdtaKDLVS 663
Cdd:cd14068  154 GFRAPEVARGNvIYNQQADVYSFGLLLYDILTCGERIVEGlkfPNEFDElAIQGKLPDPVKEYGCAPWPGV----EALIK 229
                        250
                 ....*....|....*.
gi 768032625 664 KMLHVDPHQRLTAALV 679
Cdd:cd14068  230 DCLKENPQCRPTSAQV 245
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
434-628 1.77e-14

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: 74.08  E-value: 1.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKIIdKSKRDPTEEIEI--LLRygqHPNIITLKDVYDDGKYVYVVTELMKGGELLDKI 511
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKV-RLEVFRAEELMAcaGLT---SPRVVPLYGAVREGPWVNIFMDLKEGGSLGQLI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 512 LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRICDFGFAKQLRaENGL---LMTPCY-- 586
Cdd:cd13991   90 KEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLL---SSDGSDAFLCDFGHAECLD-PDGLgksLFTGDYip 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 587 -TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTG---YTPFANGP 628
Cdd:cd13991  166 gTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGchpWTQYYSGP 211
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
67-270 1.78e-14

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: 74.31  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFlvkkisgsdaRQLY----AMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK 142
Cdd:cd14063    1 ELEIKEVIGKGRFGRVH----------RGRWhgdvAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPH 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRL--SKEVmFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDeEGHIKLTDFGLSKESid 220
Cdd:cd14063   71 LAIVTSLCKGRTLYSLIheRKEK-FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLE-NGRVVITDFGLFSLS-- 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 221 hekkAYSFCGTVE-----------YMAPEVVN------RRGH----TQSADWWSFGVLMFEMLTGTLPFQG 270
Cdd:cd14063  147 ----GLLQPGRREdtlvipngwlcYLAPEIIRalspdlDFEEslpfTKASDVYAFGTVWYELLAGRWPFKE 213
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
478-615 1.85e-14

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: 73.92  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 478 QHPNIITLKDVYDDGKYVYVVTELMKGGELLDkILR-----------QKFFSereasavlFTITKTVEYLHAQGVVHRDL 546
Cdd:cd05039   58 RHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVD-YLRsrgravitrkdQLGFA--------LDVCEGMEYLESKKFVHRDL 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 547 KPSNILyVDESGnpeSIRICDFGFAK--QLRAENGLLmtPcytANFVAPEVLKRQGYDAACDIWSLGVLLY 615
Cdd:cd05039  129 AARNVL-VSEDN---VAKVSDFGLAKeaSSNQDGGKL--P---IKWTAPEALREKKFSTKSDVWSFGILLW 190
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
434-624 2.00e-14

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: 74.65  E-value: 2.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSY-SVCKRCIHKATN-MEFAVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGE 506
Cdd:cd05089   10 IGEGNFgQVIKAMIKKDGLkMNAAIKMLkefasENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAIEYAPYGN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKF------FSEREASAVLFT----------ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGF 570
Cdd:cd05089   90 LLDFLRKSRVletdpaFAKEHGTASTLTsqqllqfasdVAKGMQYLSEKQFIHRDLAARNVLV----GENLVSKIADFGL 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 571 AK--QLRAENGLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05089  166 SRgeEVYVKKTMGRLP---VRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPY 219
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
428-685 2.37e-14

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: 75.55  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSY-SVCKRCIHKaTNMEFAVKIIDKSKR---DPTEEIEIL--LR----YGQHpNIITLKDVYDDGKYVYV 497
Cdd:cd14224   67 YEVLKVIGKGSFgQVVKAYDHK-THQHVALKMVRNEKRfhrQAAEEIRILehLKkqdkDNTM-NVIHMLESFTFRNHICM 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGgELLDKILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDE--SGnpesIRICDFGFAKq 573
Cdd:cd14224  145 TFELLSM-NLYELIKKNKFqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQgrSG----IKVIDFGSSC- 218
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 lrAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYtPFANGPDDT-------------PEEILARIG 640
Cdd:cd14224  219 --YEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGY-PLFPGEDEGdqlacmiellgmpPQKLLETSK 295
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 641 SGK-FSLSGGY----------------------------------WNSVSDTAKD-----LVSKMLHVDPHQRLTAALVL 680
Cdd:cd14224  296 RAKnFISSKGYpryctvttlpdgsvvlnggrsrrgkmrgppgskdWVTALKGCDDplfldFLKRCLEWDPAARMTPSQAL 375

                 ....*
gi 768032625 681 RHPWI 685
Cdd:cd14224  376 RHPWL 380
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
74-311 2.39e-14

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 73.85  E-value: 2.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISGSD-ARQLYAMKVLKKAT----------LKVRDRVRT----KMERDILVEVNHPFIVKL----- 133
Cdd:cd14067    1 LGQGGSGTVIYRARYQGQPvAVKRFHIKKCKKRTdgsadtmlkhLRAADAMKNfsefRQEASMLHSLQHPCIVYLigisi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 134 H---YAFQTE--GKLYLILDFLRGGDLFTRLSKevMFTEEdVKFylaELALALDHLHSLGIIYRDLKPENIL---LDEEG 205
Cdd:cd14067   81 HplcFALELAplGSLNTVLEENHKGSSFMPLGH--MLTFK-IAY---QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 206 HI--KLTDFGLSKESIdHEKkAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDR---KETMTMI 280
Cdd:cd14067  155 HIniKLSDYGISRQSF-HEG-ALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQlqiAKKLSKG 232
                        250       260       270
                 ....*....|....*....|....*....|....
gi 768032625 281 LKAKLGMP---QFLSpeAQSLLRMLFKRNPANRL 311
Cdd:cd14067  233 IRPVLGQPeevQFFR--LQALMMECWDTKPEKRP 264
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
432-626 2.92e-14

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: 73.36  E-value: 2.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATnMEFAVKIIDK---SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:cd05114   10 KELGSGLFGVVRLGKWRAQ-YKVAIKAIREgamSEEDFIEEAKVMMKL-THPKLVQLYGVCTQQKPIYIVTEFMENGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DkILRQKF--FSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENgllmtpcY 586
Cdd:cd05114   88 N-YLRQRRgkLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCL-VNDTG---VVKVSDFGMTRYVLDDQ-------Y 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 768032625 587 TANFVA--------PEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAN 626
Cdd:cd05114  156 TSSSGAkfpvkwspPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFES 204
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
67-288 3.50e-14

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: 74.78  E-value: 3.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFLVKkiSGSDARQLyAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKL-------HYAFQT 139
Cdd:cd07853    1 DVEPDRPIGYGAFGVVWSVT--DPRDGKRV-ALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSAldilqppHIDPFE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EgkLYLILDFLRGgDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLS-KES 218
Cdd:cd07853   78 E--IYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLArVEE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 219 IDHEKKAYSFCGTVEYMAPEV-VNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAkLGMP 288
Cdd:cd07853  155 PDESKHMTQEVVTQYYRAPEIlMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDL-LGTP 224
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
74-310 4.83e-14

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 72.84  E-value: 4.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVF--LVKKISgsdarQLYAMKVLKKATLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 151
Cdd:cd05052   14 LGGGQYGEVYegVWKKYN-----LTVAVKTLKEDTMEVEEFLK---EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 152 GGDL--FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYS-- 227
Cdd:cd05052   86 YGNLldYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAga 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 228 -FcgTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRMLFK 304
Cdd:cd05052  166 kF--PIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKGyRMERPEGCPPKVYELMRACWQ 243

                 ....*.
gi 768032625 305 RNPANR 310
Cdd:cd05052  244 WNPSDR 249
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
430-680 5.95e-14

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: 72.93  E-value: 5.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKEDIGVGSYSVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEILLRYGQHPNII-------TLKDVYDDGKYVYVV 498
Cdd:cd14036    4 IKRVIAEGGFAFVYEAQDVGTGKEYALKRLlsneEEKNKAIIQEINFMKKLSGHPNIVqfcsaasIGKEESDQGQAEYLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 499 -TELMKGG--ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYvdesGNPESIRICDFGFA-- 571
Cdd:cd14036   84 lTELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLI----GNQGQIKLCDFGSAtt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 572 ------------KQLRAENGLL--MTPCYTAnfvaPEVLKRQG---YDAACDIWSLGVLLYTMLTGYTPFANGPDdtpee 634
Cdd:cd14036  160 eahypdyswsaqKRSLVEDEITrnTTPMYRT----PEMIDLYSnypIGEKQDIWALGCILYLLCFRKHPFEDGAK----- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 635 ilARIGSGKFSLSGgywnsvSDTA----KDLVSKMLHVDPHQRLTAALVL 680
Cdd:cd14036  231 --LRIINAKYTIPP------NDTQytvfHDLIRSTLKVNPEERLSITEIV 272
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
428-621 6.75e-14

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: 73.52  E-value: 6.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEIEILLRYGQHP----NIITLKDVYDDGKYVYVVTE 500
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHpsyARQGQIEVGILARLSNENadefNFVRAYECFQHRNHTCLVFE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKggELLDKILRQKFFSE---REASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLraE 577
Cdd:cd14229   82 MLE--QNLYDFLKQNKFSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHV--S 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 578 NGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGY 621
Cdd:cd14229  158 KTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGW 201
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
74-268 6.79e-14

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: 72.92  E-value: 6.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLvkkisGSDARQLYAMKVLKKATLKVRDRVRTKMERDI--LVEVNHPFIVKLhYAFQTEG-KLYLILDFL 150
Cdd:cd14158   23 LGEGGFGVVFK-----GYINDKNVAVKKLAAMVDISTEDLTKQFEQEIqvMAKCQHENLVEL-LGYSCDGpQLCLVYTYM 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 151 RGGDLFTRLS--KEVMFTEEDVKFYLAE-LALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHEKKAYS 227
Cdd:cd14158   97 PNGSLLDRLAclNDTPPLSWHMRCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMT 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 228 --FCGTVEYMAPEVVnrRGH-TQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14158  177 erIVGTTAYMAPEAL--RGEiTPKSDIFSFGVVLLEIITGLPPV 218
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
174-311 7.93e-14

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 72.91  E-value: 7.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 174 LAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFG--LSKESI----DHEKKAYSFCGTVEYMAPEVVNRR 243
Cdd:cd14018  144 ILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGccLADDSIglqlPFSSWYVDRGGNACLMAPEVSTAV 223
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 244 G------HTQSADWWSFGVLMFEMLTGTLPF--QGKDRKETMTMILKAKLGMPQFLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd14018  224 PgpgvviNYSKADAWAVGAIAYEIFGLSNPFygLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRV 299
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
74-262 8.74e-14

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: 71.78  E-value: 8.74e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisGSDARQLYAmKVLKKATlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14156    1 IGSGFFSKVYKVTH--GATGKVMVV-KIYKNDV----DQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEDVKFYLA-ELALALDHLHSLGIIYRDLKPENILLDEEGHIK---LTDFGLSKE-----SIDHEKK 224
Cdd:cd14156   74 CLEELLAREELPLSWREKVELAcDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREvgempANDPERK 153
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 768032625 225 aYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14156  154 -LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
67-263 9.37e-14

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 72.70  E-value: 9.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVFL-----------VKKISGSDARQLYAMKVLKK-ATLKVRDRVRTKMErdILVEVNHPFIVKLH 134
Cdd:cd05097    6 QLRLKEKLGEGQFGEVHLceaeglaeflgEGAPEFDGQPVLVAVKMLRAdVTKTARNDFLKEIK--IMSRLKNPNIIRLL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTE------------EDVKFYLAELALALDHLHSLGIIYRDLKPENILLD 202
Cdd:cd05097   84 GVCVSDDPLCMITEYMENGDLNQFLSQREIESTfthannipsvsiANLLYMAVQIASGMKYLASLNFVHRDLATRNCLVG 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 768032625 203 EEGHIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT 263
Cdd:cd05097  164 NHYTIKIADFGMSRNlySGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFT 226
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
473-642 1.01e-13

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: 72.00  E-value: 1.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 473 LLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDkilrqkFFSEREASAVLF--------TITKTVEYLHAQGVVHR 544
Cdd:cd05072   55 LMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLD------FLKSDEGGKVLLpklidfsaQIAEGMAYIERKNYIHR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 545 DLKPSNILyVDESgnpESIRICDFGFAKQLRAENgllmtpcYTA--------NFVAPEVLKRQGYDAACDIWSLGVLLYT 616
Cdd:cd05072  129 DLRAANVL-VSES---LMCKIADFGLARVIEDNE-------YTAregakfpiKWTAPEAINFGSFTIKSDVWSFGILLYE 197
                        170       180
                 ....*....|....*....|....*..
gi 768032625 617 MLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05072  198 IVTyGKIPY---PGMSNSDVMSALQRG 221
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
74-268 1.03e-13

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: 72.03  E-value: 1.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkkiSGSDARQLY--AMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLIL 147
Cdd:cd14032    9 LGRGSFKTVY-----KGLDTETWVevAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLD-EEGHIKLTDFGLSkeSIDHEKK 224
Cdd:cd14032   84 ELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRASF 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 225 AYSFCGTVEYMAPEVVNRRgHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14032  162 AKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPY 204
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
455-628 1.10e-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: 72.75  E-value: 1.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKI----------------LR 513
Cdd:cd05100   48 AVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLrarrppgmdysfdtckLP 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 514 QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL-------RAENGLLmtpcy 586
Cdd:cd05100  128 EEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDN----VMKIADFGLARDVhnidyykKTTNGRL----- 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGP 628
Cdd:cd05100  199 PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 241
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
66-307 1.15e-13

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: 73.20  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVflvKKISGSDARQLYAMKVLKKATLKVRD-----RVRTKMERDILVEVNhpfIVKLHYAFQTE 140
Cdd:cd14228   15 NSYEVLEFLGRGTFGQV---AKCWKRSTKEIVAIKILKNHPSYARQgqievSILSRLSSENADEYN---FVRSYECFQHK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 141 GKLYLILDFLRGgDLFTRLsKEVMFTEEDVKFY---LAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFG 213
Cdd:cd14228   89 NHTCLVFEMLEQ-NLYDFL-KQNKFSPLPLKYIrpiLQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 214 lskeSIDHEKKAY--SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKlGMPQFL 291
Cdd:cd14228  167 ----SASHVSKAVcsTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEY 241
                        250
                 ....*....|....*.
gi 768032625 292 SPEAQSLLRMLFKRNP 307
Cdd:cd14228  242 LLSAGTKTSRFFNRDP 257
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
73-261 1.17e-13

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: 72.09  E-value: 1.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  73 VLGQGSFGKVFlvkkiSGSDARQLYAMKVLKkatlkVRDRVRTKMERDILVEVN--HP----FIVKLHYAFQTEGKLYLI 146
Cdd:cd13998    2 VIGKGRFGEVW-----KASLKNEPVAVKIFS-----SRDKQSWFREKEIYRTPMlkHEnilqFIAADERDTALRTELWLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 147 LDFLRGGDLFTRLSKEVMFTEEDVKFYLAeLALALDHLHS---------LGIIYRDLKPENILLDEEGHIKLTDFGLS-- 215
Cdd:cd13998   72 TAFHPNGSL*DYLSLHTIDWVSLCRLALS-VARGLAHLHSeipgctqgkPAIAHRDLKSKNILVKNDGTCCIADFGLAvr 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 216 -KESIDHEKKA-YSFCGTVEYMAPEV----VNRRgHTQS---ADWWSFGVLMFEM 261
Cdd:cd13998  151 lSPSTGEEDNAnNGQVGTKRYMAPEVlegaINLR-DFESfkrVDIYAMGLVLWEM 204
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
74-310 1.18e-13

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 72.17  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKK---ISGSDaRQLYAMKVLKKatlKVRDRVRTKMERD--ILVEVNHPFIVKLhYAFQTEGK-LYLIL 147
Cdd:cd05050   13 IGQGAFGRVFQARApglLPYEP-FTMVAVKMLKE---EASADMQADFQREaaLMAEFDHPNIVKL-LGVCAVGKpMCLLF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 148 DFLRGGDLFTRLSKEVMFTEEDVKFYLAELA------LALDHLHSLGI----------------IYRDLKPENILLDEEG 205
Cdd:cd05050   88 EYMAYGDLNEFLRHRSPRAQCSLSHSTSSARkcglnpLPLSCTEQLCIakqvaagmaylserkfVHRDLATRNCLVGENM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 206 HIKLTDFGLSKE--SIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GTLPFQGKDRKETMTMILK 282
Cdd:cd05050  168 VVKIADFGLSRNiySADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAHEEVIYYVRD 247
                        250       260
                 ....*....|....*....|....*....
gi 768032625 283 AK-LGMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd05050  248 GNvLSCPDNCPLELYNLMRLCWSKLPSDR 276
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
74-213 1.39e-13

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: 68.24  E-value: 1.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKISGSDArqlYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIG---VAVKIGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKGG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFtEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFG 213
Cdd:cd13968   78 TLIAYTQEEELD-EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
74-262 1.43e-13

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: 71.35  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFLVKKisgsdaRQLYAMKVLKKATLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 153
Cdd:cd14155    1 IGSGFFSEVYKVRH------RTSGQVMALKMNTLS-SNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 154 DLFTRLSKEVMFTEEdVKFYLA-ELALALDHLHSLGIIYRDLKPENILL--DEEGHIKLT-DFGLSKESIDH--EKKAYS 227
Cdd:cd14155   74 NLEQLLDSNEPLSWT-VRVKLAlDIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVVgDFGLAEKIPDYsdGKEKLA 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 768032625 228 FCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEML 262
Cdd:cd14155  153 VVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
PTZ00284 PTZ00284
protein kinase; Provisional
57-289 1.61e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 73.46  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  57 KEGH------EKADPS--QFELLKVLGQGSFGKVFLvkkiSGSDARQLY-AMKVLKKATLKVRD-RVRTK-MERDILVEV 125
Cdd:PTZ00284 112 EEGHfyvvlgEDIDVStqRFKILSLLGEGTFGKVVE----AWDRKRKEYcAVKIVRNVPKYTRDaKIEIQfMEKVRQADP 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 126 NHPF-IVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHS-LGIIYRDLKPENILLD- 202
Cdd:PTZ00284 188 ADRFpLMKIQRYFQNETGHMCIVMPKYGPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTeLHLMHTDLKPENILMEt 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 203 ---------------EEGHIKLTDFGlskESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLP 267
Cdd:PTZ00284 268 sdtvvdpvtnralppDPCRVRICDLG---GCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLL 344
                        250       260
                 ....*....|....*....|..
gi 768032625 268 FQGKDRKETMTMILKAKLGMPQ 289
Cdd:PTZ00284 345 YDTHDNLEHLHLMEKTLGRLPS 366
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
74-269 2.46e-13

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 71.40  E-value: 2.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkkiSGSDARQLYAMKVLKK-ATLK---VRDRVRTKMERdiLVEVNHPFIVKLH-YAFQtEGKLYLILD 148
Cdd:cd14159    1 IGEGGFGCVY-----QAVMRNTEYAVKRLKEdSELDwsvVKNSFLTEVEK--LSRFRHPNIVDLAgYSAQ-QGNYCLIYV 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 149 FLRGGDLFTRLSKEVMFT----EEDVKFYLAElALALDHLH--SLGIIYRDLKPENILLDEEGHIKLTDFGLSKESIDHE 222
Cdd:cd14159   73 YLPNGSLEDRLHCQVSCPclswSQRLHVLLGT-ARAIQYLHsdSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPK 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 768032625 223 KKAYSFC--------GTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQ 269
Cdd:cd14159  152 QPGMSSTlartqtvrGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAME 206
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
455-628 2.89e-13

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: 71.20  E-value: 2.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELlDKILRQKFFSEREAS------ 523
Cdd:cd05101   60 AVKMLkddatEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNL-REYLRARRPPGMEYSydinrv 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 -----------AVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL-------RAENGLLmtpc 585
Cdd:cd05101  139 peeqmtfkdlvSCTYQLARGMEYLASQKCIHRDLAARNVLVTENN----VMKIADFGLARDInnidyykKTTNGRL---- 210
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 586 yTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGP 628
Cdd:cd05101  211 -PVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIP 253
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
433-625 2.97e-13

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: 70.49  E-value: 2.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNMEFAV-----KIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDG----KYVYVVTELMK 503
Cdd:cd14032    8 ELGRGSFKTVYKGLDTETWVEVAWcelqdRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCakgkRCIVLVTELMT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESGnpeSIRICDFGFAKQLRAE--NG 579
Cdd:cd14032   88 SGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTG---SVKIGDLGLATLKRASfaKS 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 580 LLMTPcytaNFVAPEVLKRQgYDAACDIWSLGVLLYTMLTGYTPFA 625
Cdd:cd14032  165 VIGTP----EFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYS 205
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
143-311 3.45e-13

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: 71.43  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDE---EGHIKLTDFGLSK--- 216
Cdd:cd13977  110 LWFVMEFCDGGDMNEYLLSRRPDRQTNTSFML-QLSSALAFLHRNQIVHRDLKPDNILISHkrgEPILKVADFGLSKvcs 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 217 -ESIDHEKKA-------YSFCGTVEYMAPEVvnRRGH-TQSADWWSFGVLMFEM--------------LTGTLPFQGKDR 273
Cdd:cd13977  189 gSGLNPEEPAnvnkhflSSACGSDFYMAPEV--WEGHyTAKADIFALGIIIWAMveritfrdgetkkeLLGTYIQQGKEI 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 274 KETMTMIL---KAKLGMPQ----FLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd13977  267 VPLGEALLenpKLELQIPLkkkkSMNDDMKQLLRDMLAANPQERP 311
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
455-675 3.66e-13

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: 71.15  E-value: 3.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKI----------------LR 513
Cdd:cd05099   48 AVKMLkdnatDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLrarrppgpdytfditkVP 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 514 QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL-------RAENGLLmtpcy 586
Cdd:cd05099  128 EEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDN----VMKIADFGLARGVhdidyykKTSNGRL----- 198
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGPddtPEEILarigsgKFSLSGGYWNSVSDTAKDLVSKM 665
Cdd:cd05099  199 PVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIP---VEELF------KLLREGHRMDKPSNCTHELYMLM 269
                        250
                 ....*....|...
gi 768032625 666 ---LHVDPHQRLT 675
Cdd:cd05099  270 recWHAVPTQRPT 282
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
461-679 4.07e-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: 70.34  E-value: 4.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 461 KSKRDPTEEIEILLRYgQHPNIITLkdVYDDGKYVYVVTELMKGGELlDKILRQKFFSEREASAVLFT-----ITKTVEY 535
Cdd:cd14000   52 KNFRLLRQELTVLSHL-HHPSIVYL--LGIGIHPLMLVLELAPLGSL-DHLLQQDSRSFASLGRTLQQrialqVADGLRY 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 536 LHAQGVVHRDLKPSNI----LYVDESGNpesIRICDFGFAKQLRAENGLlmTPCYTANFVAPEVLKRQ-GYDAACDIWSL 610
Cdd:cd14000  128 LHSAMIIYRDLKSHNVlvwtLYPNSAII---IKIADYGISRQCCRMGAK--GSEGTPGFRAPEIARGNvIYNEKVDVFSF 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 611 GVLLYTMLTGYTPFANGpDDTPEEIlaRIGSGKFSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAALV 679
Cdd:cd14000  203 GMLLYEILSGGAPMVGH-LKFPNEF--DIHGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
68-288 4.14e-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: 71.21  E-value: 4.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVRdrvRTKMERDILVEVN------HPFiVKLHYAFQTEG 141
Cdd:cd14229    2 YEVLDFLGRGTFGQVV---KCWKRGTNEIVAVKILKNHPSYAR---QGQIEVGILARLSnenadeFNF-VRAYECFQHRN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 142 KLYLILDFLRGgDLFTRLsKEVMFTEEDVKFY---LAELALALDHLHSLGIIYRDLKPENILL----DEEGHIKLTDFGl 214
Cdd:cd14229   75 HTCLVFEMLEQ-NLYDFL-KQNKFSPLPLKVIrpiLQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKVIDFG- 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 215 skeSIDHEKKAY--SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKlGMP 288
Cdd:cd14229  152 ---SASHVSKTVcsTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQ-GLP 223
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
428-685 4.41e-13

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: 70.00  E-value: 4.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSK-----------RDPTEeIEILLRYGQ-HPNIITLKDVYD-DGKY 494
Cdd:cd14100    2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRvsewgelpngtRVPME-IVLLKKVGSgFRGVIRLLDWFErPDSF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpesIRICDFGfakql 574
Cdd:cd14100   81 VLVLERPEPVQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGE---LKLIDFG----- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 raENGLLMTPCY-----TANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFangpdDTPEEIlarIGSGKFslsg 648
Cdd:cd14100  153 --SGALLKDTVYtdfdgTRVYSPPEWIRFHRYHGrSAAVWSLGILLYDMVCGDIPF-----EHDEEI---IRGQVF---- 218
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 768032625 649 gYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14100  219 -FRQRVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
428-643 4.59e-13

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: 70.06  E-value: 4.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKED-------IGVGSYS-----VCKRCIHKATNMEFAVKII--DKSKRDPTE---EIEILLRYGQHpNIITLKDVYD 490
Cdd:cd05032    1 WELPREkitlireLGQGSFGmvyegLAKGVVKGEPETRVAIKTVneNASMRERIEflnEASVMKEFNCH-HVVRLLGVVS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 491 DGKYVYVVTELMKGGELLDkILRQKFFSEREA------SAVLF-----TITKTVEYLHAQGVVHRDLKPSNILYVDEsgn 559
Cdd:cd05032   80 TGQPTLVVMELMAKGDLKS-YLRSRRPEAENNpglgppTLQKFiqmaaEIADGMAYLAAKKFVHRDLAARNCMVAED--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 560 pESIRICDFGFAKQLRAEN-----GLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPE 633
Cdd:cd05032  156 -LTVKIGDFGMTRDIYETDyyrkgGKGLLP---VRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPY---QGLSNE 228
                        250
                 ....*....|
gi 768032625 634 EILARIGSGK 643
Cdd:cd05032  229 EVLKFVIDGG 238
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
469-626 4.75e-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: 4.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 469 EIEILLRYgQHPNIITLKDV-YDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVL-FTITKTVEYLH--AQGVVHR 544
Cdd:cd14064   41 EVSILCRL-NHPCVIQFVGAcLDDPSQFAIVTQYVSGGSLFSLLHEQKRVIDLQSKLIIaVDVAKGMEYLHnlTQPIIHR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 545 DLKPSNILyVDESGNPEsirICDFG---FAKQLRAENgllMTPcYTAN--FVAPEVLKRQG-YDAACDIWSLGVLLYTML 618
Cdd:cd14064  120 DLNSHNIL-LYEDGHAV---VADFGesrFLQSLDEDN---MTK-QPGNlrWMAPEVFTQCTrYSIKADVFSYALCLWELL 191

                 ....*...
gi 768032625 619 TGYTPFAN 626
Cdd:cd14064  192 TGEIPFAH 199
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
431-624 4.80e-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: 69.76  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSYSVCKRCIHKATNMEFAVKIIdkskRDPTEEIEILLRYG------QHPNIITLKDVYDDGKYVYVVTELMKG 504
Cdd:cd05052   11 KHKLGGGQYGEVYEGVWKKYNLTVAVKTL----KEDTMEVEEFLKEAavmkeiKHPNLVQLLGVCTREPPFYIITEFMPY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 505 GELLDkILRQKFFSEREASAVLFTITKT---VEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENgll 581
Cdd:cd05052   87 GNLLD-YLRECNREELNAVVLLYMATQIasaMEYLEKKNFIHRDLAARNCLV----GENHLVKVADFGLSRLMTGDT--- 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 582 mtpcYTAN--------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05052  159 ----YTAHagakfpikWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPY 206
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
461-640 4.81e-13

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: 70.31  E-value: 4.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 461 KSKRDPTEEIEILlRYGQHPNIITLKDV-YDDGKY-VYVVTELMKGGELLDKIlrQKFFSEREASAVLF---TITKTVEY 535
Cdd:cd05081   47 DQQRDFQREIQIL-KALHSDFIVKYRGVsYGPGRRsLRLVMEYLPSGCLRDFL--QRHRARLDASRLLLyssQICKGMEY 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 536 LHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQL--RAENGLLMTPCYTANF-VAPEVLKRQGYDAACDIWSLGV 612
Cdd:cd05081  124 LGSRRCVHRDLAARNILVESE----AHVKIADFGLAKLLplDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGV 199
                        170       180
                 ....*....|....*....|....*...
gi 768032625 613 LLYTMLTgytpFANGPDDTPEEILARIG 640
Cdd:cd05081  200 VLYELFT----YCDKSCSPSAEFLRMMG 223
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
168-272 4.95e-13

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: 70.68  E-value: 4.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 168 EDVKFYLAELALALDHLHS-LGIIYRDLKPENILLDE-EGHIKLTDFGLS-------KESIDhekkaysfcgTVEYMAPE 238
Cdd:cd14136  119 PLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLCIsKIEVKIADLGNAcwtdkhfTEDIQ----------TRQYRSPE 188
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 768032625 239 VVNRRGHTQSADWWSFGVLMFEMLTGTL---PFQGKD 272
Cdd:cd14136  189 VILGAGYGTPADIWSTACMAFELATGDYlfdPHSGED 225
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
434-642 5.63e-13

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: 69.62  E-value: 5.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKAT-NMEFAVKI-------IDKSKRDPTEEIEILLRYGQHpNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd05063   13 IGAGEFGEVFRGILKMPgRKEVAVAIktlkpgyTEKQRQDFLSEASIMGQFSHH-NIIRLEGVVTKFKPAMIITEYMENG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELlDKILRQK--FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENgllmT 583
Cdd:cd05063   92 AL-DKYLRDHdgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILV----NSNLECKVSDFGLSRVLEDDP----E 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 768032625 584 PCYTAN-------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAngpDDTPEEILARIGSG 642
Cdd:cd05063  163 GTYTTSggkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYW---DMSNHEVMKAINDG 226
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
434-680 5.70e-13

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: 70.23  E-value: 5.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPTE---EIEILLRYgQHPNIITLKDVYDDgkyvYVVTELMKGGEL 507
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKIlikKVTKRDCMKvlrEVKVLAGL-QHPNIVGYHTAWME----HVQLMLYIQMQL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKIL------RQKFFSEREASA-------------VLFTITKTVEYLHAQGVVHRDLKPSNILYvdeSGNPESIRICDF 568
Cdd:cd14049   89 CELSLwdwiveRNKRPCEEEFKSapytpvdvdvttkILQQLLEGVTYIHSMGIVHRDLKPRNIFL---HGSDIHVRIGDF 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 569 GFAKQLRAENGL-------LMTPCYTANF-----VAPEVLKRQGYDAACDIWSLGVLLytmLTGYTPFanGPDDTPEEIL 636
Cdd:cd14049  166 GLACPDILQDGNdsttmsrLNGLTHTSGVgtclyAAPEQLEGSHYDFKSDMYSIGVIL---LELFQPF--GTEMERAEVL 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 637 ARIGSGKFSLS-GGYWNSVSDTAKDLVSKmlhvDPHQRLTAALVL 680
Cdd:cd14049  241 TQLRNGQIPKSlCKRWPVQAKYIKLLTST----EPSERPSASQLL 281
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
432-639 6.30e-13

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: 70.41  E-value: 6.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKII--DKSKRDPTEEIE--ILLRYGQHPNIITLKDVYDDGKYVYVVTELmkggel 507
Cdd:cd07872   12 EKLGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAIRevSLLKDLKHANIVTLHDIVHTDKSLTLVFEY------ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKILRQ------KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRAENGLL 581
Cdd:cd07872   86 LDKDLKQymddcgNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLL-INERG---ELKLADFGLARAKSVPTKTY 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 582 MTPCYTANFVAPEV-LKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARI 639
Cdd:cd07872  162 SNEVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLF---PGSTVEDELHLI 217
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
411-621 6.50e-13

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: 70.89  E-value: 6.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 411 HSIVQqlHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS---KRDPTEEIEILLRYGQHP----NII 483
Cdd:cd14228    2 YQLVQ--HEILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHpsyARQGQIEVSILSRLSSENadeyNFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 484 TLKDVYDDGKYVYVVTELMKggELLDKILRQKFFSE---REASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNP 560
Cdd:cd14228   80 RSYECFQHKNHTCLVFEMLE--QNLYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQP 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 561 ESIRICDFGFAKQLraENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGY 621
Cdd:cd14228  158 YRVKVIDFGSASHV--SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGW 216
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
68-314 6.62e-13

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: 70.89  E-value: 6.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  68 FELLKVLGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVRdrvRTKMERDILVEVNHPF-----IVKLHYAFQTEGK 142
Cdd:cd14227   17 YEVLEFLGRGTFGQVV---KCWKRGTNEIVAIKILKNHPSYAR---QGQIEVSILARLSTESaddynFVRAYECFQHKNH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 143 LYLILDFLRGgDLFTRLsKEVMFTEEDVKF---YLAELALALDHLHSLGIIYRDLKPENILLDEEG----HIKLTDFGls 215
Cdd:cd14227   91 TCLVFEMLEQ-NLYDFL-KQNKFSPLPLKYirpILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFG-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 216 keSIDHEKKAY--SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILKAKlGMPQFLSP 293
Cdd:cd14227  167 --SASHVSKAVcsTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEYLL 243
                        250       260
                 ....*....|....*....|....*.
gi 768032625 294 EAQSLLRMLFKRN-----PANRLVNP 314
Cdd:cd14227  244 SAGTKTTRFFNRDtdspyPLWRLKTP 269
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
428-624 6.97e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 72.46  E-value: 6.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEI-LLRYGQHPNIITLKDVYDD--GKYVYVVTE 500
Cdd:PTZ00266   15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrglKEREKSQLVIEVnVMRELKHKNIVRYIDRFLNkaNQKLYILME 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  501 LMKGGELLDKILR-QKFFSEREASAVLfTITKtvEYLHA-------------QGVVHRDLKPSNILYV------------ 554
Cdd:PTZ00266   95 FCDAGDLSRNIQKcYKMFGKIEEHAIV-DITR--QLLHAlaychnlkdgpngERVLHRDLKPQNIFLStgirhigkitaq 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 768032625  555 --DESGNPESiRICDFGFAKQLRAENglLMTPCY-TANFVAPEVL--KRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:PTZ00266  172 anNLNGRPIA-KIGDFGLSKNIGIES--MAHSCVgTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPF 243
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
455-628 7.80e-13

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: 70.04  E-value: 7.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII--DKSKRDPTE---EIEILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQK-------------- 515
Cdd:cd05098   49 AVKMLksDATEKDLSDlisEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycynpshnp 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 516 --FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQL-------RAENGLLmtpcy 586
Cdd:cd05098  129 eeQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDN----VMKIADFGLARDIhhidyykKTTNGRL----- 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 587 TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGP 628
Cdd:cd05098  200 PVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVP 242
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
468-628 7.97e-13

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: 69.54  E-value: 7.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 468 EEIEILlRYGQHPNIITLKDVYDD--GKYVYVVTELMKGGELLDKILRQKFfseREASAVLFT--ITKTVEYLHAQGVVH 543
Cdd:cd05080   55 QEIDIL-KTLYHENIVKYKGCCSEqgGKSLQLIMEYVPLGSLRDYLPKHSI---GLAQLLLFAqqICEGMAYLHSQHYIH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 544 RDLKPSNILyVDesgNPESIRICDFGFAKQLR--------AENGllMTPCYtanFVAPEVLKRQGYDAACDIWSLGVLLY 615
Cdd:cd05080  131 RDLAARNVL-LD---NDRLVKIGDFGLAKAVPegheyyrvREDG--DSPVF---WYAPECLKEYKFYYASDVWSFGVTLY 201
                        170
                 ....*....|...
gi 768032625 616 TMLTGYTPFANGP 628
Cdd:cd05080  202 ELLTHCDSSQSPP 214
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
426-655 8.45e-13

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 70.08  E-value: 8.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 426 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKS-----KRDPTEEIEILlRYGQHPNIITLKDV-YDDGKyVYVVT 499
Cdd:cd06649    5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEikpaiRNQIIRELQVL-HECNSPYIVGFYGAfYSDGE-ISICM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 500 ELMKGGELlDKILRQ-KFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQLRae 577
Cdd:cd06649   83 EHMDGGSL-DQVLKEaKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNIL-VNSRG---EIKLCDFGVSGQLI-- 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 578 NGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFangPDDTPEEILARIGSGKFSLSGGYWNSVS 655
Cdd:cd06649  156 DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPI---PPPDAKELEAIFGRPVVDGEEGEPHSIS 230
PTZ00284 PTZ00284
protein kinase; Provisional
507-698 8.62e-13

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 71.15  E-value: 8.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LLDKILRQKFFSEREASAVLFTITKTVEYLHAQ-GVVHRDLKPSNILY------VDESGN------PESIRICDFGFAKQ 573
Cdd:PTZ00284 218 LLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMetsdtvVDPVTNralppdPCRVRICDLGGCCD 297
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 574 LRAENGLLMTpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTG---YTPFANGP-----DDT----PEEILARIGS 641
Cdd:PTZ00284 298 ERHSRTAIVS---TRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGkllYDTHDNLEhlhlmEKTlgrlPSEWAGRCGT 374
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 642 GKFSL---SGGYWNSVSDTAK--------------------DLVSKMLHVDPHQRLTAALVLRHPWIVHW----DQLPQY 694
Cdd:PTZ00284 375 EEARLlynSAGQLRPCTDPKHlariararpvrevirddllcDLIYGLLHYDRQKRLNARQMTTHPYVLKYypecRQHPNY 454

                 ....
gi 768032625 695 QLNR 698
Cdd:PTZ00284 455 PDNR 458
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
428-684 9.60e-13

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: 69.71  E-value: 9.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKII---DKSKRDPT---EEIEILLRYgQHPNIITLKDV-------YDDGK- 493
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmeNEKEGFPItalREIKILQLL-KHENVVNLIEIcrtkatpYNRYKg 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 YVYVVTELMK---GGELLDKILRqkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGF 570
Cdd:cd07865   93 SIYLVFEFCEhdlAGLLSNKNVK---FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANIL-ITKDG---VLKLADFGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 571 AKQL-RAENGllMTPCYTANFV-----APEVL--KRQgYDAACDIWSLGVLLYTMLTGYtPFANGpdDTPEEILARI--- 639
Cdd:cd07865  166 ARAFsLAKNS--QPNRYTNRVVtlwyrPPELLlgERD-YGPPIDMWGAGCIMAEMWTRS-PIMQG--NTEQHQLTLIsql 239
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 640 -GS---------------GKFSLSGGY--------WNSVSD-TAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07865  240 cGSitpevwpgvdklelfKKMELPQGQkrkvkerlKPYVKDpYALDLIDKLLVLDPAKRIDADTALNHDF 309
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
69-291 1.49e-12

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: 69.25  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  69 ELLKVLGQGSFGK--VFLVKKisgSDARQLYAMKvlkKATLKVRDRVRTK-MERDILV--EVNHPFIVKLHYAFQTEGKL 143
Cdd:cd08216    1 ELLYEIGKCFKGGgvVHLAKH---KPTNTLVAVK---KINLESDSKEDLKfLQQEILTsrQLQHPNILPYVTSFVVDNDL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 144 YLILDFLRGG---DLFTRLSKEvMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKESID 220
Cdd:cd08216   75 YVVTPLMAYGscrDLLKTHFPE-GLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVK 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 221 H-EKKAYSFCGTVE------YMAPEVV--NRRGHTQSADWWSFGVLMFEMLTGTLPFqgKDRKETMTMILKAKLGMPQFL 291
Cdd:cd08216  154 HgKRQRVVHDFPKSseknlpWLSPEVLqqNLLGYNEKSDIYSVGITACELANGVVPF--SDMPATQMLLEKVRGTTPQLL 231
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
434-614 1.51e-12

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: 68.27  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMEFAVKI--IDKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKI 511
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMntLSSNRANMLREVQLMNRL-SHPNILRFMGVCVHQGQLHALTEYINGGNLEQLL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 512 LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIrICDFGFAKQL-RAENGLLMTPCYTANF 590
Cdd:cd14155   80 DSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAV-VGDFGLAEKIpDYSDGKEKLAVVGSPY 158
                        170       180
                 ....*....|....*....|....*
gi 768032625 591 -VAPEVLKRQGYDAACDIWSLGVLL 614
Cdd:cd14155  159 wMAPEVLRGEPYNEKADVFSYGIIL 183
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
482-685 1.61e-12

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: 68.06  E-value: 1.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 482 IITLKDVYD--DGkYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGn 559
Cdd:cd14102   66 VIKLLDWYErpDG-FLIVMERPEPVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTG- 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 560 peSIRICDFGfakqlraENGLLMTPCY-----TANFVAPEVLKRQGYDA-ACDIWSLGVLLYTMLTGYTPFangpdDTPE 633
Cdd:cd14102  144 --ELKLIDFG-------SGALLKDTVYtdfdgTRVYSPPEWIRYHRYHGrSATVWSLGVLLYDMVCGDIPF-----EQDE 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 768032625 634 EILarigSGKFSlsggYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWI 685
Cdd:cd14102  210 EIL----RGRLY----FRRRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
434-624 1.72e-12

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: 68.68  E-value: 1.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATNMefAVK----IIDKSKRDPT----EEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGG 505
Cdd:cd14158   23 LGEGGFGVVFKGYINDKNV--AVKklaaMVDISTEDLTkqfeQEIQVMAKC-QHENLVELLGYSCDGPQLCLVYTYMPNG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKIL---RQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFAKQLRAENGLLM 582
Cdd:cd14158  100 SLLDRLAclnDTPPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANIL-LDETFVP---KISDFGLARASEKFSQTIM 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 768032625 583 TPCY--TANFVAPEVLkRQGYDAACDIWSLGVLLYTMLTGYTPF 624
Cdd:cd14158  176 TERIvgTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITGLPPV 218
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
428-636 1.79e-12

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: 68.05  E-value: 1.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIE--ILLRYGQHPNIITLKDVYDDGKYVYVVTELMkgG 505
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEvaVLKKLQGKPHFCRLIGCGRTERYNYIVMTLL--G 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILR---QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENG-LL 581
Cdd:cd14017   80 PNLAELRRsqpRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERTVYILDFGLARQYTNKDGeVE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 582 MTPCYTANFVAPEVL--------KRQGY-DaacDIWSLGVLLYTMLTGYTPFANGPDdtPEEIL 636
Cdd:cd14017  160 RPPRNAAGFRGTVRYasvnahrnKEQGRrD---DLWSWFYMLIEFVTGQLPWRKLKD--KEEVG 218
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
74-268 1.96e-12

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: 68.54  E-value: 1.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 149
Cdd:cd14030   33 IGRGSFKTVY---KGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDLKPENILLD-EEGHIKLTDFGLSkeSIDHEKKAY 226
Cdd:cd14030  110 MTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRASFAK 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768032625 227 SFCGTVEYMAPEVVNRRgHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14030  188 SVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPY 228
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
479-636 2.29e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 68.55  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYD-DGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHA--QGVVHRDLKPSNILYVD 555
Cdd:cd14041   69 HPRIVKLYDYFSlDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVN 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 556 ESGNPEsIRICDFGFAKQLRAEN-----GLLMTP------------CYTANFVAPEVLKRqgydaaCDIWSLGVLLYTML 618
Cdd:cd14041  149 GTACGE-IKITDFGLSKIMDDDSynsvdGMELTSqgagtywylppeCFVVGKEPPKISNK------VDVWSVGVIFYQCL 221
                        170
                 ....*....|....*...
gi 768032625 619 TGYTPFanGPDDTPEEIL 636
Cdd:cd14041  222 YGRKPF--GHNQSQQDIL 237
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
433-619 2.29e-12

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: 68.42  E-value: 2.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKA----TNMEFAVKIIDKSKR-----DPTEEIEILlRYGQHPNIITLKDVYDD--GKYVYVVTEL 501
Cdd:cd05079   11 DLGEGHFGKVELCRYDPegdnTGEQVAVKSLKPESGgnhiaDLKKEIEIL-RNLYHENIVKYKGICTEdgGNGIKLIMEF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELLDKILRQK-FFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGL 580
Cdd:cd05079   90 LPSGSLKEYLPRNKnKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIETDKEY 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 581 ------LMTPCYtanFVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05079  166 ytvkddLDSPVF---WYAPECLIQSKFYIASDVWSFGVTLYELLT 207
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
479-636 3.01e-12

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


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 68.16  E-value: 3.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYD-DGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLH--AQGVVHRDLKPSNILYVD 555
Cdd:cd14040   69 HPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVD 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 556 ESGNPEsIRICDFGFAKQLRAE----NGLLMTP------------CYTANFVAPEVLKRqgydaaCDIWSLGVLLYTMLT 619
Cdd:cd14040  149 GTACGE-IKITDFGLSKIMDDDsygvDGMDLTSqgagtywylppeCFVVGKEPPKISNK------VDVWSVGVIFFQCLY 221
                        170
                 ....*....|....*..
gi 768032625 620 GYTPFanGPDDTPEEIL 636
Cdd:cd14040  222 GRKPF--GHNQSQQDIL 236
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
74-268 3.74e-12

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


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 67.34  E-value: 3.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVFlvkKISGSDARQLYAMKVLKKATLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 149
Cdd:cd14033    9 IGRGSFKTVY---RGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 150 LRGGDLFTRLSKevmFTEEDVKF---YLAELALALDHLHSLG--IIYRDLKPENILLD-EEGHIKLTDFGLSkeSIDHEK 223
Cdd:cd14033   86 MTSGTLKTYLKR---FREMKLKLlqrWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRAS 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 224 KAYSFCGTVEYMAPEVVNRRgHTQSADWWSFGVLMFEMLTGTLPF 268
Cdd:cd14033  161 FAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPY 204
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
74-271 3.95e-12

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: 68.02  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  74 LGQGSFGKVflVKKISGSDARQLYAMKVL------KKATLKvrdrvrtkmERDILVEVN--------HpfIVKLHYAFQT 139
Cdd:cd14135    8 LGKGVFSNV--VRARDLARGNQEVAIKIIrnnelmHKAGLK---------ELEILKKLNdadpddkkH--CIRLLRHFEH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 140 EGKLYLILDFLRGG--DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH-IKLTDFGLSK 216
Cdd:cd14135   75 KNHLCLVFESLSMNlrEVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSAS 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 217 ESIDHEKKAY---SFcgtveYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGK 271
Cdd:cd14135  155 DIGENEITPYlvsRF-----YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGK 207
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
429-673 5.32e-12

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: 67.06  E-value: 5.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 429 EVKEDIGVGSY-SVCKRCIHKATNMEFAVKI------IDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKyVYVVTEL 501
Cdd:cd05056    9 TLGRCIGEGQFgDVYQGVYMSPENEKIAVAVktckncTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VWIVMEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 502 MKGGELlDKILRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDesgnPESIRICDFGFAKQLRAENg 579
Cdd:cd05056   88 APLGEL-RSYLQVNKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLVSS----PDCVKLGDFGLSRYMEDES- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 580 llmtpCYTAN-------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGPDdtpEEILARIGSG-KFSLSggy 650
Cdd:cd05056  162 -----YYKASkgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKN---NDVIGRIENGeRLPMP--- 230
                        250       260
                 ....*....|....*....|...
gi 768032625 651 wNSVSDTAKDLVSKMLHVDPHQR 673
Cdd:cd05056  231 -PNCPPTLYSLMTKCWAYDPSKR 252
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
449-624 5.67e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 68.33  E-value: 5.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 449 ATNMEFAVKIIDKSKrDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGgELLDKILRQKFFSEREASAVLFT 528
Cdd:PHA03207 117 EQRKKVIVKAVTGGK-TPGREIDIL-KTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLFTYVDRSGPLPLEQAITIQRR 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 ITKTVEYLHAQGVVHRDLKPSNIlYVDesgNPESIRICDFGFAKQLRAENGllmTP-CY----TANFVAPEVLKRQGYDA 603
Cdd:PHA03207 194 LLEALAYLHGRGIIHRDVKTENI-FLD---EPENAVLGDFGAACKLDAHPD---TPqCYgwsgTLETNSPELLALDPYCA 266
                        170       180
                 ....*....|....*....|.
gi 768032625 604 ACDIWSLGVLLYTMLTGYTPF 624
Cdd:PHA03207 267 KTDIWSAGLVLFEMSVKNVTL 287
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
432-643 5.73e-12

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: 66.60  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATN---MEFAVKIIDKSKrDPTEEIEILlRYGQ------HPNIITLKDVYDdGKYVYVVTELM 502
Cdd:cd05060    1 KELGHGNFGSVRKGVYLMKSgkeVEVAVKTLKQEH-EKAGKKEFL-REASvmaqldHPCIVRLIGVCK-GEPLMLVMELA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGLlm 582
Cdd:cd05060   78 PLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNR----HQAKISDFGMSRALGAGSDY-- 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 tpcYTA--------NFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFAngpDDTPEEILARIGSGK 643
Cdd:cd05060  152 ---YRAttagrwplKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYG---EMKGPEVIAMLESGE 215
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
455-628 6.99e-12

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: 66.67  E-value: 6.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-DKSKRDPTEEIeilLRYG------QHPNIITLKDVYDdGKYVYVVTELMKGGELLDKILRQKffsEREASAVLF 527
Cdd:cd05057   40 AIKVLrEETGPKANEEI---LDEAyvmasvDHPHLVRLLGICL-SSQVQLITQLMPLGCLLDYVRNHR---DNIGSQLLL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 528 T----ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAK-------QLRAENGllMTPCytaNFVAPEVL 596
Cdd:cd05057  113 NwcvqIAKGMSYLEEKRLVHRDLAARNVLV----KTPNHVKITDFGLAKlldvdekEYHAEGG--KVPI---KWMALESI 183
                        170       180       190
                 ....*....|....*....|....*....|...
gi 768032625 597 KRQGYDAACDIWSLGVLLYTMLT-GYTPFANGP 628
Cdd:cd05057  184 QYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIP 216
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
434-623 8.71e-12

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 66.77  E-value: 8.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSvckrCIHKAT--NMEFAVKII--------DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMK 503
Cdd:cd14159    1 IGEGGFG----CVYQAVmrNTEYAVKRLkedseldwSVVKNSFLTEVEKLSRF-RHPNIVDLAGYSAQQGNYCLIYVYLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 504 GGELLDKILRQKFF---SEREASAVLFTITKTVEYLH--AQGVVHRDLKPSNILyVDESGNPesiRICDFGFAKQLRAEN 578
Cdd:cd14159   76 NGSLEDRLHCQVSCpclSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNIL-LDAALNP---KLGDFGLARFSRRPK 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 768032625 579 GLLMTPCY--------TANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTGYTP 623
Cdd:cd14159  152 QPGMSSTLartqtvrgTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
66-310 9.44e-12

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: 66.20  E-value: 9.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVF-LVKKISGSdarqLYAMKVLKKATLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAF 137
Cdd:cd14138    5 TEFHELEKIGSGEFGSVFkCVKRLDGC----IYAIKRSKKPLAGSVD------EQNALREVyahavlgQHSHVVRYYSAW 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDFLRGGDLFTRLSKEV----MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILL------------ 201
Cdd:cd14138   75 AEDDHMLIQNEYCNGGSLADAISENYrimsYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaasee 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 202 ---DEEGH----IKLTDFG----LSKESIDHekkaysfcGTVEYMAPEVVNRR-GHTQSADWWSFGVLMFEMLTGT-LPF 268
Cdd:cd14138  155 gdeDEWASnkviFKIGDLGhvtrVSSPQVEE--------GDSRFLANEVLQENyTHLPKADIFALALTVVCAAGAEpLPT 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 269 QGKDRKEtmtmILKAKLG-MPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14138  227 NGDQWHE----IRQGKLPrIPQVLSQEFLDLLKVMIHPDPERR 265
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
135-311 9.95e-12

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 66.28  E-value: 9.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 135 YAFQTEGKLYLILDFL-------RGGDLFT---RLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEE 204
Cdd:cd13974   89 YTGRVRKRLCLVLDCLcahdfsdKTADLINlqhYVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKR 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 205 GH-IKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHT-QSADWWSFGVLMFEMLTGTLPFQGKDRKETMTMILK 282
Cdd:cd13974  169 TRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYLgKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKA 248
                        170       180       190
                 ....*....|....*....|....*....|.
gi 768032625 283 AKLGMPQ--FLSPEAQSLLRMLFKRNPANRL 311
Cdd:cd13974  249 AEYTIPEdgRVSENTVCLIRKLLVLNPQKRL 279
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
455-675 1.00e-11

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: 66.36  E-value: 1.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIdKSKRDPTE------EIEILLRYGQHPNIITLKDV-YDDGKYVYVVTELMKGGELLD--KILRQKFFSEREASAV 525
Cdd:cd05054   41 AVKML-KEGATASEhkalmtELKILIHIGHHLNVVNLLGAcTKPGGPLMVIVEFCKFGNLSNylRSKREEFVPYRDKGAR 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 526 L------------------------FTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAEngll 581
Cdd:cd05054  120 DveeeedddelykepltledlicysFQVARGMEFLASRKCIHRDLAARNILLSENN----VVKICDFGLARDIYKD---- 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 582 mtPCYTAN--------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDtpEEILARIGSGKFSLSGGYwn 652
Cdd:cd05054  192 --PDYVRKgdarlplkWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQMD--EEFCRRLKEGTRMRAPEY-- 265
                        250       260
                 ....*....|....*....|....*.
gi 768032625 653 svsdTAKDLVSKML---HVDPHQRLT 675
Cdd:cd05054  266 ----TTPEIYQIMLdcwHGEPKERPT 287
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
432-624 1.13e-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: 65.67  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKAtNMEFAVKIIDK---SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELL 508
Cdd:cd05113   10 KELGTGQFGVVKYGKWRG-QYDVAIKMIKEgsmSEDEFIEEAKVMMNL-SHEKLVQLYGVCTKQRPIFIITEYMANGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 509 DkILR--QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAKQ-LRAENGLLMTPC 585
Cdd:cd05113   88 N-YLRemRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCL-VNDQG---VVKVSDFGLSRYvLDDEYTSSVGSK 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 768032625 586 YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05113  163 FPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPY 202
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
434-645 1.29e-11

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: 65.81  E-value: 1.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRcihKATNMEFAVKIIDKSKRDPTE------EIEILlRYGQHPNIITLKDVYDDGKYVyVVTELMKGGEL 507
Cdd:cd14150    8 IGTGSFGTVFR---GKWHGDVAVKILKVTEPTPEQlqafknEMQVL-RKTRHVNILLFMGFMTRPNFA-IITQWCEGSSL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 508 LDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESgnpESIRICDFGFA--KQLRAENGLLMTP 584
Cdd:cd14150   83 YRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNI-FLHEG---LTVKIGDFGLAtvKTRWSGSQQVEQP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 585 CYTANFVAPEVLKRQG---YDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFS 645
Cdd:cd14150  159 SGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSN--INNRDQIIFMVGRGYLS 220
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
455-624 1.56e-11

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: 65.28  E-value: 1.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII--DKSKRDPTEEIEILLRYgQHPNIITLKDV-YDDGkyVYVVTELMKGGELLDKILRQKFFSEREASAVLFT--I 529
Cdd:cd05083   33 AVKNIkcDVTAQAFLEETAVMTKL-QHKNLVRLLGViLHNG--LYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSldV 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 530 TKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAK-QLRAENGLLMTPCYTAnfvaPEVLKRQGYDAACDIW 608
Cdd:cd05083  110 AEGMEYLESKKLVHRDLAARNIL-VSEDG---VAKISDFGLAKvGSMGVDNSRLPVKWTA----PEALKNKKFSSKSDVW 181
                        170
                 ....*....|....*..
gi 768032625 609 SLGVLLYTMLT-GYTPF 624
Cdd:cd05083  182 SYGVLLWEVFSyGRAPY 198
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
66-305 1.77e-11

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 66.03  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  66 SQFELLKVLGQGSFGKVflVKKISGSDARQLYAMKVLKKAtlkvrDRVRTKMERDILV-------EVNHPF-IVKLHYAF 137
Cdd:cd14213   12 ARYEIVDTLGEGAFGKV--VECIDHKMGGMHVAVKIVKNV-----DRYREAARSEIQVlehlnttDPNSTFrCVQMLEWF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 138 QTEGKLYLILDFLRGGDL-FTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGH---------- 206
Cdd:cd14213   85 DHHGHVCIVFELLGLSTYdFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYvvkynpkmkr 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 207 ---------IKLTDFGlsKESIDHEKKAySFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGTLPFQGKDRKETM 277
Cdd:cd14213  165 dertlknpdIKVVDFG--SATYDDEHHS-TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHL 241
                        250       260
                 ....*....|....*....|....*...
gi 768032625 278 TMilkaklgMPQFLSPEAQSLLRMLFKR 305
Cdd:cd14213  242 AM-------MERILGPLPKHMIQKTRKR 262
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
434-614 2.08e-11

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: 65.22  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATN----MEFAVKIIDKSKRDPTEEIEiLLRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGevmvMKELIRFDEEAQRNFLKEVK-VMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KI---LRQKFFSEReasaVLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGLLMTP 584
Cdd:cd14154   80 VLkdmARPLPWAQR----VRFAkdIASGMAYLHSMNIIHRDLNSHNCLVRED----KTVVVADFGLARLIVEERLPSGNM 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 768032625 585 C----------------YTA----NFVAPEVLKRQGYDAACDIWSLGVLL 614
Cdd:cd14154  152 SpsetlrhlkspdrkkrYTVvgnpYWMAPEMLNGRSYDEKVDIFSFGIVL 201
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
428-684 2.68e-11

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: 65.05  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVckrcIHKATNMEFAVKIID-KSKRDPTEE----------IEIL--LRYGQHPNIITLKDV-----Y 489
Cdd:cd07862    3 YECVAEIGEGAYGK----VFKARDLKNGGRFVAlKRVRVQTGEegmplstireVAVLrhLETFEHPNVVRLFDVctvsrT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 490 DDGKYVYVVTELMKGG--ELLDKILRQKFFSErEASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICD 567
Cdd:cd07862   79 DRETKLTLVFEHVDQDltTYLDKVPEPGVPTE-TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNIL-VTSSGQ---IKLAD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 568 FGFAKQLRAENGLLMTpCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTgYTPFANGPDD--------------TPE 633
Cdd:cd07862  154 FGLARIYSFQMALTSV-VVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR-RKPLFRGSSDvdqlgkildviglpGEE 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 634 EILARIGSGKFSLSG-------GYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPW 684
Cdd:cd07862  232 DWPRDVALPRQAFHSksaqpieKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPY 289
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
527-682 2.72e-11

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: 65.77  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 527 FTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAEngllmtPCYTA--------NFVAPEVLKR 598
Cdd:cd05103  186 FQVAKGMEFLASRKCIHRDLAARNILLSENN----VVKICDFGLARDIYKD------PDYVRkgdarlplKWMAPETIFD 255
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 599 QGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDtpEEILARIGSGKFSLSGGYwnsvsdTAKDLVSKML---HVDPHQRL 674
Cdd:cd05103  256 RVYTIQSDVWSFGVLLWEIFSlGASPYPGVKID--EEFCRRLKEGTRMRAPDY------TTPEMYQTMLdcwHGEPSQRP 327

                 ....*...
gi 768032625 675 TAALVLRH 682
Cdd:cd05103  328 TFSELVEH 335
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
433-624 3.86e-11

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 64.21  E-value: 3.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHKATNME--FAVKIIDKSKRDPTEEIEIL-----LRYGQHPNIITLKDVYDdGKYVYVVTELMKGG 505
Cdd:cd05116    2 ELGSGNFGTVKKGYYQMKKVVktVAVKILKNEANDPALKDELLreanvMQQLDNPYIVRMIGICE-AESWMLVMEMAELG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGLLMTPC 585
Cdd:cd05116   81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQ----HYAKISDFGLSKALRADENYYKAQT 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 768032625 586 ---YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05116  157 hgkWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPY 199
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
417-624 4.62e-11

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: 64.63  E-value: 4.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 417 LHRNSIQFTDGyevkedIGVGSY-SVCKRCIHK-ATNMEFAVKIIDK-----SKRDPTEEIEILLRYGQHPNIITLKDVY 489
Cdd:cd05088    4 LEWNDIKFQDV------IGEGNFgQVLKARIKKdGLRMDAAIKRMKEyaskdDHRDFAGELEVLCKLGHHPNIINLLGAC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 490 DDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTV----------------EYLHAQGVVHRDLKPSNILY 553
Cdd:cd05088   78 EHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLssqqllhfaadvargmDYLSQKQFIHRDLAARNILV 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 554 vdesGNPESIRICDFGFAK--QLRAENGLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05088  158 ----GENYVAKIADFGLSRgqEVYVKKTMGRLP---VRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 224
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
431-619 6.11e-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: 64.02  E-value: 6.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 431 KEDIGVGSY-----SVCKRCIHKATNMEFAVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05049   10 KRELGEGAFgkvflGECYNLEPEQDKMLVAVKTLkdassPDARKDFEREAELLTNL-QHENIVKFYGVCTEGDPLLMVFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELlDKILRQ-----KFFSEREAS----------AVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRI 565
Cdd:cd05049   89 YMEHGDL-NKFLRShgpdaAFLASEDSApgeltlsqllHIAVQIASGMVYLASQHFVHRDLATRNCLV----GTNLVVKI 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 566 CDFGFAKQLRAEN-----GLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05049  164 GDFGMSRDIYSTDyyrvgGHTMLP---IRWMPPESILYRKFTTESDVWSFGVVLWEIFT 219
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
72-311 7.70e-11

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: 63.68  E-value: 7.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  72 KVLGQGSFGKVFLVKKI-SGSDarqlYAMKVLKKAtlkvrdrvRTKMERDILVEVN-------HPFIVKLHYA------- 136
Cdd:cd14036    6 RVIAEGGFAFVYEAQDVgTGKE----YALKRLLSN--------EEEKNKAIIQEINfmkklsgHPNIVQFCSAasigkee 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 137 FQTEGKLYLIL-DFLRGG--DLFTRLSKEVMFTEEDVKFYLAELALALDHLH--SLGIIYRDLKPENILLDEEGHIKLTD 211
Cdd:cd14036   74 SDQGQAEYLLLtELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLCD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 212 FGlSKESIDHEKKaYSFC----GTVE----------YMAPEVVNRRGH---TQSADWWSFGVLMFEMLTGTLPFQ--GKD 272
Cdd:cd14036  154 FG-SATTEAHYPD-YSWSaqkrSLVEdeitrnttpmYRTPEMIDLYSNypiGEKQDIWALGCILYLLCFRKHPFEdgAKL 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 273 RketmtmILKAKLGMPQflSPEA----QSLLRMLFKRNPANRL 311
Cdd:cd14036  232 R------IINAKYTIPP--NDTQytvfHDLIRSTLKVNPEERL 266
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
430-645 7.99e-11

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: 63.54  E-value: 7.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKEDIGVGSYSVckrcIHKAT-NMEFAVKIIDKSKRDPTE------EIEILlRYGQHPNIITLKDvYDDGKYVYVVTELM 502
Cdd:cd14151   12 VGQRIGSGSFGT----VYKGKwHGDVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNILLFMG-YSTKPQLAIVTQWC 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAK--------- 572
Cdd:cd14151   86 EGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDL----TVKIGDFGLATvksrwsgsh 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 573 QLRAENGLLMtpcytanFVAPEVLKRQG---YDAACDIWSLGVLLYTMLTGYTPFANgpDDTPEEILARIGSGKFS 645
Cdd:cd14151  162 QFEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSN--INNRDQIIFMVGRGYLS 228
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
473-643 8.20e-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: 63.62  E-value: 8.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 473 LLRYGQHPNIITLKDV-YDDGKYVYVVTELMKGGELlDKILRQKFFSEREASAVLFT---------ITKTVEYLHAQGVV 542
Cdd:cd05043   60 LLYGLSHQNLLPILHVcIEDGEKPMVLYPYMNWGNL-KLFLQQCRLSEANNPQALSTqqlvhmalqIACGMSYLHRRGVI 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 543 HRDLKPSNIlYVDESGNpesIRICDFGFAKQL---------RAENGLLmtpcytaNFVAPEVLKRQGYDAACDIWSLGVL 613
Cdd:cd05043  139 HKDIAARNC-VIDDELQ---VKITDNALSRDLfpmdyhclgDNENRPI-------KWMSLESLVNKEYSSASDVWSFGVL 207
                        170       180       190
                 ....*....|....*....|....*....|.
gi 768032625 614 LYTMLT-GYTPFAngpDDTPEEILARIGSGK 643
Cdd:cd05043  208 LWELMTlGQTPYV---EIDPFEMAAYLKDGY 235
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
448-676 1.01e-10

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


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 62.95  E-value: 1.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 448 KATNMEFAVKIIDKSKRDPTEEIEILLRygQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILrqKFFSERE------ 521
Cdd:cd05576   21 TRTQETFILKGLRKSSEYSRERKTIIPR--CVPNMVCLRKYIISEESVFLVLQHAEGGKLWSYLS--KFLNDKEihqlfa 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 522 ------ASAVLFTITKT------------VEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAE-NGLLM 582
Cdd:cd05576   97 dlderlAAASRFYIPEEciqrwaaemvvaLDALHREGIVCRDLNPNNIL-LNDRGH---IQLTYFSRWSEVEDScDSDAI 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 583 TPCYTAnfvaPEVLKRQGYDAACDIWSLGVLLYTMLTGYTPFANGPddtpeeilARIGSGKfSLSGGYWnsVSDTAKDLV 662
Cdd:cd05576  173 ENMYCA----PEVGGISEETEACDWWSLGALLFELLTGKALVECHP--------AGINTHT-TLNIPEW--VSEEARSLL 237
                        250
                 ....*....|....
gi 768032625 663 SKMLHVDPHQRLTA 676
Cdd:cd05576  238 QQLLQFNPTERLGA 251
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
495-638 2.12e-10

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 62.73  E-value: 2.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDKILRQKffsEREASAVLFT----ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGF 570
Cdd:cd05108   83 VQLITQLMPFGCLLDYVREHK---DNIGSQYLLNwcvqIAKGMNYLEDRRLVHRDLAARNVLV----KTPQHVKITDFGL 155
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 571 AKQLRAENgllmtPCYTAN-------FVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDTPEEILAR 638
Cdd:cd05108  156 AKLLGAEE-----KEYHAEggkvpikWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEISSILEK 226
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
392-682 2.63e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 63.09  E-value: 2.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 392 SFVAITSDDESQAMQTVGVHSIVqqlhRNSIQfTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKiidKSKRDPTEEIE 471
Cdd:PHA03212  63 IFDIFADEDESDADASLALCAEA----RAGIE-KAGFSILETFTPGAEGFAFACIDNKTCEHVVIK---AGQRGGTATEA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 472 ILLRYGQHPNIITLKDVYDDGKYVYVVTELMKGgELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNI 551
Cdd:PHA03212 135 HILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENI 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 552 LYvdesGNPESIRICDFGFAkqlraengllmtpCY----TANFV----------APEVLKRQGYDAACDIWSLGVLLYTM 617
Cdd:PHA03212 214 FI----NHPGDVCLGDFGAA-------------CFpvdiNANKYygwagtiatnAPELLARDPYGPAVDIWSAGIVLFEM 276
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 618 LTGY------------------------------TPFANGPDDTPEEILARIG--SGKFSLSGGYWNSVSDTAKD---LV 662
Cdd:PHA03212 277 ATCHdslfekdgldgdcdsdrqikliirrsgthpNEFPIDAQANLDEIYIGLAkkSSRKPGSRPLWTNLYELPIDleyLI 356
                        330       340
                 ....*....|....*....|
gi 768032625 663 SKMLHVDPHQRLTAALVLRH 682
Cdd:PHA03212 357 CKMLAFDAHHRPSAEALLDF 376
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
473-642 2.85e-10

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: 61.83  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 473 LLRYGQHPNIITLKDVYDDgKYVYVVTELMKGGELLDkilrqkFFSEREASAVlfTITKTVE----------YLHAQGVV 542
Cdd:cd05067   55 LMKQLQHQRLVRLYAVVTQ-EPIYIITEYMENGSLVD------FLKTPSGIKL--TINKLLDmaaqiaegmaFIEERNYI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 543 HRDLKPSNILYVDESgnpeSIRICDFGFAKqlraengLLMTPCYTA--------NFVAPEVLKRQGYDAACDIWSLGVLL 614
Cdd:cd05067  126 HRDLRAANILVSDTL----SCKIADFGLAR-------LIEDNEYTAregakfpiKWTAPEAINYGTFTIKSDVWSFGILL 194
                        170       180
                 ....*....|....*....|....*....
gi 768032625 615 YTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05067  195 TEIVThGRIPY---PGMTNPEVIQNLERG 220
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
451-642 3.14e-10

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: 61.09  E-value: 3.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 451 NMEFAVKIIDKSKRDPT---EEIEILLRYgQHPNIITLKDVYDDgKYVYVVTELMKGGELLDkilrqkFFSEREASAVLF 527
Cdd:cd14203   19 TTKVAIKTLKPGTMSPEaflEEAQIMKKL-RHDKLVQLYAVVSE-EPIYIVTEFMSKGSLLD------FLKDGEGKYLKL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 528 --------TITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENgllMTPCYTANF----VAPEV 595
Cdd:cd14203   91 pqlvdmaaQIASGMAYIERMNYIHRDLRAANILV----GDNLVCKIADFGLARLIEDNE---YTARQGAKFpikwTAPEA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 768032625 596 LKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd14203  164 ALYGRFTIKSDVWSFGILLTELVTkGRVPY---PGMNNREVLEQVERG 208
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
434-614 4.70e-10

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: 61.13  E-value: 4.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATN----MEFAVKIIDKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGevmvMKELIRFDEETQRTFLKEVKVM-RCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILR---QKFFSEREASAVlfTITKTVEYLHAQGVVHRDLKPSNILyVDESGnpeSIRICDFGFAK-------------- 572
Cdd:cd14221   80 IIKSmdsHYPWSQRVSFAK--DIASGMAYLHSMNIIHRDLNSHNCL-VRENK---SVVVADFGLARlmvdektqpeglrs 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768032625 573 QLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLL 614
Cdd:cd14221  154 LKKPDRKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVL 195
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
468-626 6.62e-10

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 60.59  E-value: 6.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 468 EEIEILLRYgQHPNIITLKDV-YDDGKYVyVVTELMKGGELLdKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDL 546
Cdd:cd14027   40 EEGKMMNRL-RHSRVVKLLGViLEEGKYS-LVMEYMEKGNLM-HVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 547 KPSNILyVDESGNpesIRICDFGFA-------------KQLRAENGLLMTPCYTANFVAPEVLKRQGYDAA--CDIWSLG 611
Cdd:cd14027  117 KPENIL-VDNDFH---IKIADLGLAsfkmwskltkeehNEQREVDGTAKKNAGTLYYMAPEHLNDVNAKPTekSDVYSFA 192
                        170
                 ....*....|....*
gi 768032625 612 VLLYTMLTGYTPFAN 626
Cdd:cd14027  193 IVLWAIFANKEPYEN 207
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
434-614 1.14e-09

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: 59.96  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVCKRCIHKATN----MEFAVKIIDKSKRDPTEEIEILlRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELLD 509
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGkvmvMKELIRCDEETQKTFLTEVKVM-RSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKqLRAENGLLMTPCYTAN 589
Cdd:cd14222   80 FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDK----TVVVADFGLSR-LIVEEKKKPPPDKPTT 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 590 ---------------------FVAPEVLKRQGYDAACDIWSLGVLL 614
Cdd:cd14222  155 kkrtlrkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVL 200
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
462-619 1.81e-09

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 59.60  E-value: 1.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 462 SKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELldkilrQKFFSEREASAVL--------------- 526
Cdd:cd05097   60 ARNDFLKEIKIMSRL-KNPNIIRLLGVCVSDDPLCMITEYMENGDL------NQFLSQREIESTFthannipsvsianll 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 527 ---FTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKR 598
Cdd:cd05097  133 ymaVQIASGMKYLASLNFVHRDLATRNCLV----GNHYTIKIADFGMSRNLYSGDyyriqGRAVLPI---RWMAWESILL 205
                        170       180
                 ....*....|....*....|.
gi 768032625 599 QGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05097  206 GKFTTASDVWAFGVTLWEMFT 226
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
479-642 1.93e-09

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 59.32  E-value: 1.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNIITLKDVYDDGKYVYVVTELMKGGElLDKILRQ--------KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSN 550
Cdd:cd05036   68 HPNIVRCIGVCFQRLPRFILLELMAGGD-LKSFLREnrprpeqpSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 551 ILyVDESGNPESIRICDFGFAKQL-RAE----NGLLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05036  147 CL-LTCKGPGRVAKIGDFGMARDIyRADyyrkGGKAMLP---VKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPY 222
                        170
                 ....*....|....*...
gi 768032625 625 angPDDTPEEILARIGSG 642
Cdd:cd05036  223 ---PGKSNQEVMEFVTSG 237
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
473-642 2.19e-09

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: 58.88  E-value: 2.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 473 LLRYGQHPNIITLKDVYDDgKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSN 550
Cdd:cd05073   59 VMKTLQHDKLVKLHAVVTK-EPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSaqIAEGMAFIEQRNYIHRDLRAAN 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 551 ILYvdesGNPESIRICDFGFAKQLRAENgllmtpcYTA--------NFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GY 621
Cdd:cd05073  138 ILV----SASLVCKIADFGLARVIEDNE-------YTAregakfpiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGR 206
                        170       180
                 ....*....|....*....|.
gi 768032625 622 TPFangPDDTPEEILARIGSG 642
Cdd:cd05073  207 IPY---PGMSNPEVIRALERG 224
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
433-650 2.33e-09

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: 59.21  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYS-----VCKRCIHKATNMEFAVKIIDKSK--RDPTE---EIEILLRYGQHpNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd05061   13 ELGQGSFGmvyegNARDIIKGEAETRVAVKTVNESAslRERIEflnEASVMKGFTCH-HVVRLLGVVSKGQPTLVVMELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVE----------YLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAK 572
Cdd:cd05061   92 AHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQmaaeiadgmaYLNAKKFVHRDLAARNCMVAHDF----TVKIGDFGMTR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 573 QL-------RAENGLLmtpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMltgyTPFANGPDD--TPEEILarigsgK 643
Cdd:cd05061  168 DIyetdyyrKGGKGLL-----PVRWMAPESLKDGVFTTSSDMWSFGVVLWEI----TSLAEQPYQglSNEQVL------K 232

                 ....*..
gi 768032625 644 FSLSGGY 650
Cdd:cd05061  233 FVMDGGY 239
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
451-642 2.53e-09

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: 58.93  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 451 NMEFAVKIIDKSKRDPT---EEIEILLRYgQHPNIITLKDVYDDgKYVYVVTELMKGGELLDkilrqkFFSEREASAVLF 527
Cdd:cd05070   33 NTKVAIKTLKPGTMSPEsflEEAQIMKKL-KHDKLVQLYAVVSE-EPIYIVTEYMSKGSLLD------FLKDGEGRALKL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 528 --------TITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLR-AENGLLMTPCYTANFVAPEVLKR 598
Cdd:cd05070  105 pnlvdmaaQVAAGMAYIERMNYIHRDLRSANILV----GNGLICKIADFGLARLIEdNEYTARQGAKFPIKWTAPEAALY 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 768032625 599 QGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05070  181 GRFTIKSDVWSFGILLTELVTkGRVPY---PGMNNREVLEQVERG 222
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
473-623 2.88e-09

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 58.82  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 473 LLRYGQHPNIITLKDVYDD-----------GKYVYVVTELMKGGEL--LDKILRQKffsereasaVLFTITKTVEYLHAQ 539
Cdd:cd14067   63 MLHSLQHPCIVYLIGISIHplcfalelaplGSLNTVLEENHKGSSFmpLGHMLTFK---------IAYQIAAGLAYLHKK 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 540 GVVHRDLKPSNILY----VDESGNpesIRICDFGFAKQLRAEN--GLLMTPCYTAnfvaPEVLKRQGYDAACDIWSLGVL 613
Cdd:cd14067  134 NIIFCDLKSDNILVwsldVQEHIN---IKLSDYGISRQSFHEGalGVEGTPGYQA----PEIRPRIVYDEKVDMFSYGMV 206
                        170
                 ....*....|
gi 768032625 614 LYTMLTGYTP 623
Cdd:cd14067  207 LYELLSGQRP 216
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
434-645 2.91e-09

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: 58.89  E-value: 2.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 434 IGVGSYSVckrcIHKAT-NMEFAVKIIDKSkrDPTEEI------EI-LLRYGQHPNIITLKDVYDDGKyVYVVTELMKGG 505
Cdd:cd14149   20 IGSGSFGT----VYKGKwHGDVAVKILKVV--DPTPEQfqafrnEVaVLRKTRHVNILLFMGYMTKDN-LAIVTQWCEGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELLDKI-LRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESgnpESIRICDFGFA--KQLRAENGLLM 582
Cdd:cd14149   93 SLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI-FLHEG---LTVKIGDFGLAtvKSRWSGSQQVE 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 583 TPCYTANFVAPEVLKRQG---YDAACDIWSLGVLLYTMLTGYTPFANGPDDtpEEILARIGSGKFS 645
Cdd:cd14149  169 QPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGELPYSHINNR--DQIIFMVGRGYAS 232
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
395-639 3.18e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 60.09  E-value: 3.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 395 AITSDDESQAMQTVGVHSIVQQLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNME--------FAVKIIDKSKRDP 466
Cdd:PHA03210 117 ASHLDFDEAPPDAAGPVPLAQAKLKHDDEFLAHFRVIDDLPAGAFGKIFICALRASTEEaearrgvnSTNQGKPKCERLI 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 467 TE------------EIEIL-LRYGQHPNIITLKDVYDDGKYVYVVTE--------LMKGGELLDK---ILRQkffsereA 522
Cdd:PHA03210 197 AKrvkagsraaiqlENEILaLGRLNHENILKIEEILRSEANTYMITQkydfdlysFMYDEAFDWKdrpLLKQ-------T 269
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 523 SAVLFTITKTVEYLHAQGVVHRDLKPSNIlYVDESGnpeSIRICDFG----FAKQLRA-ENGLLMTpcYTANfvAPEVLK 597
Cdd:PHA03210 270 RAIMKQLLCAVEYIHDKKLIHRDIKLENI-FLNCDG---KIVLGDFGtampFEKEREAfDYGWVGT--VATN--SPEILA 341
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 598 RQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARI 639
Cdd:PHA03210 342 GDGYCEITDIWSCGLILLDMLSHDFCPIGDGGGKPGKQLLKI 383
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
467-675 3.44e-09

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: 58.25  E-value: 3.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 467 TEEIEILLRYG------QHPNIITLKDV-YDDGKYVYVVTELMKGGELLDKIlRQKFFSEREASAVLF--TITKTVEYLH 537
Cdd:cd05058   37 IEEVEQFLKEGiimkdfSHPNVLSLLGIcLPSEGSPLVVLPYMKHGDLRNFI-RSETHNPTVKDLIGFglQVAKGMEYLA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 538 AQGVVHRDLKPSNILyVDESgnpESIRICDFGFAKQL---------RAENGLLmtpcyTANFVAPEVLKRQGYDAACDIW 608
Cdd:cd05058  116 SKKFVHRDLAARNCM-LDES---FTVKVADFGLARDIydkeyysvhNHTGAKL-----PVKWMALESLQTQKFTTKSDVW 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 609 SLGVLLYTMLT-GYTPFangPDDTPEEILARIGSGKFSLSGGYwnsVSDTAKDLVSKMLHVDPHQRLT 675
Cdd:cd05058  187 SFGVLLWELMTrGAPPY---PDVDSFDITVYLLQGRRLLQPEY---CPDPLYEVMLSCWHPKPEMRPT 248
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
67-310 4.00e-09

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: 58.18  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVF-LVKKISGSdarqLYAMKVLKKATLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAFQ 138
Cdd:cd14051    1 EFHEVEKIGSGEFGSVYkCINRLDGC----VYAIKKSKKPVAGSVD------EQNALNEVyahavlgKHPHVVRYYSAWA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLSKE----VMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGL 214
Cdd:cd14051   71 EDDHMIIQNEYCNGGSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSEEEE 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYSFC--------------------GTVEYMAPEVVNRR-GHTQSADWWSFGVLMFEMLTG-TLPFQGKD 272
Cdd:cd14051  151 EDFEGEEDNPESNEVtykigdlghvtsisnpqveeGDCRFLANEILQENySHLPKADIFALALTVYEAAGGgPLPKNGDE 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 768032625 273 RKEtmtmILKAKLG-MPQfLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14051  231 WHE----IRQGNLPpLPQ-CSPEFNELLRSMIHPDPEKR 264
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
433-643 4.54e-09

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: 58.03  E-value: 4.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYSVCKRCIHK--ATNMEFAVKII----DKSKRDPT-EEIEILLRYgQHPNIITLKDVYDdGKYVYVVTELMKGG 505
Cdd:cd05115   11 ELGSGNFGCVKKGVYKmrKKQIDVAIKVLkqgnEKAVRDEMmREAQIMHQL-DNPYIVRMIGVCE-AEALMLVMEMASGG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 506 ELldkilrQKFFSEREAS-------AVLFTITKTVEYLHAQGVVHRDLKPSNILYVdesgNPESIRICDFGFAKQLRAEN 578
Cdd:cd05115   89 PL------NKFLSGKKDEitvsnvvELMHQVSMGMKYLEEKNFVHRDLAARNVLLV----NQHYAKISDFGLSKALGADD 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 579 GLlmtpcYTA--------NFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFA--NGPddtpeEILARIGSGK 643
Cdd:cd05115  159 SY-----YKArsagkwplKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKkmKGP-----EVMSFIEQGK 224
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
428-611 5.07e-09

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: 58.42  E-value: 5.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIdKSK----RDPTEEIEIL--------LRYGQHpnIITLKDVYDDGKYV 495
Cdd:cd14212    1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKpayfRQAMLEIAILtllntkydPEDKHH--IVRLLDHFMHHGHL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 496 YVVTELMkgGELLDKILRQKFFSEREASAV-LFT--ITKTVEYLHAQGVVHRDLKPSNILYVDEsgNPESIRICDFGFAK 572
Cdd:cd14212   78 CIVFELL--GVNLYELLKQNQFRGLSLQLIrKFLqqLLDALSVLKDARIIHCDLKPENILLVNL--DSPEIKLIDFGSAC 153
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 768032625 573 QlraENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLG 611
Cdd:cd14212  154 F---ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLG 189
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
527-624 8.28e-09

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: 58.09  E-value: 8.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 527 FTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQlraengLLMTPCYTA--------NFVAPEVLKR 598
Cdd:cd14207  187 FQVARGMEFLSSRKCIHRDLAARNILLSENN----VVKICDFGLARD------IYKNPDYVRkgdarlplKWMAPESIFD 256
                         90       100
                 ....*....|....*....|....*..
gi 768032625 599 QGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd14207  257 KIYSTKSDVWSYGVLLWEIFSlGASPY 283
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
495-633 8.49e-09

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: 57.34  E-value: 8.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 495 VYVVTELMKGGELLDKILRQKffsEREASAVLFT----ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGF 570
Cdd:cd05109   83 VQLVTQLMPYGCLLDYVRENK---DRIGSQDLLNwcvqIAKGMSYLEEVRLVHRDLAARNVLV----KSPNHVKITDFGL 155
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 768032625 571 AKQL-------RAENGLLmtpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFANGP-DDTPE 633
Cdd:cd05109  156 ARLLdideteyHADGGKV-----PIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPaREIPD 222
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
428-620 1.09e-08

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: 57.37  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 428 YEVKEDIGVGSYSVCKRCIHKATNME---FAVKIIDKSkrdPTEEIEILLRYGQHPNIITLKDVYDDGKYVYV------- 497
Cdd:cd13981    2 YVISKELGEGGYASVYLAKDDDEQSDgslVALKVEKPP---SIWEFYICDQLHSRLKNSRLRESISGAHSAHLfqdesil 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 498 VTELMKGGELLDKILRQKFFSER---EASAVLFTIT--KTVEYLHAQGVVHRDLKPSNIL-----------YVDESGNPE 561
Cdd:cd13981   79 VMDYSSQGTLLDVVNKMKNKTGGgmdEPLAMFFTIEllKVVEALHEVGIIHGDIKPDNFLlrleicadwpgEGENGWLSK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 768032625 562 SIRICDFGFAKQLRA--ENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLTG 620
Cdd:cd13981  159 GLKLIDFGRSIDMSLfpKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFG 219
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
430-624 1.41e-08

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 56.90  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKEDIGVGSY-----SVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEiLLRYGQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05092    9 LKWELGEGAFgkvflAECHNLLPEQDKMLVAVKALkeatESARQDFQREAE-LLTVLQHQHIVRFYGVCTEGEPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELlDKILRQ-----KFFSEREASA-----------VLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIR 564
Cdd:cd05092   88 YMRHGDL-NRFLRShgpdaKILDGGEGQApgqltlgqmlqIASQIASGMVYLASLHFVHRDLATRNCLV----GQGLVVK 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 768032625 565 ICDFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05092  163 IGDFGMSRDIYSTDyyrvgGRTMLPI---RWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPW 225
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
518-676 2.37e-08

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 56.35  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILY-VDESGNPESIrICDFGFAkqLRAENGLLMTPcYTANFV----- 591
Cdd:cd14018  136 SYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLeLDFDGCPWLV-IADFGCC--LADDSIGLQLP-FSSWYVdrggn 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 592 ----APEVLK-RQG------YDAAcDIWSLGVLLYTMLTGYTPFAnGPDDTPEEILARIGSGKFSLSggywNSVSDTAKD 660
Cdd:cd14018  212 aclmAPEVSTaVPGpgvvinYSKA-DAWAVGAIAYEIFGLSNPFY-GLGDTMLESRSYQESQLPALP----SAVPPDVRQ 285
                        170
                 ....*....|....*.
gi 768032625 661 LVSKMLHVDPHQRLTA 676
Cdd:cd14018  286 VVKDLLQRDPNKRVSA 301
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
527-624 6.80e-08

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: 54.99  E-value: 6.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 527 FTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAE-----NGLLMTPCytaNFVAPEVLKRQGY 601
Cdd:cd05102  179 FQVARGMEFLASRKCIHRDLAARNILLSENN----VVKICDFGLARDIYKDpdyvrKGSARLPL---KWMAPESIFDKVY 251
                         90       100
                 ....*....|....*....|....
gi 768032625 602 DAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05102  252 TTQSDVWSFGVLLWEIFSlGASPY 275
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
468-642 8.89e-08

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: 54.31  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 468 EEIEILLRYgQHPNIITLKDVYDDgKYVYVVTELMKGGELLDkILRQ---KFFSEREASAVLFTITKTVEYLHAQGVVHR 544
Cdd:cd05069   56 QEAQIMKKL-RHDKLVPLYAVVSE-EPIYIVTEFMGKGSLLD-FLKEgdgKYLKLPQLVDMAAQIADGMAYIERMNYIHR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 545 DLKPSNILYVDESgnpeSIRICDFGFAKQLR-AENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYT 622
Cdd:cd05069  133 DLRAANILVGDNL----VCKIADFGLARLIEdNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRV 208
                        170       180
                 ....*....|....*....|
gi 768032625 623 PFangPDDTPEEILARIGSG 642
Cdd:cd05069  209 PY---PGMVNREVLEQVERG 225
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
455-642 1.01e-07

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: 54.20  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIdKSKRDPTEEIEIL-----LRYGQHPNIITLKDVYDDGKYVYVVTELMKGGELlDKILRQK-------------- 515
Cdd:cd05045   34 AVKML-KENASSSELRDLLsefnlLKQVNHPHVIKLYGACSQDGPLLLIVEYAKYGSL-RSFLRESrkvgpsylgsdgnr 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 516 -----FFSEREASAV------LFTITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRAENGLLM-- 582
Cdd:cd05045  112 nssylDNPDERALTMgdlisfAWQISRGMQYLAEMKLVHRDLAARNVLVAEG----RKMKISDFGLSRDVYEEDSYVKrs 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 583 ---TPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPEEILARIGSG 642
Cdd:cd05045  188 kgrIP---VKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY---PGIAPERLFNLLKTG 245
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
478-624 1.11e-07

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: 53.86  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 478 QHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASA-----------------VLFTITKTVEYLHAQG 540
Cdd:cd05090   65 HHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSPHSDVGCSSdedgtvkssldhgdflhIAIQIAAGMEYLSSHF 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 541 VVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLLMTP--CYTANFVAPEVLKRQGYDAACDIWSLGVLLYTML 618
Cdd:cd05090  145 FVHKDLAARNILV----GEQLHVKISDLGLSREIYSSDYYRVQNksLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIF 220

                 ....*..
gi 768032625 619 T-GYTPF 624
Cdd:cd05090  221 SfGLQPY 227
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
437-694 2.24e-07

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 53.00  E-value: 2.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 437 GSYSVCKRCIHKATNMEFAVK-------IIDKSKRDPTEEIEILLRyGQHPNIITLKDVYDDGKYVYVVTELMKGGELlD 509
Cdd:cd14026    8 GAFGTVSRARHADWRVTVAIKclkldspVGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGIVTEYMTNGSL-N 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 510 KILRQKffSEREASA------VLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESgnpeSIRICDFGFAK-------QL 574
Cdd:cd14026   86 ELLHEK--DIYPDVAwplrlrILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEF----HVKIADFGLSKwrqlsisQS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 575 RAENGLLMTPcyTANFVAPEVL---KRQGYDAACDIWSLGVLLYTMLTGYTPFANGPDdtPEEILarigsgkFSLSGGYW 651
Cdd:cd14026  160 RSSKSAPEGG--TIIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSRKIPFEEVTN--PLQIM-------YSVSQGHR 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 768032625 652 NSVSDTAkdlvskmLHVDPHQRLTAALVLRHPWIVHWDQLPQY 694
Cdd:cd14026  229 PDTGEDS-------LPVDIPHRATLINLIESGWAQNPDERPSF 264
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
461-624 2.91e-07

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: 52.76  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 461 KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASA---------------- 524
Cdd:cd05048   50 KTQQDFRREAELMSDL-QHPNIVCLLGVCTKEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSdddgtassldqsdflh 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 525 VLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAEN-----GLLMTPcytANFVAPEVLKRQ 599
Cdd:cd05048  129 IAIQIAAGMEYLSSHHYVHRDLAARNCL-VGDGLT---VKISDFGLSRDIYSSDyyrvqSKSLLP---VRWMPPEAILYG 201
                        170       180
                 ....*....|....*....|....*.
gi 768032625 600 GYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05048  202 KFTTESDVWSFGVVLWEIFSyGLQPY 227
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
478-642 3.83e-07

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 52.38  E-value: 3.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 478 QHPNIITLKDVYDDgKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYvd 555
Cdd:cd05071   62 RHEKLVQLYAVVSE-EPIYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAaqIASGMAYVERMNYVHRDLRAANILV-- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 556 esGNPESIRICDFGFAKQLR-AENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFangPDDTPE 633
Cdd:cd05071  139 --GENLVCKVADFGLARLIEdNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPY---PGMVNR 213

                 ....*....
gi 768032625 634 EILARIGSG 642
Cdd:cd05071  214 EVLDQVERG 222
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
430-635 4.33e-07

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 52.32  E-value: 4.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 430 VKEDIGVGSY-----SVCKRCIHKATNMEFAVKIID----KSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTE 500
Cdd:cd05094    9 LKRELGEGAFgkvflAECYNLSPTKDKMLVAVKTLKdptlAARKDFQREAELLTNL-QHDHIVKFYGVCGDGDPLIMVFE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELlDKILR--------------QKFFSEREASAVLFTITKTVE---YLHAQGVVHRDLKPSNILYvdesGNPESI 563
Cdd:cd05094   88 YMKHGDL-NKFLRahgpdamilvdgqpRQAKGELGLSQMLHIATQIASgmvYLASQHFVHRDLATRNCLV----GANLLV 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 768032625 564 RICDFGFAKQLRAEN-----GLLMTPCytaNFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTP-FANGPDDTPEEI 635
Cdd:cd05094  163 KIGDFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPwFQLSNTEVIECI 238
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
455-624 5.53e-07

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: 51.94  E-value: 5.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-DKSKRDPTEEI--EILLRYG-QHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREAS------- 523
Cdd:cd05091   40 AIKTLkDKAEGPLREEFrhEAMLRSRlQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLVMRSPHSDVGSTdddktvk 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 ---------AVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAEN--GLLMTPCYTANFVA 592
Cdd:cd05091  120 stlepadflHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKL----NVKISDLGLFREVYAADyyKLMGNSLLPIRWMS 195
                        170       180       190
                 ....*....|....*....|....*....|...
gi 768032625 593 PEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd05091  196 PEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPY 228
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
455-638 5.81e-07

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: 51.99  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIDKSKrDPTEEIE-----ILLRYGQHPNIITLKDVYDDgKYVYVVTELMKGGELLDKILRQKffsEREASAVLFT- 528
Cdd:cd05110   40 AIKILNETT-GPKANVEfmdeaLIMASMDHPHLVRLLGVCLS-PTIQLVTQLMPHGCLLDYVHEHK---DNIGSQLLLNw 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 ---ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAENGLlmtpcYTAN-------FVAPEVLKR 598
Cdd:cd05110  115 cvqIAKGMMYLEERRLVHRDLAARNVLV----KSPNHVKITDFGLARLLEGDEKE-----YNADggkmpikWMALECIHY 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 768032625 599 QGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDTPEEILAR 638
Cdd:cd05110  186 RKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLLEK 226
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
455-619 7.72e-07

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: 51.57  E-value: 7.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGEL------------LDKILRQKFF 517
Cdd:cd05051   50 AVKMLrpdasKNAREDFLKEVKIMSQL-KDPNIVRLLGVCTRDEPLCMIVEYMENGDLnqflqkheaetqGASATNSKTL 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SereASAVLFT---ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAEN-----GLLMTPCytaN 589
Cdd:cd05051  129 S---YGTLLYMatqIASGMKYLESLNFVHRDLATRNCLV----GPNYTIKIADFGMSRNLYSGDyyrieGRAVLPI---R 198
                        170       180       190
                 ....*....|....*....|....*....|
gi 768032625 590 FVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05051  199 WMAWESILLGKFTTKSDVWAFGVTLWEILT 228
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
432-617 8.88e-07

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: 51.29  E-value: 8.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSvckrCIHKAT--NMEFAVKIID-KSKRDPTEEIEI----LLRygqHPNIITL----KDVYDDGKYVYVVTE 500
Cdd:cd13998    1 EVIGKGRFG----EVWKASlkNEPVAVKIFSsRDKQSWFREKEIyrtpMLK---HENILQFiaadERDTALRTELWLVTA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 501 LMKGGELLDkILRQKFFSEREASAVLFTITKTVEYLHAQ---------GVVHRDLKPSNILyVDESGnpeSIRICDFGFA 571
Cdd:cd13998   74 FHPNGSL*D-YLSLHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNIL-VKNDG---TCCIADFGLA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 572 kqLRAENGLLMTP------CYTANFVAPEVLKR----QGYDA--ACDIWSLGVLLYTM 617
Cdd:cd13998  149 --VRLSPSTGEEDnanngqVGTKRYMAPEVLEGainlRDFESfkRVDIYAMGLVLWEM 204
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
433-619 1.51e-06

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 50.42  E-value: 1.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 433 DIGVGSYS-----VCKRCIHKATNMEFAVKIIDKSK--RDPTE---EIEILLRYGQHpNIITLKDVYDDGKYVYVVTELM 502
Cdd:cd05062   13 ELGQGSFGmvyegIAKGVVKDEPETRVAIKTVNEAAsmRERIEflnEASVMKEFNCH-HVVRLLGVVSQGQPTLVIMELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 503 KGGELLDKILRQKFFSEREASAVLFTITKTVE----------YLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAK 572
Cdd:cd05062   92 TRGDLKSYLRSLRPEMENNPVQAPPSLKKMIQmageiadgmaYLNANKFVHRDLAARNCMVAEDF----TVKIGDFGMTR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 768032625 573 QL-------RAENGLLmtpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05062  168 DIyetdyyrKGGKGLL-----PVRWMSPESLKDGVFTTYSDVWSFGVVLWEIAT 216
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
67-310 2.26e-06

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 49.93  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625  67 QFELLKVLGQGSFGKVF-LVKKISGSdarqLYAMKVLKKATLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAFQ 138
Cdd:cd14139    1 EFLELEKIGVGEFGSVYkCIKRLDGC----VYAIKRSMRPFAGSSN------EQLALHEVyahavlgHHPHVVRYYSAWA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 139 TEGKLYLILDFLRGGDLFTRLSKEV----MFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEeghiKLTDFGL 214
Cdd:cd14139   71 EDDHMIIQNEYCNGGSLQDAISENTksgnHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFICH----KMQSSSG 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 215 SKESIDHEKKAYSFCGTV----------------------EYMAPEVVNRR-GHTQSADWWSFGvLMFEMLTGT--LPFQ 269
Cdd:cd14139  147 VGEEVSNEEDEFLSANVVykigdlghvtsinkpqveegdsRFLANEILQEDyRHLPKADIFALG-LTVALAAGAepLPTN 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 768032625 270 GKDRKEtmtmILKAKL-GMPQFLSPEAQSLLRMLFKRNPANR 310
Cdd:cd14139  226 GAAWHH----IRKGNFpDVPQELPESFSSLLKNMIQPDPEQR 263
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
460-619 2.31e-06

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 50.04  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 460 DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELldkilrQKFFSEREASAVLFT----------- 528
Cdd:cd05093   48 DNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFEYMKHGDL------NKFLRAHGPDAVLMAegnrpaeltqs 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 529 --------ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRAEN-----GLLMTPCytaNFVAPEV 595
Cdd:cd05093  121 qmlhiaqqIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIGDFGMSRDVYSTDyyrvgGHTMLPI---RWMPPES 193
                        170       180
                 ....*....|....*....|....
gi 768032625 596 LKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05093  194 IMYRKFTTESDVWSLGVVLWEIFT 217
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
469-647 2.73e-06

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: 49.77  E-value: 2.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 469 EIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGELLDKILRQKFFSEREAS---------AVLFTITKTVEYLHAQ 539
Cdd:cd05046   58 ELDMFRKL-SHKNVVRLLGLCREAEPHYMILEYTDLGDLKQFLRATKSKDEKLKPpplstkqkvALCTQIALGMDHLSNA 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 540 GVVHRDLKPSN-ILYVDESGNPESIRICDFGFAKQLRAENGLLMTpcytANFVAPEVLKRQGYDAACDIWSLGVLLYTML 618
Cdd:cd05046  137 RFVHRDLAARNcLVSSQREVKVSLLSLSKDVYNSEYYKLRNALIP----LRWLAPEAVQEDDFSTKSDVWSFGVLMWEVF 212
                        170       180       190
                 ....*....|....*....|....*....|
gi 768032625 619 T-GYTPFANGPDdtpEEILARIGSGKFSLS 647
Cdd:cd05046  213 TqGELPFYGLSD---EEVLNRLQAGKLELP 239
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
450-624 1.06e-05

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


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 48.01  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 450 TNMEFAVKIIdKSKRDPTEEIEILLRYG------QHPNIITLKDV---YDDGKYV--YVVTELMKGGELLDKILRQ---- 514
Cdd:cd14204   34 TNHKVAVKTM-KLDNFSQREIEEFLSEAacmkdfNHPNVIRLLGVcleVGSQRIPkpMVILPFMKYGDLHSFLLRSrlgs 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 515 --KFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRA-----ENGLLMTPcyt 587
Cdd:cd14204  113 gpQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDM----TVCVADFGLSKKIYSgdyyrQGRIAKMP--- 185
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 768032625 588 ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF 624
Cdd:cd14204  186 VKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPY 223
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
479-624 2.12e-05

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: 46.92  E-value: 2.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 479 HPNI-----ITLKDVYDDG-KYVYVVTELMKGGELLDKILRQK------FFSEREASAVLFTITKTVEYLHAQGVVHRDL 546
Cdd:cd05075   60 HPNVmrligVCLQNTESEGyPSPVVILPFMKHGDLHSFLLYSRlgdcpvYLPTQMLVKFMTDIASGMEYLSSKNFIHRDL 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 547 KPSNILyVDESGNpesIRICDFGFAKQLRaeNG-------LLMTPcytANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT 619
Cdd:cd05075  140 AARNCM-LNENMN---VCVADFGLSKKIY--NGdyyrqgrISKMP---VKWIAIESLADRVYTTKSDVWSFGVTMWEIAT 210

                 ....*.
gi 768032625 620 -GYTPF 624
Cdd:cd05075  211 rGQTPY 216
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
423-625 2.33e-05

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 46.83  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 423 QFTDGyevkEDIGVGSYSVCKRCIHKATNMEF---AVKIIdKSKRDPTEEIEILLRYG------QHPNIITLKDVYDDGK 493
Cdd:cd05074   10 QFTLG----RMLGKGEFGSVREAQLKSEDGSFqkvAVKML-KADIFSSSDIEEFLREAacmkefDHPNVIKLIGVSLRSR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 494 ------YVYVVTELMKGGELLDKILRQKF----FSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILyVDESgnpE 561
Cdd:cd05074   85 akgrlpIPMVILPFMKHGDLHTFLLMSRIgeepFTLPLQTLVRFMidIASGMEYLSSKNFIHRDLAARNCM-LNEN---M 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 768032625 562 SIRICDFGFAKQLRAENgLLMTPCYT---ANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFA 625
Cdd:cd05074  161 TVCVADFGLSKKIYSGD-YYRQGCASklpVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYA 227
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
432-625 3.58e-05

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: 46.33  E-value: 3.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 432 EDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEIL-----LRYGQHPNIITLKDVYDDGkyVYVVTELMKGGE 506
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLeeakkMEMAKFRHILPVYGICSEP--VGLVMEYMETGS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 507 LlDKILRQKFFSEREASAVLFTITKTVEYLHAQG--VVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLM-- 582
Cdd:cd14025   80 L-EKLLASEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHY----HVKISDFGLAKWNGLSHSHDLsr 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 768032625 583 -TPCYTANFVAPEVLKRQG--YDAACDIWSLGVLLYTMLTGYTPFA 625
Cdd:cd14025  155 dGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFA 200
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
455-618 9.98e-05

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: 44.96  E-value: 9.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKIIDKSKRDPTE-EIEI----LLRygqHPNIITL--KDVYDDGKY--VYVVTELMKGGELLDKILRQKFfSEREASAV 525
Cdd:cd14056   22 AVKIFSSRDEDSWFrETEIyqtvMLR---HENILGFiaADIKSTGSWtqLWLITEYHEHGSLYDYLQRNTL-DTEEALRL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 526 LFTITKTVEYLHAQ--------GVVHRDLKPSNILYvdesGNPESIRICDFGFA-KQLRAENGLLMTP---CYTANFVAP 593
Cdd:cd14056   98 AYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILV----KRDGTCCIADLGLAvRYDSDTNTIDIPPnprVGTKRYMAP 173
                        170       180       190
                 ....*....|....*....|....*....|..
gi 768032625 594 EVLKRQ-------GYDAAcDIWSLGVLLYTML 618
Cdd:cd14056  174 EVLDDSinpksfeSFKMA-DIYSFGLVLWEIA 204
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
450-625 3.48e-04

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 43.29  E-value: 3.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 450 TNMEFAVKIIdKSKRDPTEEIEILLRYG------QHPNIITLKDV----YDDGKYV--YVVTELMKGGELldkilRQKFF 517
Cdd:cd05035   26 SQLKVAVKTM-KVDIHTYSEIEEFLSEAacmkdfDHPNVMRLIGVcftaSDLNKPPspMVILPFMKHGDL-----HSYLL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 518 SEREASA---------VLFT--ITKTVEYLHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGLLMTPC- 585
Cdd:cd05035  100 YSRLGGLpeklplqtlLKFMvdIAKGMEYLSNRNFIHRDLAARNCMLDENM----TVCVADFGLSRKIYSGDYYRQGRIs 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 768032625 586 -YTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPFA 625
Cdd:cd05035  176 kMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYP 217
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
455-635 6.16e-04

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: 42.51  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 455 AVKII-----DKSKRDPTEEIEILLRYgQHPNIITLKDVYDDGKYVYVVTELMKGGElLDKILR------QKFFSEREAS 523
Cdd:cd05050   39 AVKMLkeeasADMQADFQREAALMAEF-DHPNIVKLLGVCAVGKPMCLLFEYMAYGD-LNEFLRhrspraQCSLSHSTSS 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 768032625 524 AVLFT-----------------ITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICDFGFAKQLRA-------ENG 579
Cdd:cd05050  117 ARKCGlnplplscteqlciakqVAAGMAYLSERKFVHRDLATRNCLV----GENMVVKIADFGLSRNIYSadyykasEND 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 768032625 580 LLmtpcyTANFVAPEVLKRQGYDAACDIWSLGVLLYTMLT-GYTPF-----------------ANGPDDTPEEI 635
Cdd:cd05050  193 AI-----PIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYygmaheeviyyvrdgnvLSCPDNCPLEL 261
 
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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