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Conserved domains on  [gi|1034674014|ref|XP_016884912|]
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ribosomal protein S6 kinase alpha-6 isoform X1 [Homo sapiens]

Protein Classification

protein kinase family protein; Byr1/STE7 family mitogen-activated protein kinase kinase( domain architecture ID 10145004)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase| Byr1/STE7 family mitogen-activated protein kinase kinase (MAP2K) is a dual-specificity protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates; MAP2Ks phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals

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; ...
94-408 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: 713.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 253
Cdd:cd05582    81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 254 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd05582   161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 334 GS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFV 408
Cdd:cd05582   241 GAgpDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV 317
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
438-732 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: 650.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLL 597
Cdd:cd14177    81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLRGENGLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd14177   161 TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALT 732
Cdd:cd14177   241 SHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAPHLVKGAMAATYSALN 295
 
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; ...
94-408 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: 713.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 253
Cdd:cd05582    81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 254 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd05582   161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 334 GS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFV 408
Cdd:cd05582   241 GAgpDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV 317
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
438-732 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: 650.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLL 597
Cdd:cd14177    81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLRGENGLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd14177   161 TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALT 732
Cdd:cd14177   241 SHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAPHLVKGAMAATYSALN 295
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
90-347 1.58e-101

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 312.93  E-value: 1.58e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014   90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDK---KTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKAYS 249
Cdd:smart00220  77 EYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD-RNETMNMILKAKLGMPQF---LSAEAQSLLRMLF 325
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLL 235
                          250       260
                   ....*....|....*....|..
gi 1034674014  326 KRNPANRLgseGVEEIKRHLFF 347
Cdd:smart00220 236 VKDPEKRL---TAEEALQHPFF 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
443-700 3.21e-94

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.67  E-value: 3.21e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerilrEIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRgENGLLL 597
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG----HVKLADFGLARQLD-PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpNDTPEEILLRIGNGKFSLSGGNWdNISDGAKDLL 677
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 1034674014  678 SHMLHMDPHQRYTAEQILKHSWI 700
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
82-405 1.51e-89

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 284.40  E-value: 1.51e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  82 YEKADPAQ-----FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKAS-LKVRDRVRTKMERDILVEVNHPFIVKL 155
Cdd:PTZ00263    7 FTKPDTSSwklsdFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:PTZ00263   84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 236 LSKESVDqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSA 315
Cdd:PTZ00263  164 FAKKVPD---RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 316 EAQSLLRMLFKRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFD--PEftakTPKDsPG 391
Cdd:PTZ00263  241 RARDLVKGLLQTDHTKRLGTlkGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkyPD----SPVD-RL 315
                         330
                  ....*....|....
gi 1034674014 392 LPASANAHQLFKGF 405
Cdd:PTZ00263  316 PPLTAAQQAEFAGF 329
Pkinase pfam00069
Protein kinase domain;
443-700 7.33e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 222.89  E-value: 7.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdknilrEIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYlhcqgvvhrdlkpsnilymdesasadsiricdfgfakqlrgeNGLL 596
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES------------------------------------------GSSL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSlsggNWDNISDGAKDL 676
Cdd:pfam00069 118 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPE----LPSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:pfam00069 194 LKKLLKKDPSKRLTATQALQHPWF 217
Pkinase pfam00069
Protein kinase domain;
90-347 1.83e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 208.64  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHlhqlgivyrdlkpenilldeighikltdfglskesvdqEKKAYS 249
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES--------------------------------------GSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFK 326
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|.
gi 1034674014 327 RNPANRLgseGVEEIKRHLFF 347
Cdd:pfam00069 200 KDPSKRL---TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
90-345 3.26e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 216.80  E-value: 3.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLKKASLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARD---LRLGRPVALKVLRPELAAdPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-KKA 247
Cdd:COG0515    86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAE-----AQSLLR 322
Cdd:COG0515   166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDlppalDAIVLR 245
                         250       260
                  ....*....|....*....|...
gi 1034674014 323 MLFKrNPANRLGSegVEEIKRHL 345
Cdd:COG0515   246 ALAK-DPEERYQS--AAELAAAL 265
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
443-696 5.94e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 174.05  E-value: 5.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII-DKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEArerfrrEARALARL-NHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGE--- 592
Cdd:COG0515    88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL----TPDGRVKLIDFGIARALGGAtlt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 --NGLLLTPCYTanfvAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:COG0515   164 qtGTVVGTPGYM----APEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---DGDSPAELLRAHLREPPPPPSELRPDLP 236
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 671 DGAKDLLSHMLHMDPHQRY-TAEQILK 696
Cdd:COG0515   237 PALDAIVLRALAKDPEERYqSAAELAA 263
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
443-688 5.93e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 141.49  E-value: 5.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-------RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkmkqvQHVAQEKSILMEL-SHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENgl 595
Cdd:PTZ00263   99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLL-LDNKGH---VKVTDFGFAKKVPDRT-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 lLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggNWdnISDGAKD 675
Cdd:PTZ00263  173 -FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFF---DDTPFRIYEKILAGRLKFP--NW--FDGRARD 244
                         250
                  ....*....|...
gi 1034674014 676 LLSHMLHMDPHQR 688
Cdd:PTZ00263  245 LVKGLLQTDHTKR 257
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
195-292 1.84e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 195 YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG----LSKESVDQEKkaySFCGTVEYMAPE-----VVNRR 265
Cdd:NF033483  112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTTMTQTN---SVLGTVHYLSPEqarggTVDAR 188
                          90       100
                  ....*....|....*....|....*..
gi 1034674014 266 ghsqsADWWSYGVLMFEMLTGTLPFQG 292
Cdd:NF033483  189 -----SDIYSLGIVLYEMLTGRPPFDG 210
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
494-652 3.57e-14

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 75.99  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESA 573
Cdd:NF033483   66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 574 sadsIRICDFGFAKQLRGE-----NGLLltpcYTANFVAPEvlmqQ---GY-DAACDIWSLGVLFYTMLAGYTPFaNGpn 644
Cdd:NF033483  146 ----VKVTDFGIARALSSTtmtqtNSVL----GTVHYLSPE----QargGTvDARSDIYSLGIVLYEMLTGRPPF-DG-- 210

                  ....*...
gi 1034674014 645 DTPEEILL 652
Cdd:NF033483  211 DSPVSVAY 218
 
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; ...
94-408 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: 713.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 253
Cdd:cd05582    81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 254 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd05582   161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 334 GS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFV 408
Cdd:cd05582   241 GAgpDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV 317
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
438-732 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: 650.15  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLL 597
Cdd:cd14177    81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLRGENGLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd14177   161 TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALT 732
Cdd:cd14177   241 SHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAPHLVKGAMAATYSALN 295
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
443-732 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: 611.95  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLLTPCYT 602
Cdd:cd14091    82 LDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFGFAKQLRAENGLLMTPCYT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 603 ANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLH 682
Cdd:cd14091   162 ANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKMLH 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034674014 683 MDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALT 732
Cdd:cd14091   242 VDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVKGAVAATFRAIN 291
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
431-762 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: 578.13  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 431 QINGNAAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYV 510
Cdd:cd14176     9 QLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKDVYDDGKYV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLR 590
Cdd:cd14176    89 YVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLR 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:cd14176   169 AENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLSGGYWNSVS 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHVVKGAMVATYSALtHKTFQPVLEPVAASSLAQ 750
Cdd:cd14176   249 DTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSAL-NRNQSPVLEPVGRSTLAQ 327
                         330
                  ....*....|..
gi 1034674014 751 RRSMKKRTSTGL 762
Cdd:cd14176   328 RRGIKKITSTAL 339
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
439-731 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: 552.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14178     1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLLT 598
Cdd:cd14178    81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPESIRICDFGFAKQLRAENGLLMT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd14178   161 PCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDIVS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVsHVVKGAMVATYSAL 731
Cdd:cd14178   241 KMLHVDPHQRLTAPQVLRHPWIVNREYLSQNQLSRQDV-HLVKGAMAATYFAL 292
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
441-731 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: 550.78  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLLLTPC 600
Cdd:cd14175    81 ELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPESLRICDFGFAKQLRAENGLLMTPC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd14175   161 YTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKM 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 681 LHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVsHVVKGAMVATYSAL 731
Cdd:cd14175   241 LHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQDV-QLVKGAMAATYSAL 290
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
93-409 3.36e-165

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: 479.59  E-value: 3.36e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLkVR---DRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05584     1 LKVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASI-VRnqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd05584    80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNP 329
Cdd:cd05584   160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 330 ANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSP-GLPASANAHQLFKGFS 406
Cdd:cd05584   240 SSRLGSgpGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVDSPdDSTLSESANQVFQGFT 319

                  ...
gi 1034674014 407 FVA 409
Cdd:cd05584   320 YVA 322
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
96-347 4.90e-144

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: 422.31  E-value: 4.90e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd05123     1 LGKGSFGKVLLVRKK---DTGKLYAMKVLRKKEIIKRKEVeHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTV 254
Cdd:cd05123    78 GELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 255 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLG 334
Cdd:cd05123   158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLG 237
                         250
                  ....*....|...
gi 1034674014 335 SEGVEEIKRHLFF 347
Cdd:cd05123   238 SGGAEEIKAHPFF 250
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
90-409 5.51e-124

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: 374.26  E-value: 5.51e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLY 166
Cdd:cd05614     2 FELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALvqKAKTVEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK- 245
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKe 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPF----QGKDRNETMNMILKAKLGMPQFLSAEAQSL 320
Cdd:cd05614   162 RTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARDL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 321 LRMLFKRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSP-GLPASAN 397
Cdd:cd05614   242 LQKLLCKDPKKRLGAgpQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPaGTPPSGA 321
                         330
                  ....*....|..
gi 1034674014 398 ahQLFKGFSFVA 409
Cdd:cd05614   322 --RVFQGYSFIA 331
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
94-408 6.67e-121

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: 365.38  E-value: 6.67e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVR-TKMERDILVEVN-HPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05570     1 KVLGKGSFGKVMLAERKK---TDELYAIKVLKKEVIIEDDDVEcTMTEKRVLALANrHPFLTGLHACFQTEDRLYFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05570    78 VNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05570   158 GTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANA--HQLFKGFSF 407
Cdd:cd05570   238 RLGCgpKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDSDLLTNidQEEFRGFSY 317

                  .
gi 1034674014 408 V 408
Cdd:cd05570   318 I 318
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
95-350 6.18e-118

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: 355.93  E-value: 6.18e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05583     1 VLGTGAYGKVFLVRKVGGHDAGKLYAMKVLKKATIvqKAKTAEHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV-DQEKKAYSF 250
Cdd:cd05583    81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpGENDRAYSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPFQGKD-RN---ETMNMILKAKLGMPQFLSAEAQSLLRML 324
Cdd:cd05583   161 CGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTVDGeRNsqsEISKRILKSHPPIPKTFSAEAKDFILKL 240
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 325 FKRNPANRLGS--EGVEEIKRHLFFANI 350
Cdd:cd05583   241 LEKDPKKRLGAgpRGAHEIKEHPFFKGL 268
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
442-699 1.72e-114

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: 346.77  E-value: 1.72e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEdeemlrREIEILKRL-DHPNIVKLYEVFEDDKNLYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQLrGENGL 595
Cdd:cd05117    80 LCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP-IKIIDFGLAKIF-EEGEK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKD 675
Cdd:cd05117   158 LKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFY---GETEQELFEKILKGKYSFDSPEWKNVSEEAKD 234
                         250       260
                  ....*....|....*....|....
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd05117   235 LIKRLLVVDPKKRLTAAEALNHPW 258
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
94-408 1.72e-114

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: 349.31  E-value: 1.72e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVE-VNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05575     1 KVIGKGSFGKVLLARHK---AEGKLYAVKVLQKKAILKRNEVKHIMaERNVLLKnVKHPFLVGLHYSFQTKDKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05575    78 VNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05575   158 GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLGS-EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQL--------F 402
Cdd:cd05575   238 RLGSgNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVPASVGKSADSVAVSAsvqeadnaF 317

                  ....*.
gi 1034674014 403 KGFSFV 408
Cdd:cd05575   318 DGFSYV 323
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
90-366 7.26e-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: 338.51  E-value: 7.26e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLY 166
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIvqKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV-DQEK 245
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLlDENE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVN--RRGHSQSADWWSYGVLMFEMLTGTLPF----QGKDRNETMNMILKAKLGMPQFLSAEAQS 319
Cdd:cd05613   162 RAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKD 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 320 LLRMLFKRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05613   242 IIQRLLMKDPKKRLGCgpNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
94-409 3.67e-110

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: 337.79  E-value: 3.67e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd05571     1 KVLGKGTFGKVILCREKA---TGELYAIKILKKEVIIAKDEVaHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 252
Cdd:cd05571    78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05571   158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 333 LGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKT-----PKDSPGLPASANAHQLFKGF 405
Cdd:cd05571   238 LGGgpRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESveltpPDRGDLLGLEEEERPHFEQF 317

                  ....
gi 1034674014 406 SFVA 409
Cdd:cd05571   318 SYSA 321
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
89-378 4.69e-110

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: 336.47  E-value: 4.69e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKAS-LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05580     2 DFEFLKTLGTGSFGRVRLVKHK---DSGKYYALKILKKAKiIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDqekKA 247
Cdd:cd05580    79 VMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD---RT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd05580   156 YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 328 NPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFD 378
Cdd:cd05580   236 DLTKRLGNlkNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
89-407 8.68e-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: 325.01  E-value: 8.68e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05573     2 DFEVIKVIGRGAFGEVWLVRDK---DTGQVYAMKILRKSDMLKREQIAhVRAERDILADADSPWIVRLHYAFQDEDHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 238
Cdd:cd05573    79 VMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTkmnksgdre 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 -------ESVDQEKK-------------AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET 298
Cdd:cd05573   159 sylndsvNTLFQDNVlarrrphkqrrvrAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 299 MNMIL--KAKLGMP--QFLSAEAQSLLRMLFKRnPANRLGSegVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDDT 374
Cdd:cd05573   239 YSKIMnwKESLVFPddPDVSPEAIDLIRRLLCD-PEDRLGS--AEEIKAHPFFKGIDWENL--RESPPPFVPELSSPTDT 313
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1034674014 375 --FCFDPEFTAKTPKDSPGLPASANAHQL-FKGFSF 407
Cdd:cd05573   314 snFDDFEDDLLLSEYLSNGSPLLGKGKQLaFVGFTF 349
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
89-373 2.45e-104

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: 322.65  E-value: 2.45e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05574     2 HFKKIKLLGKGDVGRVYLVRLK---GTGKLFAMKVLDKEEMIKRNKVkRVLTEREILATLDHPFLPTLYASFQTSTHLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd05574    79 VMDYCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 -----------------------------KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd05574   159 pvrkslrkgsrrssvksieketfvaepsaRSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 297 ETMNMILKAKLGMPQ--FLSAEAQSLLRMLFKRNPANRLGSE-GVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDD 373
Cdd:cd05574   239 ETFSNILKKELTFPEspPVSSEAKDLIRKLLVKDPSKRLGSKrGASEIKRHPFFRGVNWALI--RNMTPPIIPRPDDPID 316
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
94-408 4.65e-103

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: 319.33  E-value: 4.65e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05592     1 KVLGKGSFGKVMLAELK---GTNQYFAIKALKKDVVLEDDDVECTMiERRVLaLASQHPFLTHLFCTFQTESHLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05592    78 LNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05592   158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLGSEGVE--EIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSP---GLPASANAHQlFKGFS 406
Cdd:cd05592   238 RLGVPECPagDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPvdkKLLASMDQEQ-FKGFS 316

                  ..
gi 1034674014 407 FV 408
Cdd:cd05592   317 FT 318
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
89-393 6.64e-102

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: 316.48  E-value: 6.64e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05599     2 DFEPLKVIGRGAFGEVRLVRKK---DTGHVYAMKKLRKSEMLEKEQVaHVRAERDILAEADNPWVVKLYYSFQDEENLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 247
Cdd:cd05599    79 IMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSAEAQSLLRM 323
Cdd:cd05599   158 YSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIER 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 324 LFKrNPANRLGSEGVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDDTFCFD--------PEFTAKTPKDSPGLP 393
Cdd:cd05599   238 LLC-DAEHRLGANGVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFDefeevdlqIPSSPEAGKDSKELK 312
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
90-347 1.58e-101

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 312.93  E-value: 1.58e-101
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014   90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDK---KTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKAYS 249
Cdd:smart00220  77 EYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD-RNETMNMILKAKLGMPQF---LSAEAQSLLRMLF 325
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDqLLELFKKIGKPKPPFPPPewdISPEAKDLIRKLL 235
                          250       260
                   ....*....|....*....|..
gi 1034674014  326 KRNPANRLgseGVEEIKRHLFF 347
Cdd:smart00220 236 VKDPEKRL---TAEEALQHPFF 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
95-407 2.11e-101

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: 314.89  E-value: 2.11e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd05585     1 VIGKGSFGKVMQVRKK---DTSRIYALKTIRKAHIVSRSEVtHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 253
Cdd:cd05585    78 GGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 254 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd05585   158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRL 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 334 GSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDS--PGLPASANAHQLFKGFSF 407
Cdd:cd05585   238 GYNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSvvDDSHLSESVQQQFEGWSY 313
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
90-409 5.23e-99

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: 309.23  E-value: 5.23e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVN---HPFIVKLHYAFQTEGKL 165
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPT---GELFAIKALKKGDIIARDEVESLMcEKRIFETVNsarHPFLVNLFACFQTPEHV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd05589    78 CFVMEYAAGGDLMMHIHEDV-FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 325
Cdd:cd05589   157 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 326 KRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSP---GLPASANAHQ 400
Cdd:cd05589   237 RKNPERRLGAseRDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPpkePRPLTEEEQA 316

                  ....*....
gi 1034674014 401 LFKGFSFVA 409
Cdd:cd05589   317 LFKDFDYVA 325
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
93-408 7.79e-99

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: 308.55  E-value: 7.79e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVR-TKMERDILVEVNHP-FIVKLHYAFQTEGKLYLILD 170
Cdd:cd05587     1 LMVLGKGSFGKVMLAERK---GTDELYAIKILKKDVIIQDDDVEcTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 250
Cdd:cd05587    78 YVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 330
Cdd:cd05587   158 CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 331 NRLG--SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPA-SANAHQ-LFKGFS 406
Cdd:cd05587   238 KRLGcgPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLvIMNIDQsEFEGFS 317

                  ..
gi 1034674014 407 FV 408
Cdd:cd05587   318 FV 319
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
439-707 8.76e-99

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: 308.07  E-value: 8.76e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYEL---KEDIGVGSYSVCKRCIHATTNMEFAVKIIdkSKR-DPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14092     1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIV--SRRlDTSREVQLLRLCQGHPNIVKLHEVFQDELHTYLVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKqLRGENG 594
Cdd:cd14092    79 ELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDEDDDA-EIKIVDFGFAR-LKPENQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQ----QGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd14092   157 PLKTPCFTLPYAAPEVLKQalstQGYDESCDLWSLGVILYTMLSGQVPFqSPSRNESAAEIMKRIKSGDFSFDGEEWKNV 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLP 707
Cdd:cd14092   237 SSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPS 274
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
94-408 1.94e-97

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: 304.97  E-value: 1.94e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGpdaGQLYAMKVL-KKASLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCD---GKFYAVKVLqKKTILKKKEQNHIMAERNVLLKnLKHPFLVGLHYSFQTSEKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05603    78 VNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05603   158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLGSEG-VEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPG-----LPASANAHQLFKGF 405
Cdd:cd05603   238 RLGAKAdFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSVGrtpdlTASSSSSSSAFLGF 317

                  ...
gi 1034674014 406 SFV 408
Cdd:cd05603   318 SYA 320
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
93-407 1.31e-96

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: 303.04  E-value: 1.31e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVL-KKASLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRD---GKYYAVKVLqKKVILNRKEQKHIMAERNVLLKnVKHPFLVGLHYSFQTTDKLYFVLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 250
Cdd:cd05604    78 FVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 330
Cdd:cd05604   158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 331 NRLG-SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGL---PASANAHQL----- 401
Cdd:cd05604   238 LRLGaKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSVCVssdYSIVNASVLeadda 317

                  ....*.
gi 1034674014 402 FKGFSF 407
Cdd:cd05604   318 FVGFSY 323
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
96-407 2.16e-95

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: 299.87  E-value: 2.16e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVL-KKASLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05586     1 IGKGTFGQVYQVRKK---DTRRIYAMKVLsKKVIVAKKEVAHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05586    78 MSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ-FLSAEAQSLLRMLFKRNP 329
Cdd:cd05586   158 GTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 330 ANRLGS-EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKD--------SPGLPA------ 394
Cdd:cd05586   238 KHRLGAhDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTNASLLNanivpwaqRPGLPGatstpl 317
                         330
                  ....*....|...
gi 1034674014 395 SANAHQLFKGFSF 407
Cdd:cd05586   318 SPSVQANFRGFTF 330
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
94-390 4.74e-95

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: 298.84  E-value: 4.74e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd05595     1 KLLGKGTFGKVILVREKA---TGRYYAMKILRKEVIIAKDEVaHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 252
Cdd:cd05595    78 NGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05595   158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQR 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 333 LGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSP 390
Cdd:cd05595   238 LGGgpSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITP 297
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
89-407 1.45e-94

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: 297.69  E-value: 1.45e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05598     2 MFEKIKTIGVGAFGEVSLVRKK---DTNALYAMKTLRKKDVLKRNQVaHVKAERDILAEADNEWVVKLYYSFQDKENLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL---------SK 238
Cdd:cd05598    79 VMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVdqekkAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQF--LS 314
Cdd:cd05598   159 YYL-----AHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 315 AEAQSLLRMLFkRNPANRLGSEGVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDDTFCFDP---EFTAKTPK--DS 389
Cdd:cd05598   234 PEAKDLILRLC-CDAEDRLGRNGADEIKAHPFFAGIDWEKL--RKQKAPYIPTIRHPTDTSNFDPvdpEKLRSSDEepTT 310
                         330
                  ....*....|....*....
gi 1034674014 390 PGLPASANAHQ-LFKGFSF 407
Cdd:cd05598   311 PNDPDNGKHPEhAFYEFTF 329
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
98-352 2.50e-94

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: 294.89  E-value: 2.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  98 QGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 176
Cdd:cd05579     3 RGAYGRVYLAKKKS---TGDLYAIKVIKKRDMIRKNQVdSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 177 VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK---------------ESV 241
Cdd:cd05579    80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvrrqiklsiqkkSNG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF--LSAEAQS 319
Cdd:cd05579   160 APEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpeVSDEAKD 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 320 LLRMLFKRNPANRLGSEGVEEIKRHLFFANIDW 352
Cdd:cd05579   240 LISKLLTPDPEKRLGAKGIEEIKNHPFFKGIDW 272
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
443-700 3.21e-94

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 293.67  E-value: 3.21e-94
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerilrEIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRgENGLLL 597
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG----HVKLADFGLARQLD-PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpNDTPEEILLRIGNGKFSLSGGNWdNISDGAKDLL 677
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 1034674014  678 SHMLHMDPHQRYTAEQILKHSWI 700
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
85-407 2.73e-93

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: 294.62  E-value: 2.73e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADPAQFELLKVLGQGSFGKVFLVRKKTGPdagQLYAMKVL-KKASLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTE 162
Cdd:cd05602     4 AKPSDFHFLKVIGKGSFGKVLLARHKSDE---KFYAVKVLqKKAILKKKEEKHIMSERNVLLKnVKHPFLVGLHFSFQTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd05602    81 DKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLR 322
Cdd:cd05602   161 PNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 323 MLFKRNPANRLG-SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGL-PASA---- 396
Cdd:cd05602   241 GLLQKDRTKRLGaKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQsPDSIlvta 320
                         330
                  ....*....|....
gi 1034674014 397 ---NAHQLFKGFSF 407
Cdd:cd05602   321 sikEAAEAFLGFSY 334
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
96-354 1.00e-89

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: 1.00e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd05572     1 LGVGGFGRVELVQLKS---KGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYSFCGTV 254
Cdd:cd05572    78 GELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK-KLGSGRKTWTFCGTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 255 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN--ETMNMILKA--KLGMPQFLSAEAQSLLRMLFKRNPA 330
Cdd:cd05572   157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPE 236
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 331 NRLGSE--GVEEIKRHLFFANIDWDK 354
Cdd:cd05572   237 ERLGYLkgGIRDIKKHKWFEGFDWEG 262
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
82-405 1.51e-89

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 284.40  E-value: 1.51e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  82 YEKADPAQ-----FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKAS-LKVRDRVRTKMERDILVEVNHPFIVKL 155
Cdd:PTZ00263    7 FTKPDTSSwklsdFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:PTZ00263   84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 236 LSKESVDqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSA 315
Cdd:PTZ00263  164 FAKKVPD---RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 316 EAQSLLRMLFKRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFD--PEftakTPKDsPG 391
Cdd:PTZ00263  241 RARDLVKGLLQTDHTKRLGTlkGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkyPD----SPVD-RL 315
                         330
                  ....*....|....
gi 1034674014 392 LPASANAHQLFKGF 405
Cdd:PTZ00263  316 PPLTAAQQAEFAGF 329
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
94-409 7.53e-89

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: 282.57  E-value: 7.53e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05590     1 RVLGKGSFGKVMLARLK---ESGRLYAVKVLKKDVILQDDDVECTMtEKRILsLARNHPFLTQLYCCFQTPDRLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05590    78 VNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05590   158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLGS---EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAK----TPKDSPGLPAsanAHQ-LFK 403
Cdd:cd05590   238 RLGSltlGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEdpvlTPIEESLLPM---INQdEFR 314

                  ....*.
gi 1034674014 404 GFSFVA 409
Cdd:cd05590   315 NFSYTA 320
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
90-411 2.46e-88

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: 282.30  E-value: 2.46e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKA---TGRYYAMKILKKEVIVAKDEVaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLH-QLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 247
Cdd:cd05594   104 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd05594   184 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 328 NPANRL--GSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAK----TPKDSPGLPASANAHQL 401
Cdd:cd05594   264 DPKQRLggGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQmitiTPPDQDDSMETVDNERR 343
                         330
                  ....*....|..
gi 1034674014 402 --FKGFSFVATS 411
Cdd:cd05594   344 phFPQFSYSASA 355
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
75-390 7.83e-88

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: 280.81  E-value: 7.83e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  75 THHVKEGYEkadpaQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIV 153
Cdd:cd05593     7 THHKRKTMN-----DFDYLKLLGKGTFGKVILVREKA---SGKYYAMKILKKEVIIAKDEVaHTLTESRVLKNTRHPFLT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 154 KLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd05593    79 SLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL 313
Cdd:cd05593   159 FGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTL 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 314 SAEAQSLLRMLFKRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSP 390
Cdd:cd05593   239 SADAKSLLSGLLIKDPNKRLGGgpDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITP 317
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
89-344 1.34e-87

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: 276.28  E-value: 1.34e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKASLkvrdrVRTKMERDILVEV------NHPFIVKLHYAFQT 161
Cdd:cd14007     1 DFEIGKPLGKGKFGNVYLAReKKSG----FIVALKVISKSQL-----QKSGLEHQLRREIeiqshlRHPNILRLYGYFED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd14007    72 KKRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKaySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLL 321
Cdd:cd14007   152 SNRRK--TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLI 229
                         250       260
                  ....*....|....*....|...
gi 1034674014 322 RMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14007   230 SKLLQKDPSKRL---SLEQVLNH 249
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
94-408 2.67e-87

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: 278.22  E-value: 2.67e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtGPDagQLYAMKVLKKASLKVRDRVRTKM-ERDILV-EVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05591     1 KVLGKGSFGKVMLAERK-GTD--EVYAIKVLKKDVILQDDDVDCTMtEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05591    78 VNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05591   158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLG---SEGVEE-IKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANA--HQLFKGF 405
Cdd:cd05591   238 RLGcvaSQGGEDaIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQinQEEFRGF 317

                  ...
gi 1034674014 406 SFV 408
Cdd:cd05591   318 SFV 320
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
90-408 8.26e-87

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: 277.27  E-value: 8.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtGPDagQLYAMKVLKKASLKVRDRVRTKM--ERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERK-GTD--ELYAVKILKKDVVIQDDDVECTMveKRVLALSGKPPFLTQLHSCFQTMDRLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 247
Cdd:cd05616    79 VMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd05616   159 KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 328 NPANRL--GSEGVEEIKRHLFFANIDWDKLYKREVQPPFKP-ASGKpdDTFCFDPEFTAKTPKDSPglPASANAHQL--- 401
Cdd:cd05616   239 HPGKRLgcGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPkACGR--NAENFDRFFTRHPPVLTP--PDQEVIRNIdqs 314

                  ....*...
gi 1034674014 402 -FKGFSFV 408
Cdd:cd05616   315 eFEGFSFV 322
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
89-347 4.41e-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: 272.59  E-value: 4.41e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05578     1 HFQILRVIGKGSFGKVCIVQKK---DTKKMFAMKYMNKQKCIEKDSVRNVLnELEILQELEHPFLVNLWYSFQDEEDMYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKA 247
Cdd:cd05578    78 VVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK-LTDGTLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDR---NETMNMILKAKLGMPQFLSAEAQSLLRML 324
Cdd:cd05578   157 TSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRtsiEEIRAKFETASVLYPAGWSEEAIDLINKL 236
                         250       260
                  ....*....|....*....|...
gi 1034674014 325 FKRNPANRLGSegVEEIKRHLFF 347
Cdd:cd05578   237 LERDPQKRLGD--LSDLKNHPYF 257
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
90-408 1.03e-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: 269.10  E-value: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05619     7 FVLHKMLGKGSFGKVFLAELKG---TNQFFAIKALKKDVVLMDDDVECTMvEKRVLsLAWEHPFLTHLFCTFQTKENLFF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 247
Cdd:cd05619    84 VMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd05619   164 STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 328 NPANRLGSEGveEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANA--HQLFKGF 405
Cdd:cd05619   244 EPERRLGVRG--DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSmdQNMFRNF 321

                  ...
gi 1034674014 406 SFV 408
Cdd:cd05619   322 SFV 324
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
89-347 1.56e-83

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: 266.77  E-value: 1.56e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05581     2 DFKFGKPLGEGSYSTVVLAKEKE---TGKEYAIKVLDKRHIIKEKKVKYvTIEKEVLSRLAHPGIVKLYYTFQDESKLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 238
Cdd:cd05581    79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdsspe 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 --------ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 310
Cdd:cd05581   159 stkgdadsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 311 QFLSAEAQSLLRMLFKRNPANRLGS---EGVEEIKRHLFF 347
Cdd:cd05581   239 ENFPPDAKDLIQKLLVLDPSKRLGVnenGGYDELKAHPFF 278
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
90-407 1.67e-83

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: 268.83  E-value: 1.67e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKAS-LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05597     3 FEILKVIGRGAFGEVAVVKLK---STEKVYAMKILNKWEmLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVDQEKKA 247
Cdd:cd05597    80 MDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SCLKLREDGTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSF--CGTVEYMAPEVV--NRRGHSQ---SADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMP---QFLSA 315
Cdd:cd05597   159 QSSvaVGTPDYISPEILqaMEDGKGRygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPddeDDVSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 316 EAQSLLRMLFKRnPANRLGSEGVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDDTFCFDPEFTA--KTPKDSPGLP 393
Cdd:cd05597   239 EAKDLIRRLICS-RERRLGQNGIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFDVDDDDlrHTDSLPPPSN 315
                         330
                  ....*....|....*
gi 1034674014 394 ASANAHQL-FKGFSF 407
Cdd:cd05597   316 AAFSGLHLpFVGFTY 330
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
88-380 5.79e-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: 265.84  E-value: 5.79e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKkaslkVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQT 161
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRIS---EHYYALKVMA-----IPEVIRLKQeqhvhnEKRVLKEVSHPFIIRLFWTEHD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd05612    73 QRFLYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLL 321
Cdd:cd05612   153 D---RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLI 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 322 RMLFKRNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFD--PE 380
Cdd:cd05612   230 KKLLVVDRTRRLGNmkNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDdyPE 292
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
443-699 3.46e-82

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: 262.07  E-value: 3.46e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIeekikrEIEIMKLL-NHPNIIKLYEVIETENKIYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDEsasADSIRICDFGFAKQLRGeNGLL 596
Cdd:cd14003    81 ASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL-LDK---NGNLKIIDFGLSNEFRG-GSLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFaNGPNDtpEEILLRIGNGKFSLsggnWDNISDGAKD 675
Cdd:cd14003   156 KTFCGTPAYAAPEVLLGRKYDGpKADVWSLGVILYAMLTGYLPF-DDDND--SKLFRKILKGKYPI----PSHLSPDARD 228
                         250       260
                  ....*....|....*....|....
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14003   229 LIRRMLVVDPSKRITIEEILNHPW 252
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
90-408 1.00e-81

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: 263.79  E-value: 1.00e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKA---TGDIYAMKVLKKSETLAQEEVSFfEEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVDQEKKA 247
Cdd:cd05601    80 MEYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG-SAAKLSSDKTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSF--CGTVEYMAPEV---VNRRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSA 315
Cdd:cd05601   159 TSKmpVGTPDYIAPEVltsMNGGSkgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPEdpKVSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 316 EAQSLLRMLFKrNPANRLGSEGveeIKRHLFFANIDWDKLykREVQPPFKPASGKPDDTFCFDpEFTAKtpKDSPGLPAS 395
Cdd:cd05601   239 SAVDLIKGLLT-DAKERLGYEG---LCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFD-EFEPK--KTRPSYENF 309
                         330
                  ....*....|....*....
gi 1034674014 396 ANAHQL------FKGFSFV 408
Cdd:cd05601   310 NKSKGFsgkdlpFVGFTFT 328
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
90-400 1.56e-81

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: 265.17  E-value: 1.56e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKK---DTGKIYAMKTLLKSEMFKKDQLaHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS----------- 237
Cdd:cd05629    80 MEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsay 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 -------------------------------KESVDQEKK-----AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMF 281
Cdd:cd05629   160 yqkllqgksnknridnrnsvavdsinltmssKDQIATWKKnrrlmAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 282 EMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSAEAQSLLRMLFKrNPANRLGSEGVEEIKRHLFFANIDWDKLyk 357
Cdd:cd05629   240 ECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRRLIT-NAENRLGRGGAHEIKSHPFFRGVDWDTI-- 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 358 REVQPPFKPASGKPDDTFCFDPEFTAKTPkDSPGLPASANAHQ 400
Cdd:cd05629   317 RQIRAPFIPQLKSITDTSYFPTDELEQVP-EAPALKQAAPAQQ 358
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
89-344 2.07e-81

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: 260.14  E-value: 2.07e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARhKLTG----EKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvDQEKKA 247
Cdd:cd14003    77 VMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF-RGGSLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 326
Cdd:cd14003   156 KTFCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLV 235
                         250
                  ....*....|....*...
gi 1034674014 327 RNPANRLgseGVEEIKRH 344
Cdd:cd14003   236 VDPSKRI---TIEEILNH 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
89-333 2.41e-81

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: 260.10  E-value: 2.41e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKT---GEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKEsVDQEK 245
Cdd:cd05117    78 MELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLL 321
Cdd:cd05117   157 KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLI 236
                         250
                  ....*....|..
gi 1034674014 322 RMLFKRNPANRL 333
Cdd:cd05117   237 KRLLVVDPKKRL 248
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
94-408 6.61e-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: 261.42  E-value: 6.61e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM--ERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd05620     1 KVLGKGSFGKVLLAELK---GKGEYFAVKALKKDVVLIDDDVECTMveKRVLALAWENPFLTHLYCTFQTKEHLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd05620    78 LNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd05620   158 GTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 332 RLGSEGveEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDS---PGLPASANaHQLFKGFSFV 408
Cdd:cd05620   238 RLGVVG--NIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSysdKNLIDSMD-QSAFAGFSFI 314
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
89-407 6.98e-81

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: 263.82  E-value: 6.98e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05600    12 DFQILTQVGQGGYGSVFLARKK---DTGEICALKIMKKKVLFKLNEVNhVLTERDILTTTNSPWLVKLLYAFQDPENVYL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK-- 245
Cdd:cd05600    89 AMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKie 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 -----------------------------------KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd05600   169 smkirleevkntafleltakerrniyramrkedqnYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPF 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 291 QGKDRNETMNMIL--KAKLGMPQF--------LSAEAQSLLRMLFKrNPANRLGSegVEEIKRHLFFANIDWDKLYKReV 360
Cdd:cd05600   249 SGSTPNETWANLYhwKKTLQRPVYtdpdlefnLSDEAWDLITKLIT-DPQDRLQS--PEQIKNHPFFKNIDWDRLREG-S 324
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 361 QPPFKPASGKPDDTFCFDpEFTAKTPKDS-------------PGLPASANAHQ-LFKGFSF 407
Cdd:cd05600   325 KPPFIPELESEIDTSYFD-DFNDEADMAKykdvhekqkslegSGKNGGDNGNRsLFVGFTF 384
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
94-408 8.78e-81

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: 261.20  E-value: 8.78e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVR---DRVRTkmERDIL-VEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05588     1 RVIGRGSYAKVLMVELKK---TKRIYAMKVIKKELVNDDediDWVQT--EKHVFeTASNHPFLVGLHSCFQTESRLFFVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd05588    76 EFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ--GKDRNETMN-------MILKAKLGMPQFLSAEAQSL 320
Cdd:cd05588   156 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDivGSSDNPDQNtedylfqVILEKPIRIPRSLSVKAASV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 321 LRMLFKRNPANRLG---SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASAN 397
Cdd:cd05588   236 LKGFLNKNPAERLGchpQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPDDPDVIE 315
                         330
                  ....*....|...
gi 1034674014 398 A--HQLFKGFSFV 408
Cdd:cd05588   316 KidQSEFEGFEYV 328
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
90-410 1.05e-80

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: 261.86  E-value: 1.05e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHP-FIVKLHYAFQTEGKLYL 167
Cdd:cd05615    12 FNFLMVLGKGSFGKVMLAERKG---SDELYAIKILKKDVVIQDDDVECTMvEKRVLALQDKPpFLTQLHSCFQTVDRLYF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 247
Cdd:cd05615    89 VMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd05615   169 RTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTK 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 328 NPANRL--GSEGVEEIKRHLFFANIDWDKLYKREVQPPFKP-ASGKPDDTfcFDPEFTAKTPKDSPglPAS---ANAHQL 401
Cdd:cd05615   249 HPAKRLgcGPEGERDIREHAFFRRIDWDKLENREIQPPFKPkVCGKGAEN--FDKFFTRGQPVLTP--PDQlviANIDQA 324
                         330
                  ....*....|
gi 1034674014 402 -FKGFSFVAT 410
Cdd:cd05615   325 dFEGFSYVNP 334
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
89-378 1.45e-80

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: 259.26  E-value: 1.45e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14209     2 DFDRIKTLGTGSFGRVMLVRHKET---GNYYAMKILDKQKVvKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdqEKKA 247
Cdd:cd14209    79 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV---KGRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd14209   156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 328 NPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFD 378
Cdd:cd14209   236 DLTKRFGNlkNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFD 288
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
439-736 6.83e-80

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: 258.43  E-value: 6.83e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYEL---KEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS-KRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14179     2 FYQHYELdlkDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRmEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQLRGENG 594
Cdd:cd14179    82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE-IKIIDFGFARLKPPDNQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPND----TPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:cd14179   161 PLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctSAEEIMKKIKQGDFSFEGEAWKNVS 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPKRNDVSHvVKGAMVATYSALTHKTF 736
Cdd:cd14179   241 QEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQLSSNPLMTPDILG-SSGASVHTCVKATFHAF 305
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
93-353 6.51e-77

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: 248.93  E-value: 6.51e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVR-TKMERDIL-VEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRS---TGDYFAIKVLKKSDMIAKNQVTnVKAERAIMmIQGESPYVAKLYYSFQSKDYLYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSkESVDQEKKAYSF 250
Cdd:cd05611    78 YLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS-RNGLEKRHNKKF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 326
Cdd:cd05611   157 VGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRLLC 236
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 327 RNPANRLGSEGVEEIKRHLFFANIDWD 353
Cdd:cd05611   237 MDPAKRLGANGYQEIKSHPFFKSINWD 263
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
87-408 2.01e-76

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: 250.76  E-value: 2.01e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKAS-LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd05596    25 AEDFDVIKVIGRGAFGEVQLVRHKS---TKKVYAMKLLSKFEmIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKeVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEK 245
Cdd:cd05596   102 YMVMDYMPGGDLVNLMSN-YDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK-MDKDG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYS--FCGTVEYMAPEVVNRRGH----SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMP--QFLSA 315
Cdd:cd05596   180 LVRSdtAVGTPDYISPEVLKSQGGdgvyGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhKNSLQFPddVEISK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 316 EAQSLLRMlFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPAS 395
Cdd:cd05596   260 DAKSLICA-FLTDREVRLGRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDDIEEDETPEETFPVPKA 338
                         330
                  ....*....|....
gi 1034674014 396 ANAHQL-FKGFSFV 408
Cdd:cd05596   339 FVGNHLpFVGFTYS 352
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
441-699 2.78e-76

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: 246.90  E-value: 2.78e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS----KRDPSE-EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKalkgKEDSLEnEIAVLRKI-KHPNIVQLLDIYESKSHLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMdeSASADS-IRICDFGFAKQlrGENG 594
Cdd:cd14083    82 LVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYY--SPDEDSkIMISDFGLSKM--EDSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgPNDTpeEILLRIGNGKFSLSGGNWDNISDGAK 674
Cdd:cd14083   158 VMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYD-ENDS--KLFAQILKAEYEFDSPYWDDISDSAK 234
                         250       260
                  ....*....|....*....|....*
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14083   235 DFIRHLMEKDPNKRYTCEQALEHPW 259
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
443-699 8.18e-76

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: 245.70  E-value: 8.18e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmienEVAILRRV-KHPNIVQLIEEYDTDTELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRgenGLLL 597
Cdd:cd14095    81 KGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLKLADFGLATEVK---EPLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd14095   158 TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFR-SPDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                         250       260
                  ....*....|....*....|..
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14095   237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
96-366 1.69e-75

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: 245.51  E-value: 1.69e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd05577     1 LGRGGFGEVCACQVK---ATGKMYACKKLDKKRIKKKKGETMALnEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKAYSFCG 252
Cdd:cd05577    78 GDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQ----GKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd05577   157 THGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRqrkeKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 328 NPANRLGSEG--VEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05577   237 DPERRLGCRGgsADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
90-408 2.24e-75

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: 248.01  E-value: 2.24e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPdagQLYAMKVLKKASLKVRDRVR-TKMERDILVEVN-HPFIVKLHYAFQTEGKLYL 167
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKND---QIYAMKVVKKELVHDDEDIDwVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 247
Cdd:cd05617    94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN-------MILKAKLGMPQFLSAEAQSL 320
Cdd:cd05617   174 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNtedylfqVILEKPIRIPRFLSVKASHV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 321 LRMLFKRNPANRLGSE---GVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAK----TPKDSPGLP 393
Cdd:cd05617   254 LKGFLNKDPKERLGCQpqtGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEpvqlTPDDEDVIK 333
                         330
                  ....*....|....*
gi 1034674014 394 ASANAHqlFKGFSFV 408
Cdd:cd05617   334 RIDQSE--FEGFEYI 346
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
439-700 2.26e-75

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: 246.32  E-value: 2.26e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYE--LKED-IGVGSYSVCKRCIHATTNMEFAVKIIdkSKR---DPSEEIEILMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd14180     1 FFQCYEldLEEPaLGEGSFSVCRKCRHRQSGQEYAVKII--SRRmeaNTQREVAALRLCQSHPNIVALHEVLHDQYHTYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKqLRGE 592
Cdd:cd14180    79 VMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDGA-VLKVIDFGFAR-LRPQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGL-LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF----ANGPNDTPEEILLRIGNGKFSLSGGNWD 667
Cdd:cd14180   157 GSRpLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFqskrGKMFHNHAADIMHKIKEGDFSLEGEAWK 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 668 NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14180   237 GVSEEAKDLVRGLLTVDPAKRLKLSELRESDWL 269
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
439-699 2.21e-74

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: 242.26  E-value: 2.21e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------------EIEILMRYGQHPNIITLKDVFDD 506
Cdd:cd14093     1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSEneaeelreatrrEIEILRQVSGHPNIIELHDVFES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 507 GRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA 586
Cdd:cd14093    81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL----NVKISDFGFA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLrGENGLLLTPCYTANFVAPEVLMQQ------GYDAACDIWSLGVLFYTMLAGYTPFANgpndTPEEILLR-IGNGKF 659
Cdd:cd14093   157 TRL-DEGEKLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLLAGCPPFWH----RKQMVMLRnIMEGKY 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 660 SLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14093   232 EFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
89-352 2.80e-74

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: 242.31  E-value: 2.80e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05609     1 DFETIKLISNGAYGAVYLVRHR---ETRQRFAMKKINKQNLILRNQIqQVFVERDILTFAENPFVVSMYCSFETKRHLCM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 238
Cdd:cd05609    78 VMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmslttn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ---ESVDQEKKAYS---FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ- 311
Cdd:cd05609   158 lyeGHIEKDTREFLdkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEg 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 312 --FLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHLFFANIDW 352
Cdd:cd05609   238 ddALPDDAQDLITRLLQQNPLERLGTGGAEEVKQHPFFQDLDW 280
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
441-700 3.17e-74

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: 242.71  E-value: 3.17e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDI-GVGSYSVCKRCIHATTNMEFAVKIIDK----SKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14090     1 DLYKLTGELlGEGAYASVQTCINLYTGKEYAVKIIEKhpghSRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLRGENGL 595
Cdd:cd14090    81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENIL-CESMDKVSPVKICDFDLGSGIKLSSTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 --------LLTPCYTANFVAPEVL-----MQQGYDAACDIWSLGVLFYTMLAGYTPFAN--GPN----------DTPEEI 650
Cdd:cd14090   160 mtpvttpeLLTPVGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGrcGEDcgwdrgeacqDCQELL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034674014 651 LLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14090   240 FHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
95-366 3.63e-74

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: 241.96  E-value: 3.63e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNH----PFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05606     1 IIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGETLALnERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQEKKAYS 249
Cdd:cd05606    78 DLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF--SKKKPHA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPF---QGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 325
Cdd:cd05606   156 SVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 326 KRNPANRLGSE--GVEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05606   236 QRDVSKRLGCLgrGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
90-408 1.63e-71

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: 238.01  E-value: 1.63e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKASLKVRDRVR-TKMERDILVEV-NHPFIVKLHYAFQTEGKLY 166
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRlKKTE----RIYAMKVVKKELVNDDEDIDwVQTEKHVFEQAsNHPFLVGLHSCFQTESRLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd05618    98 FVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ--GKDRNETMN-------MILKAKLGMPQFLSAEA 317
Cdd:cd05618   178 TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDivGSSDNPDQNtedylfqVILEKQIRIPRSLSVKA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 318 QSLLRMLFKRNPANRLG---SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAK----TPKDSP 390
Cdd:cd05618   258 ASVLKSFLNKDPKERLGchpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEpvqlTPDDDD 337
                         330
                  ....*....|....*...
gi 1034674014 391 GLPASANAHqlFKGFSFV 408
Cdd:cd05618   338 IVRKIDQSE--FEGFEYI 353
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
90-407 6.53e-71

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: 236.49  E-value: 6.53e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKK---DTGHIYAMKILRKADMLEKEQVaHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL------------ 236
Cdd:cd05627    81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkkahrtef 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 ------------------SKESVDQEKK-----AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 293
Cdd:cd05627   161 yrnlthnppsdfsfqnmnSKRKAETWKKnrrqlAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 294 DRNETMNMILKAKLGM---PQFLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASgk 370
Cdd:cd05627   241 TPQETYRKVMNWKETLvfpPEVPISEKAKDLILRFCTDAENRIGSNGVEEIKSHPFFEGVDWEHIRERPAAIPIEIKS-- 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1034674014 371 PDDTFCFD--PEFTAKTPKDSPGLPASANAHQLFKGFSF 407
Cdd:cd05627   319 IDDTSNFDdfPESDILQPAPNTTEPDYKSKDWVFLNYTY 357
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
441-714 6.25e-70

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: 231.03  E-value: 6.25e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK--RDPSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPlsRDSSLENEIaVLKRIKHENIVTLEDIYESTTHYYLVMQLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYM--DESAsadSIRICDFGFAKQlrGENGL 595
Cdd:cd14166    83 SGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLtpDENS---KIMITDFGLSKM--EQNGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKD 675
Cdd:cd14166   158 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY---EETESRLFEKIKEGYYEFESPFWDDISESAKD 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWIT-----HRDQLPN--DQPKRN 714
Cdd:cd14166   235 FIRHLLEKNPSKRYTCEKALSHPWIIgntalHRDIYPSvsEQIQKN 280
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
90-366 2.15e-69

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: 229.55  E-value: 2.15e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRD-RVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05605     2 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKRKgEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 246
Cdd:cd05605    79 LTIMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGET 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 322
Cdd:cd05605   158 IRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKEDQEEYSEKFSEEAKSICS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 323 MLFKRNPANRLG--SEGVEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05605   238 QLLQKDPKTRLGcrGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
460-699 2.46e-69

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: 228.71  E-value: 2.46e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 460 CIHATTNMEFAVKII---DKSKRdpseEIEILMRYGQHPNIITLKDVF----DDGRYVYLVTDLMKGGELLDRILK--QK 530
Cdd:cd14089    20 CFHKKTGEKFALKVLrdnPKARR----EVELHWRASGCPHIVRIIDVYentyQGRKCLLVVMECMEGGELFSRIQEraDS 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 531 CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQLRGeNGLLLTPCYTANFVAPEV 610
Cdd:cd14089    96 AFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPNA-ILKLTDFGFAKETTT-KKSLQTPCYTPYYVAPEV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 611 LMQQGYDAACDIWSLGVLFYTMLAGYTPF--ANGPNDTPeEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQR 688
Cdd:cd14089   174 LGPEKYDKSCDMWSLGVIMYILLCGYPPFysNHGLAISP-GMKKRIRNGQYEFPNPEWSNVSEEAKDLIRGLLKTDPSER 252
                         250
                  ....*....|.
gi 1034674014 689 YTAEQILKHSW 699
Cdd:cd14089   253 LTIEEVMNHPW 263
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
73-411 3.22e-68

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: 230.67  E-value: 3.22e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  73 PITHHVKEGYEKADpaQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKK-ASLKVRDRVRTKMERDILVEVNHPF 151
Cdd:cd05624    59 PFTQLVKEMQLHRD--DFEIIKVIGRGAFGEVAVVKMKN---TERIYAMKILNKwEMLKRAETACFREERNVLVNGDCQW 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 152 IVKLHYAFQTEGKLYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIK 230
Cdd:cd05624   134 ITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIR 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFG----LSKESVDQEKKAysfCGTVEYMAPEVVNRR-----GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd05624   214 LADFGsclkMNDDGTVQSSVA---VGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGK 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 302 IL--KAKLGMPQFL---SAEAQSLL-RMLFKRNpaNRLGSEGVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDDTF 375
Cdd:cd05624   291 IMnhEERFQFPSHVtdvSEEAKDLIqRLICSRE--RRLGQNGIEDFKKHAFFEGLNWENI--RNLEAPYIPDVSSPSDTS 366
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 376 CFD-PEFTAKTPKDSPglPAS----ANAHQLFKGFSFVATS 411
Cdd:cd05624   367 NFDvDDDVLRNPEILP--PSShtgfSGLHLPFVGFTYTTES 405
Pkinase pfam00069
Protein kinase domain;
443-700 7.33e-68

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 222.89  E-value: 7.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdknilrEIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYlhcqgvvhrdlkpsnilymdesasadsiricdfgfakqlrgeNGLL 596
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES------------------------------------------GSSL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSlsggNWDNISDGAKDL 676
Cdd:pfam00069 118 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPE----LPSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:pfam00069 194 LKKLLKKDPSKRLTATQALQHPWF 217
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
90-378 1.33e-67

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: 228.00  E-value: 1.33e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKK---DTGHVYAMKILRKADMLEKEQVgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL------------ 236
Cdd:cd05628    80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkahrtef 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 ------------------SKESVDQEKK-----AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 293
Cdd:cd05628   160 yrnlnhslpsdftfqnmnSKRKAETWKRnrrqlAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 294 DRNETMNMILKAKLGM---PQFLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASgk 370
Cdd:cd05628   240 TPQETYKKVMNWKETLifpPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKTNPFFEGVDWEHIRERPAAIPIEIKS-- 317

                  ....*...
gi 1034674014 371 PDDTFCFD 378
Cdd:cd05628   318 IDDTSNFD 325
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
89-332 3.76e-67

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: 222.72  E-value: 3.76e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRK---SDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRL----SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd08215    78 MEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEAQSLLRM 323
Cdd:cd08215   158 DLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNS 237

                  ....*....
gi 1034674014 324 LFKRNPANR 332
Cdd:cd08215   238 MLQKDPEKR 246
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
441-700 1.37e-66

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: 221.44  E-value: 1.37e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKEtsienEIAVLHKI-KHPNIVALDDIYESGGHLYLIMQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY--MDESAsadSIRICDFGFAKqLRGEN 593
Cdd:cd14167    82 LVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYysLDEDS---KIMISDFGLSK-IEGSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgPNDTpeEILLRIGNGKFSLSGGNWDNISDGA 673
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDA--KLFEQILKAEYEFDSPYWDDISDSA 234
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14167   235 KDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
73-412 4.65e-66

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: 224.89  E-value: 4.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  73 PITHHVKEgyEKADPAQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKK-ASLKVRDRVRTKMERDILVEVNHPF 151
Cdd:cd05623    59 PFTSKVKQ--MRLHKEDFEILKVIGRGAFGEVAVVKLK---NADKVFAMKILNKwEMLKRAETACFREERDVLVNGDSQW 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 152 IVKLHYAFQTEGKLYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIK 230
Cdd:cd05623   134 ITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIR 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFG----LSKESVDQEKKAysfCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd05623   214 LADFGsclkLMEDGTVQSSVA---VGTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGK 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 302 IL--KAKLGMPQFL---SAEAQSLLRMLFKRNpANRLGSEGVEEIKRHLFFANIDWDKLykREVQPPFKPASGKPDDTFC 376
Cdd:cd05623   291 IMnhKERFQFPTQVtdvSENAKDLIRRLICSR-EHRLGQNGIEDFKNHPFFVGIDWDNI--RNCEAPYIPEVSSPTDTSN 367
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 377 FDPEftAKTPKDSPGLP-----ASANAHQLFKGFSFVATSI 412
Cdd:cd05623   368 FDVD--DDCLKNCETMPppthtAFSGHHLPFVGFTYTSSCV 406
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
443-705 5.69e-66

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: 220.76  E-value: 5.69e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDkSKRDPSEEIEILMRYG------QHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14086     3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIIN-TKKLSARDHQKLEREAricrllKHPNIVRLHDSISEEGFHYLVFDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQLRGEN--- 593
Cdd:cd14086    82 VTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGA-AVKLADFGLAIEVQGDQqaw 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 -GLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDG 672
Cdd:cd14086   161 fGFAGTPGY----LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFW---DEDQHRLYAQIKAGAYDYPSPEWDTVTPE 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQ 705
Cdd:cd14086   234 AKDLINQMLTVNPAKRITAAEALKHPWICQRDR 266
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
441-699 7.45e-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: 7.45e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhlienEVSILRRV-KHPNIIMLIEEMDTPAELYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGEngl 595
Cdd:cd14184    80 LVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGP--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKD 675
Cdd:cd14184   157 LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF-RSENNLQEDLFDQILLGKLEFPSPYWDNITDSAKE 235
                         250       260
                  ....*....|....*....|....
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14184   236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
89-384 1.43e-65

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: 221.68  E-value: 1.43e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd05610     5 EFVIVKPISRGAFGKVYLGRKK---NNSKLYAVKVVKKADMINKNMVhQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE--- 244
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRElnm 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 ------------KKAYS--------------------------------------FCGTVEYMAPEVVNRRGHSQSADWW 274
Cdd:cd05610   162 mdilttpsmakpKNDYSrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWW 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 275 SYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP---QFLSAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLFFANID 351
Cdd:cd05610   242 ALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKR---AGLKELKQHPLFHGVD 318
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034674014 352 WDKLYKREvqPPFKPASGKPDDTFCFDPEFTAK 384
Cdd:cd05610   319 WENLQNQT--MPFIPQPDDETDTSYFEARNNAQ 349
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
88-391 4.32e-65

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: 221.42  E-value: 4.32e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd05626     1 SMFVKIKTLGIGAFGEVCLACKV---DTHALYAMKTLRKKDVLNRNQVaHVKAERDILAEADNEWVVKLYYSFQDKDNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL---------- 236
Cdd:cd05626    78 FVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthns 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 ------------SKESVD-------------------------QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVL 279
Cdd:cd05626   158 kyyqkgshirqdSMEPSDlwddvsncrcgdrlktleqratkqhQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 280 MFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSAEAQSLLRMLFKrNPANRLGSEGVEEIKRHLFFANIDWDKL 355
Cdd:cd05626   238 LFEMLVGQPPFLAPTPTETQLKVInwENTLHIPPqvKLSPEAVDLITKLCC-SAEERLGRNGADDIKAHPFFSEVDFSSD 316
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1034674014 356 YKRevQP-PFKPASGKPDDTFCFDPEFTAKTPKDSPG 391
Cdd:cd05626   317 IRT--QPaPYVPKISHPMDTSNFDPVEEESPWNDASG 351
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
89-417 1.86e-64

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: 218.39  E-value: 1.86e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEV----NHPFIVKLHYAFQTEGK 164
Cdd:cd05633     6 DFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQE 244
Cdd:cd05633    83 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDF--SK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPF---QGKDRNETMNMILKAKLGMPQFLSAEAQSL 320
Cdd:cd05633   161 KKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 321 LRMLFKRNPANRLGSE--GVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDpeFTAKTPKDSPGLPASANA 398
Cdd:cd05633   241 LEGLLQRDVSKRLGCHgrGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFD--IGSFDEEDTKGIKLLDSD 318
                         330
                  ....*....|....*....
gi 1034674014 399 HQLFKGFSFVatsIAEEYK 417
Cdd:cd05633   319 QELYKNFPLV---ISERWQ 334
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
443-699 2.70e-64

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: 214.81  E-value: 2.70e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI---EILM-RYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMiesEILIiKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGEnglLLT 598
Cdd:cd14185    82 GGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVTGP---IFT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd14185   159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPF-RSPERDQEELFQIIQLGHYEFLPPYWDNISEAAKDLIS 237
                         250       260
                  ....*....|....*....|.
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14185   238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
438-700 3.28e-63

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: 212.64  E-value: 3.28e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK------------RDPSEEIEILMRYgQHPNIITLKDVFD 505
Cdd:cd14084     3 ELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrreinkpRNIETEIEILKKL-SHPCIIKIEDFFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 506 DGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADS--IRICDF 583
Cdd:cd14084    82 AEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLL---SSQEEEclIKITDF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQLrGENGLLLTPCYTANFVAPEVLM---QQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTP--EEILlrigNGK 658
Cdd:cd14084   159 GLSKIL-GETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSlkEQIL----SGK 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 659 FSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14084   234 YTFIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
90-405 7.78e-63

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: 213.37  E-value: 7.78e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEV----NHPFIVKLHYAFQTEGKL 165
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQEK 245
Cdd:cd14223    79 SFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDF--SKK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRR-GHSQSADWWSYGVLMFEMLTGTLPF---QGKDRNETMNMILKAKLGMPQFLSAEAQSLL 321
Cdd:cd14223   157 KPHASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 322 RMLFKRNPANRLG--SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDpeFTAKTPKDSPGLPASANAH 399
Cdd:cd14223   237 EGLLQRDVNRRLGcmGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPPRGEVNAADAFD--IGSFDEEDTKGIKLLESDQ 314

                  ....*.
gi 1034674014 400 QLFKGF 405
Cdd:cd14223   315 ELYRNF 320
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
88-379 1.54e-62

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: 214.53  E-value: 1.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd05625     1 SMFVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVaHVKAERDILAEADNEWVVRLYYSFQDKDNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL---------- 236
Cdd:cd05625    78 FVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthds 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 ---------SKESVD----------------------------QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVL 279
Cdd:cd05625   158 kyyqsgdhlRQDSMDfsnewgdpencrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 280 MFEMLTGTLPFQGKDRNETMNMILKAKLGM---PQF-LSAEAQSLLRMLFkRNPANRLGSEGVEEIKRHLFFANIDWDKL 355
Cdd:cd05625   238 LFEMLVGQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEASDLIIKLC-RGPEDRLGKNGADEIKAHPFFKTIDFSSD 316
                         330       340
                  ....*....|....*....|....
gi 1034674014 356 YkREVQPPFKPASGKPDDTFCFDP 379
Cdd:cd05625   317 L-RQQSAPYIPKITHPTDTSNFDP 339
Pkinase pfam00069
Protein kinase domain;
90-347 1.83e-62

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 208.64  E-value: 1.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHlhqlgivyrdlkpenilldeighikltdfglskesvdqEKKAYS 249
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES--------------------------------------GSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFK 326
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|.
gi 1034674014 327 RNPANRLgseGVEEIKRHLFF 347
Cdd:pfam00069 200 KDPSKRL---TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
90-345 3.26e-62

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 216.80  E-value: 3.26e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLKKASLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARD---LRLGRPVALKVLRPELAAdPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-KKA 247
Cdd:COG0515    86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAE-----AQSLLR 322
Cdd:COG0515   166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDlppalDAIVLR 245
                         250       260
                  ....*....|....*....|...
gi 1034674014 323 MLFKrNPANRLGSegVEEIKRHL 345
Cdd:COG0515   246 ALAK-DPEERYQS--AAELAAAL 265
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
89-344 3.81e-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: 209.18  E-value: 3.81e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKaSLKVRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTK---TGESVAIKIIDK-EQVAREGMVEQIKREIAImkLLRHPNIVELHEVMATKTKIF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS--KESVDQE 244
Cdd:cd14663    77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRM 323
Cdd:cd14663   157 GLLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKR 236
                         250       260
                  ....*....|....*....|.
gi 1034674014 324 LFKRNPANRLgseGVEEIKRH 344
Cdd:cd14663   237 ILDPNPSTRI---TVEQIMAS 254
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
90-366 4.31e-62

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: 209.88  E-value: 4.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKRKGEAMALnEKQILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 246
Cdd:cd05630    79 LTLMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 322
Cdd:cd05630   158 IKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRkkkiKREEVERLVKEVPEEYSEKFSPQARSLCS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 323 MLFKRNPANRLGSEG--VEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05630   238 MLLCKDPAERLGCRGggAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
439-697 8.31e-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: 209.00  E-value: 8.31e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIID---KSKRDPSE----------EIEILMRYGQHPNIITLKDVFD 505
Cdd:cd14182     1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEvqelreatlkEIDILRKVSGHPNIIQLKDTYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 506 DGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGF 585
Cdd:cd14182    81 TNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM----NIKLTDFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLrGENGLLLTPCYTANFVAPEVLM------QQGYDAACDIWSLGVLFYTMLAGYTPFANgpndTPEEILLR-IGNGK 658
Cdd:cd14182   157 SCQL-DPGEKLREVCGTPGYLAPEIIEcsmddnHPGYGKEVDMWSTGVIMYTLLAGSPPFWH----RKQMLMLRmIMSGN 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 659 FSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14182   232 YQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAH 270
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
436-699 1.05e-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: 208.67  E-value: 1.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIID------------KSKRDPSEEIEILMRYGQHPNIITLKDV 503
Cdd:cd14181     5 AKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeqleEVRSSTLKEIHILRQVSGHPSIITLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 504 FDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDF 583
Cdd:cd14181    85 YESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQL----HIKLSDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQLrGENGLLLTPCYTANFVAPEVL------MQQGYDAACDIWSLGVLFYTMLAGYTPFANgpndTPEEILLR-IGN 656
Cdd:cd14181   161 GFSCHL-EPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWH----RRQMLMLRmIME 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 657 GKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14181   236 GRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
441-700 1.31e-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: 209.22  E-value: 1.31e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEF-AVKIIDK-----------SKRDPSEEIEIlMRYGQHPNIITLKDVFDDGR 508
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRKadlssdnlkgsSRANILKEVQI-MKRLSHPNIVKLLDFQESDE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 509 YVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYM---------------DESA 573
Cdd:cd14096    80 YYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfipsivklrkadDDET 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 574 SADS--------------IRICDFGFAKQLRGENglLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd14096   160 KVDEgefipgvggggigiVKLADFGLSKQVWDSN--TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPF 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 640 ANgpnDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14096   238 YD---ESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
439-701 2.29e-61

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: 208.53  E-value: 2.29e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS--KRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTvdKKIVRTEIGVLLRL-SHPNIIKLKEIFETPTEISLVLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQLRGENgLL 596
Cdd:cd14085    80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDA-PLKIADFGLSKIVDQQV-TM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGNGKFSLSGGNWDNISDGAKDL 676
Cdd:cd14085   158 KTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGD--QYMFKRILNCDYDFVSPWWDDVSLNAKDL 235
                         250       260
                  ....*....|....*....|....*
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14085   236 VKKLIVLDPKKRLTTQQALQHPWVT 260
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
442-701 2.53e-61

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: 207.82  E-value: 2.53e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14169     4 VYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEamvenEIAVLRRI-NHENIVSLEDIYESPTHLYLAMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdESASADS-IRICDFGFAKQlrGENGL 595
Cdd:cd14169    83 VTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLY--ATPFEDSkIMISDFGLSKI--EAQGM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgPNDTpeEILLRIGNGKFSLSGGNWDNISDGAKD 675
Cdd:cd14169   159 LSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYD-ENDS--ELFNQILKAEYEFDSPYWDDISESAKD 235
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14169   236 FIRHLLERDPEKRFTCEQALQHPWIS 261
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
443-701 5.40e-61

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: 205.79  E-value: 5.40e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-RDPSE------EIEIlMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlQKSGLehqlrrEIEI-QSHLRHPNILRLYGYFEDKKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLrgENGL 595
Cdd:cd14007    81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENIL-LGSN---GELKLADFGWSVHA--PSNR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLsggnWDNISDGAKD 675
Cdd:cd14007   155 RKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFE---SKSHQETYKRIQNVDIKF----PSSVSPEAKD 227
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14007   228 LISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
442-700 1.01e-60

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: 205.18  E-value: 1.01e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14081     2 PYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvlmkvEREIaIMKLIEHPNVLKLYDVYENKKYLYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKqLRGENGL 595
Cdd:cd14081    82 YVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLL-LDEK---NNIKIADFGMAS-LQPEGSL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYD-AACDIWSLGVLFYTMLAGYTPFaNGPNDtpEEILLRIGNGKFSLSggnwDNISDGAK 674
Cdd:cd14081   157 LETSCGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPF-DDDNL--RQLLEKVKRGVFHIP----HFISPDAQ 229
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14081   230 DLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
443-700 4.28e-60

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: 203.53  E-value: 4.28e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDP---SEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGRevcESELNVLRRV-RHTNIIQLIEVFETKERVYMVMELATG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQLR-GENGLLLT 598
Cdd:cd14087    82 GELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPDS-KIMITDFGLASTRKkGPNCLMKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd14087   161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPF---DDDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFID 237
                         250       260
                  ....*....|....*....|..
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14087   238 RLLTVNPGERLSATQALKHPWI 259
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
437-701 8.44e-60

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: 203.30  E-value: 8.44e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 437 AQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVY 511
Cdd:cd14183     2 ASISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmiqnEVSILRRV-KHPNIVLLIEEMDMPTELY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLrg 591
Cdd:cd14183    81 LVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATVV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 eNGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDTPEEILLRIGNGKFSLSGGNWDNISD 671
Cdd:cd14183   159 -DGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF-RGSGDDQEVLFDQILMGQVDFPSPYWDNVSD 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14183   237 SAKELITMMLQVDVDQRYSALQVLEHPWVN 266
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
90-378 8.56e-60

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 205.60  E-value: 8.56e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTG--PDAgqlyAMKVLKKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:PTZ00426   32 FNFIRTLGTGSFGRVILATYKNEdfPPV----AIKRFEKSKIIKQKQVdHVFSERKILNYINHPFCVNLYGSFKDESYLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdqEKK 246
Cdd:PTZ00426  108 LVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV---DTR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 326
Cdd:PTZ00426  185 TYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLS 264
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 327 RNPANRLGS--EGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFD 378
Cdd:PTZ00426  265 HDLTKRYGNlkKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
96-345 9.14e-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: 200.96  E-value: 9.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd00180     1 LGKGSFGKVYKARDKET---GKKVAVKVIPKEKLK-KLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAYSFCG 252
Cdd:cd00180    77 SLKDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGTT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMltgtlpfqgkdrnetmnmilkaklgmpqflsAEAQSLLRMLFKRNPANR 332
Cdd:cd00180   157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKR 205
                         250
                  ....*....|...
gi 1034674014 333 LgseGVEEIKRHL 345
Cdd:cd00180   206 P---SAKELLEHL 215
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
449-699 1.05e-59

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: 202.11  E-value: 1.05e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDR 525
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIpkrDKKKEAVLREISI-LNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 526 ILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASaDSIRICDFGFAKQLRGEnGLLLTPCYTANF 605
Cdd:cd14006    80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENIL-LADRPS-PQIKIIDFGLARKLNPG-EELKEIFGTPEF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 606 VAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDP 685
Cdd:cd14006   157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFL---GEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEP 233
                         250
                  ....*....|....
gi 1034674014 686 HQRYTAEQILKHSW 699
Cdd:cd14006   234 RKRPTAQEALQHPW 247
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
443-699 1.81e-59

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: 201.86  E-value: 1.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-------RDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQvaregmvEQIKREIAI-MKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGF---AKQLRGE 592
Cdd:cd14663    81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLL-LDED---GNLKISDFGLsalSEQFRQD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 nGLLLTPCYTANFVAPEVLMQQGYD-AACDIWSLGVLFYTMLAGYTPFangpnDTPEEILL--RIGNGKFSLSggNWdnI 669
Cdd:cd14663   157 -GLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPF-----DDENLMALyrKIMKGEFEYP--RW--F 226
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14663   227 SPGAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
74-407 2.76e-59

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: 205.62  E-value: 2.76e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  74 ITHHVKEGYEKADpaQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASL-KVRDRVRTKMERDILVEVNHPFI 152
Cdd:cd05621    40 IVNKIRELQMKAE--DYDVVKVIGRGAFGEVQLVRHKA---SQKVYAMKLLSKFEMiKRSDSAFFWEERDIMAFANSPWV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 153 VKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLT 232
Cdd:cd05621   115 VQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 233 DFGLSKEsVDQEKKAY--SFCGTVEYMAPEVVNRRG----HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--K 304
Cdd:cd05621   194 DFGTCMK-MDETGMVHcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhK 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 305 AKLGMPQ--FLSAEAQSLLrMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFT 382
Cdd:cd05621   273 NSLNFPDdvEISKHAKNLI-CAFLTDREVRLGRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDDIED 351
                         330       340
                  ....*....|....*....|....*.
gi 1034674014 383 AKTPKDSPGLPASANAHQL-FKGFSF 407
Cdd:cd05621   352 DKGDVETFPIPKAFVGNQLpFVGFTY 377
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
94-347 4.68e-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: 200.86  E-value: 4.68e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLKKASLKvRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd14099     7 KFLGKGGFAKCYEV---TDMSTGKVYAGKVVPKSSLT-KPKQREKLKSEIKIhrSLKHPNIVKFHDCFEDEENVYILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd14099    83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL--SAEAQSLLRMLFKRN 328
Cdd:cd14099   163 GTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQPD 242
                         250
                  ....*....|....*....
gi 1034674014 329 PANRLgseGVEEIKRHLFF 347
Cdd:cd14099   243 PTKRP---SLDEILSHPFF 258
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
90-378 5.62e-59

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: 202.51  E-value: 5.62e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05632     4 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKRLEKKRIKKRKGESMALnEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 246
Cdd:cd05632    81 LTIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 322
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRkekvKREEVDRRVLETEEVYSAKFSEEAKSICK 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 323 MLFKRNPANRLG--SEGVEEIKRHLFFANIDWDKLYKREVQPPFKPasgKPDDTFCFD 378
Cdd:cd05632   240 MLLTKDPKQRLGcqEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP---DPRAVYCKD 294
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
441-700 7.86e-59

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: 201.41  E-value: 7.86e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDI-GVGSYSVCKRCIHATTNMEFAVKIIDK----SKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14173     1 DVYQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKrpghSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDF--GFAKQLRGEN 593
Cdd:cd14173    81 KMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENIL-CEHPNQVSPVKICDFdlGSGIKLNSDC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 G-----LLLTPCYTANFVAPEVLMQQG-----YDAACDIWSLGVLFYTMLAGYTPFAN--GPN---DTPEE-------IL 651
Cdd:cd14173   160 SpistpELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFVGrcGSDcgwDRGEAcpacqnmLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 652 LRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14173   240 ESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
90-366 1.12e-58

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: 200.60  E-value: 1.12e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKRKGEAMALnEKRILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 246
Cdd:cd05631    79 LTIMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGET 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 322
Cdd:cd05631   158 VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkervKREEVDRRVKEDQEEYSEKFSEDAKSICR 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 323 MLFKRNPANRLG--SEGVEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05631   238 MLLTKNPKERLGcrGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
78-407 1.18e-58

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: 204.47  E-value: 1.18e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  78 VKEGYEKADpaQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASL-KVRDRVRTKMERDILVEVNHPFIVKLH 156
Cdd:cd05622    65 IRDLRMKAE--DYEVVKVIGRGAFGEVQLVRHKS---TRKVYAMKLLSKFEMiKRSDSAFFWEERDIMAFANSPWVVQLF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQTEGKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05622   140 YAFQDDRYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 S-KESVDQEKKAYSFCGTVEYMAPEVVNRRG----HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK--LGM 309
Cdd:cd05622   219 CmKMNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTF 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 310 PQ--FLSAEAQSLLrMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPK 387
Cdd:cd05622   299 PDdnDISKEAKNLI-CAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEE 377
                         330       340
                  ....*....|....*....|.
gi 1034674014 388 DSPGLPASANAHQL-FKGFSF 407
Cdd:cd05622   378 ETFPIPKAFVGNQLpFVGFTY 398
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
89-345 4.70e-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: 198.19  E-value: 4.70e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKkASLKVRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLL---GRPVAIKVLR-PELAEDEEFRERFLReaRALARLSHPNIVRVYDVGEDDGRPY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK-ESVDQEK 245
Cdd:cd14014    77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARaLGDSGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL-GMPQFLSAEAQSL---- 320
Cdd:cd14014   157 QTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpPPSPLNPDVPPALdaii 236
                         250       260
                  ....*....|....*....|....*
gi 1034674014 321 LRMLfKRNPANRLGSegVEEIKRHL 345
Cdd:cd14014   237 LRAL-AKDPEERPQS--AAELLAAL 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
443-700 9.41e-58

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: 197.41  E-value: 9.41e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNME--FAVKIIDKsKRDPSE--------EIEILMRYgQHPNIITLKDVFDDGRYVYL 512
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSGLKekVACKIIDK-KKAPKDflekflprELEILRKL-RHPNIIQVYSIFERGSKVFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMdesaSADSIRICDFGFAKQLRGE 592
Cdd:cd14080    80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLD----SNNNVKLSDFGFARLCPDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLL--TPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpNDTPEEILLRIGNGK---FSLSGgnw 666
Cdd:cd14080   156 DGDVLskTFCGSAAYAAPEILQGIPYDPkKYDIWSLGVILYIMLCGSMPF----DDSNIKKMLKDQQNRkvrFPSSV--- 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 667 DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14080   229 KKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
89-347 2.42e-57

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: 195.94  E-value: 2.42e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLKKASLkVRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKL 165
Cdd:cd14081     2 PYRLGKTLGKGQTGLVKLaKHCVTG----QKVAIKIVNKEKL-SKESVLMKVEREIAIMklIEHPNVLKLYDVYENKKYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSkeSVDQE- 244
Cdd:cd14081    77 YLVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA--SLQPEg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRM 323
Cdd:cd14081   155 SLLETSCGSPHYACPEVIkGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRR 234
                         250       260
                  ....*....|....*....|....
gi 1034674014 324 LFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14081   235 MLEVNPEKRI---TIEEIKKHPWF 255
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
89-347 3.56e-57

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: 195.82  E-value: 3.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLaLNLDTG----ELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEK 245
Cdd:cd06606    77 FLEYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF-QGKDRNETMNMILKAKLG--MPQFLSAEAQSLLR 322
Cdd:cd06606   157 GTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGEPppIPEHLSEEAKDFLR 236
                         250       260
                  ....*....|....*....|....*
gi 1034674014 323 MLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd06606   237 KCLQRDPKKRP---TADELLQHPFL 258
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
439-700 9.34e-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: 194.88  E-value: 9.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYEL-KEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd14106     5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDcrneilHEIAVLELCKDCPRVVNLHEVYETRSELI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQL-R 590
Cdd:cd14106    85 LILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGD-IKLCDFGISRVIgE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GEN--GLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDN 668
Cdd:cd14106   164 GEEirEILGTPDY----VAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFG---GDDKQETFLNISQCNLDFPEELFKD 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14106   237 VSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
441-700 9.69e-57

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: 195.63  E-value: 9.69e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDI-GVGSYSVCKRCIHATTNMEFAVKIIDK----SKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14174     1 DLYRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKnaghSRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLRGENGL 595
Cdd:cd14174    81 KLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL-CESPDKVSPVKICDFDLGSGVKLNSAC 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 -------LLTPCYTANFVAPEVL---MQQG--YDAACDIWSLGVLFYTMLAGYTPFAN--GPN---DTPE-------EIL 651
Cdd:cd14174   160 tpittpeLTTPCGSAEYMAPEVVevfTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGhcGTDcgwDRGEvcrvcqnKLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 652 LRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14174   240 ESIQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
441-700 1.03e-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: 196.04  E-value: 1.03e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK---RDPSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14168    10 KIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLYLVMQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKqLRGENGLL 596
Cdd:cd14168    90 VSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQDEES-KIMISDFGLSK-MEGKGDVM 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgPNDTpeEILLRIGNGKFSLSGGNWDNISDGAKDL 676
Cdd:cd14168   168 STACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDS--KLFEQILKADYEFDSPYWDDISDSAKDF 244
                         250       260
                  ....*....|....*....|....
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14168   245 IRNLMEKDPNKRYTCEQALRHPWI 268
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
446-700 1.15e-56

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: 195.37  E-value: 1.15e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 446 KEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRdPSEEIEILMRYGQHPNIITLKDVFDDG----------RYVYLVTD 515
Cdd:cd14171    11 TQKLGTGISGPVRVCVKKSTGERFALKILLDRPK-ARTEVRLHMMCSGHPNIVQIYDVYANSvqfpgessprARLLIVME 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQlrgENGL 595
Cdd:cd14171    90 LMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEDA-PIKLCDFGFAKV---DQGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQ-----------------GYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDT-PEEILLRIGN 656
Cdd:cd14171   166 LMTPQFTPYYVAPQVLEAQrrhrkersgiptsptpyTYDKSCDMWSLGVIIYIMLCGYPPFySEHPSRTiTKDMKRKIMT 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 657 GKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14171   246 GSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
443-699 3.06e-56

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: 193.46  E-value: 3.06e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----RDP---SEEIEILMRYgQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvagndKNLqlfQREINILKSL-EHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdsIRICDFGFAKqLRGENG 594
Cdd:cd14098    81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPVI--VKISDFGLAK-VIHTGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQ------GYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDN 668
Cdd:cd14098   158 FLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFD---GSSQLPVEKRIRKGRYTQPPLVDFN 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14098   235 ISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
96-344 4.23e-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: 193.15  E-value: 4.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLK-------VRDRVRTKMER-----DILVEVNHPFIVKLHYAF--QT 161
Cdd:cd14008     1 LGRGSFGKVKLALDT---ETGQLYAIKIFNKSRLRkrregknDRGKIKNALDDvrreiAIMKKLDHPNIVRLYEVIddPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSkE 239
Cdd:cd14008    78 SDKLYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVS-E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAYSFC-GTVEYMAPEV--VNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL--GMPQFL 313
Cdd:cd14008   157 MFEDGNDTLQKTaGTPAFLAPELcdGDSKTySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDefPIPPEL 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 314 SAEAQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14008   237 SPELKDLLRRMLEKDPEKRI---TLKEIKEH 264
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
90-366 6.29e-56

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: 193.56  E-value: 6.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05608     3 FLDFRVLGKGGFGEVSACQMRA---TGKLYACKKLNKKRLKKRKGYEGAMvEKRILAKVHSRFIVSLAYAFQTKTDLCLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd05608    80 MTIMNGGDlryhIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSL 320
Cdd:cd05608   160 TKTKGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKSI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 321 LRMLFKRNPANRLGSE--GVEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05608   240 CEALLAKDPEKRLGFRdgNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
439-723 1.02e-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: 193.14  E-value: 1.02e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK---------RDPSEEIEILMRYgQHPNIITLKDVFDDGRY 509
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsspglstEDLKREASICHML-KHPHIVELLETYSSDGM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELLDRILKQK----CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGF 585
Cdd:cd14094    80 LYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASKENSA-PVKLGGFGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpndTPEEILLRIGNGKFSLSGGN 665
Cdd:cd14094   159 AIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPRQ 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 666 WDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQ------LPN--DQPKRNDVSHVVKGA 723
Cdd:cd14094   235 WSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDRyayrihLPEtvEQLRKFNARRKLKGA 300
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
449-700 1.13e-55

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: 192.00  E-value: 1.13e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSK--------------RDPSE----EIEIlMRYGQHPNIITLKDVFDD--GR 508
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRlrkrregkndrgkiKNALDdvrrEIAI-MKKLDHPNIVRLYEVIDDpeSD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 509 YVYLVTDLMKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFA 586
Cdd:cd14008    80 KLYLVLEYCEGGPVMELDSGDRvpPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL-LTAD---GTVKISDFGVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLRGENGLLLTPCYTANFVAPEVLM--QQGYDA-ACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILlrIGNGKFSLS 662
Cdd:cd14008   156 EMFEDGNDTLQKTAGTPAFLAPELCDgdSKTYSGkAADIWALGVTLYCLVFGRLPFnGDNILELYEAIQ--NQNDEFPIP 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 663 GgnwdNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14008   234 P----ELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
449-699 2.39e-55

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: 190.42  E-value: 2.39e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSK-------RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEiikrkevEHTLNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASdiLYV--ISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTP 599
Cdd:cd05123    80 LFSHLSKEGRFPEERAR--FYAaeIVLALEYLHSLGIIYRDLKPENIL-LDSDGH---IKLTDFGLAKELSSDGDRTYTF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSH 679
Cdd:cd05123   154 CGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF---YAENRKEIYEKILKSPLKFP----EYVSPEAKSLISG 226
                         250       260
                  ....*....|....*....|...
gi 1034674014 680 MLHMDPHQRYT---AEQILKHSW 699
Cdd:cd05123   227 LLQKDPTKRLGsggAEEIKAHPF 249
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
90-347 3.17e-55

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: 190.11  E-value: 3.17e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARhKKTG----QIVAIKKINLESKEKKESILN--EIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKA 247
Cdd:cd05122    76 MEFCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LSDGKTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK---AKLGMPQFLSAEAQSLLRML 324
Cdd:cd05122   155 NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATngpPGLRNPKKWSKEFKDFLKKC 234
                         250       260
                  ....*....|....*....|...
gi 1034674014 325 FKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd05122   235 LQKDPEKRP---TAEQLLKHPFI 254
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
446-700 4.11e-55

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: 190.59  E-value: 4.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 446 KEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRdPSEEIEILMRYGQHPNIITLKDVFDD----GRYVYLVTDLMKGGE 521
Cdd:cd14172     9 KQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPK-ARREVEHHWRASGGPHIVHILDVYENmhhgKRCLLIIMECMEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQLRGENGLLlTP 599
Cdd:cd14172    88 LFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAV-LKLTDFGFAKETTVQNALQ-TP 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd14172   166 CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFySNTGQAISPGMKRRIRMGQYGFPNPEWAEVSEEAKQLIR 245
                         250       260
                  ....*....|....*....|..
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14172   246 HLLKTDPTERMTITQFMNHPWI 267
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
90-366 4.31e-55

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: 190.89  E-value: 4.31e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05607     4 FYEFRVLGKGGFGEVCAVQVKN---TGQMYACKKLDKKRLKKKSGEKMALlEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 246
Cdd:cd05607    81 MSLMNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILK--AKLGMPQFlSAEAQSL 320
Cdd:cd05607   160 ITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEdeVKFEHQNF-TEEAKDI 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 321 LRMLFKRNPANRLGS-EGVEEIKRHLFFANIDWDKLYKREVQPPFKP 366
Cdd:cd05607   239 CRLFLAKKPENRLGSrTNDDDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
96-333 5.15e-55

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: 189.40  E-value: 5.15e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASlkvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14006     1 LGRGRFGVVKRCIEKA---TGREFAAKFIPKRD---KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG--HIKLTDFGLSKEsVDQEKKAYSFCGT 253
Cdd:cd14006    75 ELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARK-LNPGEELKEIFGT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 254 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG----MPQFLSAEAQSLLRMLFKRNP 329
Cdd:cd14006   154 PEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseeYFSSVSQEAKDFIRKLLVKEP 233

                  ....
gi 1034674014 330 ANRL 333
Cdd:cd14006   234 RKRP 237
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
449-698 5.95e-55

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 188.25  E-value: 5.95e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS-----EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELL 523
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleellREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 524 DRILKQ-KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQLRGENGLLLTPCYT 602
Cdd:cd00180    80 DLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSD----GTVKLADFGLAKDLDSDDSLLKTTGGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 603 AN--FVAPEVLMQQGYDAACDIWSLGVLFYTMlagytpfangpndtpeeillrigngkfslsggnwdnisDGAKDLLSHM 680
Cdd:cd00180   156 TPpyYAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------------EELKDLIRRM 197
                         250
                  ....*....|....*...
gi 1034674014 681 LHMDPHQRYTAEQILKHS 698
Cdd:cd00180   198 LQYDPKKRPSAKELLEHL 215
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
449-700 1.19e-53

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: 185.89  E-value: 1.19e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLD 524
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREdvrnEIEI-MNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RILKQKcFSEREASDILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAKQLrGENGLLLTPCYT 602
Cdd:cd14103    80 RVVDDD-FELTERDCILFMrqICEGVQYMHKQGILHLDLKPENILCVSRTGN--QIKIIDFGLARKY-DPDKKLKVLFGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 603 ANFVAPEVLmqqGYDA---ACDIWSLGVLFYTMLAGYTPFAnGPNDTpeEILLRIGNGKFSLSGGNWDNISDGAKDLLSH 679
Cdd:cd14103   156 PEFVAPEVV---NYEPisyATDMWSVGVICYVLLSGLSPFM-GDNDA--ETLANVTRAKWDFDDEAFDDISDEAKDFISK 229
                         250       260
                  ....*....|....*....|.
gi 1034674014 680 MLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14103   230 LLVKDPRKRMSAAQCLQHPWL 250
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
96-349 3.18e-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: 3.18e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14009     1 IGRGSFATVWKGRHK---QTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKeSVDQEKKAYSFCG 252
Cdd:cd14009    78 DLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFAR-SLQPASMAETLCG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFKRN 328
Cdd:cd14009   157 SPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPfpiaAQLSPDCKDLLRRLLRRD 236
                         250       260
                  ....*....|....*....|.
gi 1034674014 329 PANRLGSEGveeikrhlFFAN 349
Cdd:cd14009   237 PAERISFEE--------FFAH 249
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
89-334 6.80e-53

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: 183.75  E-value: 6.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSD---NQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEV----LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKesVDQE 244
Cdd:cd08530    78 MEYAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEAQSLLRM 323
Cdd:cd08530   156 NLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPpIPPVYSQDLQQIIRS 235
                         250
                  ....*....|.
gi 1034674014 324 LFKRNPANRLG 334
Cdd:cd08530   236 LLQVNPKKRPS 246
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
443-700 9.22e-53

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: 184.23  E-value: 9.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIE---ILMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvsrEDIErevSILRQVLHPNIITLHDVFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLrgEN 593
Cdd:cd14105    87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFGLAHKI--ED 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLL-TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDG 672
Cdd:cd14105   165 GNEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVNYDFDDEYFSNTSEL 241
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14105   242 AKDFIRQLLVKDPRKRMTIQESLRHPWI 269
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
443-700 1.34e-52

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: 183.14  E-value: 1.34e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS-------KRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKSsltkpkqREKLKSEIKI-HRSLKHPNIVKFHDCFEDEENVYILLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLRGENGL 595
Cdd:cd14099    82 LCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLF-LDENM---NVKIGDFGLAARLEYDGER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGnwDNISDGAK 674
Cdd:cd14099   158 KKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFE---TSDVKETYKRIKKNEYSFPSH--LSISDEAK 232
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14099   233 DLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
94-344 1.49e-52

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: 183.75  E-value: 1.49e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVR--------DRVRTKMErdILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14084    12 RTLGSGACGEVKLAYDKS---TCKKVAIKIINKRKFTIGsrreinkpRNIETEIE--ILKKLSHPCIIKIEDFFDAEDDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKeSVD 242
Cdd:cd14084    87 YIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSK-ILG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM-NMILKAKL--GMPQF--LS 314
Cdd:cd14084   166 ETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLkEQILSGKYtfIPKAWknVS 245
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 315 AEAQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14084   246 EEAKDLVKKMLVVDPSRRP---SIEEALEH 272
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
90-344 2.57e-52

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: 182.38  E-value: 2.57e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVrKKTGPDAGQLYAMKVL--KKASlkvRDRVrTKM---ERDILVEVNHPFIVKLHYAFQTEGK 164
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLA-EYTKSGLKEKVACKIIdkKKAP---KDFL-EKFlprELEILRKLRHPNIIQVYSIFERGSK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd14080    77 VFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYS--FCGTVEYMAPEVVnrRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP---QFLSAE 316
Cdd:cd14080   157 GDVLSktFCGSAAYAAPEIL--QGipyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPE 234
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 317 AQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14080   235 CKDLIDQLLEPDPTKRA---TIEEILNH 259
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
443-700 5.79e-52

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: 181.46  E-value: 5.79e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEIL-----MRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFqevrcMKLVQHPNVVRLYEVIDTQTKLYLILELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasaDSIRICDFGFAKQLR-GENgl 595
Cdd:cd14074    85 DGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQ---GLVKLTDFGFSNKFQpGEK-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFaNGPNDTpeEILLRIGNGKFSLSggnwDNISDGAK 674
Cdd:cd14074   160 LETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPF-QEANDS--ETLTMIMDCKYTVP----AHVSPECK 232
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14074   233 DLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
90-340 1.55e-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: 180.15  E-value: 1.55e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLK---VRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREK---QSKFILALKVLFKAQLEkagVEHQLRREVE--IQSHLRHPNILRLYGYFHDATRVY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd14116    82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 aySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 326
Cdd:cd14116   162 --TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK 239
                         250
                  ....*....|....
gi 1034674014 327 RNPANRLGSEGVEE 340
Cdd:cd14116   240 HNPSQRPMLREVLE 253
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
449-707 2.54e-51

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: 181.39  E-value: 2.54e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIID---KSKRdpseEIEILMRYGQHPNIITLKDVFDD---GRYVYL-VTDLMKGGE 521
Cdd:cd14170    10 LGLGINGKVLQIFNKRTQEKFALKMLQdcpKARR----EVELHWRASQCPHIVRIVDVYENlyaGRKCLLiVMECLDGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQLRGENGLLlTP 599
Cdd:cd14170    86 LFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNA-ILKLTDFGFAKETTSHNSLT-TP 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd14170   164 CYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIR 243
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWITHRDQLP 707
Cdd:cd14170   244 NLLKTEPTQRMTITEFMNHPWIMQSTKVP 272
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
441-700 2.66e-51

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: 180.21  E-value: 2.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK----------SKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYV 510
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKrrtkssrrgvSREDIEREVSILKEI-QHPNVITLHEVYENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLR 590
Cdd:cd14194    84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKID 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GEN---GLLLTPcytaNFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWD 667
Cdd:cd14194   164 FGNefkNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANVSAVNYEFEDEYFS 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 668 NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14194   237 NTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
88-351 5.02e-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: 178.94  E-value: 5.02e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKkasLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGK 164
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRhKPTG----KIYALKKIH---VDGDEEFRKQLLRElkTLRSCESPYVVKCYGAFYKEGE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQ-LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd06623    74 ISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL-----SAEAQ 318
Cdd:cd06623   154 LDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPSLpaeefSPEFR 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 319 SLLRMLFKRNPANRLgseGVEEIKRHLFFANID 351
Cdd:cd06623   234 DFISACLQKDPKKRP---SAAELLQHPFIKKAD 263
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
443-700 7.39e-51

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: 179.04  E-value: 7.39e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK-----SKRDPS-EEIEI---LMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKrrlssSRRGVSrEEIERevnILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGEN 593
Cdd:cd14195    87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 ---GLLLTPcytaNFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:cd14195   167 efkNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GETKQETLTNISAVNYDFDEEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14195   240 ELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
441-700 1.03e-50

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: 178.13  E-value: 1.03e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILmRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14097     1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSavklleREVDIL-KHVNHAHIIHLEEVFETPKRMYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY---MDESASADSIRICDFGFA--KQL 589
Cdd:cd14097    80 ELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssIIDNNDKLNIKVTDFGLSvqKYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTpCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd14097   160 LGEDMLQET-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAK---SEEKLFEEIRKGDLTFTQSVWQSV 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14097   236 SDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
442-700 2.84e-50

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: 176.62  E-value: 2.84e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI--EI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESIlnEIaILKKCKHPNIVKYYGSYLKKDELWIVMEFCS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDrILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLL 596
Cdd:cd05122    81 GGSLKD-LLKNTNktLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDG----EVKLIDFGLSAQLSDGKTRN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 lTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIG-NGKFSLSGGNWdnISDGAKD 675
Cdd:cd05122   156 -TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPY---SELPPMKALFLIAtNGPPGLRNPKK--WSKEFKD 229
                         250       260
                  ....*....|....*....|....*
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd05122   230 FLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
90-333 3.96e-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: 3.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKAT---DKEYALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG----HIKLTDFGLSKESVDQek 245
Cdd:cd14095    78 ELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKEP-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 kAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN--ETMNMILKAKLGMP----QFLSAEAQS 319
Cdd:cd14095   156 -LFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDqeELFDLILAGEFEFLspywDNISDSAKD 234
                         250
                  ....*....|....
gi 1034674014 320 LLRMLFKRNPANRL 333
Cdd:cd14095   235 LISRMLVVDPEKRY 248
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
441-700 5.58e-50

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: 176.30  E-value: 5.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIE---ILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsrEEIErevSILRQVLHPNIITLHDVYENRTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLrg 591
Cdd:cd14196    85 LILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEI-- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCY-TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:cd14196   163 EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVSYDFDEEFFSHTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14196   240 ELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
443-700 1.11e-49

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: 174.89  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEnlkkiyREVQI-MKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRgENGLL 596
Cdd:cd14071    81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLL-LDAN---MNIKIADFGFSNFFK-PGELL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFaNGPndTPEEILLRIGNGKFSLSGgnwdNISDGAKD 675
Cdd:cd14071   156 KTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPF-DGS--TLQTLRDRVLSGRFRIPF----FMSTDCEH 228
                         250       260
                  ....*....|....*....|....*
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14071   229 LIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
449-700 3.10e-49

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: 173.86  E-value: 3.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELL 523
Cdd:cd06606     8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEElealEREIrILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 524 DRILKQKCFSEREAS----DILYVIsktvDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRGENGL--LL 597
Cdd:cd06606    88 SLLKKFGKLPEPVVRkytrQILEGL----EYLHSNGIVHRDIKGANIL-VDSD---GVVKLADFGCAKRLAEIATGegTK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGK----FSlsggnwDNISDGA 673
Cdd:cd06606   160 SLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGN--PVAALFKIGSSGepppIP------EHLSEEA 231
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06606   232 KDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
443-699 5.37e-49

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: 173.22  E-value: 5.37e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-------EIEILmRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDmeekirrEIQIL-KLFRHPHIIRLYEVIETPTDIFMVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLR-GEng 594
Cdd:cd14079    83 YVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLL-LD---SNMNVKIADFGLSNIMRdGE-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPF--ANGPNdtpeeILLRIGNGKFSLSggnwDNISD 671
Cdd:cd14079   157 FLKTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFddEHIPN-----LFKKIKSGIYTIP----SHLSP 227
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14079   228 GARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
90-338 9.31e-49

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: 172.83  E-value: 9.31e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVrtkMERDILV--EVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHW---NENQEYAMKIIDKSKLKGKEDM---IESEILIikSLSHPNIVKLFEVYETEKEIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----DEIGHIKLTDFGLSKESVdq 243
Cdd:cd14185    76 ILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 eKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN--ETMNMIlkaKLGMPQFL-------S 314
Cdd:cd14185   154 -GPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDqeELFQII---QLGHYEFLppywdniS 229
                         250       260
                  ....*....|....*....|....
gi 1034674014 315 AEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14185   230 EAAKDLISRLLVVDPEKRYTAKQV 253
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
89-344 2.82e-48

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: 171.03  E-value: 2.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVR-DRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIER---ATGREVAIKSIKKDKIEDEqDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 247
Cdd:cd14073    79 VMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSN-LYSKDKLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSaEAQSLLRMLFK 326
Cdd:cd14073   158 QTFCGSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWMLT 236
                         250
                  ....*....|....*...
gi 1034674014 327 RNPANRlgsEGVEEIKRH 344
Cdd:cd14073   237 VNPKRR---ATIEDIANH 251
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
96-332 4.44e-48

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 170.41  E-value: 4.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd13999     1 IGSGSFGEVYKGKWR-----GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTV 254
Cdd:cd13999    76 SLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 255 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD-RNETMNMILKAKL-----GMPQFLSaeaqSLLRMLFKRN 328
Cdd:cd13999   156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSpIQIAAAVVQKGLRppippDCPPELS----KLIKRCWNED 231

                  ....
gi 1034674014 329 PANR 332
Cdd:cd13999   232 PEKR 235
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
443-695 1.16e-47

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: 169.69  E-value: 1.16e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfrerflrEARALARL-SHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrGENGL 595
Cdd:cd14014    81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL----TEDGRVKLTDFGIARAL-GDSGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTP--CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNISDGA 673
Cdd:cd14014   156 TQTGsvLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPF---DGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                         250       260
                  ....*....|....*....|...
gi 1034674014 674 KDLLSHMLHMDPHQRY-TAEQIL 695
Cdd:cd14014   233 DAIILRALAKDPEERPqSAAELL 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
89-347 1.19e-47

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: 169.43  E-value: 1.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGK-LY 166
Cdd:cd14069     2 DWDLVQTLGEGAFGEVFLaVNRNTE----EAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRF-YGHRREGEfQY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSkeSV----D 242
Cdd:cd14069    77 LFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLA--TVfrykG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK----AKLGMPQFLSAEA 317
Cdd:cd14069   155 KERLLNKMCGTLPYVAPELLAKKKyRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKenkkTYLTPWKKIDTAA 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 318 QSLLRMLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14069   235 LSLLRKILTENPNKRI---TIEDIKKHPWY 261
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
438-700 1.31e-47

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: 169.82  E-value: 1.31e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDiGVGSYSVCKRcihattnmeFAVKIIDKSKRDPSEEIEILmRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14088    13 EFCEIFRAKDK-TTGKLYTCKK---------FLKRDGRKVRKAAKNEINIL-KMVKHPNILQLVDVFETRKEYFIFLELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQlrgENGLLL 597
Cdd:cd14088    82 TGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKNS-KIVISDFHLAKL---ENGLIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEE-----ILLRIGNGKFSLSGGNWDNISDG 672
Cdd:cd14088   158 EPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknLFRKILAGDYEFDSPYWDDISQA 237
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14088   238 AKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
443-700 2.76e-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: 2.76e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS---EEIEILMRYG---QHPNIITLKDVFDD--GRYVYLVT 514
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKHLNdveGHPNIVKLLDVFEHrgGNHLCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMkgGELLDRILK--QKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASAdsIRICDFGFAKQLRge 592
Cdd:cd05118    81 ELM--GMNLYELIKdyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENIL-INLELGQ--LKLADFGLARSFT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 nglllTPCYTANFV-----APEVLMQ-QGYDAACDIWSLGVLFYTMLAGYtPFANGPN--DTPEEILLRIGNgkfslsgg 664
Cdd:cd05118   154 -----SPPYTPYVAtrwyrAPEVLLGaKPYGSSIDIWSLGCILAELLTGR-PLFPGDSevDQLAKIVRLLGT-------- 219
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 665 nwdnisDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd05118   220 ------PEALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
443-697 2.86e-47

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: 168.41  E-value: 2.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEreealnEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKC----FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQLRGE 592
Cdd:cd08215    81 ADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKD----GVVKLGDFGISKVLEST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNdtPEEILLRIGNGKFS-LSggnwDNISD 671
Cdd:cd08215   157 TDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPF-EANN--LPALVYKIVKGQYPpIP----SQYSS 229
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd08215   230 ELRDLVNSMLQKDPEKRPSANEILSS 255
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
443-696 5.94e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 174.05  E-value: 5.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII-DKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEArerfrrEARALARL-NHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGE--- 592
Cdd:COG0515    88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL----TPDGRVKLIDFGIARALGGAtlt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 --NGLLLTPCYTanfvAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:COG0515   164 qtGTVVGTPGYM----APEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---DGDSPAELLRAHLREPPPPPSELRPDLP 236
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 671 DGAKDLLSHMLHMDPHQRY-TAEQILK 696
Cdd:COG0515   237 PALDAIVLRALAKDPEERYqSAAELAA 263
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
443-699 6.04e-47

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: 167.51  E-value: 6.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID--KSKRDPSEEI--EI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDmkRAPGDCPENIkkEVcIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLR--GENGL 595
Cdd:cd14069    83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLL-LDEN---DNLKISDFGLATVFRykGKERL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFaNGPNDTPEEILLRIGNGKFSLsgGNWDNISDGAK 674
Cdd:cd14069   159 LNKMCGTLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAGELPW-DQPSDSCQEYSDWKENKKTYL--TPWKKIDTAAL 235
                         250       260
                  ....*....|....*....|....*
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14069   236 SLLRKILTENPNKRITIEDIKKHPW 260
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
89-332 6.46e-47

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: 167.30  E-value: 6.46e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKE---DGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd08218    78 MDYCDGGDLYKRINAQrgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVEL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ-GKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 325
Cdd:cd08218   158 ARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEaGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLF 237

                  ....*..
gi 1034674014 326 KRNPANR 332
Cdd:cd08218   238 KRNPRDR 244
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
90-363 7.00e-47

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: 167.73  E-value: 7.00e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLkVRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14117     8 FDIGRPLGKGKFGNVYLAREK---QSKFIVALKVLFKSQI-EKEGVEHQLRREIEIQshLRHPNILRLYNYFHDRKRIYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKa 247
Cdd:cd14117    84 ILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRR- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 ySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd14117   163 -TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRY 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 328 NPANRLGSEGVEEikrHlffaniDWDKLYKREVQPP 363
Cdd:cd14117   242 HPSERLPLKGVME---H------PWVKANSRRVLPP 268
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
449-699 1.51e-46

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: 166.24  E-value: 1.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKlqenleSEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLRgENGLLLTPCYT 602
Cdd:cd14009    80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLL-LSTSGDDPVLKIADFGFARSLQ-PASMAETLCGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 603 ANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNdtPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLH 682
Cdd:cd14009   158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPF-RGSN--HVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLR 234
                         250
                  ....*....|....*..
gi 1034674014 683 MDPHQRYTAEQILKHSW 699
Cdd:cd14009   235 RDPAERISFEEFFAHPF 251
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
89-346 5.29e-46

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: 165.16  E-value: 5.29e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMK-VLKKASLKVRDRVRTkmerdiLVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14010     1 NYVLYDEIGRGKHSVVYKGRRKG---TIEFVAIKcVDKSKRPEVLNEVRL------THELKHPNVLKFYEWYETSNHLWL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 238
Cdd:cd14010    72 VVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkel 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 -------ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA-----K 306
Cdd:cd14010   152 fgqfsdeGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEdppppP 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 307 LGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLF 346
Cdd:cd14010   232 PKVSSKPSPDFKSLLKGLLEKDPAKRLSW---DELVKHPF 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
89-344 5.53e-46

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: 165.02  E-value: 5.53e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpDaGQLYAMKVLKKASLKVRDRvrtKM---ERDILVEVNHPFIVKLHYAF--QTEG 163
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKS--D-GKILVWKEIDYGKMSEKEK---QQlvsEVNILRELKHPNIVRYYDRIvdRANT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGD---VFTRLSKEVLFTEED-VKFYLAELALALDHLHQLG-----IVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd08217    75 TLYIVMEYCEGGDlaqLIKKCKKENQYIPEEfIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 235 GLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNEtmnMILKAKLGM----P 310
Cdd:cd08217   155 GLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLE---LAKKIKEGKfpriP 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 311 QFLSAEAQSLLRMLFKRNPANRlgsEGVEEIKRH 344
Cdd:cd08217   232 SRYSSELNEVIKSMLNVDPDKR---PSVEELLQL 262
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
443-700 6.47e-46

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: 164.43  E-value: 6.47e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDP------SEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQktqrllSREISSMEKL-HHPNIIRLYEVVETLSKLHLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENgLL 596
Cdd:cd14075    83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFY----ASNNCVKVGDFGFSTHAKRGE-TL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGY-DAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGAKD 675
Cdd:cd14075   158 NTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFR---AETVAKLKKCILEGTYTIP----SYVSEPCQE 230
                         250       260
                  ....*....|....*....|....*
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14075   231 LIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
89-334 1.13e-45

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: 163.96  E-value: 1.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14002     2 NYHVLELIGEGSFGKVYKGRRK---YTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAY 248
Cdd:cd14002    79 TEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRN 328
Cdd:cd14002   158 SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKD 237

                  ....*.
gi 1034674014 329 PANRLG 334
Cdd:cd14002   238 PSKRLS 243
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
90-347 1.41e-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: 1.41e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKkasLKVRDRVRTKMERDILVEVN----HPFIVKLHYAF--QTEG 163
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDK---VTGEKVAIKKIK---NDFRHPKAALREIKLLKHLNdvegHPNIVKLLDVFehRGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI-GHIKLTDFGLSKESV 241
Cdd:cd05118    75 HLCLVFELM-GMNLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKkaYSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMPQFLsaeaqSL 320
Cdd:cd05118   154 SPPY--TPYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR-LLGTPEAL-----DL 225
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 321 LRMLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd05118   226 LSKMLKYDPAKRI---TASQALAHPYF 249
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
443-699 1.67e-45

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: 164.67  E-value: 1.67e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEhvlnekrILSEV-RHPFIVNLLGSFQDDRNLYMVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSERE----ASDILYVIsktvDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLRG 591
Cdd:cd05580    82 YVPGGELFSLLRRSGRFPNDVakfyAAEVVLAL----EYLHSLDIVYRDLKPENLL-LD---SDGHIKITDFGFAKRVKD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENgllLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILlrigNGKFSLSggnwDNIS 670
Cdd:cd05580   154 RT---YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFfDENPMKIYEKIL----EGKIRFP----SFFD 222
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 671 DGAKDLLSHMLHMDPHQRY-----TAEQILKHSW 699
Cdd:cd05580   223 PDAKDLIKRLLVVDLTKRLgnlknGVEDIKNHPW 256
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
442-700 5.20e-45

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: 162.01  E-value: 5.20e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06627     1 NYQLGDLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlksvmgEIDLLKKL-NHPNIVKYIGSVKTKDSLYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdeSASADSIRICDFGFAKQLRGENGL 595
Cdd:cd06627    80 YVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANIL----TTKDGLVKLADFGVATKLNEVEKD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNgkfslsggnwD-------N 668
Cdd:cd06627   156 ENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYY---DLQPMAALFRIVQ----------DdhpplpeN 222
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06627   223 ISPELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
443-700 5.34e-45

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: 162.17  E-value: 5.34e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK--RD-PSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgDDlPRVKTEIeALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGF-AKQLRGENGLLL 597
Cdd:cd14078    85 GGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLL-LDED---QNLKLIDFGLcAKPKGGMDHHLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGY-DAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSggNWdnISDGAKDL 676
Cdd:cd14078   161 TCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPF---DDDNVMALYRKIQSGKYEEP--EW--LSPSSKLL 233
                         250       260
                  ....*....|....*....|....
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14078   234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
442-699 3.23e-44

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: 160.06  E-value: 3.23e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEIEILMRYGqHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14107     3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIplrSSTRARAFQERDILARLS-HRRLTCLLDQFETRKTLILILELCS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMdeSASADSIRICDFGFAKQLRGENgLLLT 598
Cdd:cd14107    82 SEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMV--SPTREDIKICDFGFAQEITPSE-HQFS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDtpEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd14107   159 KYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFA-GEND--RATLLNVAEGVVSWDTPEITHLSEDAKDFIK 235
                         250       260
                  ....*....|....*....|.
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14107   236 RVLQPDPEKRPSASECLSHEW 256
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
90-336 4.24e-44

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: 160.54  E-value: 4.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLkVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRS---TGKLYALKCIKKSPL-SRD---SSLENEIAVlkRIKHENIVTLEDIYESTTHYYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKesVDQE 244
Cdd:cd14166    78 VMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--MEQN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETmNMILKAKLGMPQF-------LSAEA 317
Cdd:cd14166   156 GIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY--EETES-RLFEKIKEGYYEFespfwddISESA 232
                         250
                  ....*....|....*....
gi 1034674014 318 QSLLRMLFKRNPANRLGSE 336
Cdd:cd14166   233 KDFIRHLLEKNPSKRYTCE 251
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
96-336 5.16e-44

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: 158.93  E-value: 5.16e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVF-LVRKKTGpdagQLYAMKVLKKASLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd14103     1 LGRGKFGTVYrCVEKATG----KELAAKFIKCRKAKDREDVR--NEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKE--VLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIGH-IKLTDFGLSKEsVDQEKKAYSF 250
Cdd:cd14103    75 GELFERVVDDdfEL-TERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARK-YDPDKKLKVL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK--LGMPQF--LSAEAQSLLRMLFK 326
Cdd:cd14103   153 FGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKwdFDDEAFddISDEAKDFISKLLV 232
                         250
                  ....*....|
gi 1034674014 327 RNPANRLGSE 336
Cdd:cd14103   233 KDPRKRMSAA 242
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
96-346 5.28e-44

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: 159.43  E-value: 5.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKV-----FLVRKKTgpdagqlyAMKVLKKAslKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14075    10 LGSGNFSQVklgihQLTKEKV--------AIKILDKT--KLDQKTQRLLSREIssMEKLHHPNIIRLYEVVETLSKLHLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvDQEKKAY 248
Cdd:cd14075    80 MEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHA-KRGETLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVV---NRRGHsqSADWWSYGVLMFEMLTGTLPFqgkdRNETM----NMILKAKLGMPQFLSAEAQSLL 321
Cdd:cd14075   159 TFCGSPPYAAPELFkdeHYIGI--YVDIWALGVLLYFMVTGVMPF----RAETVaklkKCILEGTYTIPSYVSEPCQELI 232
                         250       260
                  ....*....|....*....|....*
gi 1034674014 322 RMLFKRNPANRLgseGVEEIKRHLF 346
Cdd:cd14075   233 RGILQPVPSDRY---SIDEIKNSEW 254
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
90-332 5.38e-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: 159.46  E-value: 5.38e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKA---TGKLVAIKCIDKKALKGKE---DSLENEIAVlrKIKHPNIVQLLDIYESKSHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL---LDEIGHIKLTDFGLSKesVDQE 244
Cdd:cd14083    79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLgmpQF-------LSAEA 317
Cdd:cd14083   157 GVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEY---EFdspywddISDSA 233
                         250
                  ....*....|....*
gi 1034674014 318 QSLLRMLFKRNPANR 332
Cdd:cd14083   234 KDFIRHLMEKDPNKR 248
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
89-344 6.26e-44

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: 158.96  E-value: 6.26e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVflvrKKTGPDAGQLYAMKVLKKASLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14161     4 RYEFLETLGKGTYGRV----KKARDSSGRLVAIKSIRKDRIKdEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 247
Cdd:cd14161    80 VMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSN-LYNQDKFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSaEAQSLLRMLFK 326
Cdd:cd14161   159 QTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLM 237
                         250
                  ....*....|....*...
gi 1034674014 327 RNPANRlgsEGVEEIKRH 344
Cdd:cd14161   238 VNPERR---ATLEDVASH 252
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
89-332 6.34e-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: 6.34e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVL---TGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAy 248
Cdd:cd14072    78 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLD- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd14072   157 TFCGSPPYAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVL 236

                  ....*
gi 1034674014 328 NPANR 332
Cdd:cd14072   237 NPSKR 241
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
90-344 1.12e-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: 158.35  E-value: 1.12e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDV-KFYLAELALALDHLHQLGIVYRDLKPENILLDE-IGHIKLTDFGLSKeSVDQEKKA 247
Cdd:cd14074    82 ELGDGGDMYDYIMKHENGLNEDLaRKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSN-KFQPGEKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVnrRGHSQSA---DWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRML 324
Cdd:cd14074   161 ETSCGSLAYSAPEIL--LGDEYDApavDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRM 238
                         250       260
                  ....*....|....*....|
gi 1034674014 325 FKRNPANRLgseGVEEIKRH 344
Cdd:cd14074   239 LIRDPKKRA---SLEEIENH 255
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
443-699 1.14e-43

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: 158.61  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKsKRDPSE--------EIEIlMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSK-KKAPEDylqkflprEIEV-IKGLKHPNLICFYEAIETTSRVYIIM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAK-QLRGEN 593
Cdd:cd14162    80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLL-LDKN---NNLKITDFGFARgVMKTKD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 G---LLLTPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpNDTPEEILL-RIGNG-KFSLSggnwD 667
Cdd:cd14162   156 GkpkLSETYCGSYAYASPEILRGIPYDPfLSDIWSMGVVLYTMVYGRLPF----DDSNLKVLLkQVQRRvVFPKN----P 227
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 668 NISDGAKDLLSHMLHMDPhQRYTAEQILKHSW 699
Cdd:cd14162   228 TVSEECKDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
94-347 1.14e-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: 158.17  E-value: 1.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14189     7 RLLGKGGFARCY---EMTDLATNKTYAVKVIPHSRVaKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKaySF 250
Cdd:cd14189    84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAArlEPPEQRKK--TI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 330
Cdd:cd14189   162 CGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPG 241
                         250
                  ....*....|....*..
gi 1034674014 331 NRLgseGVEEIKRHLFF 347
Cdd:cd14189   242 DRL---TLDQILEHEFF 255
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
94-340 1.19e-43

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: 160.16  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKaslkvrdRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14092    12 EALGDGSFS---VCRKCVHKKTGQEFAVKIVSR-------RLDTSREVQLLRLCqGHPNIVKLHEVFQDELHTYLVMELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQEKKAyS 249
Cdd:cd14092    82 RGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQPLK-T 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRR----GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNE-TMNMILKAKLGMPQF-------LSAEA 317
Cdd:cd14092   161 PCFTLPYAAPEVLKQAlstqGYDESCDLWSLGVILYTMLSGQVPFQSPSRNEsAAEIMKRIKSGDFSFdgeewknVSSEA 240
                         250       260
                  ....*....|....*....|...
gi 1034674014 318 QSLLRMLFKRNPANRLGSEGVEE 340
Cdd:cd14092   241 KSLIQGLLTVDPSKRLTMSELRN 263
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
94-338 1.24e-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: 160.21  E-value: 1.24e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKaslkvrdRVRTKMERDI----LVEvNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14179    13 KPLGEGSFS---ICRKCLHKKTNQEYAVKIVSK-------RMEANTQREIaalkLCE-GHPNIVKLHEVYHDQLHTFLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd14179    82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET----MNMILKAKLGMPQF-------LSA 315
Cdd:cd14179   162 LKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTctsaEEIMKKIKQGDFSFegeawknVSQ 241
                         250       260
                  ....*....|....*....|...
gi 1034674014 316 EAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14179   242 EAKDLIQGLLTVDPNKRIKMSGL 264
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
89-332 1.56e-43

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: 157.83  E-value: 1.56e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLK--KASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVN---SDQKYAMKEIRlpKSSSAVED---SRKEAVLLAKMKHPNIVAFKESFEADGHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTR--LSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd08219    75 IVMEYCDGGDLMQKikLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrNETMNMILKAKLG----MPQFLSAEAQSL 320
Cdd:cd08219   155 AYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQA---NSWKNLILKVCQGsykpLPSHYSYELRSL 231
                         250
                  ....*....|..
gi 1034674014 321 LRMLFKRNPANR 332
Cdd:cd08219   232 IKQMFKRNPRSR 243
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
89-336 1.83e-43

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: 159.12  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14086     2 EYDLKEELGKGAFS---VVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd14086    79 FDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEAQSLL 321
Cdd:cd14086   159 AWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLI 238
                         250
                  ....*....|....*
gi 1034674014 322 RMLFKRNPANRLGSE 336
Cdd:cd14086   239 NQMLTVNPAKRITAA 253
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
443-699 2.93e-43

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: 157.76  E-value: 2.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPSE----EIEILMRYGqHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRhiiKEKKVKyvtiEKEVLSRLA-HPGIVKLYYTFQDESKLYFVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGL 595
Cdd:cd05581    82 YAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENIL-LDEDMH---IKITDFGTAKVLGPDSSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTP-----------------CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDTpeEILLRIGNGK 658
Cdd:cd05581   158 ESTKgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPF-RGSNEY--LTFQKIVKLE 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 659 FSLSggnwDNISDGAKDLLSHMLHMDPHQR------YTAEQILKHSW 699
Cdd:cd05581   235 YEFP----ENFPPDAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
89-332 2.96e-43

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: 157.43  E-value: 2.96e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpDAGQLyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKS--DSEHC-VIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHI-KLTDFGLSKESVDQEK 245
Cdd:cd08225    78 MEYCDGGDLMKRINRQrgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSME 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG--MPQFlSAEAQSLLRM 323
Cdd:cd08225   158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApiSPNF-SRDLRSLISQ 236

                  ....*....
gi 1034674014 324 LFKRNPANR 332
Cdd:cd08225   237 LFKVSPRDR 245
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
88-347 3.22e-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: 157.52  E-value: 3.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVN-------HPFIVKLHYAF 159
Cdd:cd14093     3 AKYEPKEILGRGVSSTVRrCIEKETG----QEFAVKIIDITGEKSSENEAEELREATRREIEilrqvsgHPNIIELHDVF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 239
Cdd:cd14093    79 ESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 sVDQEKKAYSFCGTVEYMAPEVV------NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK--LGMPQ 311
Cdd:cd14093   159 -LDEGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKyeFGSPE 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 312 F--LSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd14093   238 WddISDTAKDLISKLLVVDPKKRLTA---EEALEHPFF 272
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
89-332 4.22e-43

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: 157.98  E-value: 4.22e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvRKKTGPDAGQLYAMKVLKKASLKvrDRVRTKMERD-ILVEVN------HPFIVKLHYAFQT 161
Cdd:cd14096     2 NYRLINKIGEGAFSNVY--KAVPLRNTGKPVAIKVVRKADLS--SDNLKGSSRAnILKEVQimkrlsHPNIVKLLDFQES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL------------------- 222
Cdd:cd14096    78 DEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkaddd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 223 ---LDE-----------IGHIKLTDFGLSKESVDQEKKaySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTL 288
Cdd:cd14096   158 etkVDEgefipgvggggIGIVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 289 PFQGKDRNETMNMILKaklGMPQFL-------SAEAQSLLRMLFKRNPANR 332
Cdd:cd14096   236 PFYDESIETLTEKISR---GDYTFLspwwdeiSKSAKDLISHLLTVDPAKR 283
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
444-705 5.34e-43

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: 156.60  E-value: 5.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 444 ELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdKSKRDPSE------EIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFrkqllrELKTLRS-CESPYVVKCYGAFYKEGEISIVLEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrgENGLL 596
Cdd:cd06623    82 DGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLI----NSKGEVKIADFGISKVL--ENTLD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCY--TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNG-KFSLSGGNWdniSDGA 673
Cdd:cd06623   156 QCNTFvgTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGpPPSLPAEEF---SPEF 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWITHRDQ 705
Cdd:cd06623   233 RDFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
90-338 9.39e-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: 9.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRK-KTGPDAgqlyAMKVL-KKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSlHTGLEV----AIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVfTRLSKEVL--FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd14186    79 VLEMCHNGEM-SRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 325
Cdd:cd14186   158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLL 237
                         250
                  ....*....|...
gi 1034674014 326 KRNPANRLGSEGV 338
Cdd:cd14186   238 RKNPADRLSLSSV 250
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
90-336 1.10e-42

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: 155.96  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14167     5 YDFREVLGTGAFSEVVLAEEKR---TQKLVAIKCIAKKALEGKE---TSIENEIAVlhKIKHPNIVALDDIYESGGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL---LDEIGHIKLTDFGLSKESvDQE 244
Cdd:cd14167    79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIE-GSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA--KLGMPQF--LSAEAQSL 320
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAeyEFDSPYWddISDSAKDF 237
                         250
                  ....*....|....*.
gi 1034674014 321 LRMLFKRNPANRLGSE 336
Cdd:cd14167   238 IQHLMEKDPEKRFTCE 253
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
88-335 1.43e-42

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: 155.38  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKaslKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14087     1 AKYDIKALIGRGSFSRVVRVEHRV---TRQPYAIKMIET---KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGL-SKESVDQ 243
Cdd:cd14087    75 VMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLaSTRKKGP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM-PQF---LSAEAQS 319
Cdd:cd14087   155 NCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsGEPwpsVSNLAKD 234
                         250
                  ....*....|....*.
gi 1034674014 320 LLRMLFKRNPANRLGS 335
Cdd:cd14087   235 FIDRLLTVNPGERLSA 250
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
441-700 1.53e-42

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: 155.16  E-value: 1.53e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIID----KSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKaysaKEKENIRQEISI-MNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAKQLRGEnGL 595
Cdd:cd14191    81 VSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGT--KIKLIDFGLARRLENA-GS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTpeEILLRIGNGKFSLSGGNWDNISDGAKD 675
Cdd:cd14191   158 LKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFM-GDNDN--ETLANVTSATWDFDDEAFDEISDDAKD 234
                         250       260
                  ....*....|....*....|....*
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14191   235 FISNLLKKDMKARLTCTQCLQHPWL 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
89-367 1.54e-42

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: 156.25  E-value: 1.54e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVrtkmerDILVEV-NHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCIHKA---TGKEYAVKIIDKSKRDPSEEI------EILLRYgQHPNIITLRDVYDDGNSVYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL-DEIGH---IKLTDFGLSKESVDQ 243
Cdd:cd14091    72 VTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQLRAE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFqGKDRNETMNMILKaKLGMPQF---------LS 314
Cdd:cd14091   152 NGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILA-RIGSGKIdlsggnwdhVS 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 315 AEAQSLLRMLFKRNPANRLGSegvEEIKRHLFFANidWDKLYKREVQPPFKPA 367
Cdd:cd14091   230 DSAKDLVRKMLHVDPSQRPTA---AQVLQHPWIRN--RDSLPQRQLTDPQDAA 277
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
79-347 6.36e-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: 6.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  79 KEGYEKADPAQfellkVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLK----KASLKVRDRVR--TKMERDILVEV-NHPF 151
Cdd:cd14181     6 KEFYQKYDPKE-----VIGRGVSS---VVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVRssTLKEIHILRQVsGHPS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 152 IVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKL 231
Cdd:cd14181    78 IITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 232 TDFGLSKEsVDQEKKAYSFCGTVEYMAPEVV------NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA 305
Cdd:cd14181   158 SDFGFSCH-LEPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEG 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 306 K--LGMPQF--LSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd14181   237 RyqFSSPEWddRSSTVKDLISRLLVVDPEIRLTA---EQALQHPFF 279
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
439-700 7.73e-42

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: 153.55  E-value: 7.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELK--EDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYGQHPNIITLKDVFDDGRYV 510
Cdd:cd14197     5 FQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmeiiHEIAVLELAQANPWVINLHEVYETASEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRIL--KQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQ 588
Cdd:cd14197    85 ILVLEYAAGGEIFNQCVadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGD-IKIVDFGLSRI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGL---LLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGN 665
Cdd:cd14197   164 LKNSEELreiMGTPEY----VAPEILSYEPISTATDMWSIGVLAYVMLTGISPFL---GDDKQETFLNISQMNVSYSEEE 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 666 WDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14197   237 FEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
442-701 8.21e-42

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: 153.14  E-value: 8.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-KSKRDPSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRlRKQNKELIINEIlIMKECKHPNIVDYYDSYLVGDELWVVMEYMDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDRI-LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesaSAD-SIRICDFGFAKQLRGE----N 593
Cdd:cd06614    81 GSLTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL-----SKDgSVKLADFGFAAQLTKEkskrN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPcYtanFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG-NGKFSLSGGNwdNISDG 672
Cdd:cd06614   156 SVVGTP-Y---WMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYL---EEPPLRALFLITtKGIPPLKNPE--KWSPE 226
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06614   227 FKDFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
443-700 8.77e-42

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: 153.40  E-value: 8.77e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK--RDPSE-----EIEILMRYgQHPNIITLKDVFD--DGRyVYLV 513
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKapDDFVEkflprELEILARL-NHKSIIKTYEIFEtsDGK-VYIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQL-RGE 592
Cdd:cd14165    81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDF----NIKLTDFGFSKRClRDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NG---LLLTPCYTANFVAPEVLMQQGYDAAC-DIWSLGVLFYTMLAGYTPFangpNDTPEEILLRIgNGKFSLSGGNWDN 668
Cdd:cd14165   157 NGrivLSKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPY----DDSNVKKMLKI-QKEHRVRFPRSKN 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14165   232 LTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
90-333 1.17e-41

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: 152.54  E-value: 1.17e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHIL---TGEKVAIKIMDKKALG-DDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRL-SKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL-SKESVDQEKKA 247
Cdd:cd14078    81 EYCPGGELFDYIvAKDRL-SEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGGMDHHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQS-ADWWSYGVLMFEMLTGTLPFqgkDRNETMNM---ILKAKLGMPQFLSAEAQSLLRM 323
Cdd:cd14078   160 ETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPF---DDDNVMALyrkIQSGKYEEPEWLSPSSKLLLDQ 236
                         250
                  ....*....|
gi 1034674014 324 LFKRNPANRL 333
Cdd:cd14078   237 MLQVDPKKRI 246
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
443-700 1.26e-41

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: 152.80  E-value: 1.26e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSvcKRCI--HATTNMEFAVKIIDKSK-------RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05578     2 FQILRVIGKGSFG--KVCIvqKKDTKKMFAMKYMNKQKciekdsvRNVLNELEILQEL-EHPFLVNLWYSFQDEEDMYMV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASAdsiRICDFGFAKQLRgEN 593
Cdd:cd05578    79 VDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNIL-LDEQGHV---HITDFNIATKLT-DG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGnWdniSDGA 673
Cdd:cd05578   154 TLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRAKFETASVLYPAG-W---SEEA 229
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 674 KDLLSHMLHMDPHQRY-TAEQILKHSWI 700
Cdd:cd05578   230 IDLINKLLERDPQKRLgDLSDLKNHPYF 257
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
96-333 1.27e-41

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: 153.09  E-value: 1.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLYAMKVL---KKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14097     9 LGQGSFGVVI---EATHKETQTKWAIKKInreKAGSSAVKLLER---EVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL--------DEIgHIKLTDFGLS--KESVD 242
Cdd:cd14097    83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnnDKL-NIKVTDFGLSvqKYGLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 qEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQ 318
Cdd:cd14097   162 -EDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAK 240
                         250
                  ....*....|....*
gi 1034674014 319 SLLRMLFKRNPANRL 333
Cdd:cd14097   241 NVLQQLLKVDPAHRM 255
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
449-699 2.53e-41

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: 151.99  E-value: 2.53e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPSEEI----EILMRyGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhivQTRQQEHIfsekEILEE-CNSPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLlTPCY 601
Cdd:cd05572    80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLL-LDSNGY---VKLVDFGFAKKLGSGRKTW-TFCG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDTP----EEILLRIGNGKFSlsggnwDNISDGAKDLL 677
Cdd:cd05572   155 TPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPF-GGDDEDPmkiyNIILKGIDKIEFP------KYIDKNAKNLI 227
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 678 SHMLHMDPHQRY-----TAEQILKHSW 699
Cdd:cd05572   228 KQLLRRNPEERLgylkgGIRDIKKHKW 254
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
443-700 3.04e-41

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: 151.39  E-value: 3.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-------RDP-----SEEIEIL--MRYGQHPNIITLKDVFDDGR 508
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdtwvRDRklgtvPLEIHILdtLNKRSHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 509 YVYLVTDLMKGG-ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAK 587
Cdd:cd14004    82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVI-LDGNG---TIKLIDFGSAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QLrgENGLLLTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFANgpndtPEEIL---LRIGNGkfslsg 663
Cdd:cd14004   158 YI--KSGPFDTFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFYN-----IEEILeadLRIPYA------ 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 664 gnwdnISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14004   225 -----VSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
94-347 3.66e-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: 151.32  E-value: 3.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKvRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd14188     7 KVLGKGGFAKCY---EMTDLTTNKVYAAKIIPHSRVS-KPHQREKIDKEIELHriLHHKHVVQFYHYFEDKENIYILLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 251
Cdd:cd14188    83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTIC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd14188   163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPED 242
                         250
                  ....*....|....*.
gi 1034674014 332 RlgsEGVEEIKRHLFF 347
Cdd:cd14188   243 R---PSLDEIIRHDFF 255
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
89-332 3.99e-41

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: 151.47  E-value: 3.99e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVflvRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14098     1 KYQIIDRLGSGTFAEV---KKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQReiNILKSLEHPGIVRLIDWYEDDQHIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG--HIKLTDFGLSKeSVDQE 244
Cdd:cd14098    78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAK-VIHTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRR------GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL----S 314
Cdd:cd14098   157 TFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVdfniS 236
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd14098   237 EEAIDFILRLLDVDPEKR 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
89-347 6.31e-41

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: 150.50  E-value: 6.31e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDrVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14079     3 NYILGKTLGVGSFGKVKLAEHEL---TGHKVAVKILNRQKIKSLD-MEEKIRREIqiLKLFRHPHIIRLYEVIETPTDIF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd14079    79 MVMEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSfCGTVEYMAPEVVNRRGHSQS-ADWWSYGVLMFEMLTGTLPFqgkDRNETMNMILKAKLGM---PQFLSAEAQSLLR 322
Cdd:cd14079   159 KTS-CGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPF---DDEHIPNLFKKIKSGIytiPSHLSPGARDLIK 234
                         250       260
                  ....*....|....*....|....*
gi 1034674014 323 MLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14079   235 RMLVVDPLKRI---TIPEIRQHPWF 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
90-332 6.56e-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: 150.64  E-value: 6.56e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVD---GRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 247
Cdd:cd08529    79 EYAENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRMLFK 326
Cdd:cd08529   159 QTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKyPPISASYSQDLSQLIDSCLT 238

                  ....*.
gi 1034674014 327 RNPANR 332
Cdd:cd08529   239 KDYRQR 244
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
443-700 8.80e-41

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: 149.98  E-value: 8.80e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSslqklfREVRI-MKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLRGENGlL 596
Cdd:cd14072    81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLL-LDADM---NIKIADFGFSNEFTPGNK-L 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFaNGPNdtPEEILLRIGNGKFSLSGgnwdNISDGAKD 675
Cdd:cd14072   156 DTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPF-DGQN--LKELRERVLRGKYRIPF----YMSTDCEN 228
                         250       260
                  ....*....|....*....|....*
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14072   229 LLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
443-700 9.25e-41

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: 150.59  E-value: 9.25e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS-----EEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd06610     3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSmdelrKEIQA-MSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLD---RILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFA-------- 586
Cdd:cd06610    82 SGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILL----GEDGSVKIADFGVSaslatggd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLRGENGLLLTPCYtanfVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNGKFSLSGGN 665
Cdd:cd06610   158 RTRKVRKTFVGTPCW----MAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYP---PMKVLMLTLQNDPPSLETG 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 666 WDN--ISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06610   231 ADYkkYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
443-700 1.03e-40

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: 150.04  E-value: 1.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS----KRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPhesdKETVRKEIQI-MNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQK-CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIlyMDESASADSIRICDFGFAKQLRGENGLLL 597
Cdd:cd14114    83 GGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENI--MCTTKRSNEVKLIDFGLATHLDPKESVKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDtpEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd14114   161 TTG-TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFA-GEND--DETLRNVKSCDWNFDDSAFSGISEEAKDFI 236
                         250       260
                  ....*....|....*....|...
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14114   237 RKLLLADPNKRMTIHQALEHPWL 259
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
89-332 1.04e-40

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: 150.07  E-value: 1.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd06627     1 NYQLGDLIGRGAFGSVY---KGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAY 248
Cdd:cd06627    78 LEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK-AKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:cd06627   158 SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQdDHPPLPENISPELRDFLLQCFQK 237

                  ....*
gi 1034674014 328 NPANR 332
Cdd:cd06627   238 DPTLR 242
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
439-700 2.97e-40

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: 148.97  E-value: 2.97e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELkediGVGSYSVCKRCIHATTNMEFAVKIIDKS--KRDP-SEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14113     9 YSEVAEL----GRGRFSVVKKCDQRGTKRAVATKFVNKKlmKRDQvTHELGVLQSL-QHPQLVGLLDTFETPTSYILVLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLRGE--- 592
Cdd:cd14113    84 MADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENIL-VDQSLSKPTIKLADFGDAVQLNTTyyi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTPcytaNFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDG 672
Cdd:cd14113   163 HQLLGSP----EFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFL---DESVEETCLNICRLDFSFPDDYFKGVSQK 235
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14113   236 AKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
89-332 3.27e-40

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: 148.74  E-value: 3.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKV--LKKASlkVRDRVRTKMERDILVEVNHPFIVKLHYAFQTE-GKL 165
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRD---RKQYVIKKlnLKNAS--KRERKAAEQEAKLLSKLKHPNIVSYKESFEGEdGFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLS--KEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd08223    76 YIVMGFCEGGDLYTRLKeqKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL-GMPQFLSAEAQSLLR 322
Cdd:cd08223   156 SDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIK 235
                         250
                  ....*....|
gi 1034674014 323 MLFKRNPANR 332
Cdd:cd08223   236 AMLHQDPEKR 245
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
94-333 3.95e-40

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: 148.65  E-value: 3.95e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKaslkvrdRVRTKMER-DILVEV-------NHPFIVKLHYAFQTEGKL 165
Cdd:cd14106    14 TPLGRGKFA---VVRKCIHKETGKEYAAKFLRK-------RRRGQDCRnEILHEIavlelckDCPRVVNLHEVYETRSEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKeSVD 242
Cdd:cd14106    84 ILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISR-VIG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL----SAEAQ 318
Cdd:cd14106   163 EGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAI 242
                         250
                  ....*....|....*
gi 1034674014 319 SLLRMLFKRNPANRL 333
Cdd:cd14106   243 DFIKRLLVKDPEKRL 257
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
99-347 5.56e-40

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: 148.08  E-value: 5.56e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  99 GSFGKVFLVRKktgPDAGQLYAMKVLKKASLKVRDRvRTKMERDIlvevnhPFIVKLHYAFQTEGKLYLILDFLRGGDVF 178
Cdd:cd05576    10 GVIDKVLLVMD---TRTQETFILKGLRKSSEYSRER-KTIIPRCV------PNMVCLRKYIISEESVFLVLQHAEGGKLW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 179 TRLSKEV-------LFT---------------EEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05576    80 SYLSKFLndkeihqLFAdlderlaaasrfyipEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDqekkaySFCG-TVE--YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ----GKDRNETMNmilkaklgM 309
Cdd:cd05576   160 WSEVED------SCDSdAIEnmYCAPEVGGISEETEACDWWSLGALLFELLTGKALVEchpaGINTHTTLN--------I 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANRLGS--EGVEEIKRHLFF 347
Cdd:cd05576   226 PEWVSEEARSLLQQLLQFNPTERLGAgvAGVEDIKSHPFF 265
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
443-700 5.66e-40

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: 147.92  E-value: 5.66e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-RDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiEDEQDmvrirrEIEIMSSL-NHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAkQLRGENGL 595
Cdd:cd14073    82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENIL-LDQNG---NAKIADFGLS-NLYSKDKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFaNGPNDTpeeILLR-IGNGKF----SLSggnwdni 669
Cdd:cd14073   157 LQTFCGSPLYASPEIVNGTPYQGPeVDCWSLGVLLYTLVYGTMPF-DGSDFK---RLVKqISSGDYreptQPS------- 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 sdGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14073   226 --DASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
90-344 6.30e-40

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: 147.54  E-value: 6.30e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDAgqlYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTE---VAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAyS 249
Cdd:cd14071    79 EYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLK-T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRN 328
Cdd:cd14071   158 WCGSPPYAAPEVFEgKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLD 237
                         250
                  ....*....|....*.
gi 1034674014 329 PANRLgseGVEEIKRH 344
Cdd:cd14071   238 PSKRL---TIEQIKKH 250
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
470-696 6.93e-40

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: 147.30  E-value: 6.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIDKSKRDPS------EEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQK-CFSEREASDILY 542
Cdd:cd13999    20 AIKKLKVEDDNDEllkefrREVSI-LSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLLHKKKiPLSWSLRLKIAL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 543 VISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDI 622
Cdd:cd13999    99 DIARGMNYLHSPPIIHRDLKSLNIL-LDEN---FTVKIADFGLSRIKNSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADV 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 623 WSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGKFSLSGgnwDNISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd13999   175 YSFGIVLWELLTGEVPFKELSP--IQIAAAVVQKGLRPPIP---PDCPPELSKLIKRCWNEDPEKRPSFSEIVK 243
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
90-333 7.52e-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: 148.02  E-value: 7.52e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDR--VRTKMERD--ILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKS---TGLEYAAKFIKKRRSKASRRgvSREDIEREvsILRQVLHPNIITLHDVFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDE----IGHIKLTDFGLSKEsV 241
Cdd:cd14105    84 VLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHK-I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL----SAEA 317
Cdd:cd14105   163 EDGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYfsntSELA 242
                         250
                  ....*....|....*.
gi 1034674014 318 QSLLRMLFKRNPANRL 333
Cdd:cd14105   243 KDFIRQLLVKDPRKRM 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
88-336 7.65e-40

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: 148.11  E-value: 7.65e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14169     3 SVYELKEKLGEGAFSEVVLAQER---GSQRLVALKCIPKKALRGKEAM-VENEIAVLRRINHENIVSLEDIYESPTHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD---EIGHIKLTDFGLSKesVDQE 244
Cdd:cd14169    79 AMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA--KLGMPQF--LSAEAQSL 320
Cdd:cd14169   157 GMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAeyEFDSPYWddISESAKDF 236
                         250
                  ....*....|....*.
gi 1034674014 321 LRMLFKRNPANRLGSE 336
Cdd:cd14169   237 IRHLLERDPEKRFTCE 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
90-347 8.82e-40

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: 147.49  E-value: 8.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd06605     3 LEYLGELGEGNGGVVSKVRHRP---SGQIMAVKVIR-LEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDvFTRLSKEVLFTEEDvkfYLAELALA----LDHLH-QLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQe 244
Cdd:cd06605    79 EYMDGGS-LDKILKEVGRIPER---ILGKIAVAvvkgLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 kKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI--LKAKLGMP------QFLSAE 316
Cdd:cd06605   154 -LAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFelLSYIVDEPppllpsGKFSPD 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 317 AQSLLRMLFKRNPANRlgsEGVEEIKRHLFF 347
Cdd:cd06605   233 FQDFVSQCLQKDPTER---PSYKELMEHPFI 260
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
94-337 1.11e-39

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: 147.42  E-value: 1.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVflvRKKTGPDAGQLYAMKVLKKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd14192    10 EVLGGGRFGQV---HKCTELSTGLTLAAKIIKVKGAKEREEV--KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIGH-IKLTDFGLSKESVDQEKKAYSF 250
Cdd:cd14192    85 GGELFDRITDESYqLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 cGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 326
Cdd:cd14192   165 -GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLV 243
                         250
                  ....*....|.
gi 1034674014 327 RNPANRLGSEG 337
Cdd:cd14192   244 KEKSCRMSATQ 254
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
443-700 1.17e-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: 148.01  E-value: 1.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD---PS---EEIEILMRYgQHPNIITLKDVFDDGRYVYLV--- 513
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegiPStalREISLLKEL-KHPNIVKLLDVIHTENKLYLVfey 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 --TDLMKggeLLDRILKQkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRg 591
Cdd:cd07829    80 cdQDLKK---YLDKRPGP--LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLL-INRD---GVLKLADFGLARAFG- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 englLLTPCYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIgngkFSLSG-- 663
Cdd:cd07829   150 ----IPLRTYTHEVVtlwyrAPEILLgSKHYSTAVDIWSVGCIFAELITGKPLF---PGDSEIDQLFKI----FQILGtp 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 664 -----------GNWD----------------NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07829   219 teeswpgvtklPDYKptfpkwpkndlekvlpRLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
96-290 1.81e-39

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: 146.68  E-value: 1.81e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgPDAGQLYAMKVLKKASL-----KVRDRVRTkmERDILVEVNHPFIVKLHYAFQTE-GKLYLIL 169
Cdd:cd13994     1 IGKGATSVVRIVTKKN-PRSGVLYAVKEYRRRDDeskrkDYVKRLTS--EYIISSKLHHPNIVKVLDLCQDLhGKWCLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS-KESVDQEKKAY 248
Cdd:cd13994    78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKESP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 249 SF---CGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd13994   158 MSaglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPW 203
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
441-700 2.22e-39

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: 146.16  E-value: 2.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS-------EEIEILMRYgQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAgmvqrvrNEVEIHCQL-KHPSILELYNYFEDSNYVYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELlDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRG 591
Cdd:cd14186    80 LEMCHNGEM-SRYLKNrkKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLL----TRNMNIKIADFGLATQLKM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSggnwDNISD 671
Cdd:cd14186   155 PHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPF---DTDTVKNTLNKVVLADYEMP----AFLSR 227
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14186   228 EAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
94-332 2.91e-39

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: 146.12  E-value: 2.91e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVflvRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd14070     8 RKLGEGSFAKV---REGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRREgrIQQMIRHPNITQLLDILETENSYYLVMEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAYS 249
Cdd:cd14070    85 CPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcaGILGYSDPFST 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD---RNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 326
Cdd:cd14070   165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfslRALHQKMVDKEMNPLPTDLSPGAISFLRSLLE 244

                  ....*.
gi 1034674014 327 RNPANR 332
Cdd:cd14070   245 PDPLKR 250
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
449-699 4.14e-39

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: 145.10  E-value: 4.14e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDK--SKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRI 526
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKkmKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 527 LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLRGE---NGLLLTPcyta 603
Cdd:cd14115    81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQISGHrhvHHLLGNP---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 604 NFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHM 683
Cdd:cd14115   156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFL---DESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQE 232
                         250
                  ....*....|....*.
gi 1034674014 684 DPHQRYTAEQILKHSW 699
Cdd:cd14115   233 DPRRRPTAATCLQHPW 248
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
441-701 6.73e-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: 145.47  E-value: 6.73e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-KSKRDPSEEI--EILMRYGQH-PNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDlEEAEDEIEDIqqEIQFLSQCDsPYITKYYGSFLKGSKLWIIMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRgengll 596
Cdd:cd06609    81 CGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEG----DVKLADFGVSGQLT------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFV------APEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRI-GNGKFSLSGGNWdni 669
Cdd:cd06609   150 STMSKRNTFVgtpfwmAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLS---DLHPMRVLFLIpKNNPPSLEGNKF--- 223
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06609   224 SKPFKDFVELCLNKDPKERPSAKELLKHKFIK 255
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
443-711 7.57e-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: 7.57e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSY-SVCKrCIHATTNMEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDVF-----DDGRYV 510
Cdd:cd07834     2 YELLKPIGSGAYgVVCS-AYDKRTGRKVAIKKISNVFDDLIDakrilrEIKIL-RHLKHENIIGLLDILrppspEEFNDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMkggEL-LDRILKqkcfSEREASD-----ILYVISKTVDYLHCQGVVHRDLKPSNILymdesASAD-SIRICDF 583
Cdd:cd07834    80 YIVTELM---ETdLHKVIK----SPQPLTDdhiqyFLYQILRGLKYLHSAGVIHRDLKPSNIL-----VNSNcDLKICDF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQLRG-ENGLLLTPcytanFV------APEVLMQ-QGYDAACDIWSLGVLFYTMLAGyTPFANGPN----------- 644
Cdd:cd07834   148 GLARGVDPdEDKGFLTE-----YVvtrwyrAPELLLSsKKYTKAIDIWSVGCIFAELLTR-KPLFPGRDyidqlnlivev 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 645 -DTP-EEILLRIGNGKF-----SLS---GGNWDNISDG----AKDLLSHMLHMDPHQRYTAEQILKHSWI-THRDqlPND 709
Cdd:cd07834   222 lGTPsEEDLKFISSEKArnylkSLPkkpKKPLSEVFPGaspeAIDLLEKMLVFNPKKRITADEALAHPYLaQLHD--PED 299

                  ..
gi 1034674014 710 QP 711
Cdd:cd07834   300 EP 301
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
91-332 1.68e-38

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: 143.84  E-value: 1.68e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014   91 ELLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLKK-ASLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTlKGKGDGKEVEVAVKTLKEdASEQQIEEFL--REARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  169 LDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVDQEK 245
Cdd:smart00221  80 MEYMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDlYDDDYY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRM 323
Cdd:smart00221 160 KVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYrLPKPPNCPPELYKLMLQ 239

                   ....*....
gi 1034674014  324 LFKRNPANR 332
Cdd:smart00221 240 CWAEDPEDR 248
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
89-306 1.73e-38

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: 144.18  E-value: 1.73e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPdaGQLYAMKVLKKASLKVRdrvRTKMERD-----ILVEVN-------HPFIVKLH 156
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKSNG--QTLLALKEINMTNPAFG---RTEQERDksvgdIISEVNiikeqlrHPNIVRYY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQTEGKLYLILDFLRG---GDVFTRL-SKEVLFTEEDVKFYLAELALALDHLH-QLGIVYRDLKPENILLDEIGHIKL 231
Cdd:cd08528    76 KTFLENDRLYIVMELIEGaplGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTI 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 232 TDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK 306
Cdd:cd08528   156 TDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAE 230
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
89-344 3.29e-38

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: 142.99  E-value: 3.29e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKAsLKVRDRVrtkmERDIL--VEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNK---ETKELVAVKYIERG-LKIDENV----QREIInhRSLRHPNIIRFKEVVLTPTHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD--EIGHIKLTDFGLSKESVDQE 244
Cdd:cd14662    73 IVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVLHS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAySFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQGKD--RN--ETMNMILKAKLGMPQF--LSAEA 317
Cdd:cd14662   153 QPK-STVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDdpKNfrKTIQRIMSVQYKIPDYvrVSQDC 231
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 318 QSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14662   232 RHLLSRIFVANPAKRI---TIPEIKNH 255
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
441-700 3.93e-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: 142.79  E-value: 3.93e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSY-SVCKrCIHATTNMEFAVKI--IDKSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd06612     3 EVFDILEKLGEGSYgSVYK-AIHKETGQVVAIKVvpVEEDLQEIIKEISI-LKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRI-LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASAdsiRICDFGFAKQLRGENG-- 594
Cdd:cd06612    81 GAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNIL-LNEEGQA---KLADFGVSGQLTDTMAkr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 --LLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNG---KFSlSGGNWdni 669
Cdd:cd06612   157 ntVIGTPFW----MAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIH---PMRAIFMIPNKpppTLS-DPEKW--- 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06612   226 SPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
443-699 3.99e-38

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: 142.60  E-value: 3.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKR-DPSEEIEIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKiDENVQREIInHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsADSIRICDFGFAK------QLRGENG 594
Cdd:cd14662    82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSP-APRLKICDFGYSKssvlhsQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 lllTPCYtanfVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFANgPNDtPEEI---LLRIGNGKFSLSggNWDNIS 670
Cdd:cd14662   160 ---TPAY----IAPEVLSRKEYDGkVADVWSCGVTLYVMLVGAYPFED-PDD-PKNFrktIQRIMSVQYKIP--DYVRVS 228
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14662   229 QDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
89-349 4.08e-38

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: 143.15  E-value: 4.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKV--LKKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGIdKRTN----QVVAIKVidLEEAEDEIEDIQQ---EIQFLSQCDSPYITKYYGSFLKGSKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTrLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd06609    75 WIIMEYCGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA---KLGMPQFlSAEAQSLLR 322
Cdd:cd06609   154 KRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNnppSLEGNKF-SKPFKDFVE 232
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 323 MLFKRNPANRLGSegvEEIKRHLFFAN 349
Cdd:cd06609   233 LCLNKDPKERPSA---KELLKHKFIKK 256
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
447-700 4.95e-38

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: 142.79  E-value: 4.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFAVKIID----KSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKvkgaKEREEVKNEINI-MNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKcFSEREASDILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDESAsaDSIRICDFGFAKQLRGENGLLLTpC 600
Cdd:cd14192    89 FDRITDES-YQLTELDAILFTrqICEGVHYLHQHYILHLDLKPENILCVNSTG--NQIKIIDFGLARRYKPREKLKVN-F 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd14192   165 GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFL---GETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRL 241
                         250       260
                  ....*....|....*....|
gi 1034674014 681 LHMDPHQRYTAEQILKHSWI 700
Cdd:cd14192   242 LVKEKSCRMSATQCLKHEWL 261
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
96-345 4.96e-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: 142.46  E-value: 4.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRtkmERDILVEVN-HPFIVKLH-YAFQTEGKLYLILDFLR 173
Cdd:cd13987     1 LGEGTYGKVLLAVHKG---SGTKMALKFVPKPSTKLKDFLR---EYNISLELSvHPHIIKTYdVAFETEDYYVFAQEYAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL--DEIGHIKLTDFGLSKeSVDQEKKAYSfc 251
Cdd:cd13987    75 YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTR-RVGSTVKRVS-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHS-----QSADWWSYGVLMFEMLTGTLPFQ---GKDRNETMNM-ILKAKLGMP--QF--LSAEAQ 318
Cdd:cd13987   152 GTIPYTAPEVCEAKKNEgfvvdPSIDVWAFGVLLFCCLTGNFPWEkadSDDQFYEEFVrWQKRKNTAVpsQWrrFTPKAL 231
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 319 SLLRMLFKRNPaNRLGSegVEEIKRHL 345
Cdd:cd13987   232 RMFKKLLAPEP-ERRCS--IKEVFKYL 255
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
96-340 5.55e-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: 143.86  E-value: 5.55e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKaslkvrdRVRTKMERDI----LVEvNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd14180    14 LGEGSFS---VCRKCRHRQSGQEYAVKIISR-------RMEANTQREVaalrLCQ-SHPNIVALHEVLHDQYHTYLVMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGLSKESVDQEKKAY 248
Cdd:cd14180    83 LRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN-------ETMNMILKAKLGMP----QFLSAEA 317
Cdd:cd14180   163 TPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEgeawKGVSEEA 242
                         250       260
                  ....*....|....*....|...
gi 1034674014 318 QSLLRMLFKRNPANRLGSEGVEE 340
Cdd:cd14180   243 KDLVRGLLTVDPAKRLKLSELRE 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
96-333 6.17e-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: 142.04  E-value: 6.17e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGPDagQLYAMKVLKKASLK--VRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd14121     3 LGSGTYATVYKAYRKSGAR--EVVAVKCVSKSSLNkaSTENLLTEIE--LLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDV--FTRlSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG--HIKLTDFGLSKeSVDQEKKAYS 249
Cdd:cd14121    79 GGDLsrFIR-SRRTL-PESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQ-HLKPNDEAHS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK-LGMPQF--LSAEAQSLLRMLFK 326
Cdd:cd14121   156 LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQ 235

                  ....*..
gi 1034674014 327 RNPANRL 333
Cdd:cd14121   236 RDPDRRI 242
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
449-701 7.72e-38

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: 142.36  E-value: 7.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIdkSKRDPSE---------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVI--KKRDMIRknqvdsvlaERNILSQA-QNPFVVKLYYSFQGKKNLYLVMEYLPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLdRILKQ-KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAK----------- 587
Cdd:cd05579    78 GDLY-SLLENvGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILI----DANGHLKLTDFGLSKvglvrrqikls 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 --------QLRGENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGpnDTPEEILLRIGNGKF 659
Cdd:cd05579   153 iqkksngaPEKEDRRIVGTPDY----LAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPF-HA--ETPEEIFQNILNGKI 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 660 slsggNW---DNISDGAKDLLSHMLHMDPHQR---YTAEQILKHSWIT 701
Cdd:cd05579   226 -----EWpedPEVSDEAKDLISKLLTPDPEKRlgaKGIEEIKNHPFFK 268
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
441-699 8.02e-38

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: 141.78  E-value: 8.02e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKED--IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYL 512
Cdd:cd14082     1 QLYQIFPDevLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQesqlrnEVAILQQL-SHPGVVNLECMFETPERVFV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGgELLDRILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdSIRICDFGFAKQLr 590
Cdd:cd14082    80 VMEKLHG-DMLEMILSSEKgrLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFP-QVKLCDFGFARII- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangpnDTPEEILLRIGNGKFSLSGGNWDNIS 670
Cdd:cd14082   157 GEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDINDQIQNAAFMYPPNPWKEIS 231
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14082   232 PDAIDLINNLLQVKMRKRYSVDKSLSHPW 260
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
89-290 1.02e-37

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: 141.63  E-value: 1.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd06612     4 VFDILEKLGEGSYGSVYKAIHK---ETGQVVAIKVVPVEE----DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGG---DVFTRLSKEvlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd06612    77 MEYCGAGsvsDIMKITNKT--LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd06612   155 KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY 199
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
90-338 1.10e-37

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: 141.82  E-value: 1.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVL-------------KKASLKVRDRVRTKMERDILVEVNHPFIVKLH 156
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIR---TGEKCAIKIIprasnaglkkereKRLEKEISRDIRTIREAALSSLLNHPHICRLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd14077    80 DFLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKeSVDQEKKAYSFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSA 315
Cdd:cd14077   160 SN-LYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSS 238
                         250       260
                  ....*....|....*....|...
gi 1034674014 316 EAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14077   239 ECKSLISRMLVVDPKKRATLEQV 261
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
443-699 1.32e-37

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: 142.16  E-value: 1.32e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILM------RYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLnekrilQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLRGENgll 596
Cdd:cd14209    83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLL-ID---QQGYIKVTDFGFAKRVKGRT--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGnwdnISDGAKDL 676
Cdd:cd14209   156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKIVSGKVRFPSH----FSSDLKDL 228
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 677 LSHMLHMDPHQRY-----TAEQILKHSW 699
Cdd:cd14209   229 LRNLLQVDLTKRFgnlknGVNDIKNHKW 256
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
443-699 2.44e-37

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: 143.19  E-value: 2.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPS----EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSdmlKREQIahvrAERDILADA-DSPWIVRLHYAFQDEDHLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLR--GEN 593
Cdd:cd05573    82 YMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNIL-LDADGH---IKLADFGLCTKMNksGDR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLL---------------------------TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDT 646
Cdd:cd05573   158 ESYLndsvntlfqdnvlarrrphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFY---SDS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 647 PEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLhMDPHQRYT-AEQILKHSW 699
Cdd:cd05573   235 LVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGsAEEIKAHPF 287
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
94-335 2.54e-37

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: 140.44  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMerDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKR---TGLKLAAKVINKQNSKDKEMVLLEI--QVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL-DEIGH-IKLTDFGLSKESVDQEKKAYSF 250
Cdd:cd14190    85 GGELFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNPREKLKVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 cGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 326
Cdd:cd14190   165 -GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVSNLII 243

                  ....*....
gi 1034674014 327 RNPANRLGS 335
Cdd:cd14190   244 KERSARMSA 252
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
96-337 2.93e-37

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: 140.20  E-value: 2.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGPDagQLYAMKVLKKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKPD--LPVAIKCITKKNLSKSQNLLGK-EIKILKELSHENVVALLDCQETSSSVYLVMEYCNGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG---------HIKLTDFGLSKeSVDQEKK 246
Cdd:cd14120    78 DLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFAR-FLQDGMM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRM 323
Cdd:cd14120   157 AATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIpsgTSPALKDLLLG 236
                         250
                  ....*....|....
gi 1034674014 324 LFKRNPANRLGSEG 337
Cdd:cd14120   237 LLKRNPKDRIDFED 250
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
448-701 3.82e-37

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: 140.57  E-value: 3.82e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----------------------RDPSE----EIEILMRYgQHPNIITL 500
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKllkqagffrrppprrkpgalgkpLDPLDrvyrEIAILKKL-DHPNVVKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 501 KDVFDDGR--YVYLVTDLMKGGELLdRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSI 578
Cdd:cd14118    80 VEVLDDPNedNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDG----HV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 579 RICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYD---AACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG 655
Cdd:cd14118   155 KIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFE---DDHILGLHEKIK 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 656 NGkfSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14118   232 TD--PVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
447-700 4.61e-37

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: 139.66  E-value: 4.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFAVKIID----KSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKarsqKEKEEVKNEIEV-MNQLNHANLIQLYDAFESRNDIVLVMEYVDGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKcFSEREASDILYV--ISKTVDYLHCQGVVHRDLKPSNILYMdeSASADSIRICDFGFAKQLRGENGLLLTpC 600
Cdd:cd14193    89 FDRIIDEN-YNLTELDTILFIkqICEGIQYMHQMYILHLDLKPENILCV--SREANQVKIIDFGLARRYKPREKLRVN-F 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTpeEILLRIGNGKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd14193   165 GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFL-GEDDN--ETLNNILACQWDFEDEEFADISEEAKDFISKL 241
                         250       260
                  ....*....|....*....|
gi 1034674014 681 LHMDPHQRYTAEQILKHSWI 700
Cdd:cd14193   242 LIKEKSWRMSASEALKHPWL 261
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
90-348 4.69e-37

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: 140.95  E-value: 4.69e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLAEERA---TGKLFAVKCIPKKALKGKE---SSIENEIAVlrKIKHENIVALEDIYESPNHLYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQE 244
Cdd:cd14168    86 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSfCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA--KLGMPQF--LSAEAQSL 320
Cdd:cd14168   166 VMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyEFDSPYWddISDSAKDF 244
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 321 LRMLFKRNPANRlgsEGVEEIKRHLFFA 348
Cdd:cd14168   245 IRNLMEKDPNKR---YTCEQALRHPWIA 269
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
443-701 4.83e-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: 140.49  E-value: 4.83e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK--------------------------RDPSE----EIEILMRYg 492
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraapegctqpRGPIErvyqEIAILKKL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 493 QHPNIITLKDVFDDGR--YVYLVTDLMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMD 570
Cdd:cd14199    83 DHPNVVKLVEVLDDPSedHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 571 ESasadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYD---AACDIWSLGVLFYTMLAGYTPFANgpndtp 647
Cdd:cd14199   162 DG----HIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSETRKIfsgKALDVWAMGVTLYCFVFGQCPFMD------ 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 648 EEILL---RIGNGKFSLSggNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14199   232 ERILSlhsKIKTQPLEFP--DQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
94-346 5.44e-37

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: 139.46  E-value: 5.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLvrkKTGPDAGQLYAMKVLKKASL-KVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd06632     6 QLLGSGSFGSVYE---GFNGDTGDFFAVKEVSLVDDdKKSRESVKQLEQEIalLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQeKKAYSF 250
Cdd:cd06632    83 YVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRR--GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL--GMPQFLSAEAQSLLRMLFK 326
Cdd:cd06632   162 KGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLCLQ 241
                         250       260
                  ....*....|....*....|
gi 1034674014 327 RNPANRlgsEGVEEIKRHLF 346
Cdd:cd06632   242 RDPEDR---PTASQLLEHPF 258
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
443-688 5.93e-37

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 141.49  E-value: 5.93e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-------RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkmkqvQHVAQEKSILMEL-SHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENgl 595
Cdd:PTZ00263   99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLL-LDNKGH---VKVTDFGFAKKVPDRT-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 lLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggNWdnISDGAKD 675
Cdd:PTZ00263  173 -FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFF---DDTPFRIYEKILAGRLKFP--NW--FDGRARD 244
                         250
                  ....*....|...
gi 1034674014 676 LLSHMLHMDPHQR 688
Cdd:PTZ00263  245 LVKGLLQTDHTKR 257
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
89-338 6.00e-37

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: 139.40  E-value: 6.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14184     2 KYKIGKVIGDGNFA---VVKECVERSTGKEFALKIIDKAKCCGKEHL-IENEVSILRRVKHPNIIMLIEEMDTPAELYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----DEIGHIKLTDFGLSKESvdqE 244
Cdd:cd14184    78 MELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV---E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD--RNETMNMILKAKLGMPQ----FLSAEAQ 318
Cdd:cd14184   155 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSpywdNITDSAK 234
                         250       260
                  ....*....|....*....|
gi 1034674014 319 SLLRMLFKRNPANRLGSEGV 338
Cdd:cd14184   235 ELISHMLQVNVEARYTAEQI 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
90-333 6.03e-37

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: 139.77  E-value: 6.03e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDR--VRTKMERD--ILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKS---TGLQYAAKFIKKRRTKSSRRgvSREDIEREvsILKEIQHPNVITLHEVYENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG----HIKLTDFGLSKEsV 241
Cdd:cd14194    84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHK-I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEA 317
Cdd:cd14194   163 DFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeyfsNTSALA 242
                         250
                  ....*....|....*.
gi 1034674014 318 QSLLRMLFKRNPANRL 333
Cdd:cd14194   243 KDFIRRLLVKDPKKRM 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
90-332 6.49e-37

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: 139.17  E-value: 6.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFL-VRKKTGPDAGQLYAMKVLKKASlkvRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLY 166
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKgTLKGEGENTKIKVAVKTLKEGA---DEEEREDFLEEASImkKLDHPNIVKLLGVCTQGEPLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDV--FTRLSKEVLFTEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKesvDQE 244
Cdd:pfam07714  78 IVTEYMPGGDLldFLRKHKRKLTLKDLLSM-ALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR---DIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGT-----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEA 317
Cdd:pfam07714 154 DDDYYRKRGggklpIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGYrLPQPENCPDEL 233
                         250
                  ....*....|....*
gi 1034674014 318 QSLLRMLFKRNPANR 332
Cdd:pfam07714 234 YDLMKQCWAYDPEDR 248
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
449-699 6.91e-37

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: 138.93  E-value: 6.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSK--RDPS------EEIEILMRYgQHPNIITLKDVFDDGRY--VYLVTDLMK 518
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrRIPNgeanvkREIQILRRL-NHRNVIKLVDVLYNEEKqkLYMVMEYCV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GG--ELLDRIlKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLR--GENG 594
Cdd:cd14119    80 GGlqEMLDSA-PDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLL----TTDGTLKISDFGVAEALDlfAEDD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDA--ACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDG 672
Cdd:cd14119   155 TCTTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFE---GDNIYKLFENIGKGEYTIP----DDVDPD 227
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14119   228 LQDLLRGMLEKDPEKRFTIEQIRQHPW 254
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
96-344 7.10e-37

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: 139.80  E-value: 7.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVR----------------DRVRTKMER-----DILVEVNHPFIVK 154
Cdd:cd14118     2 IGKGSYGIVKLAYNE---EDNTLYAMKILSKKKLLKQagffrrppprrkpgalGKPLDPLDRvyreiAILKKLDHPNVVK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 155 LHYAFQ--TEGKLYLILDFLRGGDVFtRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLT 232
Cdd:cd14118    79 LVEVLDdpNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 233 DFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQS---ADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM 309
Cdd:cd14118   158 DFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVF 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 310 PQ--FLSAEAQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14118   238 PDdpVVSEQLKDLILRMLDKNPSERI---TLPEIKEH 271
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
89-344 7.28e-37

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: 138.96  E-value: 7.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKAslkvrDRVRTKMERDIL--VEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQ---TKELVAVKYIERG-----EKIDENVQREIInhRSLRHPNIVRFKEVILTPTHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD--EIGHIKLTDFGLSKESV--D 242
Cdd:cd14665    73 IVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVlhS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKkaySFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQG----KDRNETMNMILKAKLGMPQF--LSA 315
Cdd:cd14665   153 QPK---STVGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYvhISP 229
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 316 EAQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14665   230 ECRHLISRIFVADPATRI---TIPEIRNH 255
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
443-699 7.76e-37

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: 138.88  E-value: 7.76e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID---KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvraKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVVIIVTELCHE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 gELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDEsaSADSIRICDFGFAKQLR-GEnglllt 598
Cdd:cd14108    83 -ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQ--KTDQVRICDFGNAQELTpNE------ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCY----TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDtpEEILLRIGNGKFSLSGGNWDNISDGAK 674
Cdd:cd14108   154 PQYckygTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFV-GEND--RTTLMNIRNYNVAFEESMFKDLCREAK 230
                         250       260
                  ....*....|....*....|....*
gi 1034674014 675 DLLSHMLHMDpHQRYTAEQILKHSW 699
Cdd:cd14108   231 GFIIKVLVSD-RLRPDAEETLEHPW 254
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
443-700 8.62e-37

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: 139.16  E-value: 8.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTN-----MEFAVKIIDKSK-RDPSEEIEI-----LMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd14076     3 YILGRTLGEGEFGKVKLGWPLPKAnhrsgVQVAIKLIRRDTqQENCQTSKImreinILKGLTHPNIVRLLDVLKTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRG 591
Cdd:cd14076    83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLL-LDKN---RNLVITDFGFANTFDH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENG-LLLTPCYTANFVAPE-VLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFANGP-NDTPEEI--LLR-IGNGKFSLSgg 664
Cdd:cd14076   159 FNGdLMSTSCGSPCYAAPElVVSDSMYAGrKADIWSCGVILYAMLAGYLPFDDDPhNPNGDNVprLYRyICNTPLIFP-- 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 665 nwDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14076   237 --EYVTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
443-699 1.08e-36

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: 138.58  E-value: 1.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKR-DPSEEIEIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKiDENVQREIInHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdESASADSIRICDFGFAK------QLRGENG 594
Cdd:cd14665    82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLL--DGSPAPRLKICDFGYSKssvlhsQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 lllTPCYtanfVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFANgPNDTPE--EILLRIGNGKFSLSggNWDNISD 671
Cdd:cd14665   160 ---TPAY----IAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFED-PEEPRNfrKTIQRILSVQYSIP--DYVHISP 229
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14665   230 ECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
447-699 1.11e-36

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: 138.58  E-value: 1.11e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEF-AVKIIDKSKRDPS------EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSKSSLNKAstenllTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMdeSASADSIRICDFGFAK---------QLR 590
Cdd:cd14121    80 GDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLS--SRYNPVLKLADFGFAQhlkpndeahSLR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GenglllTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGK-FSLSGGnwDNI 669
Cdd:cd14121   158 G------SPLY----MAPEMILKKKYDARVDLWSVGVILYECLFGRAPFA---SRSFEELEEKIRSSKpIEIPTR--PEL 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14121   223 SADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
449-698 1.15e-36

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: 138.68  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIID------KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd08530     8 LGKGSYGSVYKVKRLSDNQVYALKEVNlgslsqKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIVMEYAPFGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKC----FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDesasADSIRICDFGFAKQLRgeNGLLLT 598
Cdd:cd08530    87 SKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSA----GDLVKIGDLGISKVLK--KNLAKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGpnDTPEEILLRIGNGKFSLSGGNWdniSDGAKDLLS 678
Cdd:cd08530   161 QIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPF-EA--RTMQELRYKVCRGKFPPIPPVY---SQDLQQIIR 234
                         250       260
                  ....*....|....*....|
gi 1034674014 679 HMLHMDPHQRYTAEQILKHS 698
Cdd:cd08530   235 SLLQVNPKKRPSCDKLLQSP 254
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
91-332 1.15e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 138.43  E-value: 1.15e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014   91 ELLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLKK-ASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlKGKGGKKKVEVAVKTLKEdASEQQIEEFLR--EARIMRKLDHPNVVKLLGVCTEEEPLYIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  169 LDFLRGGDV--FTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVDQEK 245
Cdd:smart00219  80 MEYMEGGDLlsYLRKNRPKL-SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDlYDDDYY 158
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRM 323
Cdd:smart00219 159 RKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYrLPQPPNCPPELYDLMLQ 238

                   ....*....
gi 1034674014  324 LFKRNPANR 332
Cdd:smart00219 239 CWAEDPEDR 247
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
89-332 1.15e-36

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: 138.71  E-value: 1.15e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDAGQLyamKVLKKAS---LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKATADEEL---KVLKEISvgeLQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLS----KEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEiGHIKLTDFGLSKESV 241
Cdd:cd08222    78 CIVTEYCEGGDLDDKISeykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRILM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL-GMPQFLSAEAQSL 320
Cdd:cd08222   157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAI 236
                         250
                  ....*....|..
gi 1034674014 321 LRMLFKRNPANR 332
Cdd:cd08222   237 YSRMLNKDPALR 248
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
96-347 1.30e-36

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: 138.76  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVflvRKKTGPDAGQLYAMKVL--KKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQT-EGKLYLILDFL 172
Cdd:cd14165     9 LGEGSYAKV---KSAYSERLKCNVAIKIIdkKKAPDDFVEKFLPR-ELEILARLNHKSIIKTYEIFETsDGKVYIVMELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV-DQEKK---AY 248
Cdd:cd14165    85 VQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLrDENGRivlSK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVnrRGHS---QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ--FLSAEAQSLLRM 323
Cdd:cd14165   165 TFCGSAAYAAPEVL--QGIPydpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRskNLTSECKDLIYR 242
                         250       260
                  ....*....|....*....|....
gi 1034674014 324 LFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14165   243 LLQPDVSQRL---CIDEVLSHPWL 263
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
94-335 1.41e-36

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: 138.51  E-value: 1.41e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd14193    10 EILGGGRFGQVHKCEEKS---SGLKLAAKIIKARSQKEKEEV--KNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL--DEIGHIKLTDFGLSKESVDQEKKAYSF 250
Cdd:cd14193    85 GGELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKPREKLRVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 cGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 326
Cdd:cd14193   165 -GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEEAKDFISKLLI 243

                  ....*....
gi 1034674014 327 RNPANRLGS 335
Cdd:cd14193   244 KEKSWRMSA 252
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
82-347 1.59e-36

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: 138.89  E-value: 1.59e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  82 YEKADPAQfellkVLGQGSFGkvfLVRKKTGPDAGQLYAMKVL------KKASLKVRD-RVRTKMERDILVEVN-HPFIV 153
Cdd:cd14182     2 YEKYEPKE-----ILGRGVSS---VVRRCIHKPTRQEYAVKIIditgggSFSPEEVQElREATLKEIDILRKVSgHPNII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 154 KLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd14182    74 QLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKEsVDQEKKAYSFCGTVEYMAPEVV------NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA-- 305
Cdd:cd14182   154 FGFSCQ-LDPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGny 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 306 KLGMPQF--LSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd14182   233 QFGSPEWddRSDTVKDLISRFLVVQPQKRYTA---EEALAHPFF 273
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
439-700 1.66e-36

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: 138.52  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYEL-KEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKR------DPSEEIEILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd14198     5 FNNFYILtSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRgqdcraEILHEIAVLELAKSNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQL 589
Cdd:cd14198    85 LILEYAAGGEIFNLCVPDlaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGD-IKIVDFGMSRKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 rGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtpEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd14198   164 -GHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDN---QETFLNISQVNVDYSEETFSSV 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14198   240 SQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
52-363 1.83e-36

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 143.62  E-value: 1.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  52 DEPMEEGEADSchDEGVVKEIPITHHVKEGYEKADPAQ--FELLKVLGQGSFGKVFLVRKKTGPdagqlyAMKVLKKASL 129
Cdd:PTZ00267   31 EEAFEKYCADL--DPEAYKKCVDLPEGEEVPESNNPREhmYVLTTLVGRNPTTAAFVATRGSDP------KEKVVAKFVM 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 130 KVRDRVRT--KMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALAL 203
Cdd:PTZ00267  103 LNDERQAAyaRSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDlnkqIKQRLKEHLPFQEYEVGLLFYQIVLAL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 204 DHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK--KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMF 281
Cdd:PTZ00267  183 DEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSldVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILY 262
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 282 EMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHLFFANIDWDKLYKREV 360
Cdd:PTZ00267  263 ELLTLHRPFKGPSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFLKYVANLFQDIVRHSET 342

                  ...
gi 1034674014 361 QPP 363
Cdd:PTZ00267  343 ISP 345
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
449-698 1.91e-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: 1.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIH-ATTNMEFAVKIID-----KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd14120     1 IGHGAFAVVFKGRHrKKPDLPVAIKCITkknlsKSQNLLGKEIKILKEL-SHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIL----YMDESASAD-SIRICDFGFAKQLRGeNGLLL 597
Cdd:cd14120    80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILlshnSGRKPSPNDiRLKIADFGFARFLQD-GMMAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDtpeeilLRigngKFSLSGGNWD-NI----SD 671
Cdd:cd14120   159 TLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFqAQTPQE------LK----AFYEKNANLRpNIpsgtSP 228
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd14120   229 ALKDLLLGLLKRNPKDRIDFEDFFSHP 255
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
90-332 2.62e-36

Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 137.87  E-value: 2.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRK-KTGpdagQLYAMKVLKKASLKVRD----RVRTKM-ERDILVEV-NHPFIVKLHYAFQTE 162
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDlRTG----RKYAIKCLYKSGPNSKDgndfQKLPQLrEIDLHRRVsRHPNIITLHDVFETE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFT--RLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI-GHIKLTDFGLSKe 239
Cdd:cd13993    78 VAIYIVLEYCPNGDLFEaiTENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 svdQEKKAYSF-CGTVEYMAPEVVNRRGHSQ------SADWWSYGVLMFEMLTGTLPFQ--GKDRNETMNMILKAKLGMP 310
Cdd:cd13993   157 ---TEKISMDFgVGSEFYMAPECFDEVGRSLkgypcaAGDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPNLFD 233
                         250       260
                  ....*....|....*....|....
gi 1034674014 311 QFL--SAEAQSLLRMLFKRNPANR 332
Cdd:cd13993   234 VILpmSDDFYNLLRQIFTVNPNNR 257
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
90-332 2.69e-36

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: 137.51  E-value: 2.69e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKV---DGCLYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGG---DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG----LSKESV 241
Cdd:cd13997    79 MELCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGlatrLETSGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEkkaysfcGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGT-LPFQGKDRNEtmnmILKAKLGMP--QFLSAEA 317
Cdd:cd13997   159 VEE-------GDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEpLPRNGQQWQQ----LRQGKLPLPpgLVLSQEL 227
                         250
                  ....*....|....*
gi 1034674014 318 QSLLRMLFKRNPANR 332
Cdd:cd13997   228 TRLLKVMLDPDPTRR 242
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
443-701 3.76e-36

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: 137.85  E-value: 3.76e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD---PSE---EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEggiPNQalrEIKALQACQGHPYVVKLRDVFPHGTGFVLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGelLDRILK--QKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENG 594
Cdd:cd07832    82 MLSS--LSEVLRdeERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLI----SSTGVLKIADFGLARLFSEEDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTP-CYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGyTPFANGPND------------TPEE-------ILLR 653
Cdd:cd07832   156 RLYSHqVATRWYRAPELLYgSRKYDEGVDLWAVGCIFAELLNG-SPLFPGENDieqlaivlrtlgTPNEktwpeltSLPD 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 654 IGNGKFSLSGGN-WDNI----SDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd07832   235 YNKITFPESKGIrLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
90-333 4.51e-36

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: 136.94  E-value: 4.51e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERA---TGNNFAAKFIMTPHESDKETVRK--EIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKE-VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD--EIGHIKLTDFGLSKEsVDQEKK 246
Cdd:cd14114    79 EFLSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH-LDPKES 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLR 322
Cdd:cd14114   158 VKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIR 237
                         250
                  ....*....|.
gi 1034674014 323 MLFKRNPANRL 333
Cdd:cd14114   238 KLLLADPNKRM 248
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
90-347 4.53e-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: 137.04  E-value: 4.53e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKAslKVRDRVRTK-MERDILV--EVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTK---HKCKVAIKIVSKK--KAPEDYLQKfLPREIEVikGLKHPNLICFYEAIETTSRVY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK---ESVDQ 243
Cdd:cd14162    77 IIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgvmKTKDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKK-AYSFCGTVEYMAPEVVnrRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMP--QFLSAEA 317
Cdd:cd14162   157 KPKlSETYCGSYAYASPEIL--RGipyDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR-RVVFPknPTVSEEC 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 318 QSLL-RML---FKRNPanrlgsegVEEIKRHLFF 347
Cdd:cd14162   234 KDLIlRMLspvKKRIT--------IEEIKRDPWF 259
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
443-701 5.42e-36

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: 137.39  E-value: 5.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK---------RDPS---------------------EEIEILMRYg 492
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygfprRPPPrgskaaqgeqakplaplervyQEIAILKKL- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 493 QHPNIITLKDVFDDGRY--VYLVTDLMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMD 570
Cdd:cd14200    81 DHVNIVKLIEVLDDPAEdnLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 571 ESasadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYD---AACDIWSLGVLFYTMLAGYTPFANgpndtp 647
Cdd:cd14200   160 DG----HVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSfsgKALDVWAMGVTLYCFVYGKCPFID------ 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 648 EEILL---RIGNGKFSLSGGnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14200   230 EFILAlhnKIKNKPVEFPEE--PEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
95-338 6.70e-36

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: 137.55  E-value: 6.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMErdILVEV-NHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd14090     9 LLGEGAYASVQTCINLY---TGKEYAVKIIEKHPGHSRSRVFREVE--TLHQCqGHPNILQLIEYFEDDERFYLVFEKMR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL---LDEIGHIKLTDFGLSKESVDQEKKA--- 247
Cdd:cd14090    84 GGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKLSSTSMtpv 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 -----YSFCGTVEYMAPEVVNR-RGHSQS----ADWWSYGVLMFEMLTGTLPFQGK-------DRNET----MNMILKA- 305
Cdd:cd14090   164 ttpelLTPVGSAEYMAPEVVDAfVGEALSydkrCDLWSLGVILYIMLCGYPPFYGRcgedcgwDRGEAcqdcQELLFHSi 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 306 KLGMPQF-------LSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14090   244 QEGEYEFpekewshISAEAKDLISHLLVRDASQRYTAEQV 283
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
443-700 7.34e-36

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: 136.49  E-value: 7.34e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-RDPSEEIEILMRYGQ------HPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKaKKDSYVTKNLRREGRiqqmirHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRGENGL 595
Cdd:cd14070    84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLL-LDEN---DNIKLIDFGLSNCAGILGYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 --LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTpEEILLRIGNGKFS-LSGGnwdnISDG 672
Cdd:cd14070   160 dpFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSL-RALHQKMVDKEMNpLPTD----LSPG 234
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14070   235 AISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
86-332 7.40e-36

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: 137.47  E-value: 7.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLK-KASLKVRDRVrtkMERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd06644     9 DPNEvWEIIGELGDGAFGKVYKAKNK---ETGALAAAKVIEtKSEEELEDYM---VEIEILATCNHPYIVKLLGAFYWDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06644    83 KLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVV-----NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK---LGMPQFLS 314
Cdd:cd06644   163 TLQRRDSFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWS 242
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd06644   243 MEFRDFLKTALDKHPETR 260
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
443-700 7.75e-36

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: 136.42  E-value: 7.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-------KSKRDPSEEIEI-----------LMRYGQHPNIITLKDVF 504
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglKKEREKRLEKEIsrdirtireaaLSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 505 DDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFG 584
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL-ISKS---GNIKIIDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 585 FAKQLRGENgLLLTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFangpNDTPEEIL-LRIGNGKFSLS 662
Cdd:cd14077   159 LSNLYDPRR-LLRTFCGSLYFAAPELLQAQPYTGPeVDVWSFGVVLYVLVCGKVPF----DDENMPALhAKIKKGKVEYP 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 663 ggNWdnISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14077   234 --SY--LSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
94-332 8.07e-36

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: 136.28  E-value: 8.07e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd06626     6 NKIGEGTFGKVYTA---VNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ-----EKKAY 248
Cdd:cd06626    83 EGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNtttmaPGEVN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDrNETMNMIlkaKLGM---PQF-----LSAEA 317
Cdd:cd06626   163 SLVGTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWSELD-NEWAIMY---HVGMghkPPIpdslqLSPEG 238
                         250
                  ....*....|....*
gi 1034674014 318 QSLLRMLFKRNPANR 332
Cdd:cd06626   239 KDFLSRCLESDPKKR 253
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
443-645 1.08e-35

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: 136.29  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATT-NMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14202     4 FSRKDLIGHGAFAVVFKGRHKEKhDLEVAVKCINKKNLAKSQtllgkEIKILKEL-KHENIVALYDFQEIANSVYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDES---ASADSIRI--CDFGFAKQLRG 591
Cdd:cd14202    83 CNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrkSNPNNIRIkiADFGFARYLQN 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 592 eNGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPND 645
Cdd:cd14202   163 -NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFqASSPQD 216
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
95-333 1.18e-35

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: 136.12  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLvrkktGPDA--GQLYAMK--VLKKASLKVRDRVRT-----KMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd06628     7 LIGSGSFGSVYL-----GMNAssGELMAVKqvELPSVSAENKDRKKSmldalQREIALLRELQHENIVQYLGSSSDANHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE------ 239
Cdd:cd06628    82 NIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleansl 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRnetMNMILK----AKLGMPQFLSA 315
Cdd:cd06628   162 STKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ---MQAIFKigenASPTIPSNISS 238
                         250       260
                  ....*....|....*....|...
gi 1034674014 316 EAQSLLRMLF-----KRNPANRL 333
Cdd:cd06628   239 EARDFLEKTFeidhnKRPTADEL 261
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
90-344 1.20e-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: 136.24  E-value: 1.20e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDR--VRTKMER--DILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKS---TGLEYAAKFIKKRQSRASRRgvSREEIERevSILRQVLHPNIITLHDVYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENI-LLDE---IGHIKLTDFGLSKESV 241
Cdd:cd14196    84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKnipIPHIKLIDFGLAHEIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM-PQFLSAE---A 317
Cdd:cd14196   164 DGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdEEFFSHTselA 242
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 318 QSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14196   243 KDFIRKLLVKETRKRL---TIQEALRH 266
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
90-347 1.29e-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: 136.51  E-value: 1.29e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKmERDILVEVN-HPFIVKLHYAFQTEGKLYLI 168
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNK---ETGELVAIKKMKKKFYSWEECMNLR-EVKSLRKLNeHPNIVKLKEVFRENDELYFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGgDVF--TRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQEKK 246
Cdd:cd07830    77 FEYMEG-NLYqlMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI--RSRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AY-SFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGkdRNET--MNMI-----------------LKA 305
Cdd:cd07830   154 PYtDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPG--SSEIdqLYKIcsvlgtptkqdwpegykLAS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 306 KLG--MPQFL-----------SAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd07830   232 KLGfrFPQFAptslhqlipnaSPEAIDLIKDMLRWDPKKRPTA---SQALQHPYF 283
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
441-700 1.69e-35

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: 135.33  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYEL-KEDIGVGSYSVCKRCIHATTNMEFAVKIIdksKRDPS--EEIEIlMRYGQHPNIITLKDVFDD-GRYVYLVTDL 516
Cdd:cd14109     3 ELYEIgEEDEKRAAQGAPFHVTERSTGRNFLAQLR---YGDPFlmREVDI-HNSLDHPNIVQMHDAYDDeKLAVTVIDNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRIL---KQKCfSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDesasaDSIRICDFGFAKQLrgEN 593
Cdd:cd14109    79 ASTIELVRDNLlpgKDYY-TERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD-----DKLKLADFGQSRRL--LR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCY-TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTpeEILLRIGNGKFSLSGGNWDNISDG 672
Cdd:cd14109   151 GKLTTLIYgSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFL-GDNDR--ETLTNVRSGKWSFDSSPLGNISDD 227
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14109   228 ARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
86-357 1.93e-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: 1.93e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQF-ELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLK-KASLKVRDRVrtkMERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd06611     2 NPNDIwEIIGELGDGAFGKVYKAQHKE---TGLFAAAKIIQiESEEELEDFM---VEIDILSECKHPNIVGLYEAYFYEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06611    76 KLWILIEFCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPfqgkdRNET--MNMILK------AKLGM 309
Cdd:cd06611   156 TLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPP-----HHELnpMRVLLKilksepPTLDQ 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFFANIDWDKLYK 357
Cdd:cd06611   231 PSKWSSSFNDFLKSCLVKDPDDRPTA---AELLKHPFVSDQSDNKAIK 275
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
94-336 2.74e-35

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: 135.06  E-value: 2.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASlKVRDrVRTKMERDILV---EVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd14197    15 RELGRGKFA---VVRKCVEKDSGKEFAAKFMRKRR-KGQD-CRMEIIHEIAVlelAQANPWVINLHEVYETASEMILVLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRL--SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDE---IGHIKLTDFGLSKeSVDQEK 245
Cdd:cd14197    90 YAAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSespLGDIKIVDFGLSR-ILKNSE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLL 321
Cdd:cd14197   169 ELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSeeefEHLSESAIDFI 248
                         250
                  ....*....|....*
gi 1034674014 322 RMLFKRNPANRLGSE 336
Cdd:cd14197   249 KTLLIKKPENRATAE 263
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
94-347 3.65e-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: 3.65e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVL------KKASLKVRdrvrtKMERDI--LVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd06625     6 KLLGQGAFGQVYLCYDA---DTGRELAVKQVeidpinTEASKEVK-----ALECEIqlLKNLQHERIVQYYGCLQDEKSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQ 243
Cdd:cd06625    78 SIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILK-----AKLGMPQFLSAEAQ 318
Cdd:cd06625   158 STGMKSVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWA---EFEPMAAIFKiatqpTNPQLPPHVSEDAR 234
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 319 SLLRMLFKRNPANRlgsEGVEEIKRHLFF 347
Cdd:cd06625   235 DFLSLIFVRNKKQR---PSAEELLSHSFV 260
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
94-332 3.90e-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: 134.29  E-value: 3.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLKKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14187    13 RFLGKGGFAKCYEI---TDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL-SKESVDQEKKAySFC 251
Cdd:cd14187    90 RRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLaTKVEYDGERKK-TLC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd14187   169 GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA 248

                  .
gi 1034674014 332 R 332
Cdd:cd14187   249 R 249
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
94-332 4.50e-35

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: 134.20  E-value: 4.50e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLkvrDRVRTKMERDILV--EVNHPFIVKLhYAFQTE-GKLYLILD 170
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDAS---ESERKDFLKEARVmkKLGHPNVVRL-LGVCTEeEPLYLVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVL---------FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsV 241
Cdd:cd00192    77 YMEGGDLLDFLRKSRPvfpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD-I 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK-AKLGMPQFLSAE 316
Cdd:cd00192   156 YDDDYYRKKTGGklpIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKgYRLPKPENCPDE 235
                         250
                  ....*....|....*.
gi 1034674014 317 AQSLLRMLFKRNPANR 332
Cdd:cd00192   236 LYELMLSCWQLDPEDR 251
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
446-700 5.60e-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: 133.89  E-value: 5.60e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 446 KEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd14190     9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEmvllEIQV-MNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMdeSASADSIRICDFGFAKQLRGENGLLLTpC 600
Cdd:cd14190    88 LFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCV--NRTGHQVKIIDFGLARRYNPREKLKVN-F 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTpeEILLRIGNGKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd14190   165 GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFL-GDDDT--ETLNNVLMGNWYFDEETFEHVSDEAKDFVSNL 241
                         250       260
                  ....*....|....*....|
gi 1034674014 681 LHMDPHQRYTAEQILKHSWI 700
Cdd:cd14190   242 IIKERSARMSATQCLKHPWL 261
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
443-699 5.99e-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: 5.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSY-SVCKrCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd07830     1 YKVIKQLGDGTFgSVYL-ARNKETGELVAIKKMKKKFYSWEEcmnlrEVKSLRKLNEHPNIVKLKEVFRENDELYFVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGgELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMdesaSADSIRICDFGFAKQLRGEng 594
Cdd:cd07830    80 MEG-NLYQLMKDRkgKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVS----GPEVVKIADFGLAREIRSR-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 llltPCYTAnFV------APEVLMQQG-YDAACDIWSLGVLF---YTMlagyTPFANGPNDTPEeiLLRIgngkFSLSG- 663
Cdd:cd07830   153 ----PPYTD-YVstrwyrAPEILLRSTsYSSPVDIWALGCIMaelYTL----RPLFPGSSEIDQ--LYKI----CSVLGt 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 664 -GNWD----------------------------NISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07830   218 pTKQDwpegyklasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
443-645 1.04e-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: 133.60  E-value: 1.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIH-ATTNMEFAVKIIDKSKRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQillgkEIKILKEL-QHENIVALYDVQEMPNSVFLVMEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIL--YMDESASADS---IRICDFGFAKQLRg 591
Cdd:cd14201    87 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILlsYASRKKSSVSgirIKIADFGFARYLQ- 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPND 645
Cdd:cd14201   166 SNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFqANSPQD 220
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
86-354 1.16e-34

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: 133.61  E-value: 1.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQF-ELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKaslKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd06643     2 NPEDFwEIVGELGDGAFGKVYKAQNK---ETGILAAAKVIDT---KSEEELEDYMvEIDILASCDHPNIVKLLDAFYYEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06643    76 NLWILIEFCAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVV-----NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK---LGMPQFLS 314
Cdd:cd06643   156 TLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWS 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 315 AEAQSLLRMLFKRNPANRLGSegvEEIKRHLFFANIDWDK 354
Cdd:cd06643   236 PEFKDFLRKCLEKNVDARWTT---SQLLQHPFVSVLVSNK 272
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
96-333 1.33e-34

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: 132.82  E-value: 1.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVF-LVRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd14191    10 LGSGKFGQVFrLVEKKTK----KVWAGKFFKAYSAKEKENIRQEIS--IMNCLHHPKLVQCVDAFEEKANIVMVLEMVSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIG-HIKLTDFGLSK--ESVDQEKKAYs 249
Cdd:cd14191    84 GELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARrlENAGSLKVLF- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 fcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLF 325
Cdd:cd14191   163 --GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKDFISNLL 240

                  ....*...
gi 1034674014 326 KRNPANRL 333
Cdd:cd14191   241 KKDMKARL 248
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
92-344 1.45e-34

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: 132.99  E-value: 1.45e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFL--VRKKTGPDAGQLYAMKVLKKASLKVRDRVrTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14076     5 LGRTLGEGEFGKVKLgwPLPKANHRSGVQVAIKLIRRDTQQENCQT-SKIMREIniLKGLTHPNIVRLLDVLKTKKYIGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVDQEKK 246
Cdd:cd14076    84 VLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRG--HSQSADWWSYGVLMFEMLTGTLPF-------QGKDRNETMNMILKAKLGMPQFLSAEA 317
Cdd:cd14076   164 MSTSCGSPCYAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKA 243
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 318 QSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14076   244 RDLLRRILVPNPRKRI---RLSAIMRH 267
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
99-349 1.78e-34

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 132.67  E-value: 1.78e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  99 GSFGKVFLVRKKTGPdagQLYAMKVLKKaslkvrdrvrtKMERDILVEV-----NHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:PHA03390   27 GKFGKVSVLKHKPTQ---KLFVQKIIKA-----------KNFNAIEPMVhqlmkDNPNFIKLYYSVTTLKGHVLIMDYIK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDE-IGHIKLTDFGLSK----ESVDQekkay 248
Cdd:PHA03390   93 DGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLCDYGLCKiigtPSCYD----- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 sfcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNE-----TMNMILKAKLGMPQFLSAEAQSLLRM 323
Cdd:PHA03390  168 ---GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK-EDEDEeldleSLLKRQQKKLPFIKNVSKNANDFVQS 243
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 324 LFKRNPANRLGSegVEEIKRHLFFAN 349
Cdd:PHA03390  244 MLKYNINYRLTN--YNEIIKHPFLKI 267
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
430-711 1.83e-34

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: 134.73  E-value: 1.83e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 430 VQINGNAAQFGEVYELKEDIGVGSY-SVCKrCIHATTNMEFAVKIIDK-------SKRdPSEEIEILmRYGQHPNIITLK 501
Cdd:cd07851     4 QELNKTVWEVPDRYQNLSPVGSGAYgQVCS-AFDTKTGRKVAIKKLSRpfqsaihAKR-TYRELRLL-KHMKHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 502 DVF------DDGRYVYLVTDLMkgGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasa 575
Cdd:cd07851    81 DVFtpasslEDFQDVYLVTHLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDC--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 576 dSIRICDFGFAKQLRGE-NGLLLTPCYTanfvAPEVL---MQqgYDAACDIWSLGVLFYTMLAGYTPF-ANGPND----- 645
Cdd:cd07851   156 -ELKILDFGLARHTDDEmTGYVATRWYR----APEIMlnwMH--YNQTVDIWSVGCIMAELLTGKTLFpGSDHIDqlkri 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 646 -----TP-EEILLRIG-----------------NGKFSLSGGNWDNIsdgakDLLSHMLHMDPHQRYTAEQILKHSWIT- 701
Cdd:cd07851   229 mnlvgTPdEELLKKISsesarnyiqslpqmpkkDFKEVFSGANPLAI-----DLLEKMLVLDPDKRITAAEALAHPYLAe 303
                         330
                  ....*....|
gi 1034674014 702 HRDqlPNDQP 711
Cdd:cd07851   304 YHD--PEDEP 311
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
476-704 2.11e-34

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: 134.07  E-value: 2.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 476 KSKRDPSEEIeilmrygQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQG 555
Cdd:cd05584    48 KAERNILEAV-------KHPFIVDLHYAFQTGGKLYLILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 556 VVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAG 635
Cdd:cd05584   121 IIYRDLKPENIL-LDAQGH---VKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTG 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 636 YTPF-ANGPNDTPEEILlrigNGKFSLSggnwDNISDGAKDLLSHMLHMDPHQRY-----TAEQILKHSWITHRD 704
Cdd:cd05584   197 APPFtAENRKKTIDKIL----KGKLNLP----PYLTNEARDLLKKLLKRNVSSRLgsgpgDAEEIKAHPFFRHIN 263
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
96-293 2.26e-34

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: 132.19  E-value: 2.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd13978     1 LGSGGFGTVSKARHV---SWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHQL--GIVYRDLKPENILLDEIGHIKLTDFGLSK-----ESVDQEKKA 247
Cdd:cd13978    78 SLKSLLEREIQDVPWSLRFRIIhEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 248 YSFCGTVEYMAPEV---VNRRGHSQSaDWWSYGVLMFEMLTGTLPFQGK 293
Cdd:cd13978   158 ENLGGTPIYMAPEAfddFNKKPTSKS-DVYSFAIVIWAVLTRKEPFENA 205
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
89-353 2.50e-34

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: 133.05  E-value: 2.50e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRT---KMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14094     4 VYELCEVIGKGPFS---VVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTedlKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSK 238
Cdd:cd14094    81 YMVFEFMDGADlcfeIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKdRNETMNMILKAKLGM--PQF--LS 314
Cdd:cd14094   161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMnpRQWshIS 239
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 315 AEAQSLLRMLFKRNPANRLgseGVEEIKRHLFFANIDWD 353
Cdd:cd14094   240 ESAKDLVRRMLMLDPAERI---TVYEALNHPWIKERDRY 275
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
441-701 2.71e-34

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: 132.00  E-value: 2.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS-------EEIEIlMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAgvehqlrREVEI-QSHLRHPNILRLYGYFHDATRVYLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAkqLRGEN 593
Cdd:cd14116    84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL----GSAGELKIADFGWS--VHAPS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGA 673
Cdd:cd14116   158 SRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFE---ANTYQETYKRISRVEFTFP----DFVTEGA 230
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14116   231 RDLISRLLKHNPSQRPMLREVLEHPWIT 258
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
443-697 3.33e-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: 132.63  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEIlMRYGQHPNIITLKDVF------DDGRYVYLVTDL 516
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQI-MRRLKHPNIVKLKYFFyssgekKDEVYLNLVMEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MkgGELLDRILKQKcFSEREASDILYV------ISKTVDYLHCQGVVHRDLKPSNILYMDESAsadSIRICDFGFAKQL- 589
Cdd:cd14137    85 M--PETLYRVIRHY-SKNKQTIPIIYVklysyqLFRGLAYLHSLGICHRDIKPQNLLVDPETG---VLKLCDFGSAKRLv 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLlltpCY--TANFVAPEvLMQ--QGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGN--GKFSLS- 662
Cdd:cd14137   159 PGEPNV----SYicSRYYRAPE-LIFgaTDYTTAIDIWSAGCVLAELLLGQPLF---PGESSVDQLVEIIKvlGTPTREq 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 663 -----------------GGNWDNI-----SDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14137   231 ikamnpnytefkfpqikPHPWEKVfpkrtPPDAIDLLSKILVYNPSKRLTALEALAH 287
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
90-336 3.71e-34

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: 132.03  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKkasLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVD---GVTYAIKKIR---LTEKSSASEKVLREVkaLAKLNHPNIVRYYTAWVEEPPLYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYL---AELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFGLSKESVDQ 243
Cdd:cd13996    82 QMELCEGGTLRDWIDRRNSSSKNDRKLALelfKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIGNQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAY--------------SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLtgtLPFQ-GKDRNETMNMILKAKLg 308
Cdd:cd13996   162 KRELNnlnnnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKtAMERSTILTDLRNGIL- 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 309 mPQFLSA----EAQSLLRMLfKRNPANRLGSE 336
Cdd:cd13996   238 -PESFKAkhpkEADLIQSLL-SKNPEERPSAE 267
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
441-700 4.08e-34

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: 131.22  E-value: 4.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGS----YSVCKRCIHATTNMEFAVKIiDKSKRDPS---EEIEIlMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14002     1 ENYHVLELIGEGSfgkvYKGRRKYTGQVVALKFIPKR-GKSEKELRnlrQEIEI-LRKLNHPNIIEMLDSFETKKEFVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGgELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrGEN 593
Cdd:cd14002    79 TEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILI----GKGGVVKLCDFGFARAM-SCN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLL-----TPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpndtpeeillrigNGKFSL------S 662
Cdd:cd14002   153 TLVLtsikgTPLY----MAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYT--------------NSIYQLvqmivkD 214
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 663 GGNW-DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14002   215 PVKWpSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
89-347 4.23e-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: 132.07  E-value: 4.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlKKASLKVRDRVRTKMERDI--LVEVN-HPFIVKLHYAFQTEGKL 165
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRE---TGETVALK--KVALRKLEGGIPNQALREIkaLQACQgHPYVVKLRDVFPHGTGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLrGGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd07832    76 VLVFEYM-LSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSF-CGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQF---------- 312
Cdd:cd07832   155 PRLYSHqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRT-LGTPNEktwpeltslp 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 313 ---------------------LSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd07832   234 dynkitfpeskgirleeifpdCSPEAIDLLKGLLVYNPKKRLSA---EEALRHPYF 286
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
90-335 6.41e-34

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: 130.78  E-value: 6.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLkkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14107     4 YEVKEEIGRGTFG---FVKRVTHKGNGECCAAKFI---PLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL--DEIGHIKLTDFGLSKEsVDQEKKA 247
Cdd:cd14107    78 ELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQE-ITPSEHQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL--GMPQF--LSAEAQSLLRM 323
Cdd:cd14107   157 FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVswDTPEIthLSEDAKDFIKR 236
                         250
                  ....*....|..
gi 1034674014 324 LFKRNPANRLGS 335
Cdd:cd14107   237 VLQPDPEKRPSA 248
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
443-700 6.59e-34

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: 130.82  E-value: 6.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI--EIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd06647     9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY-MDesasaDSIRICDFGFAKQLRGENGLLLT 598
Cdd:cd06647    89 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMD-----GSVKLTDFGFCAQITPEQSKRST 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG-NGKFSLSggNWDNISDGAKDLL 677
Cdd:cd06647   163 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQ--NPEKLSAIFRDFL 237
                         250       260
                  ....*....|....*....|...
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06647   238 NRCLEMDVEKRGSAKELLQHPFL 260
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
439-699 6.73e-34

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: 130.68  E-value: 6.73e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYeLKEDIGVGSYsvckrcihattnmeFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd05611     9 FGSVY-LAKKRSTGDY--------------FAIKVLKKSDMIAKNQVTnvkaeraIMMIQGESPYVAKLYYSFQSKDYLY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAK--QL 589
Cdd:cd05611    74 LVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLL-IDQTGH---LKLTDFGLSRngLE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd05611   150 KRHNKKFVG---TPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAE---TPDAVFDNILSRRINWPEEVKEFC 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTA---EQILKHSW 699
Cdd:cd05611   224 SPEAVDLINRLLCMDPAKRLGAngyQEIKSHPF 256
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
89-333 7.87e-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: 130.90  E-value: 7.87e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDAGqlYAMKVLKKASLKVRDRVRTKmERDILVEVNHPFIVKLhYAFQT-EGKLYL 167
Cdd:cd14202     3 EFSRKDLIGHGAFAVVFKGRHKEKHDLE--VAVKCINKKNLAKSQTLLGK-EIKILKELKHENIVAL-YDFQEiANSVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG---------HIKLTDFGLSK 238
Cdd:cd14202    79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 eSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL---GMPQFLSA 315
Cdd:cd14202   159 -YLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSlspNIPRETSS 237
                         250
                  ....*....|....*...
gi 1034674014 316 EAQSLLRMLFKRNPANRL 333
Cdd:cd14202   238 HLRQLLLGLLQRNQKDRM 255
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-700 8.52e-34

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: 130.35  E-value: 8.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDVFDD--GRYVYLVT 514
Cdd:cd08217     2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEkqqlvsEVNIL-RELKHPNIVRYYDRIVDraNTTLYIVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELldRILKQKC------FSEREASDILYVISKTVDYLHC-----QGVVHRDLKPSNIlYMDESasaDSIRICDF 583
Cdd:cd08217    81 EYCEGGDL--AQLIKKCkkenqyIPEEFIWKIFTQLLLALYECHNrsvggGKILHRDLKPANI-FLDSD---NNVKLGDF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQLRGENGL----LLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDtpEEILLRIGNGKF 659
Cdd:cd08217   155 GLARVLSHDSSFaktyVGTPYY----MSPELLNEQSYDEKSDIWSLGCLIYELCALHPPF-QAANQ--LELAKKIKEGKF 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 660 SlsggNWDNI-SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd08217   228 P----RIPSRySSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
94-336 8.59e-34

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: 130.81  E-value: 8.59e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKaslkvRDRVRtKMERDILVEV-------NHPFIVKLHYAFQTEGKLY 166
Cdd:cd14198    14 KELGRGKFA---VVRQCISKSTGQEYAAKFLKK-----RRRGQ-DCRAEILHEIavlelakSNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI---GHIKLTDFGLSKEsV 241
Cdd:cd14198    85 LILEYAAGGEIFNLCVPDLaeMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK-I 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEA 317
Cdd:cd14198   164 GHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsSVSQLA 243
                         250
                  ....*....|....*....
gi 1034674014 318 QSLLRMLFKRNPANRLGSE 336
Cdd:cd14198   244 TDFIQKLLVKNPEKRPTAE 262
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
90-332 9.03e-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: 130.20  E-value: 9.03e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLK----VRDRVRTK--MERDILVEVN---HPFIVKLHYAFQ 160
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYK---SKGKEVVIKFIFKERILvdtwVRDRKLGTvpLEIHILDTLNkrsHPNIVKLLDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILD-FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSke 239
Cdd:cd14004    79 DDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAYSFCGTVEYMAPEVVnrRGHS---QSADWWSYGVLMFEMLTGTLPFQGKDRnetmnmILKAKLGMPQFLSAE 316
Cdd:cd14004   157 AYIKSGPFDTFVGTIDYAAPEVL--RGNPyggKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSED 228
                         250
                  ....*....|....*.
gi 1034674014 317 AQSLLRMLFKRNPANR 332
Cdd:cd14004   229 LIDLISRMLNRDVGDR 244
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
442-701 9.94e-34

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: 130.75  E-value: 9.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS---EEIEILmRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVlvkKEISIL-NIARHRNILRLHESFESHEELVMIFEFIS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAKQLR-GEN-GL 595
Cdd:cd14104    80 GVDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGS--YIKIIEFGQSRQLKpGDKfRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKD 675
Cdd:cd14104   158 QYT---SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFE---AETNQQTIENIRNAEYAFDDEAFKNISIEALD 231
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd14104   232 FVDRLLVKERKSRMTAQEALNHPWLK 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
449-701 1.02e-33

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: 130.44  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS-------KRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllkphqKEKMSMEIAI-HRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd14187    94 LLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM----EVKIGDFGLATKVEYDGERKKTLCG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSHML 681
Cdd:cd14187   170 TPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYSIP----KHINPVAASLIQKML 242
                         250       260
                  ....*....|....*....|
gi 1034674014 682 HMDPHQRYTAEQILKHSWIT 701
Cdd:cd14187   243 QTDPTARPTINELLNDEFFT 262
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
90-337 1.11e-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: 131.10  E-value: 1.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKK-ASLKVrdrVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQK---GTQKPYAVKKLKKtVDKKI---VRT--EIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGLSKeSVDQEK 245
Cdd:cd14085    77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSK-IVDQQV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM-NMILKAKLGM--PQF--LSAEAQSL 320
Cdd:cd14085   156 TMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMfKRILNCDYDFvsPWWddVSLNAKDL 235
                         250
                  ....*....|....*..
gi 1034674014 321 LRMLFKRNPANRLGSEG 337
Cdd:cd14085   236 VKKLIVLDPKKRLTTQQ 252
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
90-348 1.64e-33

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: 129.25  E-value: 1.64e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLKkasLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd06614     2 YKNLEKIGEGASGEVYKaTDRATG----KEVAIKKMR---LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGG---DVFTRlsKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd06614    75 MEYMDGGsltDIITQ--NPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQF-----LSAEAQSL 320
Cdd:cd06614   153 KRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYL--EEPPLRALFLITTKGIPPLknpekWSPEFKDF 230
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 321 LRMLFKRNPANRLGSegvEEIKRHLFFA 348
Cdd:cd06614   231 LNKCLVKDPEKRPSA---EELLQHPFLK 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
90-333 2.00e-33

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: 129.74  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDR--VRTKMER--DILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14195     7 YEMGEELGSGQFA---IVRKCREKGTGKEYAAKFIKKRRLSSSRRgvSREEIERevNILREIQHPNIITLHDIFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG----HIKLTDFGLSKEsV 241
Cdd:cd14195    84 VLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHK-I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEA 317
Cdd:cd14195   163 EAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEeyfsNTSELA 242
                         250
                  ....*....|....*.
gi 1034674014 318 QSLLRMLFKRNPANRL 333
Cdd:cd14195   243 KDFIRRLLVKDPKKRM 258
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
88-332 2.60e-33

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: 129.41  E-value: 2.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKvlkkaslKVRDRVRTKMERDILVEV------NHPFIVKLHYAFQT 161
Cdd:cd14046     6 TDFEELQVLGKGAFGQVVKVRNKLD---GRYYAIK-------KIKLRSESKNNSRILREVmllsrlNHQHVVRYYQAWIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDF-----LRggDVFTRlskEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd14046    76 RANLYIQMEYcekstLR--DLIDS---GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SK------ESVDQE-KKAYSFC-----------GTVEYMAPEVVNRRG--HSQSADWWSYGVLMFEMltgTLPFQ-GKDR 295
Cdd:cd14046   151 ATsnklnvELATQDiNKSTSAAlgssgdltgnvGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM---CYPFStGMER 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 296 NETMNMILKAKLGMPQ-FLS---AEAQSLLRMLFKRNPANR 332
Cdd:cd14046   228 VQILTALRSVSIEFPPdFDDnkhSKQAKLIRWLLNHDPAKR 268
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
443-713 2.96e-33

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: 129.86  E-value: 2.96e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-------KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAipevirlKQEQHVHNEKRVLKEV-SHPFIIRLFWTEHDQRFLYMLME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENgl 595
Cdd:cd05612    82 YVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEG----HIKLTDFGFAKKLRDRT-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 lLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFslsggNWDNISD-GAK 674
Cdd:cd05612   156 -WTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFF---DDNPFGIYEKILAGKL-----EFPRHLDlYAK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 675 DLLSHMLHMDPHQRY-----TAEQILKHSWITHRDQlpNDQPKR 713
Cdd:cd05612   227 DLIKKLLVVDRTRRLgnmknGADDVKNHRWFKSVDW--DDVPQR 268
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
96-347 3.18e-33

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: 128.53  E-value: 3.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVflvrkKTGPDAGQL--YAMKVLKKASLKV----RDRVRTKMErdILVEVNHPFIVKLHYAFQTE--GKLYL 167
Cdd:cd14119     1 LGEGSYGKV-----KEVLDTETLcrRAVKILKKRKLRRipngEANVKREIQ--ILRRLNHRNVIKLVDVLYNEekQKLYM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGdvftrlSKEVLFTEEDVKF-------YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd14119    74 VMEYCVGG------LQEMLDSAPDKRLpiwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 --VDQEKKAYSFCGTVEYMAPEVVN--RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAE 316
Cdd:cd14119   148 dlFAEDDTCTTSQGSPAFQPPEIANgqDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPD 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 317 AQSLLRMLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14119   228 LQDLLRGMLEKDPEKRF---TIEQIRQHPWF 255
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
443-700 4.03e-33

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: 128.44  E-value: 4.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS-------EEIEILMRYgQHPNIITLKDVFD-DGRYVYLVt 514
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfvqkflpRELSILRRV-NHPNIVQMFECIEvANGRLYIV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 dlMKGGE--LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFAKQLRGE 592
Cdd:cd14164    80 --MEAAAtdLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL---SADDRKIKIADFGFARFVEDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpNDTPEEILLRIGNGKFSLSGgnwDNISD 671
Cdd:cd14164   155 PELSTTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPF----DETNVRRLRLQQRGVLYPSG---VALEE 227
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14164   228 PCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
441-700 4.58e-33

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: 128.40  E-value: 4.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEIEILmRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14111     3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqAEEKQGVLQEYEIL-KSLHHERIMALHEAYITPRYLVLIAEFC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrgeNGLLL 597
Cdd:cd14111    82 SGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMV----TNLNAIKIVDFGSAQSF---NPLSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCY----TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSlSGGNWDNISDGA 673
Cdd:cd14111   155 RQLGrrtgTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE---DQDPQETEAKILVAKFD-AFKLYPNVSQSA 230
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14111   231 SLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
438-711 6.22e-33

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: 130.18  E-value: 6.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILmRYGQHPNIITLKDVF------D 505
Cdd:cd07855     2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTtakrtlRELKIL-RHFKHDNIIAIRDILrpkvpyA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 506 DGRYVYLVTDLMKGGelLDRILK-QKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFG 584
Cdd:cd07855    81 DFKDVYVVLDLMESD--LHHIIHsDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL-VNENC---ELKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 585 FAKQLRG---ENGLLLTPcYTAN--FVAPEVLMQ-QGYDAACDIWSLGVLFYTMLaGYTPFANGPN-------------D 645
Cdd:cd07855   155 MARGLCTspeEHKYFMTE-YVATrwYRAPELMLSlPEYTQAIDMWSVGCIFAEML-GRRQLFPGKNyvhqlqliltvlgT 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 646 TPEEILLRIGNG---KFSLSGGN-----WDNISDGAK----DLLSHMLHMDPHQRYTAEQILKHSWI-THRDqlPNDQP 711
Cdd:cd07855   233 PSQAVINAIGADrvrRYIQNLPNkqpvpWETLYPKADqqalDLLSQMLRFDPSERITVAEALQHPFLaKYHD--PDDEP 309
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
96-290 6.81e-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: 128.72  E-value: 6.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLK-KASLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKL-YLI 168
Cdd:cd13989     1 LGSGGFGYVTLWKHQ---DTGEYVAIKKCRqELSPSDKNRERWCLEVQIMKKLNHPNVVSArdvppELEKLSPNDLpLLA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGD---VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGLSKEsVD 242
Cdd:cd13989    78 MEYCSGGDlrkVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKE-LD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd13989   157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
94-338 6.91e-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: 6.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLkkaslkvRDRVRTKMERDILVEV-NHPFIVKLH--YA--FQTEGKLYL 167
Cdd:cd14089     7 QVLGLGINGKVLeCFHKKTG----EKFALKVL-------RDNPKARREVELHWRAsGCPHIVRIIdvYEntYQGRKCLLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGLSKEsVD 242
Cdd:cd14089    76 VMECMEGGELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKE-TT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMILKAKLGMPQF---------L 313
Cdd:cd14089   155 TKKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKKRIRNGQYefpnpewsnV 233
                         250       260
                  ....*....|....*....|....*
gi 1034674014 314 SAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14089   234 SEEAKDLIRGLLKTDPSERLTIEEV 258
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
443-697 7.35e-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. 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: 128.59  E-value: 7.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKiidKSKRDPSEEI-------EI-LMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIK---KFKESEDDEDvkktalrEVkVLRQLRHENIVNLKEAFRRKGRLYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGG--ELLDRilKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQLRGE 592
Cdd:cd07833    80 EYVERTllELLEA--SPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIL-VSES---GVLKLCDFGFARALTAR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTPcYTAN--FVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFAnGPND--------------TPEEILLRIG 655
Cdd:cd07833   154 PASPLTD-YVATrwYRAPELLVgDTNYGKPVDVWAIGCIMAELLDGEPLFP-GDSDidqlyliqkclgplPPSHQELFSS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 656 NGKFslSGGNWDNI--------------SDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07833   232 NPRF--AGVAFPEPsqpeslerrypgkvSSPALDFLKACLRMDPKERLTCDELLQH 285
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
94-290 8.65e-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: 8.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVF-LVRKKTGPDAgqlyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14082     9 EVLGSGQFGIVYgGKHRKTGRDV----AIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEV-LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG---HIKLTDFGLSKeSVDQEKKAY 248
Cdd:cd14082    85 HGDMLEMILSSEKgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR-IIGEKSFRR 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 249 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14082   164 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
93-332 9.30e-33

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: 127.16  E-value: 9.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKkTGPDAGQLYAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd08221     5 VRVLGRGAFGEAVLYRK-TEDNSLVVWKEVNLSRLSEKERRDALN--EIDILSLLNHDNIITYYNHFLDGESLFIEMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 250
Cdd:cd08221    82 NGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM--PQFlSAEAQSLLRMLFKRN 328
Cdd:cd08221   162 VGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDidEQY-SEEIIQLVHDCLHQD 240

                  ....
gi 1034674014 329 PANR 332
Cdd:cd08221   241 PEDR 244
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
440-700 1.02e-32

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: 127.80  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDkSKRDPSEEIE----ILMRYGQHPNIITLKDVF--------DDG 507
Cdd:cd06608     5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD-IIEDEEEEIKleinILRKFSNHPNIATFYGAFikkdppggDDQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 RYVYL-------VTDLMKGGELLDRILKqkcfsEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRI 580
Cdd:cd06608    84 LWLVMeycgggsVTDLVKGLRKKGKRLK-----EEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEA----EVKL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 581 CDFGFAKQLRGENGLLLTPCYTANFVAPEVLM-----QQGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIG 655
Cdd:cd06608   155 VDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMH---PMRALFKIP 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 656 NGKFS--LSGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06608   232 RNPPPtlKSPEKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
443-700 1.19e-32

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: 126.99  E-value: 1.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCiHATTNMEFAVKIIDKSK-RDPSE------EIEIlMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd14161     5 YEFLETLGKGTYGRVKKA-RDSSGRLVAIKSIRKDRiKDEQDllhirrEIEI-MSSLNHPHIISVYEVFENSSKIVIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLRGENgL 595
Cdd:cd14161    83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENIL-LDANG---NIKIADFGLSNLYNQDK-F 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAA-CDIWSLGVLFYTMLAGYTPFANGPNDTpeeILLRIGNGKFSLSggnwDNISDgAK 674
Cdd:cd14161   158 LQTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKI---LVKQISSGAYREP----TKPSD-AC 229
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14161   230 GLIRWLLMVNPERRATLEDVASHWWV 255
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
89-310 1.59e-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: 127.62  E-value: 1.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRkktGPDAGQLYAMK-VLKKASLKVRdrvrtkmERDILVEVNHPFIVKLHYAFQTEGK--- 164
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAK---LLETGEVVAIKkVLQDKRYKNR-------ELQIMRRLKHPNIVKLKYFFYSSGEkkd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 ---LYLILDFL--------RggdVFTRLSKEvlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLT 232
Cdd:cd14137    75 evyLNLVMEYMpetlyrviR---HYSKNKQT--IPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 233 DFGLSKESVDQEK-KAYsFCgTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd14137   150 DFGSAKRLVPGEPnVSY-IC-SRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKV-LGTP 226
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
89-340 3.15e-32

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: 126.26  E-value: 3.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14183     7 RYKVGRTIGDGNFA---VVKECVERSTGREYALKIINKSKCRGKEHM-IQNEVSILRRVKHPNIVLLIEEMDMPTELYLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----DEIGHIKLTDFGLSKeSVDqe 244
Cdd:cd14183    83 MELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT-VVD-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQG--KDRNETMNMILKAKLGMP----QFLSAEAQ 318
Cdd:cd14183   160 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFPspywDNVSDSAK 239
                         250       260
                  ....*....|....*....|..
gi 1034674014 319 SLLRMLFKRNPANRLGSEGVEE 340
Cdd:cd14183   240 ELITMMLQVDVDQRYSALQVLE 261
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
443-699 3.34e-32

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: 126.25  E-value: 3.34e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVC-----KRCIHAttnmeFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14010     2 YVLYDEIGRGKHSVVykgrrKGTIEF-----VAIKCVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAK---------- 587
Cdd:cd14010    77 TGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNIL-LDGNGT---LKLSDFGLARregeilkelf 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 ----------QLRGENGLLLTPCYTAnfvaPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNG 657
Cdd:cd14010   153 gqfsdegnvnKVSKKQAKRGTPYYMA----PELFQGGVHSFASDLWALGCVLYEMFTGKPPFV---AESFTELVEKILNE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 658 KF-SLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHS-W 699
Cdd:cd14010   226 DPpPPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
443-700 3.62e-32

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: 125.49  E-value: 3.62e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKrDPSE--------EIEILMRYgQHPNIITLKDVFD--DGRyVYL 512
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSG-GPEEfiqrflprELQIVERL-DHKNIIHVYEMLEsaDGK-IYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesaSADSIRICDFGFAKQL-RG 591
Cdd:cd14163    79 VMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-----QGFTLKLTDFGFAKQLpKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpNDTPEEILLRIGNGKFSLSGGNwdNIS 670
Cdd:cd14163   154 GRELSQTFCGSTAYAAPEVLQGVPHDSrKGDIWSMGVVLYVMLCAQLPF----DDTDIPKMLCQQQKGVSLPGHL--GVS 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14163   228 RTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
440-711 4.19e-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: 127.81  E-value: 4.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKiidksKRDPSE----------EIEILMRYgQHPNIITLKDV-----F 504
Cdd:cd07849     4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK-----KISPFEhqtyclrtlrEIKILLRF-KHENIIGILDIqrpptF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 505 DDGRYVYLVTDLMKGGelLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADsIRICDFG 584
Cdd:cd07849    78 ESFKDVYIVQELMETD--LYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLL---NTNCD-LKICDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 585 FAK--QLRGENGLLLTPcYTAN--FVAPEV-LMQQGYDAACDIWSLGVLFYTMLAGyTPFANGPN------------DTP 647
Cdd:cd07849   152 LARiaDPEHDHTGFLTE-YVATrwYRAPEImLNSKGYTKAIDIWSVGCILAEMLSN-RPLFPGKDylhqlnlilgilGTP 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 648 -EEILLRIGNGKF-----SL---SGGNWD----NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI-THRDqlPNDQP 711
Cdd:cd07849   230 sQEDLNCIISLKArnyikSLpfkPKVPWNklfpNADPKALDLLDKMLTFNPHKRITVEEALAHPYLeQYHD--PSDEP 305
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
449-700 5.20e-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: 125.25  E-value: 5.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLD 524
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRREllfnEVVI-MRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 rILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGE----NGLLLTPC 600
Cdd:cd06648    94 -IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILL----TSDGRVKLSDFGFCAQVSKEvprrKSLVGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTAnfvaPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNGKFSLSgGNWDNISDGAKDLLSHM 680
Cdd:cd06648   169 WMA----PEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEP---PLQAMKRIRDNEPPKL-KNLHKVSPRLRSFLDRM 240
                         250       260
                  ....*....|....*....|
gi 1034674014 681 LHMDPHQRYTAEQILKHSWI 700
Cdd:cd06648   241 LVRDPAQRATAAELLNHPFL 260
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
449-700 5.94e-32

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: 125.11  E-value: 5.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHAT--TNMEFAVKIIdksKRDPSEEIE-----------ILMRYGQHPNIITLKDVFDDGRYVY-LVT 514
Cdd:cd13994     1 IGKGATSVVRIVTKKNprSGVLYAVKEY---RRRDDESKRkdyvkrltseyIISSKLHHPNIVKVLDLCQDLHGKWcLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLRGENG 594
Cdd:cd13994    78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGV----LKLTDFGTAEVFGMPAE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 llLTPCYTAN------FVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFANgPNDTPEEILLRIGNGKFSLSGGNWD 667
Cdd:cd13994   154 --KESPMSAGlcgsepYMAPEVFTSGSYDGrAVDVWSCGIVLFALFTGRFPWRS-AKKSDSAYKAYEKSGDFTNGPYEPI 230
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 668 NISDG--AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd13994   231 ENLLPseCRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
94-338 9.85e-32

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: 125.52  E-value: 9.85e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVflvRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMErdILVEVN-HPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14173     8 EVLGEGAYARV---QTCINLITNKEYAVKIIEKRPGHSRSRVFREVE--MLYQCQgHRNVLELIEFFEEEDKFYLVFEKM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGL-------SKESVD 242
Cdd:cd14173    83 RGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLgsgiklnSDCSPI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQS-----ADWWSYGVLMFEMLTGTLPFQGK-------DRNET----MNM----I 302
Cdd:cd14173   163 STPELLTPCGSAEYMAPEVVEAFNEEASiydkrCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEAcpacQNMlfesI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 303 LKAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14173   243 QEGKYEFPEkdwaHISCAAKDLISKLLVRDAKQRLSAAQV 282
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
90-344 1.08e-31

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: 124.20  E-value: 1.08e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpdagqlyamKVLKKASLKVRDRVRTK---------MERDILVEVNHPFIVKLHYAFQ 160
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQ-----------KYCCKVAIKIVDRRRASpdfvqkflpRELSILRRVNHPNIVQMFECIE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 -TEGKLYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG-HIKLTDFGLSK 238
Cdd:cd14164    71 vANGRLYIVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFAR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFQGkdrnETMNMILKAKLGM--PQFLSA 315
Cdd:cd14164   150 FVEDYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDE----TNVRRLRLQQRGVlyPSGVAL 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 316 E--AQSLLRMLFKRNPANRlgsEGVEEIKRH 344
Cdd:cd14164   226 EepCRALIRTLLQFNPSTR---PSIQQVAGN 253
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
449-699 1.21e-31

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: 126.19  E-value: 1.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPSE----EIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05599     9 IGRGAFGEVRLVRKKDTGHVYAMKKLRKSemlEKEQVAhvraERDILAE-ADNPWVVKLYYSFQDEENLYLIMEFLPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASdilYVISKTV---DYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENgLLLT 598
Cdd:cd05599    88 MMTLLMKKDTLTEEETR---FYIAETVlaiESIHKLGYIHRDIKPDNLL-LDARGH---IKLSDFGLCTGLKKSH-LAYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLS 678
Cdd:cd05599   160 TVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFC---SDDPQETCRKIMNWRETLVFPPEVPISPEAKDLIE 236
                         250       260
                  ....*....|....*....|....
gi 1034674014 679 HMLhMDPHQR---YTAEQILKHSW 699
Cdd:cd05599   237 RLL-CDAEHRlgaNGVEEIKSHPF 259
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
68-335 1.35e-31

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 129.60  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  68 VVKEIPITHHVKEGYEKADPAQFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEV 147
Cdd:PTZ00283   12 VCRTFPDTFAKDEATAKEQAKKYWISRVLGSGATGTVLCAKRVSD---GEPFAVKVVDMEGMSEADKNRAQAEVCCLLNC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 148 NHPFIVKLHYAFQTEGK--------LYLILDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRD 215
Cdd:PTZ00283   89 DFFSIVKCHEDFAKKDPrnpenvlmIALVLDYANAGDlrqeIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 216 LKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 293
Cdd:PTZ00283  169 IKSANILLCSNGLVKLGDFGFSKmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGE 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 294 DRNETMNMILKAKLG-MPQFLSAEAQSLLRMLFKRNPANRLGS 335
Cdd:PTZ00283  249 NMEEVMHKTLAGRYDpLPPSISPEMQEIVTALLSSDPKRRPSS 291
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
90-310 1.55e-31

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: 124.52  E-value: 1.55e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLK-------VRdrvrtkmERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKT---GEIVALKKIRLDNEEegipstaLR-------EISLLKELKHPNIVKLLDVIHTE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGgDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-S 240
Cdd:cd07829    71 NKLYLVFEYCDQ-DLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAfG 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 241 VdqEKKAYsfcgTVE-----YMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMP 310
Cdd:cd07829   150 I--PLRTY----THEvvtlwYRAPEIlLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQ-ILGTP 218
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
94-346 1.57e-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: 124.03  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMK---VLKKASLKVRDRVRT-----KMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd06629     7 ELIGKGTYGRVYLAMNAT---TGEMLAVKqveLPKTSSDRADSRQKTvvdalKSEIDTLKDLDHPNIVQYLGFEETEDYF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD--Q 243
Cdd:cd06629    84 SIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDiyG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEA 317
Cdd:cd06629   164 NNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPvpedVNLSPEA 243
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 318 QSLLRMLFKRNPANRlgsEGVEEIKRHLF 346
Cdd:cd06629   244 LDFLNACFAIDPRDR---PTAAELLSHPF 269
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
89-349 1.74e-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: 124.99  E-value: 1.74e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKV------RDRVRtkmERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDK---ETGRIVAIKKIKLGERKEakdginFTALR---EIKLLQELKHPNIIGLLDVFGHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLrggdvFTRLS-----KEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd07841    75 SNINLVFEFM-----ETDLEkvikdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP------ 310
Cdd:cd07841   150 RSFGSPNRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEA-LGTPteenwp 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 311 ---------QF--------------LSAEAQSLLRMLFKRNPANRLgseGVEEIKRHLFFAN 349
Cdd:cd07841   229 gvtslpdyvEFkpfpptplkqifpaASDDALDLLQRLLTLNPNKRI---TARQALEHPYFSN 287
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
95-337 2.27e-31

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: 123.97  E-value: 2.27e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKTGPDAGqlYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd14201    13 LVGHGAFAVVFKGRHRKKTDWE--VAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG---------HIKLTDFGLSKeSVDQEK 245
Cdd:cd14201    90 GDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFAR-YLQSNM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLR 322
Cdd:cd14201   169 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIpreTSPYLADLLL 248
                         250
                  ....*....|....*
gi 1034674014 323 MLFKRNPANRLGSEG 337
Cdd:cd14201   249 GLLQRNQKDRMDFEA 263
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
119-338 2.69e-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: 123.98  E-value: 2.69e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 119 YAMKVLKKASlkvRDRVRtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLA 197
Cdd:cd14175    29 YAVKVIDKSK---RDPSE---EIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASSVLH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 198 ELALALDHLHQLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADW 273
Cdd:cd14175   103 TICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDI 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 274 WSYGVLMFEMLTGTLPFqGKDRNETMNMILkAKLGMPQF---------LSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14175   183 WSLGILLYTMLAGYTPF-ANGPSDTPEEIL-TRIGSGKFtlsggnwntVSDAAKDLVSKMLHVDPHQRLTAKQV 254
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
94-338 2.85e-31

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: 123.99  E-value: 2.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKV-FLVRKKTGPDagqlYAMKVLKKASLKVRDRVRTKMERDILVEVNHPfIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd14174     8 ELLGEGAYAKVqGCVSLQNGKE----YAVKIIEKNAGHSRSRVFREVETLYQCQGNKN-ILELIEFFEDDTRFYLVFEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGL-------SKESVD 242
Cdd:cd14174    83 RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLgsgvklnSACTPI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVV-----NRRGHSQSADWWSYGVLMFEMLTGTLPFQGK-------DRNETMNM--------I 302
Cdd:cd14174   163 TTPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwDRGEVCRVcqnklfesI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 303 LKAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14174   243 QEGKYEFPDkdwsHISSEAKDLISKLLVRDAKERLSAAQV 282
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
440-699 5.96e-31

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: 123.89  E-value: 5.96e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYeLKEDIGVGSYsvckrcihattnmeFAVKIIDKS---KRDP----SEEIEILMRYgQHPNIITLKDVFDDGRYVYL 512
Cdd:cd05574    15 GRVY-LVRLKGTGKL--------------FAMKVLDKEemiKRNKvkrvLTEREILATL-DHPFLPTLYASFQTSTHLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDRILKQ--KCFSERE----ASDILYVIsktvDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFA 586
Cdd:cd05574    79 VMDYCPGGELFRLLQKQpgKRLPEEVarfyAAEVLLAL----EYLHLLGFVYRDLKPENIL-LHESG---HIMLTDFDLS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQL----------------RGENGLLLTPCY-------------TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYT 637
Cdd:cd05574   151 KQSsvtpppvrkslrkgsrRSSVKSIEKETFvaepsarsnsfvgTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTT 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 638 PFAnGPNDtpEEILLRIGNGKFSLSGGnwDNISDGAKDLLSHMLHMDPHQR----YTAEQILKHSW 699
Cdd:cd05574   231 PFK-GSNR--DETFSNILKKELTFPES--PPVSSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPF 291
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
86-346 6.12e-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: 122.80  E-value: 6.12e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPA-QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKkaslkvrdrVRTKMERDILVEVN-------HPFIVKLHY 157
Cdd:cd06608     3 DPAgIFELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMD---------IIEDEEEEIKLEINilrkfsnHPNIATFYG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 158 AFQT------EGKLYLILDFLRGGDVfTRLSKEVL-----FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI 226
Cdd:cd06608    71 AFIKkdppggDDQLWLVMEYCGGGSV-TDLVKGLRkkgkrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd06608   150 AEVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFK 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 302 ILK---AKLGMPQFLSAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLF 346
Cdd:cd06608   230 IPRnppPTLKSPEKWSKEFNDFISECLIKNYEQR---PFTEELLEHPF 274
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
449-701 7.15e-31

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: 122.07  E-value: 7.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIdKSKRDPSE------EIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVI-RLEIDEALqkqilrELDVLHK-CNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 lDRILKQ-KCFSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrgENGLLLTPC 600
Cdd:cd06605    87 -DKILKEvGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILV----NSRGQVKLCDFGVSGQL--VDSLAKTFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAN---GPNDTPEEILLRIGNGKF-SLSGGNWdniSDGAKDL 676
Cdd:cd06605   160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPpnaKPSMMIFELLSYIVDEPPpLLPSGKF---SPDFQDF 236
                         250       260
                  ....*....|....*....|....*
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06605   237 VSQCLQKDPTERPSYKELMEHPFIK 261
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
462-697 8.49e-31

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: 123.48  E-value: 8.49e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 462 HATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSE 534
Cdd:cd05570    16 RKKTDELYAIKVLKKEVIIEDDDVEctmtekrVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGGDLMFHIQRARRFTE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 535 REAsdILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLM 612
Cdd:cd05570    96 ERA--RFYAaeICLALQFLHERGIIYRDLKLDNVLLDAEG----HIKIADFGMCKEGIWGGNTTSTFCGTPDYIAPEILR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 613 QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSHMLHMDPHQR---- 688
Cdd:cd05570   170 EQDYGFSVDWWALGVLLYEMLAGQSPF---EGDDEDELFEAILNDEVLYP----RWLSREAVSILKGLLTKDPARRlgcg 242
                         250
                  ....*....|
gi 1034674014 689 -YTAEQILKH 697
Cdd:cd05570   243 pKGEADIKAH 252
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
443-700 9.36e-31

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: 121.61  E-value: 9.36e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK---RDPSEEIEILMRYGQHP-----NIITLKDVFDDGRYVYLVT 514
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKdylDQSLDEIRLLELLNKKDkadkyHIVRLKDVFYFKNHLCIVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGG--ELLdRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdsIRICDFGFAkqlrge 592
Cdd:cd14133    81 ELLSQNlyEFL-KQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQ--IKIIDFGSS------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 ngllltpCYTANFV----------APEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGN--GKFS 660
Cdd:cd14133   152 -------CFLTQRLysyiqsryyrAPEVILGLPYDEKIDMWSLGCILAELYTGEPLF---PGASEVDQLARIIGtiGIPP 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 661 ---LSGGNWDNisDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14133   222 ahmLDQGKADD--ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
90-301 9.89e-31

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: 121.61  E-value: 9.89e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMK---VLKKASLKVRDR-VRtkmERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCL---LDGRLVALKkvqIFEMMDAKARQDcLK---EIDLLQQLNHPNIIKYLASFIENNEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVfTRLSKE-----VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd08224    76 NIVLELADAGDL-SRLIKHfkkqkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 241 VDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrnETMNM 301
Cdd:cd08224   155 SSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYG----EKMNL 211
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
89-347 1.35e-30

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: 121.31  E-value: 1.35e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdagqlYAMKV-LKKASLkvrDRVRTKMErDILVEV------NHPFIVKLHYAFQT 161
Cdd:cd06610     2 DYELIEVIGSGATAVVYAAYCLP-------KKEKVaIKRIDL---EKCQTSMD-ELRKEIqamsqcNHPNVVSYYTSFVV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGG---DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd06610    71 GDELWLVMPLLSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ---ESVDQEKKA-YSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaklGMPQFL 313
Cdd:cd06610   151 slaTGGDRTRKVrKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQ---NDPPSL 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 314 SAEAQS---------LLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd06610   228 ETGADYkkysksfrkMISLCLQKDPSKRPTA---EELLKHKFF 267
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
90-338 1.44e-30

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: 121.90  E-value: 1.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlkkaslkvrdRVRTKMERD-----------ILVEVNHPFIVKLH-- 156
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKK---TGELVALK-----------KIRMENEKEgfpitaireikLLQKLDHPNVVRLKei 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 ----YAFQTEGKLYLILDFLRGgDvFTRL--SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIK 230
Cdd:cd07840    67 vtskGSAKYKGSIYMVFEYMDH-D-LTGLldNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFGLSKESVDQEKKAY-SFCGTVEYMAPEVVnrRGHSQSA---DWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAk 306
Cdd:cd07840   145 LADFGLARPYTKENNADYtNRVITLWYRPPELL--LGATRYGpevDMWSVGCILAELFTGKPIFQGKTELEQLEKIFEL- 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 307 LGMP--------------------------------QFLSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd07840   222 CGSPteenwpgvsdlpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRISADQA 285
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
90-282 1.59e-30

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: 121.37  E-value: 1.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQTEGKLY 166
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVPT--GKVYAVKKLKPNYAGAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEED---VKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS-----K 238
Cdd:cd14052    80 IQTELCENGSLDVFLSELGLLGRLDefrVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwplI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 239 ESVDQEkkaysfcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFE 282
Cdd:cd14052   160 RGIERE-------GDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
97-332 1.72e-30

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: 120.70  E-value: 1.72e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  97 GQGSFGKVFLVRKKTgpdAGQLYAMKVLkkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 176
Cdd:cd14111    12 ARGRFGVIRRCRENA---TGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 177 VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVD----QEKKAYSfcG 252
Cdd:cd14111    86 LLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG-SAQSFNplslRQLGRRT--G 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFKRNP 329
Cdd:cd14111   163 TLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKLypnVSQSASLFLKKVLSSYP 242

                  ...
gi 1034674014 330 ANR 332
Cdd:cd14111   243 WSR 245
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
94-333 1.80e-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: 121.25  E-value: 1.80e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVL---KKASLKVRDRVRTKmerdilvevNHPFIVKLHYAFQT--EGK--LY 166
Cdd:cd14172    10 QVLGLGVNGKVLECFHR---RTGQKCALKLLydsPKARREVEHHWRAS---------GGPHIVHILDVYENmhHGKrcLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESV 241
Cdd:cd14172    78 IIMECMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 dQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMILKAKLGMPQF--------- 312
Cdd:cd14172   158 -VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFY-SNTGQAISPGMKRRIRMGQYgfpnpewae 235
                         250       260
                  ....*....|....*....|.
gi 1034674014 313 LSAEAQSLLRMLFKRNPANRL 333
Cdd:cd14172   236 VSEEAKQLIRHLLKTDPTERM 256
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
484-700 1.90e-30

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: 121.12  E-value: 1.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 484 EIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKP 563
Cdd:cd14117    56 EIEI-QSHLRHPNILRLYNYFHDRKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKP 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 564 SNIL--YMDEsasadsIRICDFGF---AKQLRGEnglllTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTP 638
Cdd:cd14117   135 ENLLmgYKGE------LKIADFGWsvhAPSLRRR-----TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPP 203
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 639 FANGPNDTPEEILLRIgNGKFSLSggnwdnISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14117   204 FESASHTETYRRIVKV-DLKFPPF------LSDGSRDLISKLLRYHPSERLPLKGVMEHPWV 258
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
443-700 2.05e-30

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: 120.79  E-value: 2.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIpykPEDKQLVLREYQVLRRL-SHPRIAQLHSAYLSPRHLVLIEELCSG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLRGENGLLLTP 599
Cdd:cd14110    84 PELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNL----LKIVDLGNAQPFNQGKVLMTDK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 C-YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGnWDNISDGAKDLLS 678
Cdd:cd14110   160 KgDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVS---SDLNWERDRNIRKGKVQLSRC-YAGLSGGAVNFLK 235
                         250       260
                  ....*....|....*....|..
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14110   236 STLCAKPWGRPTASECLQNPWL 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
89-347 2.39e-30

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: 120.42  E-value: 2.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLK----VRDRVRTKMERDILVEVN---HPFIVKLHYAFQT 161
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRD---GLPVAVKFVPKSRVTewamINGPVPVPLEIALLLKASkpgVPGVIRLLDWYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGG-DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFG---L 236
Cdd:cd14005    78 PDGFLLIMERPEPCqDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGcgaL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVdqekkaYS-FCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFqgkdRNETmnMILKAKLGMPQFLS 314
Cdd:cd14005   158 LKDSV------YTdFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPF----ENDE--QILRGNVLFRPRLS 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 315 AEAQSLLRMLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14005   226 KECCDLISRCLQFDPSKRP---SLEQILSHPWF 255
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
89-344 2.43e-30

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: 121.21  E-value: 2.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVR--------------------------DRVRTKMErd 142
Cdd:cd14200     1 QYKLQSEIGKGSYG---VVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplaplERVYQEIA-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 143 ILVEVNHPFIVKLHYAFQ--TEGKLYLILDFLRGGDVFtRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPEN 220
Cdd:cd14200    76 ILKKLDHVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 221 ILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSA---DWWSYGVLMFEMLTGTLPFQGKDRNE 297
Cdd:cd14200   155 LLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYGKCPFIDEFILA 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 298 TMNMILKAKLGMPQ--FLSAEAQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14200   235 LHNKIKNKPVEFPEepEISEELKDLILKMLDKNPETRI---TVPEIKVH 280
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
442-707 2.63e-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: 2.63e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSE---EIEIL--MRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd06917     2 LYRRLELVGRGSYGAVYRGYHVKTGRVVALKVLnlDTDDDDVSDiqkEVALLsqLKLGQPKNIIKYYGSYLKGPSLWIIM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELlDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENG 594
Cdd:cd06917    82 DYCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILV----TNTGNVKLCDFGVAASLNQNSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANgpNDTPEEILLRIGNGKFSLSGGNWdniSDGA 673
Cdd:cd06917   157 KRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSD--VDALRAVMLIPKSKPPRLEGNGY---SPLL 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLP 707
Cdd:cd06917   232 KEFVAACLDEEPKDRLSADELLKSKWIKQHSKTP 265
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
90-351 2.90e-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: 122.44  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKV-FLVRKKTGPDagqlYAMKVLKKASlkvRDRVRtkmERDILVEV-NHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14176    21 YEVKEDIGVGSYSVCkRCIHKATNME----FAVKIIDKSK---RDPTE---EIEILLRYgQHPNIITLKDVYDDGKYVYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQ 243
Cdd:cd14176    91 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF-QGKDrnETMNMILkAKLGMPQF---------L 313
Cdd:cd14176   171 NGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFaNGPD--DTPEEIL-ARIGSGKFslsggywnsV 247
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 314 SAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFFANID 351
Cdd:cd14176   248 SDTAKDLVSKMLHVDPHQRLTA---ALVLRHPWIVHWD 282
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
89-283 3.07e-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: 120.10  E-value: 3.07e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIA---TGELAAVKVIK---LEPGDDFEIiQQEISMLKECRHPNIVAYFGSYLRRDKLWI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGG---DVFTRLSKevlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd06613    75 VMEYCGGGslqDIYQVTGP---LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATI 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 245 KKAYSFCGTVEYMAPEV--VNRR-GHSQSADWWSYGVLMFEM 283
Cdd:cd06613   152 AKRKSFIGTPYWMAPEVaaVERKgGYDGKCDIWALGITAIEL 193
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
443-700 4.67e-30

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: 121.90  E-value: 4.67e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYGQHPNIITLKDVF--DDGRYVYLV- 513
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKKIFDAFRNATDaqrtfrEIMFLQELNDHPNIIKLLNVIraENDKDIYLVf 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 ----TDL---MKGGeLLDRILKQKcfsereasdILYVISKTVDYLHCQGVVHRDLKPSNILYmdesaSAD-SIRICDFGF 585
Cdd:cd07852    89 eymeTDLhavIRAN-ILEDIHKQY---------IMYQLLKALKYLHSGGVIHRDLKPSNILL-----NSDcRVKLADFGL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLR----GENGLLLTPcYTAN--FVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGyTPFANGPN--DTPEEILLRIGN 656
Cdd:cd07852   154 ARSLSqleeDDENPVLTD-YVATrwYRAPEILLgSTRYTKGVDMWSVGCILGEMLLG-KPLFPGTStlNQLEKIIEVIGR 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 657 ------------------------GKFSLSgGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07852   232 psaediesiqspfaatmleslppsRPKSLD-ELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYV 298
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
443-700 4.77e-30

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: 120.60  E-value: 4.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI--EIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd06656    21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY-MDesasaDSIRICDFGFAKQLRGENGLLLT 598
Cdd:cd06656   101 GSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLgMD-----GSVKLTDFGFCAQITPEQSKRST 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG-NGKFSLSggNWDNISDGAKDLL 677
Cdd:cd06656   175 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQ--NPERLSAVFRDFL 249
                         250       260
                  ....*....|....*....|...
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06656   250 NRCLEMDVDRRGSAKELLQHPFL 272
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
449-688 5.59e-30

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: 121.27  E-value: 5.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPSEEI----EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKailKRNEVKHImaerNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05575    83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQG----HVVLTDFGLCKEGIEPSDTTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpNDTpEEILLRIGNGKFSLSggnwDNISDGAKDLLSHML 681
Cdd:cd05575   159 TPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYS--RDT-AEMYDNILHKPLRLR----TNVSPSARDLLEGLL 231

                  ....*..
gi 1034674014 682 HMDPHQR 688
Cdd:cd05575   232 QKDRTKR 238
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
449-691 6.86e-30

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: 120.84  E-value: 6.86e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS----KRDPSE---EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtilkKKEQNHimaERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05603    83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENIL-LD---CQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEIL---LRIGNGKfslsggnwdniSDGAKDLL 677
Cdd:cd05603   159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFySRDVSQMYDNILhkpLHLPGGK-----------TVAACDLL 227
                         250
                  ....*....|....
gi 1034674014 678 SHMLHMDPHQRYTA 691
Cdd:cd05603   228 QGLLHKDQRRRLGA 241
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
443-639 8.03e-30

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: 118.99  E-value: 8.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS-----------KRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpnskdgndfqKLPQLREIDLHRRVSRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFsEREASDILYVISKTVD---YLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFA-- 586
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIY-VGKTELIKNVFLQLIDavkHCHSLGIYHRDIKPENILL---SQDEGTVKLCDFGLAtt 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 587 KQLRGENGllltpCYTANFVAPEVLMQ-----QGYD-AACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd13993   158 EKISMDFG-----VGSEFYMAPECFDEvgrslKGYPcAAGDIWSLGIILLNLTFGRNPW 211
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
449-692 9.47e-30

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: 120.89  E-value: 9.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPSEEI----EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKailKKKEEKHImserNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05602    95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENIL-LD---SQGHIVLTDFGLCKENIEPNGTTSTFCG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSHML 681
Cdd:cd05602   171 TPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFY---SRNTAEMYDNILNKPLQLK----PNITNSARHLLEGLL 243
                         250
                  ....*....|.
gi 1034674014 682 HMDPHQRYTAE 692
Cdd:cd05602   244 QKDRTKRLGAK 254
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
88-336 1.41e-29

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: 118.73  E-value: 1.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFlvRKKTGPdAGQLYAMKVLkkaSLKVRDRVRTKMERDI-----LVEVNHPFIVKLHYAFQTE 162
Cdd:cd06917     1 SLYRRLELVGRGSYGAVY--RGYHVK-TGRVVALKVL---NLDTDDDDVSDIQKEVallsqLKLGQPKNIIKYYGSYLKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTrLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06917    75 PSLWIIMDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKlgmPQFL-----SAE 316
Cdd:cd06917   154 NSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSK---PPRLegngySPL 230
                         250       260
                  ....*....|....*....|
gi 1034674014 317 AQSLLRMLFKRNPANRLGSE 336
Cdd:cd06917   231 LKEFVAACLDEEPKDRLSAD 250
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
90-380 1.45e-29

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: 119.94  E-value: 1.45e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQ-----TEGK 164
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDK---RTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRppspeEFND 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRggdvfTRL-----SKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 239
Cdd:cd07834    79 VYIVTELME-----TDLhkvikSPQPL-TDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAY--SFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP------ 310
Cdd:cd07834   153 VDPDEDKGFltEYVVTRWYRAPELLlSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEV-LGTPseedlk 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 311 QFLSAEAQSLLRMLFKR--------------------------NPANRLgseGVEEIKRHLFFAnidwdKLYKREVQPPF 364
Cdd:cd07834   232 FISSEKARNYLKSLPKKpkkplsevfpgaspeaidllekmlvfNPKKRI---TADEALAHPYLA-----QLHDPEDEPVA 303
                         330
                  ....*....|....*.
gi 1034674014 365 KPasgkPDDTFCFDPE 380
Cdd:cd07834   304 KP----PFDFPFFDDE 315
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
449-699 1.58e-29

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: 118.11  E-value: 1.58e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSK-RDPSE------EIEiLMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRvAKPHQrekivnEIE-LHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNiLYMDESASadsIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd14189    88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN-FFINENME---LKVGDFGLAARLEPPEQRKKTICG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFSLSGgnwdNISDGAKDLLSHML 681
Cdd:cd14189   164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETL---DLKETYRCIKQVKYTLPA----SLSLPARHLLAGIL 236
                         250
                  ....*....|....*...
gi 1034674014 682 HMDPHQRYTAEQILKHSW 699
Cdd:cd14189   237 KRNPGDRLTLDQILEHEF 254
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
119-352 1.59e-29

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: 118.96  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 119 YAMKVLKKASlkvRDrvrTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLA 197
Cdd:cd14178    31 YAVKIIDKSK---RD---PSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQKCFSEREASAVLC 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 198 ELALALDHLHQLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADW 273
Cdd:cd14178   105 TITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 274 WSYGVLMFEMLTGTLPF-QGKDrnETMNMILkAKLGMPQF---------LSAEAQSLLRMLFKRNPANRLGSegvEEIKR 343
Cdd:cd14178   185 WSLGILLYTMLAGFTPFaNGPD--DTPEEIL-ARIGSGKYalsggnwdsISDAAKDIVSKMLHVDPHQRLTA---PQVLR 258

                  ....*....
gi 1034674014 344 HLFFANIDW 352
Cdd:cd14178   259 HPWIVNREY 267
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
443-700 1.77e-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: 119.06  E-value: 1.77e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI--EIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd06654    22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY-MDesasaDSIRICDFGFAKQLRGENGLLLT 598
Cdd:cd06654   102 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLgMD-----GSVKLTDFGFCAQITPEQSKRST 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG-NGKFSLSggNWDNISDGAKDLL 677
Cdd:cd06654   176 MVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL---NENPLRALYLIAtNGTPELQ--NPEKLSAIFRDFL 250
                         250       260
                  ....*....|....*....|...
gi 1034674014 678 SHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06654   251 NRCLEMDVEKRGSAKELLQHQFL 273
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
439-711 2.17e-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: 119.60  E-value: 2.17e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKE------DIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEiLMRYGQHPNIITLKDVF-- 504
Cdd:cd07856     2 FGTVFEITTrysdlqPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVlakrtyRELK-LLKHLRHENIISLSDIFis 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 505 --DDgryVYLVTDLMkgGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICD 582
Cdd:cd07856    81 plED---IYFVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNIL-VNENC---DLKICD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 583 FGFAK-QLRGENGLLLTPCYTanfvAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGyTPFANGPN-------------DTP 647
Cdd:cd07856   152 FGLARiQDPQMTGYVSTRYYR----APEIMLTwQKYDVEVDIWSAGCIFAEMLEG-KPLFPGKDhvnqfsiitellgTPP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 648 EEILLRIGNG---KF--SLSGGN-------WDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT-HRDqlPNDQP 711
Cdd:cd07856   227 DDVINTICSEntlRFvqSLPKRErvpfsekFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLApYHD--PTDEP 301
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
140-347 2.60e-29

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: 117.23  E-value: 2.60e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 140 ERDILVEVNHPFIVKLHYAFQTEGK-LYLILDFLRGGDVFTR--LSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDL 216
Cdd:cd14109    46 EVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLASTIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 217 KPENILLdEIGHIKLTDFGLSKESVDqEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd14109   126 RPEDILL-QDDKLKLADFGQSRRLLR-GKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDR 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 297 ETMNMILKAKLGMP----QFLSAEAQSLLRMLFKRNPANRLgseGVEEIKRHLFF 347
Cdd:cd14109   204 ETLTNVRSGKWSFDssplGNISDDARDFIKKLLVYIPESRL---TVDEALNHPWF 255
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
443-707 2.94e-29

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: 119.34  E-value: 2.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS-------KRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSetlaqeeVSFFEEERDI-MAKANSPWITKLQYAFQDSENLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQK-CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLrGENG 594
Cdd:cd05601    82 YHPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENIL-IDRTGH---IKLADFGSAAKL-SSDK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLT--PCYTANFVAPEVLM------QQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNW 666
Cdd:cd05601   157 TVTSkmPVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFT---EDTVIKTYSNIMNFKKFLKFPED 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 667 DNISDGAKDLLSHMLhMDPHQRYTAEQILKHS------WITHRDQLP 707
Cdd:cd05601   234 PKVSESAVDLIKGLL-TDAKERLGYEGLCCHPffsgidWNNLRQTVP 279
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
443-707 3.87e-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: 118.06  E-value: 3.87e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKR-------DPSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkeakdgiNFTALREIkLLQELKHPNIIGLLDVFGHKSNINLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGelLDRILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrGE 592
Cdd:cd07841    82 EFMETD--LEKVIKDKSivLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLI----ASDGVLKLADFGLARSF-GS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTP-CYTANFVAPEVLMqqG---YDAACDIWSLGVLFYTMLAGyTPFANGPND------------TPEE------- 649
Cdd:cd07841   155 PNRKMTHqVVTRWYRAPELLF--GarhYGVGVDMWSVGCIFAELLLR-VPFLPGDSDidqlgkifealgTPTEenwpgvt 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 650 -ILLRIGNGKFslSGGNWDNI----SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI------THRDQLP 707
Cdd:cd07841   232 sLPDYVEFKPF--PPTPLKQIfpaaSDDALDLLQRLLTLNPNKRITARQALEHPYFsndpapTPPSQLP 298
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
90-332 4.27e-29

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: 116.76  E-value: 4.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRK---DDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLS--KEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHI-KLTDFGLSKEsVDQEKK 246
Cdd:cd08220    79 EYAPGGTLFEYIQqrKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKI-LSSKSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEAQSLLRMLF 325
Cdd:cd08220   158 AYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSML 237

                  ....*..
gi 1034674014 326 KRNPANR 332
Cdd:cd08220   238 HLDPNKR 244
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
441-700 4.90e-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: 4.90e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKiidKSKRDPSE---------EIEILMRyGQHPNIITLKDVF--DDGRY 509
Cdd:cd07843     5 DEYEKLNRIEEGTYGVVYRARDKKTGEIVALK---KLKMEKEKegfpitslrEINILLK-LQHPNIVTVKEVVvgSNLDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLM----KGgeLLDRILKQkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADsIRICDFGF 585
Cdd:cd07843    81 IYMVMEYVehdlKS--LMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLL---NNRGI-LKICDFGL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLrGENgllLTPcYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGyTPFANGPND------------TP 647
Cdd:cd07843   153 AREY-GSP---LKP-YTQLVVtlwyrAPELLLgAKEYSTAIDMWSVGCIFAELLTK-KPLFPGKSEidqlnkifkllgTP 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 648 -EEI------LLRIGNGKFSLSGGNW-------DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07843   227 tEKIwpgfseLPGAKKKTFTKYPYNQlrkkfpaLSLSDNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
84-348 6.89e-29

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: 116.39  E-value: 6.89e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  84 KADP-AQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAmkvLKKASLKVRDRvRTKM--ERDILVEVNHPFIVKLHYAFQ 160
Cdd:cd06648     2 PGDPrSDLDNFVKIGEGSTGIVCIATDKS---TGRQVA---VKKMDLRKQQR-RELLfnEVVIMRDYQHPNIVEMYSSYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd06648    75 VGDELWVVMEFLEGG-ALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 VDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI---LKAKLGMPQFLSAEA 317
Cdd:cd06648   154 SKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIrdnEPPKLKNLHKVSPRL 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 318 QSLLRMLFKRNPANRLGSegvEEIKRHLFFA 348
Cdd:cd06648   234 RSFLDRMLVRDPAQRATA---AELLNHPFLA 261
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
449-700 8.66e-29

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: 116.25  E-value: 8.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYgQHPNIITLK--DVFDDGRYVYL-------V 513
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtikeiaDEMKVLEGL-DHPNLVRYYgvEVHREEVYIFMeycqegtL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQkcfseREASDILyvisKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQL---- 589
Cdd:cd06626    87 EELLRHGRILDEAVIR-----VYTLQLL----EGLAYLHENGIVHRDIKPANIFL----DSNGLIKLGDFGSAVKLknnt 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 ----RGE-NGLLLTPCYTanfvAPEVLMQQ---GYDAACDIWSLGVLFYTMLAGYTPFANgpNDTPEEILLRIGNG-KFS 660
Cdd:cd06626   154 ttmaPGEvNSLVGTPAYM----APEVITGNkgeGHGRAADIWSLGCVVLEMATGKRPWSE--LDNEWAIMYHVGMGhKPP 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 661 LSGGnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06626   228 IPDS--LQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
443-696 8.91e-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: 115.83  E-value: 8.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-------KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemmdaKARQDCLKEIDLLQQL-NHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELlDRILKQ-----KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdesASAD-SIRICDFGFAKQL 589
Cdd:cd08224    81 LADAGDL-SRLIKHfkkqkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVF-----ITANgVVKLGDLGLGRFF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGE----NGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTPEEILLRIGNGKFS-LSGg 664
Cdd:cd08224   155 SSKttaaHSLVGTPYY----MSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFY-GEKMNLYSLCKKIEKCEYPpLPA- 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 665 nwDNISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd08224   229 --DLYSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
443-700 1.02e-28

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: 116.75  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI--EIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd06655    21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIinEILvMKELKNPNIVNFLDSFLVGDELFVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTP 599
Cdd:cd06655   101 GSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDG----SVKLTDFGFCAQITPEQSKRSTM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG-NGKFSLSggNWDNISDGAKDLLS 678
Cdd:cd06655   176 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQ--NPEKLSPIFRDFLN 250
                         250       260
                  ....*....|....*....|..
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06655   251 RCLEMDVEKRGSAKELLQHPFL 272
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
96-338 1.65e-28

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: 116.02  E-value: 1.65e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVL---KKASLKVRDRVRTKmerdilvevNHPFIVKLHYAFQTE---------- 162
Cdd:cd14171    14 LGTGISGPVRVCVKK---STGERFALKILldrPKARTEVRLHMMCS---------GHPNIVQIYDVYANSvqfpgesspr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLSKE 239
Cdd:cd14171    82 ARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAKV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SvDQEKKAYSFcgTVEYMAPEVV--------NRRG---------HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM--N 300
Cdd:cd14171   162 D-QGDLMTPQF--TPYYVAPQVLeaqrrhrkERSGiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTItkD 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 301 M---ILKAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd14171   239 MkrkIMTGSYEFPEeewsQISEMAKDIVRKLLCVDPEERMTIEEV 283
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
90-344 1.90e-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: 115.09  E-value: 1.90e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVflvrkktgpdaGQLYAMKVLKKASLKVRDR-------VRTKMERD--ILVEVNHPFIVKLHYAFQ 160
Cdd:cd14163     2 YQLGKTIGEGTYSKV-----------KEAFSKKHQRKVAIKIIDKsggpeefIQRFLPRElqIVERLDHKNIIHVYEMLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 -TEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIgHIKLTDFGLSKE 239
Cdd:cd14163    71 sADGKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 -SVDQEKKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFqgkDRNETMNMILKAKLG--MPQFL-- 313
Cdd:cd14163   150 lPKGGRELSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF---DDTDIPKMLCQQQKGvsLPGHLgv 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 314 SAEAQSLLRMLFKRNPANRlgsEGVEEIKRH 344
Cdd:cd14163   227 SRTCQDLLKRLLEPDMVLR---PSIEEVSWH 254
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
90-290 2.62e-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: 115.21  E-value: 2.62e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASlkvrdrvRTKMERDILVEVN------HPFIVKLHYAF--QT 161
Cdd:cd06621     3 IVELSSLGEGAGGSVTKCRLRNT---KTIFALKTITTDP-------NPDVQKQILRELEinkscaSPYIVKYYGAFldEQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVfTRLSKEVLF----TEEDVKFYLAELAL-ALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd06621    73 DSSIGIAMEYCEGGSL-DSIYKKVKKkggrIGEKVLGKIAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 237 SKESVdqEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd06621   152 SGELV--NSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF 203
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
449-700 2.91e-28

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: 114.55  E-value: 2.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII---------DKSKRDPSE----EIEILmRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsaenKDRKKSMLDalqrEIALL-RELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLrgENGL 595
Cdd:cd06628    87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANIL-VDNKGG---IKISDFGISKKL--EANS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTAN--------FVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNgkfSLSGGNWD 667
Cdd:cd06628   161 LSTKNNGARpslqgsvfWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF---PDCTQMQAIFKIGE---NASPTIPS 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 668 NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06628   235 NISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
96-290 3.07e-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: 115.06  E-value: 3.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL------YLIL 169
Cdd:cd14038     2 LGTGGFGNVLRWINQ---ETGEQVAIKQCRQ-ELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDV---FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDE----IGHiKLTDFGLSKEsVD 242
Cdd:cd14038    78 EYCQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgeqrLIH-KIIDLGYAKE-LD 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14038   156 QGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
443-697 3.10e-28

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: 115.07  E-value: 3.10e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdkskRDPSEEI--------EI-LMR---YGQHPNIITLKDVF---DDG 507
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV----RVPLSEEgiplstirEIaLLKqleSFEHPNVVRLLDVChgpRTD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 RY--VYLVTdlmkggELLDRILKQ---KC----FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSI 578
Cdd:cd07838    77 RElkLTLVF------EHVDQDLATyldKCpkpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILV----TSDGQV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 579 RICDFGFAKQLrgENGLLLTPCY-TANFVAPEVLMQQGYDAACDIWSLGVLFYTMlAGYTPFANGPNDT----------- 646
Cdd:cd07838   147 KLADFGLARIY--SFEMALTSVVvTLWYRAPEVLLQSSYATPVDMWSVGCIFAEL-FNRRPLFRGSSEAdqlgkifdvig 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 647 -------PEEILLRIGNGKFSLSGGNWD---NISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07838   224 lpseeewPRNSALPRSSFPSYTPRPFKSfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQH 284
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
89-344 3.37e-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: 115.06  E-value: 3.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLkVRD--------------------RVRTKMER-----DI 143
Cdd:cd14199     3 QYKLKDEIGKGSYGVVKLAYNE---DDNTYYAMKVLSKKKL-MRQagfprrppprgaraapegctQPRGPIERvyqeiAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 144 LVEVNHPFIVKLHYAFQ--TEGKLYLILDFLRGGDVFtRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENI 221
Cdd:cd14199    79 LKKLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 222 LLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVN--RRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNET 298
Cdd:cd14199   158 LVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSetRKIFSgKALDVWAMGVTLYCFVFGQCPFMDERILSL 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 299 MNMILKAKLGMPQF--LSAEAQSLLRMLFKRNPANRLgseGVEEIKRH 344
Cdd:cd14199   238 HSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI---SVPEIKLH 282
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
90-351 4.64e-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: 114.73  E-value: 4.64e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASlkvRDrvrTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14177     6 YELKEDIGVGSYS---VCKRCIHRATNMEFAVKIIDKSK---RD---PSEEIEILMRYgQHPNIITLKDVYDDGRYVYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQE 244
Cdd:cd14177    77 TELMKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGEN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFqGKDRNETMNMILkAKLGMPQF---------LSA 315
Cdd:cd14177   157 GLLLTPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF-ANGPNDTPEEIL-LRIGSGKFslsggnwdtVSD 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 316 EAQSLLRMLFKRNPANRLGSegvEEIKRHLFFANID 351
Cdd:cd14177   235 AAKDLLSHMLHVDPHQRYTA---EQVLKHSWIACRD 267
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
443-711 4.74e-28

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: 115.58  E-value: 4.74e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYS-VCK-RCIHATTNMEFAVK----IIDKS---KRdPSEEIEILMRYGQHPNIITLKD---VFDDG-RY 509
Cdd:cd07857     2 YELIKELGQGAYGiVCSaRNAETSEEETVAIKkitnVFSKKilaKR-ALRELKLLRHFRGHKNITCLYDmdiVFPGNfNE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGelLDRILKqkcfSEREASD-----ILYVISKTVDYLHCQGVVHRDLKPSNILymdesASAD-SIRICDF 583
Cdd:cd07857    81 LYLYEELMEAD--LHQIIR----SGQPLTDahfqsFIYQILCGLKYIHSANVLHRDLKPGNLL-----VNADcELKICDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQL---RGENGLLLTPcYTAN--FVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGyTPFANGPN------------D 645
Cdd:cd07857   150 GLARGFsenPGENAGFMTE-YVATrwYRAPEIMLSfQSYTKAIDVWSVGCILAELLGR-KPVFKGKDyvdqlnqilqvlG 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 646 TP-EEILLRIGNGK-----FSLS-------GGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT-HRDqlPNDQP 711
Cdd:cd07857   228 TPdEETLSRIGSPKaqnyiRSLPnipkkpfESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAiWHD--PDDEP 305
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
443-699 5.17e-28

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: 114.29  E-value: 5.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYGQHPNIITLKDVFDD---GRyVYLVT 514
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQvnnlrEIQALRRLSPHPNILRLIEVLFDrktGR-LALVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGgELLDRILKQK-CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDesasaDSIRICDFGFAKqlrgen 593
Cdd:cd07831    80 ELMDM-NLYELIKGRKrPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-----DILKLADFGSCR------ 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTAN-----FVAPEVLMQQG-YDAACDIWSLGVLFYTMLAGYtPFANGPND------------TPEEILL--- 652
Cdd:cd07831   148 GIYSKPPYTEYistrwYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLF-PLFPGTNEldqiakihdvlgTPDAEVLkkf 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 653 ---RIGNGKFSLSGGNW-----DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07831   227 rksRHMNYNFPSKKGTGlrkllPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
438-696 5.23e-28

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: 113.80  E-value: 5.23e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  438 QFGEVY--ELKEDIGVGSYSVckrcihattnmefAVKII-----DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYV 510
Cdd:smart00221  11 AFGEVYkgTLKGKGDGKEVEV-------------AVKTLkedasEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  511 YLVTDLMKGGELLDRILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQ 588
Cdd:smart00221  77 MIVMEYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV----GENLVVKISDFGLSRD 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  589 LRGENgllLTPCYTANF----VAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNGKFSLSG 663
Cdd:smart00221 153 LYDDD---YYKVKGGKLpirwMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPY---PGMSNAEVLEYLKKGYRLPKP 226
                          250       260       270
                   ....*....|....*....|....*....|...
gi 1034674014  664 gnwDNISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:smart00221 227 ---PNCPPELYKLMLQCWAEDPEDRPTFSELVE 256
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
88-296 5.52e-28

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 113.97  E-value: 5.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVF-----LVRKKTGPDAGQLYAMkvlkkasLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd08228     2 ANFQIEKKIGRGQFSEVYratclLDRKPVALKKVQIFEM-------MDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRL----SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd08228    75 NELNIVLELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd08228   155 FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMN 212
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
465-712 7.69e-28

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: 115.10  E-value: 7.69e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 465 TNMEFAVKIIDKSKRDPSEEI------EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREAS 538
Cdd:cd05595    19 TGRYYAMKILRKEVIIAKDEVahtvteSRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGELFFHLSRERVFTEDRAR 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 DILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDA 618
Cdd:cd05595    99 FYGAEIVSALEYLHSRDVVYRDIKLENLM-LDKDGH---IKITDFGLCKEGITDGATMKTFCGTPEYLAPEVLEDNDYGR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 619 ACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLrIGNGKFSlsggnwDNISDGAKDLLSHMLHMDPHQRY-----TAEQ 693
Cdd:cd05595   175 AVDWWGLGVVMYEMMCGRLPFYNQDHERLFELIL-MEEIRFP------RTLSPEAKSLLAGLLKKDPKQRLgggpsDAKE 247
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 694 ILKH------SW--ITHRDQLPNDQPK 712
Cdd:cd05595   248 VMEHrfflsiNWqdVVQKKLLPPFKPQ 274
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
96-332 7.88e-28

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: 112.59  E-value: 7.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLvrkktGPDAGQLYAMKvlkkaslKVRDRVRTKMERdiLVEVNHPFIVKLHyAFQTEGKLYLIL-DFLRG 174
Cdd:cd14059     1 LGSGAQGAVFL-----GKFRGEEVAVK-------KVRDEKETDIKH--LRKLNHPNIIKFK-GVCTQAPCYCILmEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAySFCGTV 254
Cdd:cd14059    66 GQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKM-SFAGTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 255 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM-----NMIlkaKLGMPQFLSAEAQSLLRMLFKRNP 329
Cdd:cd14059   145 AWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIwgvgsNSL---QLPVPSTCPDGFKLLMKQCWNSKP 221

                  ...
gi 1034674014 330 ANR 332
Cdd:cd14059   222 RNR 224
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
443-707 1.08e-27

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: 115.17  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPS----EEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05596    28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFemiKRSDSaffwEERDI-MAHANSEWIVQLHYAFQDDKYLYMVMD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDrILKQKCFSEREAsdILYvISKTV---DYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLrGE 592
Cdd:cd05596   107 YMPGGDLVN-LMSNYDVPEKWA--RFY-TAEVVlalDAIHSMGFVHRDVKPDNML-LDASGH---LKLADFGTCMKM-DK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLL--TPCYTANFVAPEVLMQQG----YDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILlrigNGKFSLSGGN 665
Cdd:cd05596   178 DGLVRsdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFyADSLVGTYGKIM----NHKNSLQFPD 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 666 WDNISDGAKDLLSHMLHMDPHQ--RYTAEQILKH--------SWITHRDQLP 707
Cdd:cd05596   254 DVEISKDAKSLICAFLTDREVRlgRNGIEEIKAHpffkndqwTWDNIRETVP 305
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
96-306 1.11e-27

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: 114.13  E-value: 1.11e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKAS----LKVRDRvrtkmERDILVEVNHPFIVKLhYAFQTE----GKLy 166
Cdd:cd13988     1 LGQGATANVFRGRhKKTG----DLYAVKVFNNLSfmrpLDVQMR-----EFEVLKKLNHKNIVKL-FAIEEElttrHKV- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRL---SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL--LDEIGH--IKLTDFGLSKE 239
Cdd:cd13988    70 LVMELCPCGSLYTVLeepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 240 SVDQEKKAySFCGTVEYMAPEVVNR---RGHSQ-----SADWWSYGVLMFEMLTGTLPFQ---GKDRN-ETMNMILKAK 306
Cdd:cd13988   150 LEDDEQFV-SLYGTEEYLHPDMYERavlRKDHQkkygaTVDLWSIGVTFYHAATGSLPFRpfeGPRRNkEVMYKIITGK 227
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
449-699 1.38e-27

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: 112.42  E-value: 1.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSK---RDPSEEIEILMRYGQHPNIITLKDVF--DDGRYVYlVTDLMKGGELL 523
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStklKDFLREYNISLELSVHPHIIKTYDVAfeTEDYYVF-AQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 524 DRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAkqlRGENGLLLTPCYTA 603
Cdd:cd13987    80 SIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCR--RVKLCDFGLT---RRVGSTVKRVSGTI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 604 NFVAPEVL---MQQGY--DAACDIWSLGVLFYTMLAGYTPF--ANGpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDL 676
Cdd:cd13987   155 PYTAPEVCeakKNEGFvvDPSIDVWAFGVLLFCCLTGNFPWekADS-DDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRM 233
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 677 LSHMLHMDPHQRYTAEQI---LKHSW 699
Cdd:cd13987   234 FKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
443-697 2.27e-27

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: 112.79  E-value: 2.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYS----VCKRCIHATTNMeFAVKIIDKS----KRDPSE----EIEILMRYGQHPNIITLKDVFDDGRYV 510
Cdd:cd05613     2 FELLKVLGTGAYGkvflVRKVSGHDAGKL-YAMKVLKKAtivqKAKTAEhtrtERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQ-L 589
Cdd:cd05613    81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENIL-LD---SSGHVVLTDFGLSKEfL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTPCYTANFVAPEVLM--QQGYDAACDIWSLGVLFYTMLAGYTPFA-NGPNDTPEEILLRIGNGKFSLSggnw 666
Cdd:cd05613   157 LDENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRILKSEPPYP---- 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 667 DNISDGAKDLLSHMLHMDPHQRY-----TAEQILKH 697
Cdd:cd05613   233 QEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKH 268
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
449-699 2.31e-27

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: 111.64  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSK-RDPSE------EIEiLMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRvSKPHQrekidkEIE-LHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNiLYMDESASadsIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd14188    88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN-FFINENME---LKVGDFGLAARLEPLEHRRRTICG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSHML 681
Cdd:cd14188   164 TPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFE---TTNLKETYRCIREARYSLP----SSLLAPAKHLIASML 236
                         250
                  ....*....|....*...
gi 1034674014 682 HMDPHQRYTAEQILKHSW 699
Cdd:cd14188   237 SKNPEDRPSLDEIIRHDF 254
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
89-290 2.77e-27

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: 111.66  E-value: 2.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMK-VLKKASLKVRDRvrTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14088     2 RYDLGQVIKTEEFCEIFRAKDKT---TGKLYTCKkFLKRDGRKVRKA--AKNEINILKMVKHPNILQLVDVFETRKEYFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIGHIK--LTDFGLSKESVDQE 244
Cdd:cd14088    77 FLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNSKivISDFHLAKLENGLI 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 245 KKAysfCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14088   157 KEP---CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPF 199
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
85-348 3.00e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 113.77  E-value: 3.00e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADPAQFELLKV--LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASlkvRDRVRTKMERDI--LVEVNHPFIVKLHYAFQ 160
Cdd:PLN00034   69 AAKSLSELERVnrIGSGAGGTVYKVIHRP---TGRLYALKVIYGNH---EDTVRRQICREIeiLRDVNHPNVVKCHDMFD 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDFLRGGDV-FTRLSKEVlfteedvkfYLAELAL----ALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:PLN00034  143 HNGEIQVLLEFMDGGSLeGTHIADEQ---------FLADVARqilsGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFG 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 236 LSKESVDQEKKAYSFCGTVEYMAPEVVNR-----RGHSQSADWWSYGVLMFEMLTGTLPF----QGkDRNETMNMI-LKA 305
Cdd:PLN00034  214 VSRILAQTMDPCNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQG-DWASLMCAIcMSQ 292
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 306 KLGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFFA 348
Cdd:PLN00034  293 PPEAPATASREFRHFISCCLQREPAKRWSA---MQLLQHPFIL 332
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
90-332 3.41e-27

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: 112.03  E-value: 3.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKAslKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNK---ATGEIVAIKKFKES--EDDEDVKKTALREVkvLRQLRHENIVNLKEAFRRKGRLYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFlrggdvFTRLSKEVL------FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd07833    78 VFEY------VERTLLELLeaspggLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAY-SFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQflsaEAQS 319
Cdd:cd07833   152 ARPASPLtDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPP----SHQE 227
                         250
                  ....*....|...
gi 1034674014 320 llrmLFKRNPANR 332
Cdd:cd07833   228 ----LFSSNPRFA 236
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
464-699 4.06e-27

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: 112.83  E-value: 4.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 464 TTNMEFAVKIIDKSKRDPSEEIE------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREA 537
Cdd:cd05571    18 ATGELYAIKILKKEVIIAKDEVAhtltenRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGELFFHLSRERVFSEDRT 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 538 SDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYD 617
Cdd:cd05571    98 RFYGAEIVLALGYLHSQGIVYRDLKLENLL-LDKDGH---IKITDFGLCKEEISYGATTKTFCGTPEYLAPEVLEDNDYG 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 618 AACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLrIGNGKFSlsggnwDNISDGAKDLLSHMLHMDPHQRY-----TAE 692
Cdd:cd05571   174 RAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELIL-MEEVRFP------STLSPEAKSLLAGLLKKDPKKRLgggprDAK 246

                  ....*..
gi 1034674014 693 QILKHSW 699
Cdd:cd05571   247 EIMEHPF 253
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
95-294 4.73e-27

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: 110.95  E-value: 4.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLK----KASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd14061     1 VIGVGGFGKVYRGIWR-----GEEVAVKAARqdpdEDISVTLENVRQ--EARLFWMLRHPNIIALRGVCLQPPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSK-----EVLFTeedvkfYLAELALALDHLHQLG---IVYRDLKPENILLDE-IGH-------IKLTDF 234
Cdd:cd14061    74 YARGGALNRVLAGrkippHVLVD------WAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaIENedlenktLKITDF 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 235 GLSKESVDQEKkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD 294
Cdd:cd14061   148 GLAREWHKTTR--MSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGID 205
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
90-332 5.02e-27

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: 110.48  E-value: 5.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKvlkkaslKVRDRVRTKMER-DILVEVN-------HPFIVKLHYAFQT 161
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSR---EDGKLYAVK-------RSRSRFRGEKDRkRKLEEVErheklgeHPNCVRFIKAWEE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsV 241
Cdd:cd14050    73 KGILYIQTE-LCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-L 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNrrGH-SQSADWWSYGVLMFEMLTGT-LPFQGKDRNETMNMILKAKLGMPqfLSAEAQS 319
Cdd:cd14050   151 DKEDIHDAQEGDPRYMAPELLQ--GSfTKAADIFSLGITILELACNLeLPSGGDGWHQLRQGYLPEEFTAG--LSPELRS 226
                         250
                  ....*....|...
gi 1034674014 320 LLRMLFKRNPANR 332
Cdd:cd14050   227 IIKLMMDPDPERR 239
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
96-332 5.10e-27

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 110.83  E-value: 5.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKvRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14113    15 LGRGRFS---VVKKCDQRGTKRAVATKFVNKKLMK-RDQV--THELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGlskESVDQEKKAY--SF 250
Cdd:cd14113    89 RLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFG---DAVQLNTTYYihQL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 251 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 326
Cdd:cd14113   166 LGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQ 245

                  ....*.
gi 1034674014 327 RNPANR 332
Cdd:cd14113   246 MDPAKR 251
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
86-289 5.52e-27

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: 111.32  E-value: 5.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKV--LKKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd06641     1 DPEElFTKLEKIGKGSFGEVF---KGIDNRTQKVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYLKD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06641    75 TKLWIIMEYLGGGSALDLLEPGPL-DETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLP 289
Cdd:cd06641   154 TQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
449-700 5.53e-27

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: 110.91  E-value: 5.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKI--IDKSKRDPSEEI-----EI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEVkalecEIqLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdeSASADSIRICDFGFAKQL---RGENGlLL 597
Cdd:cd06625    88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL----RDSNGNVKLGDFGASKRLqtiCSSTG-MK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIG--NGKFSLSggnwDNISDGAKD 675
Cdd:cd06625   163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEF---EPMAAIFKIAtqPTNPQLP----PHVSEDARD 235
                         250       260
                  ....*....|....*....|....*
gi 1034674014 676 LLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06625   236 FLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
431-711 5.92e-27

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: 112.83  E-value: 5.92e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 431 QINGNAAQFGEVYELKEDIGVGSY-SVCKrCIHATTNMEFAVKIIDK-------SKRDPSEEIeiLMRYGQHPNIITLKD 502
Cdd:cd07877     7 ELNKTIWEVPERYQNLSPVGSGAYgSVCA-AFDTKTGLRVAVKKLSRpfqsiihAKRTYRELR--LLKHMKHENVIGLLD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 503 VFDDGRY------VYLVTDLMkgGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNiLYMDESAsad 576
Cdd:cd07877    84 VFTPARSleefndVYLVTHLM--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSN-LAVNEDC--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 577 SIRICDFGFAKQLRGE-NGLLLTPCYTanfvAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANGPN---------- 644
Cdd:cd07877   158 ELKILDFGLARHTDDEmTGYVATRWYR----APEIMLNwMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHidqlklilrl 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 645 -DTPE-EILLRIGNGKF--------SLSGGNWDNISDGAK----DLLSHMLHMDPHQRYTAEQILKHSWITHRDQlPNDQ 710
Cdd:cd07877   234 vGTPGaELLKKISSESArnyiqsltQMPKMNFANVFIGANplavDLLEKMLVLDSDKRITAAQALAHAYFAQYHD-PDDE 312

                  .
gi 1034674014 711 P 711
Cdd:cd07877   313 P 313
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
441-699 5.95e-27

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: 111.31  E-value: 5.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYgQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVikkialREIRMLKQL-KHPNLVNLIEVFRRKRKLHLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGEL--LDRilKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGE 592
Cdd:cd07847    80 EYCDHTVLneLEK--NPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILI----TKQGQIKLCDFGFARILTGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTPCYTANFVAPEVL---MQqgYDAACDIWSLGVLFYTMLAGyTPFANGPNDTPEEILLRIGNGKF-----SLSGG 664
Cdd:cd07847   154 GDDYTDYVATRWYRAPELLvgdTQ--YGPPVDVWAIGCVFAELLTG-QPLWPGKSDVDQLYLIRKTLGDLiprhqQIFST 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 665 N--------------------WDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07847   231 NqffkglsipepetrepleskFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
443-700 7.56e-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: 110.29  E-value: 7.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEreesrkEVAVLSKM-KHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLRGENG 594
Cdd:cd08218    81 CDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGI----IKLGDFGIARVLNSTVE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFSLSGGNWdniSDGAK 674
Cdd:cd08218   157 LARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAG---NMKNLVLKIIRGSYPPVPSRY---SYDLR 230
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd08218   231 SLVSQLFKRNPRDRPSINSILEKPFI 256
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
438-696 7.66e-27

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 110.31  E-value: 7.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  438 QFGEVY--ELKEDIGVGSYSVckrcihattnmefAVKIIDKSKrDPSEEIEIL-----MRYGQHPNIITLKDVFDDGRYV 510
Cdd:smart00219  11 AFGEVYkgKLKGKGGKKKVEV-------------AVKTLKEDA-SEQQIEEFLreariMRKLDHPNVVKLLGVCTEEEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  511 YLVTDLMKGGELLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQL 589
Cdd:smart00219  77 YIVMEYMEGGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV----GENLVVKISDFGLSRDL 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  590 ------RGENGLLltPcytanfV---APEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNGKF 659
Cdd:smart00219 153 ydddyyRKRGGKL--P------IrwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPY---PGMSNEEVLEYLKNGYR 221
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1034674014  660 SLSGgnwDNISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:smart00219 222 LPQP---PNCPPELYDLMLQCWAEDPEDRPTFSELVE 255
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
449-699 1.03e-26

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: 110.18  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYS----VCKRCIHATTNMeFAVKIIDKS----KRDPSE----EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd05583     2 LGTGAYGkvflVRKVGGHDAGKL-YAMKVLKKAtivqKAKTAEhtmtERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASdiLYV--ISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQ-LRGEN 593
Cdd:cd05583    81 VNGGELFTHLYQREHFTESEVR--IYIgeIVLALEHLHKLGIIYRDIKLENIL-LDSEGH---VVLTDFGLSKEfLPGEN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTANFVAPEVLM--QQGYDAACDIWSLGVLFYTMLAGYTPFA-NGPNDTPEEILLRIGNGKFSLSggnwDNIS 670
Cdd:cd05583   155 DRAYSFCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTvDGERNSQSEISKRILKSHPPIP----KTFS 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 671 DGAKDLLSHMLHMDPHQR-----YTAEQILKHSW 699
Cdd:cd05583   231 AEAKDFILKLLEKDPKKRlgagpRGAHEIKEHPF 264
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
494-651 1.03e-26

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: 111.34  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESA 573
Cdd:cd05582    56 HPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEDG 134
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 574 sadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEIL 651
Cdd:cd05582   135 ---HIKLTDFGLSKESIDHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFqGKDRKETMTMIL 210
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
437-700 1.03e-26

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 109.95  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 437 AQFGEVYELKEDIGV--GSY---SVCKrciHATTNMEFAVKIIDKSKRDPSE-EIEILMRygQHPNIITLKDVFDDGRYV 510
Cdd:PHA03390   10 VQFLKNCEIVKKLKLidGKFgkvSVLK---HKPTQKLFVQKIIKAKNFNAIEpMVHQLMK--DNPNFIKLYYSVTTLKGH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFAKqLR 590
Cdd:PHA03390   85 VLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY---DRAKDRIYLCDYGLCK-II 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GenglllTP-CY--TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPND--TPEEILLRIGNGKFSLSggn 665
Cdd:PHA03390  161 G------TPsCYdgTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEelDLESLLKRQQKKLPFIK--- 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 666 wdNISDGAKDLLSHMLHMDPHQR-YTAEQILKHSWI 700
Cdd:PHA03390  232 --NVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFL 265
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
449-698 1.13e-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: 109.78  E-value: 1.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKEraralrEVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 ---LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRG----ENGl 595
Cdd:cd13997    88 qdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI----SNKGTCKIGDFGLATRLETsgdvEEG- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 lltpcyTANFVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtpeeiLLRIGNGKFSLSGGnwDNISDGAK 674
Cdd:cd13997   163 ------DSRYLAPELLNEnYTHLPKADIFSLGVTVYEAATGEPLPRNGQQ------WQQLRQGKLPLPPG--LVLSQELT 228
                         250       260
                  ....*....|....*....|....
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd13997   229 RLLKVMLDPDPTRRPTADQLLAHD 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
449-700 1.36e-26

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: 109.41  E-value: 1.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII-----DKSKRDPSEEI--EILMRYG-QHPNII----TLKDvfDDGRYVYLvtDL 516
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKEVslvddDKKSRESVKQLeqEIALLSKlRHPNIVqyygTERE--EDNLYIFL--EY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLRgENGLL 596
Cdd:cd06632    84 VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANIL-VDTNG---VVKLADFGMAKHVE-AFSFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQ--GYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFSLSGGnwDNISDGAK 674
Cdd:cd06632   159 KSFKGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQY---EGVAAIFKIGNSGELPPIP--DHLSPDAK 233
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06632   234 DFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
96-290 1.51e-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: 110.39  E-value: 1.51e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKvLKKASLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKLYLILD 170
Cdd:cd14039     1 LGTGGFGNVCLYQNQ---ETGEKIAIK-SCRLELSVKNKDRWCHEIQIMKKLNHPNVVKAcdvpeEMNFLVNDVPLLAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKE---VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG----HiKLTDFGLSKEsVDQ 243
Cdd:cd14039    77 YCSGGDLRKLLNKPencCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivH-KIIDLGYAKD-LDQ 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14039   155 GSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
449-711 1.64e-26

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: 111.31  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDK-------SKRDpSEEIEiLMRYGQHPNIITLKDV--------FDDgryVYLV 513
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIANafdnridAKRT-LREIK-LLRHLDHENVIAIKDImppphreaFND---VYIV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMkggellDRILKQKCFSEREASD-----ILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADsIRICDFGFAKQ 588
Cdd:cd07858    88 YELM------DTDLHQIIRSSQTLSDdhcqyFLYQLLRGLKYIHSANVLHRDLKPSNLLL---NANCD-LKICDFGLART 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTPCYTANFVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFA---------------NGPNDTPEEILL 652
Cdd:cd07858   158 TSEKGDFMTEYVVTRWYRAPELLLNcSEYTTAIDVWSVGCIFAELLGRKPLFPgkdyvhqlklitellGSPSEEDLGFIR 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 653 RIGNGKFSLSGGN---------WDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT-HRDqlPNDQP 711
Cdd:cd07858   238 NEKARRYIRSLPYtprqsfarlFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLAsLHD--PSDEP 304
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
93-332 1.73e-26

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: 109.73  E-value: 1.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLkkaSLKVRDRVRT-KMERDILVEV-NHPFIVKL--HYAFQTEG-KLYL 167
Cdd:cd13985     5 TKQLGEGGFSYVYLAHDVN---TGRRYALKRM---YFNDEEQLRVaIKEIEIMKRLcGHPNIVQYydSAILSSEGrKEVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILLDEIGHIKLTDFGlskeSVDQ 243
Cdd:cd13985    79 LLMEYCPGSLVDILEKSPpsPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG----SATT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAY---SFCGTVE----------YMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrNETMNmILKAKL 307
Cdd:cd13985   155 EHYPLeraEEVNIIEeeiqknttpmYRAPEMIDlysKKPIGEKADIWALGCLLYKLCFFKLPFDE---SSKLA-IVAGKY 230
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 308 GMPQF--LSAEAQSLLRMLFKRNPANR 332
Cdd:cd13985   231 SIPEQprYSPELHDLIRHMLTPDPAER 257
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
468-697 1.74e-26

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: 109.61  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDKSKRDPSE------EIEILMRYGQHPNIITLKD--VFDDGRYVYLVtdlMKGGEL-LDRILKQKcfsEREAS 538
Cdd:cd14131    27 IYALKRVDLEGADEQTlqsyknEIELLKKLKGSDRIIQLYDyeVTDEDDYLYMV---MECGEIdLATILKKK---RPKPI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 DILYVIS------KTVDYLHCQGVVHRDLKPSNILYMDesasaDSIRICDFGFAKQLRGE--NGLLLTPCYTANFVAPEV 610
Cdd:cd14131   101 DPNFIRYywkqmlEAVHTIHEEGIVHSDLKPANFLLVK-----GRLKLIDFGIAKAIQNDttSIVRDSQVGTLNYMSPEA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 611 LMQQGYDA----------ACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGKFSLsggNWDNISDgaKDLLSHM 680
Cdd:cd14131   176 IKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQHITN--PIAKLQAIIDPNHEI---EFPDIPN--PDLIDVM 248
                         250       260
                  ....*....|....*....|
gi 1034674014 681 ---LHMDPHQRYTAEQILKH 697
Cdd:cd14131   249 krcLQRDPKKRPSIPELLNH 268
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
449-748 2.06e-26

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: 110.35  E-value: 2.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05585     2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVThtlaertVLAQV-DCPFIVPLKFSFQSPEKLYLVLAFINGGE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05585    81 LFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENIL-LDYTGH---IALCDFGLCKLNMKDDDKTNTFCG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpNDTPE---EIL---LRIGngkfslsggnwDNISDGAKD 675
Cdd:cd05585   157 TPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYD--ENTNEmyrKILqepLRFP-----------DGFDRDAKD 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 676 LLSHMLHMDPHQRY---TAEQILKHSWITHRDqlpndqpkrndvshvvkgamvatYSALTHKTFQPVLEPVAASSL 748
Cdd:cd05585   224 LLIGLLNRDPTKRLgynGAQEIKNHPFFDQID-----------------------WKRLLMKKIQPPFKPAVENAI 276
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
469-688 2.07e-26

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: 110.82  E-value: 2.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKS-------KRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDIL 541
Cdd:cd05604    24 YAVKVLQKKvilnrkeQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGELFFHLQRERSFPEPRARFYA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACD 621
Cdd:cd05604   104 AEIASALGYLHSINIVYRDLKPENIL-LD---SQGHIVLTDFGLCKEGISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVD 179
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 622 IWSLGVLFYTMLAGYTPFANgpNDTpEEILLRIGNGKFSLSGGnwdnISDGAKDLLSHMLHMDPHQR 688
Cdd:cd05604   180 WWCLGSVLYEMLYGLPPFYC--RDT-AEMYENILHKPLVLRPG----ISLTAWSILEELLEKDRQLR 239
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
86-289 2.42e-26

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: 109.37  E-value: 2.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKV--LKKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd06640     1 DPEElFTKLERIGKGSFGEVF---KGIDNRTQQVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYLKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRLsKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06640    75 TKLWIIMEYLGGGSALDLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLP 289
Cdd:cd06640   154 TQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
449-700 2.70e-26

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: 109.69  E-value: 2.70e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCkrCI--HATTNMEFAVKIIDKSKRDPSE----EIeILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGEL 522
Cdd:cd06659    29 IGEGSTGVV--CIarEKHSGRQVAVKMMDLRKQQRREllfnEV-VIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGE----NGLLLT 598
Cdd:cd06659   106 TD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG----RVKLSDFGFCAQISKDvpkrKSLVGT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKfSLSGGNWDNISDGAKDLLS 678
Cdd:cd06659   181 PYW----MAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYF---SDSPVQAMKRLRDSP-PPKLKNSHKASPVLRDFLE 252
                         250       260
                  ....*....|....*....|..
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06659   253 RMLVRDPQERATAQELLDHPFL 274
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
441-697 3.07e-26

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: 108.46  E-value: 3.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYS-VCK-RCIH-----ATTNMEFAVK-IIDKSKrdPS---EEIEILMRYGQHPNIITLKDVFDDGRY 509
Cdd:cd14019     1 NKYRIIEKIGEGTFSsVYKaEDKLhdlydRNKGRLVALKhIYPTSS--PSrilNELECLERLGGSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELLDRILKqkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdsiRICDFGFA--- 586
Cdd:cd14019    79 VVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKG---VLVDFGLAqre 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 ---KQLRGengllltPCY-TANFVAPEVLMQ---QGydAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGngkf 659
Cdd:cd14019   153 edrPEQRA-------PRAgTRGFRAPEVLFKcphQT--TAIDIWSAGVILLSILSGRFPFFFSSDD--IDALAEIA---- 217
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 660 SLSGgnwdniSDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14019   218 TIFG------SDEAYDLLDKLLELDPSKRITAEEALKH 249
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
90-347 3.18e-26

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: 109.05  E-value: 3.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLI 168
Cdd:cd06617     3 LEVIEELGRGAYG---VVDKMRHVPTGTIMAVKRIR-ATVNSQEQKRLLMDLDISMRSVDcPYTVTFYGALFREGDVWIC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGG--DVFTRLSKEVLFTEEDVkfyLAELAL----ALDHLH-QLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd06617    79 MEVMDTSldKFYKKVYDKGLTIPEDI---LGKIAVsivkALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSfCGTVEYMAPEVVN----RRGHSQSADWWSYGVLMFEMLTGTLPFqgkDRNETMNMILK-------AKLGMP 310
Cdd:cd06617   156 DSVAKTID-AGCKPYMAPERINpelnQKGYDVKSDVWSLGITMIELATGRFPY---DSWKTPFQQLKqvveepsPQLPAE 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 311 QFlSAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLFF 347
Cdd:cd06617   232 KF-SPEFQDFVNKCLKKNYKER---PNYPELLQHPFF 264
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
441-695 3.38e-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: 3.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELkedIGVGSYSVCKRCIHATTNMEFAVKIID-KSKRDPSEEIE---ILMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd13996     9 EEIEL---LGSGGFGSVYKVRNKVDGVTYAIKKIRlTEKSSASEKVLrevKALAKLNHPNIVRYYTAWVEEPPLYIQMEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGEL---LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFAK---QLR 590
Cdd:cd13996    86 CEGGTLrdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL---DNDDLQVKIGDFGLATsigNQK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTAN-----------FVAPEVLMQQGYDAACDIWSLGVLFYTMLAgytpfangPNDTPEE---ILLRIGN 656
Cdd:cd13996   163 RELNNLNNNNNGNTsnnsvgigtplYASPEQLDGENYNEKADIYSLGIILFEMLH--------PFKTAMErstILTDLRN 234
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 657 GKFSLSGGNWDNISdgaKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd13996   235 GILPESFKAKHPKE---ADLIQSLLSKNPEERPSAEQLL 270
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
87-346 4.22e-26

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: 108.19  E-value: 4.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVL--KKASLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQ--T 161
Cdd:cd06653     1 PVNWRLGKLLGRGAFGEVYLCYDA---DTGRELAVKQVpfDPDSQETSKEVNAlECEIQLLKNLRHDRIVQYYGCLRdpE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--E 239
Cdd:cd06653    78 EKKLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKriQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAY-SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILK-----AKLGMPQFL 313
Cdd:cd06653   158 TICMSGTGIkSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKiatqpTKPQLPDGV 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 314 SAEAQSLLRMLF---KRNPAnrlgsegVEEIKRHLF 346
Cdd:cd06653   235 SDACRDFLRQIFveeKRRPT-------AEFLLRHPF 263
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
95-346 4.35e-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: 108.29  E-value: 4.35e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKTGpdagQLYAmkvLKKASLKVRDRVRTKM-------ERDILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06631     8 VLGKGAYGTVYCGLTSTG----QLIA---VKQVELDTSDKEKAEKeyeklqeEVDLLKTLKHVNIVGYLGTCLEDNVVSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE------SV 241
Cdd:cd06631    81 FMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRlcinlsSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQ 318
Cdd:cd06631   161 SQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLpdkFSPEAR 240
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 319 SLLRMLFKRNPANRLGSegvEEIKRHLF 346
Cdd:cd06631   241 DFVHACLTRDQDERPSA---EQLLKHPF 265
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
90-347 5.50e-26

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: 107.69  E-value: 5.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDA----GQLYAMKVLKKASLKVRdrvrTKMERDILVEVN-HPFIVKLHYAFQTEGK 164
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKLHDLYdrnkGRLVALKHIYPTSSPSR----ILNELECLERLGgSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSKevlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFGLSKESVDQ 243
Cdd:cd14019    79 VVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQREEDR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSA-DWWSYGVLMFEMLTGTLP-FQGKDRNETMNMIlkaklgMPQFLSAEAQSLL 321
Cdd:cd14019   156 PEQRAPRAGTRGFRAPEVLFKCPHQTTAiDIWSAGVILLSILSGRFPfFFSSDDIDALAEI------ATIFGSDEAYDLL 229
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 322 RMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd14019   230 DKLLELDPSKRITA---EEALKHPFF 252
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
482-697 7.47e-26

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: 107.74  E-value: 7.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 482 SEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG--ELLDRILKQKCF--SEREASDILYVISKTVDYLHCQGVV 557
Cdd:cd13982    42 DREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAASlqDLVESPRESKLFlrPGLEPVRLLRQIASGLAHLHSLNIV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 558 HRDLKPSNILY-MDESASADSIRICDFGFAKQL-RGENGLLLT--PCYTANFVAPEVLMQQGYD---AACDIWSLG-VLF 629
Cdd:cd13982   122 HRDLKPQNILIsTPNAHGNVRAMISDFGLCKKLdVGRSSFSRRsgVAGTSGWIAPEMLSGSTKRrqtRAVDIFSLGcVFY 201
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 630 YTMLAGYTPFanGPNdtpeeiLLRIGN---GKFSLSggnwDNISDG-----AKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd13982   202 YVLSGGSHPF--GDK------LEREANilkGKYSLD----KLLSLGehgpeAQDLIERMIDFDPEKRPSAEEVLNH 265
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
94-347 8.80e-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: 107.52  E-value: 8.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRK-KTGpdagQLYAMKVLK--KASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd06630     6 PLLGTGAFSSCYQARDvKTG----TLMAVKQVSfcRNSSSEQEEVVEAIREEIrmMARLNHPNIVRMLGATQHKSHFNIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG-HIKLTDFGLSKESVDQEKKA 247
Cdd:cd06630    82 VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSF----CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM-----PQFLSAEAQ 318
Cdd:cd06630   162 GEFqgqlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATtpppiPEHLSPGLR 241
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 319 SLLRMLFKRNPANRlgsEGVEEIKRHLFF 347
Cdd:cd06630   242 DVTLRCLELQPEDR---PPARELLKHPVF 267
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-688 9.43e-26

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: 107.59  E-value: 9.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSY-SVCKRCIHATTNMEFAVKII--------------DKSKRDPSEEIEILMRYGQHPNIITLKDVFDDG 507
Cdd:cd08528     2 YAVLELLGSGAFgCVYKVRKKSNGQTLLALKEInmtnpafgrteqerDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 RYVYLVTDLMKGGELLDRI--LKQKC--FSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYMDEsasaDSIRICD 582
Cdd:cd08528    82 DRLYIVMELIEGAPLGEHFssLKEKNehFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLGED----DKVTITD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 583 FGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFS-L 661
Cdd:cd08528   158 FGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFY---STNMLTLATKIVEAEYEpL 234
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 662 SGGNWdniSDGAKDLLSHMLHMDPHQR 688
Cdd:cd08528   235 PEGMY---SDDITFVIRSCLTPDPEAR 258
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
443-699 1.02e-25

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: 108.04  E-value: 1.02e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVK-IIDKSKRDPS-----EEIEILMRYgQHPNIITLKDV---FDDGRY---V 510
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkIRMENEKEGFpitaiREIKLLQKL-DHPNVVRLKEIvtsKGSAKYkgsI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLM----KGgeLLDRILKQkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA 586
Cdd:cd07840    80 YMVFEYMdhdlTG--LLDNPEVK--FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDG----VLKLADFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLRGENGLLLTP-CYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIgngkFSLSGG 664
Cdd:cd07840   152 RPYTKENNADYTNrVITLWYRPPELLLgATRYGPEVDMWSVGCILAELFTGKPIF---QGKTELEQLEKI----FELCGS 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 665 ----NWDNISD---------------------------GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07840   225 pteeNWPGVSDlpwfenlkpkkpykrrlrevfknvidpSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
96-339 1.17e-25

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: 107.25  E-value: 1.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14104     8 LGRGQFGIVHRCVETS---SKKTYMAKFVK---VKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFEFISGV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLS-KEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENIL-LDEIGH-IKLTDFGLSKESVDQEKKAYSFCg 252
Cdd:cd14104    82 DIFERITtARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyCTRRGSyIKIIEFGQSRQLKPGDKFRLQYT- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLL-RMLFKR 327
Cdd:cd14104   161 SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDFVdRLLVKE 240
                         250
                  ....*....|..
gi 1034674014 328 NPANRLGSEGVE 339
Cdd:cd14104   241 RKSRMTAQEALN 252
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
88-296 1.28e-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: 107.81  E-value: 1.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd08229    24 ANFRIEKKIGRGQFSEVY---RATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRL----SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd08229   101 IVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSS 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd08229   181 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMN 234
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
462-704 1.48e-25

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: 107.11  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 462 HATTNMEFAVKIIDKSK---RDPSEEIEI---LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE---LLDRI------ 526
Cdd:cd05609    21 HRETRQRFAMKKINKQNlilRNQIQQVFVerdILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatLLKNIgplpvd 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 527 LKQKCFSEReasdILyviskTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQlrgenGLL-LTP------ 599
Cdd:cd05609   101 MARMYFAET----VL-----ALEYLHSYGIVHRDLKPDNLLI----TSMGHIKLTDFGLSKI-----GLMsLTTnlyegh 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 -------------CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNw 666
Cdd:cd05609   163 iekdtrefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF---GDTPEELFGQVISDEIEWPEGD- 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 667 DNISDGAKDLLSHMLHMDPHQRY---TAEQILKHSWITHRD 704
Cdd:cd05609   239 DALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQDLD 279
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
439-691 1.60e-25

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: 108.43  E-value: 1.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDigvgsysvckrcihaTTNMEFAVKIIDKSKRDPSEEI-------EILMR--YGQHPNIITLKDVFDDGRY 509
Cdd:cd05586     6 FGQVYQVRKK---------------DTRRIYAMKVLSKKVIVAKKEVahtigerNILVRtaLDESPFIVGLKFSFQTPTD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQL 589
Cdd:cd05586    71 LYLVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENIL-LDANG---HIALCDFGLSKAD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtpEEILLRIGNGKFSLSGgnwDN 668
Cdd:cd05586   147 LTDNKTTNTFCGTTEYLAPEVLLdEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDT---QQMYRNIAFGKVRFPK---DV 220
                         250       260
                  ....*....|....*....|...
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRYTA 691
Cdd:cd05586   221 LSDEGRSFVKGLLNRNPKHRLGA 243
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
90-301 1.89e-25

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: 107.52  E-value: 1.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06615     3 FEKLGELGAGNGGVVTKVLHRP---SGLIMARKLIH---LEIKPAIRNQIIRElkVLHECNSPYIVGFYGAFYSDGEISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEdvkfYLAELALA----LDHLHQ-LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06615    77 CMEHMDGGSLDQVLKKAGRIPEN----ILGKISIAvlrgLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 243 QekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd06615   153 S--MANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAM 209
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
86-296 1.94e-25

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: 106.75  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLV-RKKTGpdagqlyamKVLKKASLKV--RDRVRTKM--ERDILVEVNHPFIVKLHYAFQ 160
Cdd:cd06620     3 KNQDLETLKDLGAGNGGSVSKVlHIPTG---------TIMAKKVIHIdaKSSVRKQIlrELQILHECHSPYIVSFYGAFL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TE-GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKfylaELALA----LDHLH-QLGIVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd06620    74 NEnNNIIICMEYMDCGSLDKILKKKGPFPEEVLG----KIAVAvlegLTYLYnVHRIIHRDIKPSNILVNSKGQIKLCDF 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 235 GLSKESVDQekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd06620   150 GVSGELINS--IADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDD 209
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
475-700 1.98e-25

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: 105.97  E-value: 1.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 475 DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQK--CFSEREASDILYVISKTVDYLH 552
Cdd:cd08221    40 EKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 553 CQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTM 632
Cdd:cd08221   119 KAGILHRDIKTLNIFL----TKADLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYEL 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 633 LAGYTPF-ANGPNDTPEEILlrigngkfslsGGNWDNI----SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd08221   195 LTLKRTFdATNPLRLAVKIV-----------QGEYEDIdeqySEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
96-343 2.20e-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: 106.20  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGpdagQLYAMKVLKKASLKVRDRV-RTKMErdILVEVNHPFIVKLhYAFQTEGKLY-LILDFLR 173
Cdd:cd14066     1 IGSGGFGTVYKGVLENG----TVVAVKRLNEMNCAASKKEfLTELE--MLGRLRHPNLVRL-LGYCLESDEKlLVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRL----SKEVLFTEEDVKFYLaELALALDHLHQ---LGIVYRDLKPENILLDEIGHIKLTDFGLSKESV--DQE 244
Cdd:cd14066    74 NGSLEDRLhchkGSPPLPWPQRLKIAK-GIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPpsESV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAklgmpqFLSAEAQSLLRML 324
Cdd:cd14066   153 SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEW------VESKGKEELEDIL 226
                         250
                  ....*....|....*....
gi 1034674014 325 FKRnpANRLGSEGVEEIKR 343
Cdd:cd14066   227 DKR--LVDDDGVEEEEVEA 243
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
94-333 2.38e-25

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: 107.04  E-value: 2.38e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLKKASlKVRDRVRTKMERDilvevNHPFIVKL----HYAFQTEGKLYLI 168
Cdd:cd14170     8 QVLGLGINGKVLqIFNKRTQ----EKFALKMLQDCP-KARREVELHWRAS-----QCPHIVRIvdvyENLYAGRKCLLIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI---GHIKLTDFGLSKESVDQ 243
Cdd:cd14170    78 MECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMILKAKLGMPQF---------LS 314
Cdd:cd14170   158 NSLT-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKTRIRMGQYefpnpewseVS 235
                         250
                  ....*....|....*....
gi 1034674014 315 AEAQSLLRMLFKRNPANRL 333
Cdd:cd14170   236 EEVKMLIRNLLKTEPTQRM 254
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
443-696 2.65e-25

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: 105.57  E-value: 2.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMreeaidEARVLSKL-NSPYVIKYYDSFVDKGKLNIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIlYMDESasaDSIRICDFGFAKQLRGENG 594
Cdd:cd08529    81 AENGDLHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNI-FLDKG---DNVKIGDLGVAKILSDTTN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWdniSDGAK 674
Cdd:cd08529   157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFE---AQNQGALILKIVRGKYPPISASY---SQDLS 230
                         250       260
                  ....*....|....*....|..
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd08529   231 QLIDSCLTKDYRQRPDTTELLR 252
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
431-712 3.33e-25

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: 107.83  E-value: 3.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 431 QINGNAAQFGEVYELKEDIGVGSY-SVCKrCIHATTNMEFAVKIIDKS------KRDPSEEIEiLMRYGQHPNIITLKDV 503
Cdd:cd07878     5 ELNKTVWEVPERYQNLTPVGSGAYgSVCS-AYDTRLRQKVAVKKLSRPfqslihARRTYRELR-LLKHMKHENVIGLLDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 504 F------DDGRYVYLVTDLMkgGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadS 577
Cdd:cd07878    83 FtpatsiENFNEVYLVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC----E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 578 IRICDFGFAKQLRGE-NGLLLTPCYTanfvAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANgpND---------- 645
Cdd:cd07878   157 LRILDFGLARQADDEmTGYVATRWYR----APEIMLNwMHYNQTVDIWSVGCIMAELLKGKALFPG--NDyidqlkrime 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 646 ---TPE-EILLRIGNGKFS--------LSGGNWDNISDGAK----DLLSHMLHMDPHQRYTAEQILKHSWITHRDQlPND 709
Cdd:cd07878   231 vvgTPSpEVLKKISSEHARkyiqslphMPQQDLKKIFRGANplaiDLLEKMLVLDSDKRISASEALAHPYFSQYHD-PED 309

                  ...
gi 1034674014 710 QPK 712
Cdd:cd07878   310 EPE 312
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
443-700 3.57e-25

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 105.58  E-value: 3.57e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCI--HATTNMEFAV-KIIDKSKRDPSEEIEILMRYG-----QHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSdlKATADEELKVlKEISVGELQPDETVDANREAKllsklDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRI--LKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDesasaDSIRICDFGFAKQLR 590
Cdd:cd08222    82 EYCEGGDLDDKIseYKKsgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-----NVIKVGDFGISRILM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTpeEILLRIGNGKF-SLSggnwDNI 669
Cdd:cd08222   157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFD-GQNLL--SVMYKIVEGETpSLP----DKY 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd08222   230 SKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
90-415 3.62e-25

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: 107.06  E-value: 3.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06650     7 FEKISELGAGNGGVVFKVSHKP---SGLVMARKLIH---LEIKPAIRNQIIRElqVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEdvkfYLAELALA----LDHLHQL-GIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06650    81 CMEHMDGGSLDQVLKKAGRIPEQ----ILGKVSIAvikgLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNEtmnmilkakLGMPQFLSAEAQSLLR 322
Cdd:cd06650   157 S--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKE---------LELMFGCQVEGDAAET 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 323 MLFKRNPANRLGSEGVEEIKRHLFFANIDWDKlykreVQPPFKPASGkpddtfCFDPEFTAKTPKDSPGLPAS-ANAHQL 401
Cdd:cd06650   226 PPRPRTPGRPLSSYGMDSRPPMAIFELLDYIV-----NEPPPKLPSG------VFSLEFQDFVNKCLIKNPAErADLKQL 294
                         330
                  ....*....|....
gi 1034674014 402 FKgFSFVATSIAEE 415
Cdd:cd06650   295 MV-HAFIKRSDAEE 307
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
91-333 3.68e-25

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: 105.89  E-value: 3.68e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  91 ELLKVLGQGSFGKVF--LVRKKTGPDAGQLYAMKVLKKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd05032     9 TLIRELGQGSFGMVYegLAKGVVKGEPETRVAIKTVNENA-SMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRL----SKEVLFTEEDV----KFYL--AELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd05032    88 MELMAKGDLKSYLrsrrPEAENNPGLGPptlqKFIQmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQE--KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKL-----GMP 310
Cdd:cd05032   168 DIYETDyyRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLKFVIDGGHldlpeNCP 247
                         250       260
                  ....*....|....*....|...
gi 1034674014 311 QFLsaeaQSLLRMLFKRNPANRL 333
Cdd:cd05032   248 DKL----LELMRMCWQYNPKMRP 266
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
448-695 3.85e-25

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: 105.88  E-value: 3.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHATTNMEFAVKII----DKSKRDPSEEIEILMRYGQHPNIITLKD---VFDDGRYVYLVtdLMK-- 518
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALKRMyfndEEQLRVAIKEIEIMKRLCGHPNIVQYYDsaiLSSEGRKEVLL--LMEyc 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILK--QKCFSEREASDILYVISKTVDYLHCQG--VVHRDLKPSNILYMDESAsadsIRICDFGFA-----KQL 589
Cdd:cd13985    85 PGSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGR----FKLCDFGSAttehyPLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGEN--------GLLLTPCYTAnfvaPEVLMQQGYDAAC---DIWSLGVLFYTMLAGYTPFAngpndtpEEILLRIGNGK 658
Cdd:cd13985   161 RAEEvniieeeiQKNTTPMYRA----PEMIDLYSKKPIGekaDIWALGCLLYKLCFFKLPFD-------ESSKLAIVAGK 229
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 659 FSLSggNWDNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd13985   230 YSIP--EQPRYSPELHDLIRHMLTPDPAERPDIFQVI 264
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
449-711 3.99e-25

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 107.60  E-value: 3.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII-----DKSKRDPSEEIEILmRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELL 523
Cdd:PLN00034   82 IGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVRRQICREIEIL-RDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 524 DRILKQkcfsEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrgenGLLLTPCY-- 601
Cdd:PLN00034  161 GTHIAD----EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI----NSAKNVKIADFGVSRIL----AQTMDPCNss 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 --TANFVAPEV----LMQQGYDA-ACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGngkFSLSGGNWDNISDGAK 674
Cdd:PLN00034  229 vgTIAYMSPERintdLNHGAYDGyAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAIC---MSQPPEAPATASREFR 305
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQP 711
Cdd:PLN00034  306 HFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGG 342
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
438-658 4.21e-25

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: 105.27  E-value: 4.21e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYE--LKEDIGVGSYSVckrcihattnmefAVKIIDKSKRDPS-----EEIEILMRYgQHPNIITLKDVFDDGRYV 510
Cdd:pfam07714  11 AFGEVYKgtLKGEGENTKIKV-------------AVKTLKEGADEEEredflEEASIMKKL-DHPNIVKLLGVCTQGEPL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQK-CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQL 589
Cdd:pfam07714  77 YIVTEYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLV----SENLVVKISDFGLSRDI 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 590 RGE------NGLLLTPCYTanfvAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNGK 658
Cdd:pfam07714 153 YDDdyyrkrGGGKLPIKWM----APESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY---PGMSNEEVLEFLEDGY 221
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
89-310 4.69e-25

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: 106.47  E-value: 4.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKaslkvrdrvRTKMERDILVEV--------NHP----FIVKL 155
Cdd:cd14210    14 RYEVLSVLGKGSFGQVVKCLdHKTG----QLVAIKIIRN---------KKRFHQQALVEVkilkhlndNDPddkhNIVRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQTEGKLYLildflrggdVFTRLSK---EVL-------FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDE 225
Cdd:cd14210    81 KDSFIFRGHLCI---------VFELLSInlyELLksnnfqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 226 IGH--IKLTDFGLS-KESvdqeKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI 302
Cdd:cd14210   152 PSKssIKVIDFGSScFEG----EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACI 227

                  ....*...
gi 1034674014 303 LKAkLGMP 310
Cdd:cd14210   228 MEV-LGVP 234
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
86-290 5.20e-25

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: 105.52  E-value: 5.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKV--LKKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd06642     1 DPEElFTKLERIGKGSFGEVY---KGIDNRTKEVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYITRYYGSYLKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd06642    75 TKLWIIMEYLGGGSALDLLKPGPL-EETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 243 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd06642   154 TQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
94-332 5.34e-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: 104.70  E-value: 5.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFlvrKKTGPDAGQLyAMKVLKKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd05085     2 ELLGKGNFGEVY---KGTLKDKTPV-AVKTCKE-DLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDV--FTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKKAYSFC 251
Cdd:cd05085    77 GGDFlsFLRKKKDELKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ---EDDGVYSSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 G----TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLF 325
Cdd:cd05085   153 GlkqiPIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCW 232

                  ....*..
gi 1034674014 326 KRNPANR 332
Cdd:cd05085   233 DYNPENR 239
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
96-348 5.53e-25

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: 105.88  E-value: 5.53e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKvlkkaSLKVRDRVRTKM---ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd06657    28 IGEGSTGIVCIATVKS---SGKLVAVK-----KMDLRKQQRRELlfnEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 252
Cdd:cd06657   100 EGG-ALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVG 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI---LKAKLGMPQFLSAEAQSLLRMLFKRNP 329
Cdd:cd06657   179 TPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSPSLKGFLDRLLVRDP 258
                         250
                  ....*....|....*....
gi 1034674014 330 ANRLGSegvEEIKRHLFFA 348
Cdd:cd06657   259 AQRATA---AELLKHPFLA 274
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
96-321 5.75e-25

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: 105.01  E-value: 5.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFL-VRKKTGPDAGqlyamkvLKKASLKVRDRvRTKMERDILV--EVNHPFIVKLHYAFQTEGKLYLILDFL 172
Cdd:cd06647    15 IGQGASGTVYTaIDVATGQEVA-------IKQMNLQQQPK-KELIINEILVmrENKNPNIVNYLDSYLVGDELWVVMEYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 252
Cdd:cd06647    87 AGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQFLSAEAQSLL 321
Cdd:cd06647   166 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPELQNPEKLSAI 232
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
89-310 6.10e-25

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 105.26  E-value: 6.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLK------KASLKVRdrvrtkmERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd07836     1 NFKQLEKLGEGTYATVYKGRNRT---TGEIVALKEIHldaeegTPSTAIR-------EISLMKELKHENIVRLHDVIHTE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGG-----DVFTRLSKEVLFTeedVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd07836    71 NKLMLVFEYMDKDlkkymDTHGVRGALDPNT---VKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 238 KESVDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07836   148 RAFGIPVNTFSNEVVTLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRI-MGTP 220
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
441-701 6.14e-25

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: 105.21  E-value: 6.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEdfmvEIDILSEC-KHPNIVGLYEAYFYENKLWILIEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILK-QKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENGL 595
Cdd:cd06611    84 CDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILL----TLDGDVKLADFGVSAKNKSTLQK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLM-----QQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNG---KFSLSGGnWd 667
Cdd:cd06611   160 RDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPPHH---ELNPMRVLLKILKSeppTLDQPSK-W- 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 668 niSDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06611   235 --SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
90-333 6.45e-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: 105.43  E-value: 6.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLKKaslkvrdRVRTKMERDILVEVN-------HPFIVKLHYAF-- 159
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQsRKTG----KYYAIKCMKK-------HFKSLEQVNNLREIQalrrlspHPNILRLIEVLfd 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGKLYLIL--------DFLRGgdvftrlsKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIgHIKL 231
Cdd:cd07831    70 RKTGRLALVFelmdmnlyELIKG--------RKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 232 TDFGlSKESVDQeKKAYS-FCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTgTLP-FQGKDRNETMNMILKAkLG 308
Cdd:cd07831   141 ADFG-SCRGIYS-KPPYTeYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILS-LFPlFPGTNELDQIAKIHDV-LG 216
                         250       260
                  ....*....|....*....|....*
gi 1034674014 309 MPQflsaeaqslLRMLFKRNPANRL 333
Cdd:cd07831   217 TPD---------AEVLKKFRKSRHM 232
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
88-381 9.30e-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: 106.11  E-value: 9.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASlKVRDRvrTKMERDILVEVNH------PFIVKLHYAFQT 161
Cdd:cd14134    12 NRYKILRLLGEGTFGKVLECWDRK---RKRYVAVKIIRNVE-KYREA--AKIEIDVLETLAEkdpngkSHCVQLRDWFDY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLrGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----------DEIGH- 228
Cdd:cd14134    86 RGHMCIVFELL-GPSLYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynPKKKRq 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 --------IKLTDFGLSkeSVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN 300
Cdd:cd14134   165 irvpkstdIKLIDFGSA--TFDDEYHS-SIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 301 MILKAkLG-MPQFLSAEAQSLLRMLFKRNpaNRLG-SEGVEEIKrhlffanidwdklYKREVQPPFKPasgKPDDTFCFD 378
Cdd:cd14134   242 MMERI-LGpLPKRMIRRAKKGAKYFYFYH--GRLDwPEGSSSGR-------------SIKRVCKPLKR---LMLLVDPEH 302

                  ...
gi 1034674014 379 PEF 381
Cdd:cd14134   303 RLL 305
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
440-681 9.44e-25

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: 107.40  E-value: 9.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK---SKRDPS----EEIEIlMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd05622    72 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKfemIKRSDSaffwEERDI-MAFANSPWVVQLFYAFQDDRYLYM 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGE 592
Cdd:cd05622   151 VMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKE 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NgllLTPCYTA----NFVAPEVLMQQG----YDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGG 664
Cdd:cd05622   226 G---MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVGTYSKIMNHKNSLTFP 299
                         250
                  ....*....|....*..
gi 1034674014 665 NWDNISDGAKDLLSHML 681
Cdd:cd05622   300 DDNDISKEAKNLICAFL 316
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
95-294 9.60e-25

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 104.35  E-value: 9.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKA----SLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd14146     1 IIGVGGFGKVYRATWK-----GQEVAVKAARQDpdedIKATAESVR--QEAKLFSMLRHPNIIKLEGVCLEEPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDV---------------FTRLSKEVLFTeedvkfYLAELALALDHLHQ---LGIVYRDLKPENILL------DEI 226
Cdd:cd14146    74 FARGGTLnralaaanaapgprrARRIPPHILVN------WAVQIARGMLYLHEeavVPILHRDLKSSNILLlekiehDDI 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GH--IKLTDFGLSKESVDQEKkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD 294
Cdd:cd14146   148 CNktLKITDFGLAREWHRTTK--MSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGID 215
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
459-700 9.86e-25

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: 103.66  E-value: 9.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 459 RCIHATTNMEFAVKIIDKSkrDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDlMKGGELLDRILKQKCFSEREAS 538
Cdd:cd13976    11 RCVDIHTGEELVCKVVPVP--ECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFE-RDHGDLHSYVRSRKRLREPEAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 DILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQG-YD 617
Cdd:cd13976    88 RLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERT--KLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEILNSGAtYS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 618 A-ACDIWSLGVLFYTMLAGYTPFangpNDT-PEEILLRIGNGKFSLSGGnwdnISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd13976   166 GkAADVWSLGVILYTMLVGRYPF----HDSePASLFAKIRRGQFAIPET----LSPRARCLIRSLLRREPSERLTAEDIL 237

                  ....*
gi 1034674014 696 KHSWI 700
Cdd:cd13976   238 LHPWL 242
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
487-701 9.91e-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: 105.96  E-value: 9.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 487 ILMRYGQHPNIITLKDVF------DDGRYVYLVTDLMKGGelLDRILKQKCFSEReASDILYVISKTVDYLHCQGVVHRD 560
Cdd:cd07850    51 VLMKLVNHKNIIGLLNVFtpqkslEEFQDVYLVMELMDAN--LCQVIQMDLDHER-MSYLLYQMLCGIKHLHSAGIIHRD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 561 LKPSNILYMDESasadSIRICDFGFAKQlrGENGLLLTP-CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd07850   128 LKPSNIVVKSDC----TLKILDFGLART--AGTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLF 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 640 -----------------------------------ANGPNDTPEEILLRIGNGKF-SLSGGNWDNISDGAKDLLSHMLHM 683
Cdd:cd07850   202 pgtdhidqwnkiieqlgtpsdefmsrlqptvrnyvENRPKYAGYSFEELFPDVLFpPDSEEHNKLKASQARDLLSKMLVI 281
                         250
                  ....*....|....*...
gi 1034674014 684 DPHQRYTAEQILKHSWIT 701
Cdd:cd07850   282 DPEKRISVDDALQHPYIN 299
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
83-347 9.95e-25

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: 105.07  E-value: 9.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  83 EKADPAQF-ELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKkaslkVRDRVRTKM---ERDILVEVNHPFIVKLHYA 158
Cdd:cd06659    15 DQGDPRQLlENYVKIGEGSTGVVCIAREK---HSGRQVAVKMMD-----LRKQQRRELlfnEVVIMRDYQHPNVVEMYKS 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd06659    87 YLVGEELWVLMEYLQGG-ALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA---KLGMPQFLSA 315
Cdd:cd06659   166 QISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKASP 245
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 316 EAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd06659   246 VLRDFLERMLVRDPQERATA---QELLDHPFL 274
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
469-701 1.31e-24

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: 105.93  E-value: 1.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKSKRDPSEEI------EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILY 542
Cdd:cd05593    43 YAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 543 VISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDI 622
Cdd:cd05593   123 EIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGTPEYLAPEVLEDNDYGRAVDW 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 623 WSLGVLFYTMLAGYTPFANGPNDTPEEILLrIGNGKFSLSggnwdnISDGAKDLLSHMLHMDPHQRY-----TAEQILKH 697
Cdd:cd05593   199 WGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFPRT------LSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRH 271

                  ....
gi 1034674014 698 SWIT 701
Cdd:cd05593   272 SFFT 275
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-700 1.57e-24

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: 103.67  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-----KSKRDPSEEIEILMRYGQHPNIITLKDVFDDGR-YVYLVTDL 516
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNlknasKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENG 594
Cdd:cd08223    82 CEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFL----TKSNIIKVGDLGIARVLESSSD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNdtpeEILLRIGNGKFSLSGGNWdniSDGA 673
Cdd:cd08223   158 MATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFnAKDMN----SLVYKILEGKLPPMPKQY---SPEL 230
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd08223   231 GELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
96-332 1.70e-24

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 103.12  E-value: 1.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKaslKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14115     1 IGRGRFS---IVKKCLHKATRKDVAVKFVSK---KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD---EIGHIKLTDFGLSKEsVDQEKKAYSFCG 252
Cdd:cd14115    75 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQ-ISGHRHVHHLLG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ--F--LSAEAQSLLRMLFKRN 328
Cdd:cd14115   154 NPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDeyFgdVSQAARDFINVILQED 233

                  ....
gi 1034674014 329 PANR 332
Cdd:cd14115   234 PRRR 237
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
443-697 1.71e-24

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: 105.39  E-value: 1.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYS---VCKRCIHATTNMEFAVKIIDKS----KRDPSE----EIEILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd05614     2 FELLKVLGTGAYGkvfLVRKVSGHDANKLYAMKVLRKAalvqKAKTVEhtrtERNVLEHVRQSPFLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQ-LR 590
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENIL-LD---SEGHVVLTDFGLSKEfLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFA-NGPNDTPEEILLRIGNGKFSLSggnwDN 668
Cdd:cd05614   158 EEKERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLTGASPFTlEGEKNTQSEVSRRILKCDPPFP----SF 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQR-----YTAEQILKH 697
Cdd:cd05614   234 IGPVARDLLQKLLCKDPKKRlgagpQGAQEIKEH 267
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
443-699 1.73e-24

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: 103.91  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD---PSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYLV---- 513
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDegvPSTAIrEIsLLKELNHPNIVRLLDVVHSENKLYLVfefl 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 -TDLMKggeLLDRILKQKcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQ---- 588
Cdd:cd07835    81 dLDLKK---YMDSSPLTG-LDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGA----LKLADFGLARAfgvp 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGengllltpcYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIgngkFSLS 662
Cdd:cd07835   153 VRT---------YTHEVVtlwyrAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLF---PGDSEIDQLFRI----FRTL 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 663 G----GNW-------------------------DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07835   217 GtpdeDVWpgvtslpdykptfpkwarqdlskvvPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
95-346 1.89e-24

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: 103.64  E-value: 1.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpdagqlyamkvlkkaSLKVRDRVRTKMERDI-----LVE-------VNHPFIVKLHYAFQTE 162
Cdd:cd06624    15 VLGKGTFGVVYAARDL-----------------STQVRIAIKEIPERDSrevqpLHEeialhsrLSHKNIVQYLGSVSED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDVFTRL-SK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI-GHIKLTDFGLSK 238
Cdd:cd06624    78 GFFKIFMEQVPGGSLSALLrSKwgPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYsGVVKISDFGTSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMIlkaKLGM------- 309
Cdd:cd06624   158 RLAGINPCTETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFI-ELGEPQAAMF---KVGMfkihpei 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLF 346
Cdd:cd06624   234 PESLSEEAKSFILRCFEPDPDKR---ATASDLLQDPF 267
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
87-346 2.03e-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: 103.59  E-value: 2.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLK--KASLKVRDRVRT-KMERDILVEVNHPFIVKlHYAF---Q 160
Cdd:cd06652     1 PTNWRLGKLLGQGAFGRVYLCYDA---DTGRELAVKQVQfdPESPETSKEVNAlECEIQLLKNLLHERIVQ-YYGClrdP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd06652    77 QERTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 VD---QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILKAKLG-----MPQF 312
Cdd:cd06652   157 QTiclSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQptnpqLPAH 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 313 LSAEAQSLLRMLF---KRNPAnrlgsegVEEIKRHLF 346
Cdd:cd06652   234 VSDHCRDFLKRIFveaKLRPS-------ADELLRHTF 263
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
443-699 2.04e-24

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: 103.09  E-value: 2.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----------RDPSEeIEILMR--YGQHPNIITLKDVFD--DG 507
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewamingpvPVPLE-IALLLKasKPGVPGVIRLLDWYErpDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 -----RYVYLVTDLmkggelLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadSIRICD 582
Cdd:cd14005    81 fllimERPEPCQDL------FDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTG---EVKLID 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 583 FGFAKQLRgeNGLLLTPCYTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFANgpndtPEEILLRigNGKFsl 661
Cdd:cd14005   152 FGCGALLK--DSVYTDFDGTRVYSPPEWIRHGRYHGrPATVWSLGILLYDMLCGDIPFEN-----DEQILRG--NVLF-- 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 662 sggnWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14005   221 ----RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
443-700 2.25e-24

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: 103.26  E-value: 2.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKED-----IGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEiEI-LMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd06624     5 YEYDESgervvLGKGTFGVVYAARDLSTQVRIAIKEIperDSREVQPLHE-EIaLHSRLSHKNIVQYLGSVSEDGFFKIF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDrILKQKC--FSEREASDILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDESASadsIRICDFGFAKQL 589
Cdd:cd06624    84 MEQVPGGSLSA-LLRSKWgpLKDNENTIGYYTkqILEGLKYLHDNKIVHRDIKGDNVLVNTYSGV---VKISDFGTSKRL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTPCYTANFVAPEVL--MQQGYDAACDIWSLGVLFYTMLAGYTPFAN-GPndtPEEILLRIgnGKFSLSGGNW 666
Cdd:cd06624   160 AGINPCTETFTGTLQYMAPEVIdkGQRGYGPPADIWSLGCTIIEMATGKPPFIElGE---PQAAMFKV--GMFKIHPEIP 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 667 DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06624   235 ESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
90-292 2.40e-24

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: 103.52  E-value: 2.40e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAmkvLKKASLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLT---GEIVA---LKKIRLETEDEgVPSTAIREIslLKELNHPNIVRLLDVVHSENKLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLrggDV----FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVD 242
Cdd:cd07835    75 LVFEFL---DLdlkkYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLAR-AFG 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 243 QEKKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQG 292
Cdd:cd07835   151 VPVRTYTHeVVTLWYRAPEIlLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPG 202
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
83-310 2.58e-24

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: 103.20  E-value: 2.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  83 EKADPAQFELLKVLGQGSFGKVFlvRKKTGpdaGQLYAMKVLKKAS----LKVRDRVRtkMERDILVEVNHPFIVKLHYA 158
Cdd:cd14145     1 LEIDFSELVLEEIIGIGGFGKVY--RAIWI---GDEVAVKAARHDPdediSQTIENVR--QEAKLFAMLKHPNIIALRGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKfYLAELALALDHLHQLGIV---YRDLKPENILL------DEIGH- 228
Cdd:cd14145    74 CLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVN-WAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvenGDLSNk 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 -IKLTDFGLSKESVDQEKkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL 307
Cdd:cd14145   153 iLKITDFGLAREWHRTTK--MSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKL 230

                  ...
gi 1034674014 308 GMP 310
Cdd:cd14145   231 SLP 233
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
441-700 2.58e-24

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: 103.61  E-value: 2.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06641     4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaedeiEDIQQEITVLSQC-DSPYVTKYYGSYLKDTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG---- 591
Cdd:cd06641    83 YLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHG----EVKLADFGVAGQLTDtqik 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWdniSD 671
Cdd:cd06641   158 RN*FVGTPFW----MAPEVIKQSAYDSKADIWSLGITAIELARGEPPHS---ELHPMKVLFLIPKNNPPTLEGNY---SK 227
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06641   228 PLKEFVEACLNKEPSFRPTAKELLKHKFI 256
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
90-311 2.76e-24

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: 103.51  E-value: 2.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKvlkkaslKVR-----DRVRTKMERDI-----LVEVNHPFIVKLH--- 156
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQD---GRFVALK-------KVRvplseEGIPLSTIREIallkqLESFEHPNVVRLLdvc 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 --YAFQTEGKLYLILDFLRGgDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLT 232
Cdd:cd07838    71 hgPRTDRELKLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 233 DFGLSkesvdqekKAYSF-------CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKa 305
Cdd:cd07838   150 DFGLA--------RIYSFemaltsvVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFD- 220

                  ....*.
gi 1034674014 306 KLGMPQ 311
Cdd:cd07838   221 VIGLPS 226
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
449-700 3.09e-24

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: 103.58  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI---EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDR 525
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLfneVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 526 ILKQKCFSEREASDILYVIsKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENGLLLTPCYTANF 605
Cdd:cd06658   110 VTHTRMNEEQIATVCLSVL-RALSYLHNQGVIHRDIKSDSILL----TSDGRIKLSDFGFCAQVSKEVPKRKSLVGTPYW 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 606 VAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNgKFSLSGGNWDNISDGAKDLLSHMLHMDP 685
Cdd:cd06658   185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEP---PLQAMRRIRD-NLPPRVKDSHKVSSVLRGFLDLMLVREP 260
                         250
                  ....*....|....*
gi 1034674014 686 HQRYTAEQILKHSWI 700
Cdd:cd06658   261 SQRATAQELLQHPFL 275
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
431-738 3.12e-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: 104.65  E-value: 3.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 431 QINGNAAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK-------SKRdPSEEIEiLMRYGQHPNIITLKDV 503
Cdd:cd07880     5 EVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLYRpfqselfAKR-AYRELR-LLKHMKHENVIGLLDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 504 F------DDGRYVYLVTDLMkgGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadS 577
Cdd:cd07880    83 FtpdlslDRFHDFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDC----E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 578 IRICDFGFAKQLRGE-NGLLLTPCYTanfvAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRI 654
Cdd:cd07880   157 LKILDFGLARQTDSEmTGYVVTRWYR----APEVILNwMHYTQTVDIWSVGCIMAEMLTGKPLFkGHDHLDQLMEIMKVT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 655 GN--GKF-----SLSGGNW----------------DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITH-RDqlPNDQ 710
Cdd:cd07880   233 GTpsKEFvqklqSEDAKNYvkklprfrkkdfrsllPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEfHD--PEDE 310
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1034674014 711 PKRNDVSHVVKGA--MVATYSALTHK---TFQP 738
Cdd:cd07880   311 TEAPPYDDSFDEVdqSLEEWKRLTFTeilSFQP 343
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
89-344 3.15e-24

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: 102.62  E-value: 3.15e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASL----KVRDRVRTKMERDILVEV----NHPFIVKLHYAFQ 160
Cdd:cd14101     1 QYTMGNLLGKGGFGTVYAGHRISD---GLQVAIKQISRNRVqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDF-LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFGlsK 238
Cdd:cd14101    78 IPEGFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFG--S 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQgKDRNetmnmILKAKLGMPQFLSAEA 317
Cdd:cd14101   156 GATLKDSMYTDFDGTRVYSPPEWILYHQyHALPATVWSLGILLYDMVCGDIPFE-RDTD-----ILKAKPSFNKRVSNDC 229
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 318 QSLLRMLFKRNPANRlgsEGVEEIKRH 344
Cdd:cd14101   230 RSLIRSCLAYNPSDR---PSLEQILLH 253
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
90-332 3.30e-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: 102.69  E-value: 3.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLkkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14110     5 YAFQTEINRGRFSVVRQCEEKR---SGQMLAAKII---PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVDQEKKAYS 249
Cdd:cd14110    79 ELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG-NAQPFNQGKVLMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 --FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRML 324
Cdd:cd14110   158 dkKGDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGAVNFLKST 237

                  ....*...
gi 1034674014 325 FKRNPANR 332
Cdd:cd14110   238 LCAKPWGR 245
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
83-332 3.70e-24

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: 103.19  E-value: 3.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  83 EKADPAQF--ELLKVlGQGSFGKVFLVRKKtgpDAGQLYAMKvlkkaSLKVRDRVRTKM---ERDILVEVNHPFIVKLHY 157
Cdd:cd06658    16 SPGDPREYldSFIKI-GEGSTGIVCIATEK---HTGKQVAVK-----KMDLRKQQRRELlfnEVVIMRDYHHENVVDMYN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 158 AFQTEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd06658    87 SYLVGDELWVVMEFLEGG-ALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI---LKAKLGMPQFLS 314
Cdd:cd06658   166 AQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIrdnLPPRVKDSHKVS 245
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd06658   246 SVLRGFLDLMLVREPSQR 263
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
449-704 3.71e-24

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: 104.32  E-value: 3.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYS----VCKRcihaTTNMEFAVKIIDKS---KRDP----SEEIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd05598     9 IGVGAFGevslVRKK----DTNALYAMKTLRKKdvlKRNQvahvKAERDILAE-ADNEWVVKLYYSFQDKENLYFVMDYI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGEN---- 593
Cdd:cd05598    84 PGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNIL-IDRDGH---IKLTDFGLCTGFRWTHdsky 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 ----GLLLTPcytaNFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd05598   160 ylahSLVGTP----NYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFL---AQTPAETQLKVINWRTTLKIPHEANL 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 670 SDGAKDLLSHMLhMDPHQR---YTAEQILKHSWITHRD 704
Cdd:cd05598   233 SPEAKDLILRLC-CDAEDRlgrNGADEIKAHPFFAGID 269
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
443-654 3.87e-24

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: 104.73  E-value: 3.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDwvqtekhVFEQASNHPFLVGLHSCFQTESRLFFVIE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGL 595
Cdd:cd05618   102 YVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEG----HIKLTDYGMCKEGLRPGDT 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-----ANGPNDTPEEILLRI 654
Cdd:cd05618   178 TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgsSDNPDQNTEDYLFQV 241
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
438-697 4.30e-24

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: 102.23  E-value: 4.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYElkedigvGSYSvckrcIHATTNMEFAVKII-----DKSKRDPSEEIEILMRYGqHPNIITLKDVFDDGRYVYL 512
Cdd:cd00192     7 AFGEVYK-------GKLK-----GGDGKTVDVAVKTLkedasESERKDFLKEARVMKKLG-HPNVVRLLGVCTEEEPLYL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDRILKQKC---------FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDF 583
Cdd:cd00192    74 VMEYMEGGDLLDFLRKSRPvfpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLV----GEDLVVKISDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQLRGENglllTPCYTANFV------APEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtpEEILLRIGN 656
Cdd:cd00192   150 GLSRDIYDDD----YYRKKTGGKlpirwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSN---EEVLEYLRK 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 657 GKFSLSGgnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd00192   223 GYRLPKP---ENCPDELYELMLSCWQLDPEDRPTFSELVER 260
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
85-319 4.47e-24

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: 103.27  E-value: 4.47e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADPAQ-FELLKVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLKKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd06655    15 GDPKKkYTRYEKIGQGASGTVFTA---IDVATGQEVAIKQINLQKQPKKELIINEIL--VMKELKNPNIVNFLDSFLVGD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd06655    90 ELFVVMEYLAGGSL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPE 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQFLSAEAQS 319
Cdd:cd06655   169 QSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPELQNPEKLS 242
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
86-335 4.72e-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: 102.46  E-value: 4.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKASLKVRDRVRTKMERDILvEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd13979     1 DWEPLRLQEPLGSGGFGSVYKATYK-----GETVAVKIVRRRRKNRASRQSFWAELNAA-RLRHENIVRVLAAETGTDFA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YL---ILDFLRGGDVFTRL--SKEVLFTEEDVKfYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS--- 237
Cdd:cd13979    75 SLgliIMEYCGNGTLQQLIyeGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSvkl 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkDRNETMNMILKAKL-----GMPQF 312
Cdd:cd13979   154 GEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG-LRQHVLYAVVAKDLrpdlsGLEDS 232
                         250       260
                  ....*....|....*....|....
gi 1034674014 313 LSAEA-QSLLRMLFKRNPANRLGS 335
Cdd:cd13979   233 EFGQRlRSLISRCWSAQPAERPNA 256
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
90-415 5.06e-24

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: 103.98  E-value: 5.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06649     7 FERISELGAGNGGVVTKVQHKP---SGLIMARKLIH---LEIKPAIRNQIIRElqVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDV-KFYLAEL-ALA-LDHLHQlgIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQe 244
Cdd:cd06649    81 CMEHMDGGSLDQVLKEAKRIPEEILgKVSIAVLrGLAyLREKHQ--IMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 kKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNEtmnmiLKAKLGMPQFLSAEAQSLLRML 324
Cdd:cd06649   158 -MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKE-----LEAIFGRPVVDGEEGEPHSISP 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 325 FKRNPANRLGSEGVEEIKRHLFFANIDWDKlykreVQPPFKPASGkpddtfCFDPEFTAKTPKDSPGLPASANAHQLFKG 404
Cdd:cd06649   232 RPRPPGRPVSGHGMDSRPAMAIFELLDYIV-----NEPPPKLPNG------VFTPDFQEFVNKCLIKNPAERADLKMLMN 300
                         330
                  ....*....|.
gi 1034674014 405 FSFVATSIAEE 415
Cdd:cd06649   301 HTFIKRSEVEE 311
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
96-346 5.19e-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: 101.74  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKASLKVRDRVrtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14058     1 VGRGSFGVVCKARWR-----NQIVAVKIIESESEKKAFEV----EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRL-SKEVL--FTEEDVKFYLAELALALDHLHQLG---IVYRDLKPENILLDEIGH-IKLTDFGLSkesVDQEKKAY 248
Cdd:cd14058    72 SLYNVLhGKEPKpiYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTA---CDISTHMT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL---KAKLGMPQFLSAEAQSLLRMLF 325
Cdd:cd14058   149 NNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAvhnGERPPLIKNCPKPIESLMTRCW 228
                         250       260
                  ....*....|....*....|.
gi 1034674014 326 KRNPANRLGSEGVEEIKRHLF 346
Cdd:cd14058   229 SKDPEKRPSMKEIVKIMSHLM 249
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-700 6.02e-24

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: 101.96  E-value: 6.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSY---------SVCKRCIHATTNMEfavKIIDKSKRDPSEEIeILMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd08225     2 YEIIKKIGEGSFgkiylakakSDSEHCVIKEIDLT---KMPVKEKEASKKEV-ILLAKMKHPNIVTFFASFQENGRLFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFAKQLRG 591
Cdd:cd08225    78 MEYCDGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFL---SKNGMVAKLGDFGIARQLND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWdniSD 671
Cdd:cd08225   155 SMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE---GNNLHQLVLKICQGYFAPISPNF---SR 228
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd08225   229 DLRSLISQLFKVSPRDRPSITSILKRPFL 257
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
85-290 6.12e-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: 102.76  E-value: 6.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADPA-QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASlKVRDRVRTkmERDILVEV-NHPFIVKLHYAFQTE 162
Cdd:cd06639    18 ADPSdTWDIIETIGKGTYGKVYKVTNKKD---GSLAAVKILDPIS-DVDEEIEA--EYNILRSLpNHPNVVKFYGMFYKA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 -----GKLYLILDFLRGGDVfTRLSKEVL-----FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLT 232
Cdd:cd06639    92 dqyvgGQLWLVLELCNGGSV-TELVKGLLkcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 233 DFGLSKESVDQEKKAYSFCGTVEYMAPEVV---NRRGHSQSA--DWWSYGVLMFEMLTGTLPF 290
Cdd:cd06639   171 DFGVSAQLTSARLRRNTSVGTPFWMAPEVIaceQQYDYSYDArcDVWSLGITAIELADGDPPL 233
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
85-347 6.53e-24

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: 102.88  E-value: 6.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADPAQ-FELLKVLGQGSFGKVFlvrkkTGPD--AGQLYAMKVLKKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQT 161
Cdd:cd06656    15 GDPKKkYTRFEKIGQGASGTVY-----TAIDiaTGQEVAIKQMNLQQQPKKELIINEIL--VMRENKNPNIVNYLDSYLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd06656    88 GDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL---KAKLGMPQFLSAEAQ 318
Cdd:cd06656   167 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPERLSAVFR 246
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 319 SLLRMLFKRNpANRLGSegVEEIKRHLFF 347
Cdd:cd06656   247 DFLNRCLEMD-VDRRGS--AKELLQHPFL 272
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
443-699 6.60e-24

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: 103.41  E-value: 6.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEIEILMRYGQH-----PNIITLKDVFDDGRYVYLVT 514
Cdd:cd14134    14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrnvEKYREAAKIEIDVLETLAEKdpngkSHCVQLRDWFDYRGHMCIVF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMkGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADS--------------- 577
Cdd:cd14134    94 ELL-GPSLYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYnpkkkrqirvpkstd 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 578 IRICDFGFAkqlrgengllltpCY----------TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-------- 639
Cdd:cd14134   173 IKLIDFGSA-------------TFddeyhssivsTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFqthdnleh 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 640 ------ANGPndTPEEILLRIGNG--KFSLSGG--NWDN-ISDGAK-----------------------DLLSHMLHMDP 685
Cdd:cd14134   240 lammerILGP--LPKRMIRRAKKGakYFYFYHGrlDWPEgSSSGRSikrvckplkrlmllvdpehrllfDLIRKMLEYDP 317
                         330
                  ....*....|....
gi 1034674014 686 HQRYTAEQILKHSW 699
Cdd:cd14134   318 SKRITAKEALKHPF 331
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
443-697 7.18e-24

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: 102.62  E-value: 7.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII-----DKSKRdpseEIEILMRYGQHPNIITLKDVFDD---GRYVyLVT 514
Cdd:cd14132    20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkpvkkKKIKR----EIKILQNLRGGPNIVKLLDVVKDpqsKTPS-LIF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKqkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmDEsaSADSIRICDFGFAKqlrgeng 594
Cdd:cd14132    95 EYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI-DH--EKRKLRLIDWGLAE------- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 llltpCYTAN-----------FVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGN------ 656
Cdd:cd14132   162 -----FYHPGqeynvrvasryYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDN--YDQLVKIAKvlgtdd 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 657 -----GKFSLS----------------------GGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14132   235 lyaylDKYGIElpprlndilgrhskkpwerfvnSENQHLVTPEALDLLDKLLRYDHQERITAKEAMQH 302
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
442-700 7.20e-24

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: 101.61  E-value: 7.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdksKRDPSEEIEIL------MRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVI---KLEPGDDFEIIqqeismLKECRHPNIVAYFGSYLRRDKLWIVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDrILKQKC-FSEREasdILYVISKTV---DYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG 591
Cdd:cd06613    78 YCGGGSLQD-IYQVTGpLSELQ---IAYVCRETLkglAYLHSTGKIHRDIKGANILLTEDG----DVKLADFGVSAQLTA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVL---MQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKF---SLSG-G 664
Cdd:cd06613   150 TIAKRKSFIGTPYWMAPEVAaveRKGGYDGKCDIWALGITAIELAELQPPMF---DLHPMRALFLIPKSNFdppKLKDkE 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 665 NWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06613   227 KW---SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
441-701 7.33e-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: 102.06  E-value: 7.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06642     4 ELFTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaedeiEDIQQEITVLSQC-DSPYITRYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG---- 591
Cdd:cd06642    83 YLGGGSALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQG----DVKLADFGVAGQLTDtqik 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRI-GNGKFSLSGgnwdNIS 670
Cdd:cd06642   158 RNTFVGTPFW----MAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNS---DLHPMRVLFLIpKNSPPTLEG----QHS 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06642   227 KPFKEFVEACLNKDPRFRPTAKELLKHKFIT 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
88-356 7.76e-24

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: 103.21  E-value: 7.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL- 165
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCsAIDTKSG----QKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYa 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 -----YLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG----L 236
Cdd:cd07855    81 dfkdvYVVLD-LMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGmargL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP--QFL 313
Cdd:cd07855   160 CTSPEEHKYFMTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTV-LGTPsqAVI 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 314 SAEAQSLLRMLFKrNPANRlgsegveeikrhlffANIDWDKLY 356
Cdd:cd07855   239 NAIGADRVRRYIQ-NLPNK---------------QPVPWETLY 265
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
449-701 9.53e-24

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: 102.02  E-value: 9.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI---EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDr 525
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRRELLfneVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD- 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 526 ILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCYTANF 605
Cdd:cd06657   107 IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDG----RVKLSDFGFCAQVSKEVPRRKSLVGTPYW 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 606 VAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNgKFSLSGGNWDNISDGAKDLLSHMLHMDP 685
Cdd:cd06657   183 MAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMIRD-NLPPKLKNLHKVSPSLKGFLDRLLVRDP 258
                         250
                  ....*....|....*.
gi 1034674014 686 HQRYTAEQILKHSWIT 701
Cdd:cd06657   259 AQRATAAELLKHPFLA 274
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
89-332 1.05e-23

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: 101.96  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKV---FLVRKKTGPDAGQLyAMKVLKKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd05045     1 NLVLGKTLGEGEFGKVvkaTAFRLKGRAGYTTV-AVKMLKENASSSELRDLLS-EFNLLKQVNHPHVIKLYGACSQDGPL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDV--FTRLSKEV----------------------LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENI 221
Cdd:cd05045    79 LLIVEYAKYGSLrsFLRESRKVgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 222 LLDEIGHIKLTDFGLSKESVDQEKKAYSFCG--TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNET 298
Cdd:cd05045   159 LVAEGRKMKISDFGLSRDVYEEDSYVKRSKGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERL 238
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 299 MNMiLKAKLGM--PQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05045   239 FNL-LKTGYRMerPENCSEEMYNLMLTCWKQEPDKR 273
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
90-301 1.14e-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: 101.13  E-value: 1.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLkkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKS---SDLSFAAKFI---PVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG--HIKLTDFGLSKESVDQEKKa 247
Cdd:cd14108    78 E-LCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQ- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 248 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK-DRNETMNM 301
Cdd:cd14108   156 YCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGEnDRTTLMNI 210
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
429-699 1.22e-23

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: 102.81  E-value: 1.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 429 IVQINGNAAqFGEVyelkedigvgsySVCKRcihATTNMEFAVKIIDKS---KRDPS----EEIEILMRyGQHPNIITLK 501
Cdd:cd05597     5 ILKVIGRGA-FGEV------------AVVKL---KSTEKVYAMKILNKWemlKRAETacfrEERDVLVN-GDRRWITKLH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 502 DVFDDGRYVYLVTDLMKGGELLDRILKqkcFSEREASDIL-YVISKTV---DYLHCQGVVHRDLKPSNILyMDESASads 577
Cdd:cd05597    68 YAFQDENYLYLVMDYYCGGDLLTLLSK---FEDRLPEEMArFYLAEMVlaiDSIHQLGYVHRDIKPDNVL-LDRNGH--- 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 578 IRICDFGFAKQLRgENGLL--LTPCYTANFVAPEVL--MQQG---YDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEE 649
Cdd:cd05597   141 IRLADFGSCLKLR-EDGTVqsSVAVGTPDYISPEILqaMEDGkgrYGPECDWWSLGVCMYEMLYGETPFyAESLVETYGK 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 650 ILLRIGNGKFSLSGgnwDNISDGAKDLLSHMLhMDPHQRY---TAEQILKHSW 699
Cdd:cd05597   220 IMNHKEHFSFPDDE---DDVSEEAKDLIRRLI-CSRERRLgqnGIDDFKKHPF 268
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
462-656 1.24e-23

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: 102.76  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 462 HATTNMEFAVKIIDKSKRDPSEEIEILM---------RYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRIlKQKCF 532
Cdd:cd05589    20 YKPTGELFAIKALKKGDIIARDEVESLMcekrifetvNSARHPFLVNLFACFQTPEHVCFVMEYAAGGDLMMHI-HEDVF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 533 SEREAsdILYV--ISKTVDYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEV 610
Cdd:cd05589    99 SEPRA--VFYAacVVLGLQFLHEHKIVYRDLKLDNLL-LD---TEGYVKIADFGLCKEGMGFGDRTSTFCGTPEFLAPEV 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 611 LMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGN 656
Cdd:cd05589   173 LTDTSYTRAVDWWGLGVLIYEMLVGESPF---PGDDEEEVFDSIVN 215
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
90-310 1.37e-23

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 101.43  E-value: 1.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLkkaslkvrdRVRTKME-------RDI--LVEVNHPFIVKLHYAFQ 160
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKL---TGEVVALKKI---------RLDTETEgvpstaiREIslLKELNHPNIVKLLDVIH 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDFLRGgDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd07860    70 TENKLYLVFEFLHQ-DLkkFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLAR 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 239 eSVDQEKKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07860   149 -AFGVPVRTYTHeVVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRT-LGTP 220
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
443-697 1.48e-23

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: 100.58  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII-----DKSKRDPSE-EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmTKEERQAALnEVKVLSML-HHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASAdsIRICDFGFAKQLRGE-- 592
Cdd:cd08220    81 APGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNIL-LNKKRTV--VKIGDFGISKILSSKsk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 -NGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFY--TMLAGYTPFANGPndtpeEILLRIGNGKFSLSGGNWdni 669
Cdd:cd08220   158 aYTVVGTPCY----ISPELCEGKPYNQKSDIWALGCVLYelASLKRAFEAANLP-----ALVLKIMRGTFAPISDRY--- 225
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd08220   226 SEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
89-310 1.56e-23

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: 100.99  E-value: 1.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLkvrdRVRTKMERDILVEVN-HPFIVKLHYAFQTEGKLYL 167
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKT---GEEVAIKIEKKDSK----HPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLrGGDVftrlskEVLFTEEDVKFYL------AELALA-LDHLHQLGIVYRDLKPENILL---DEIGHIKLTDFGLS 237
Cdd:cd14016    74 VMDLL-GPSL------EDLFNKCGRKFSLktvlmlADQMISrLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDQE-------KKAYSFCGTVEYMApevVNR-RGHSQSA--DWWSYG-VLMFeMLTGTLPFQG---KDRNETMNMIL 303
Cdd:cd14016   147 KKYRDPRtgkhipyREGKSLTGTARYAS---INAhLGIEQSRrdDLESLGyVLIY-FLKGSLPWQGlkaQSKKEKYEKIG 222

                  ....*..
gi 1034674014 304 KAKLGMP 310
Cdd:cd14016   223 EKKMNTS 229
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
449-697 1.57e-23

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: 100.97  E-value: 1.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd06630     8 LGTGAFSSCYQARDVKTGTLMAVKQVSFCRNSSSEqeevveaireEIRMMARL-NHPNIVRMLGATQHKSHFNIFVEWMA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDesASADSIRICDFGFAKQLR------GE 592
Cdd:cd06630    87 GGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLL-VD--STGQRLRIADFGAAARLAskgtgaGE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 -NGLLLTpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIG--NGKFSLSggnwDNI 669
Cdd:cd06630   164 fQGQLLG---TIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIAsaTTPPPIP----EHL 236
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd06630   237 SPGLRDVTLRCLELQPEDRPPARELLKH 264
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
87-327 1.65e-23

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: 102.76  E-value: 1.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKV-FLVRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd07851    14 PDRYQNLSPVGSGAYGQVcSAFDTKTG----RKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 ------YLILDFLrGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 239
Cdd:cd07851    90 edfqdvYLVTHLM-GADLNNIVKCQKL-SDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SvdqEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQ--FL--- 313
Cdd:cd07851   168 T---DDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNL-VGTPDeeLLkki 243
                         250
                  ....*....|....*
gi 1034674014 314 -SAEAQSLLRMLFKR 327
Cdd:cd07851   244 sSESARNYIQSLPQM 258
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
439-697 1.65e-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: 101.24  E-value: 1.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYE---LKEDigvgSYSVCKrcIHA-TTNMEFAVKiiDKSKRDPSEEIEIlMRYGQHPNIITLKDVFD-DGRYVYLV 513
Cdd:cd13990    13 FSEVYKafdLVEQ----RYVACK--IHQlNKDWSEEKK--QNYIKHALREYEI-HKSLDHPRIVKLYDVFEiDTDSFCTV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELlDRILKQ-KCFSEREASDILYVISKTVDYL--HCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLR 590
Cdd:cd13990    84 LEYCDGNDL-DFYLKQhKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNIL-LHSGNVSGEIKITDFGLSKIMD 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GEN----GLLLTP--CYTANFVAPEVLMQQG----YDAACDIWSLGVLFYTMLAGYTPFANGPNDTP---EEILLRIGNG 657
Cdd:cd13990   162 DESynsdGMELTSqgAGTYWYLPPECFVVGKtppkISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAileENTILKATEV 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 658 KFSlsggNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd13990   242 EFP----SKPVVSSEAKDFIRRCLTYRKEDRPDVLQLAND 277
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
89-304 1.66e-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: 101.11  E-value: 1.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLK-KASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYL 167
Cdd:cd06619     2 DIQYQEILGHGNGGTVY---KAYHLLTRRILAVKVIPlDITVELQKQIMSELE--ILYKCDSPYIIGFYGAFFVENRISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGG--DVFTRLSKEVLfteedvkfylAELALA----LDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd06619    77 CTEFMDGGslDVYRKIPEHVL----------GRIAVAvvkgLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 242 DQEKKAYsfCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK 304
Cdd:cd06619   147 NSIAKTY--VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQ 207
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
443-699 1.92e-23

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: 101.98  E-value: 1.92e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSY-SVCK-RCIHATTNMEFAVKIIDKSKRD-----PSEEIEI-LMRYGQHPNIITLKDVFDDG--RYVYL 512
Cdd:cd07842     2 YEIEGCIGRGTYgRVYKaKRKNGKDGKEYAIKKFKGDKEQytgisQSACREIaLLRELKHENVVSLVEVFLEHadKSVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLM--------------KGGELLDRILKQkcfsereasdILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSI 578
Cdd:cd07842    82 LFDYAehdlwqiikfhrqaKRVSIPPSMVKS----------LLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERGVV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 579 RICDFGFA-------KQLRGENGLLLTPCYTanfvAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFANGPND----T 646
Cdd:cd07842   152 KIGDLGLArlfnaplKPLADLDPVVVTIWYR----APELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGREAKikksN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 647 P--EEILLRIgngkFSLSG----GNWDNI--------------------SDGAK-------------DLLSHMLHMDPHQ 687
Cdd:cd07842   228 PfqRDQLERI----FEVLGtpteKDWPDIkkmpeydtlksdtkastypnSLLAKwmhkhkkpdsqgfDLLRKLLEYDPTK 303
                         330
                  ....*....|..
gi 1034674014 688 RYTAEQILKHSW 699
Cdd:cd07842   304 RITAEEALEHPY 315
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
96-347 2.07e-23

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: 100.42  E-value: 2.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKV---FLVRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGkLYLILDFL 172
Cdd:cd05116     3 LGSGNFGTVkkgYYQMKKVV----KTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEMA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYSFCG 252
Cdd:cd05116    78 ELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSK-ALRADENYYKAQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 T----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRMLFK 326
Cdd:cd05116   157 HgkwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCWT 236
                         250       260
                  ....*....|....*....|.
gi 1034674014 327 RNPANRLGSEGVEEIKRHLFF 347
Cdd:cd05116   237 YDVDERPGFAAVELRLRNYYY 257
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
469-718 2.10e-23

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: 101.91  E-value: 2.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKS---KRDPSE----EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDIL 541
Cdd:cd05590    23 YAVKVLKKDvilQDDDVEctmtEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACD 621
Cdd:cd05590   103 AEITSALMFLHDKGIIYRDLKLDNVLLDHEG----HCKLADFGMCKEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 622 IWSLGVLFYTMLAGYTPF-ANGPNDTPEEILlrigNGKFSLSGgnWdnISDGAKDLLSHMLHMDPHQRYTA------EQI 694
Cdd:cd05590   179 WWAMGVLLYEMLCGHAPFeAENEDDLFEAIL----NDEVVYPT--W--LSQDAVDILKAFMTKNPTMRLGSltlggeEAI 250
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 695 LKHSWIT--------HRDQLPNDQPK---RNDVSH 718
Cdd:cd05590   251 LRHPFFKeldweklnRRQIEPPFRPRiksREDVSN 285
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
440-712 2.37e-23

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: 100.96  E-value: 2.37e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELkEDIGVGSYSVCKRCIHATTNMEFAVKIIdksKRDPSEEI--EIL-----MRYGQHPNIITLKDVFDDGR--YV 510
Cdd:cd06621     1 DKIVEL-SSLGEGAGGSVTKCRLRNTKTIFALKTI---TTDPNPDVqkQILreleiNKSCASPYIVKYYGAFLDEQdsSI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELlDRILKQ------KCfSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFG 584
Cdd:cd06621    77 GIAMEYCEGGSL-DSIYKKvkkkggRI-GEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQ----VKLCDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 585 FAKQLrgENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANG-PNDTPEEILLRIGNGK-FSL 661
Cdd:cd06621   151 VSGEL--VNSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFpPEGePPLGPIELLSYIVNMPnPEL 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 662 SGGNWDNI--SDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQPK 712
Cdd:cd06621   229 KDEPENGIkwSESFKDFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKKVNMAK 281
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
470-699 2.93e-23

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: 102.80  E-value: 2.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIDKSkrdpseeieILMRYGQHPNIITLKDV---------------FDDGRYVYLVTDLMKGGELLDRILKQKCFSE 534
Cdd:cd05600    40 ALKIMKKK---------VLFKLNEVNHVLTERDIltttnspwlvkllyaFQDPENVYLAMEYVPGGDFRTLLNNSGILSE 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 535 REASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAK----------------QLRGENGLLLT 598
Cdd:cd05600   111 EHARFYIAEMFAAISSLHQLGYIHRDLKPENFL-IDSSGH---IKLTDFGLASgtlspkkiesmkirleEVKNTAFLELT 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTAN---------------------FVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNG 657
Cdd:cd05600   187 AKERRNiyramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFS---GSTPNETWANLYHW 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 658 KFSLSGGNWD------NISDGAKDLLSHMLhMDPHQRYTA-EQILKHSW 699
Cdd:cd05600   264 KKTLQRPVYTdpdlefNLSDEAWDLITKLI-TDPQDRLQSpEQIKNHPF 311
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
441-700 3.79e-23

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: 100.13  E-value: 3.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06640     4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaedeiEDIQQEITVLSQC-DSPYVTKYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGL 595
Cdd:cd06640    83 YLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQG----DVKLADFGVAGQLTDTQIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPfanGPNDTPEEILLRI-GNGKFSLSGgnwdNISDGAK 674
Cdd:cd06640   158 RNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP---NSDMHPMRVLFLIpKNNPPTLVG----DFSKPFK 230
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06640   231 EFIDACLNKDPSFRPTAKELLKHKFI 256
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
526-698 3.88e-23

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: 100.17  E-value: 3.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 526 ILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasaDSIRICDFGFAKQLRGENGLLL----TPCY 601
Cdd:cd13974   123 VIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRT---RKITITNFCLGKHLVSEDDLLKdqrgSPAY 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 tanfVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSL-SGGnwdNISDGAKDLLSH 679
Cdd:cd13974   200 ----ISPDVLSGKPYLGkPSDMWALGVVLFTMLYGQFPFY---DSIPQELFRKIKAAEYTIpEDG---RVSENTVCLIRK 269
                         170
                  ....*....|....*....
gi 1034674014 680 MLHMDPHQRYTAEQILKHS 698
Cdd:cd13974   270 LLVLNPQKRLTASEVLDSL 288
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
86-346 4.23e-23

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: 100.09  E-value: 4.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFLV-RKKTGpdagqlyamkvlKKASLKVRDRVRtKMERDILVEVN-------HPFIVKLH 156
Cdd:cd06638    15 DPSDtWEIIETIGKGTYGKVFKVlNKKNG------------SKAAVKILDPIH-DIDEEIEAEYNilkalsdHPNVVKFY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAF-----QTEGKLYLILDFLRGGDVfTRLSKEVL-----FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI 226
Cdd:cd06638    82 GMYykkdvKNGDQLWLVLELCNGGSV-TDLVKGFLkrgerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd06638   161 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 302 ILK---AKLGMPQFLSAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLF 346
Cdd:cd06638   241 IPRnppPTLHQPELWSNEFNDFIRKCLTKDYEKR---PTVSDLLQHVF 285
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
443-677 5.08e-23

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: 101.67  E-value: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI-------EILMRyGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVahiraerDILVE-ADGAWVVKMFYSFQDKRNLYLIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASdilYVISKTV---DYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQLR-- 590
Cdd:cd05627    83 FLPGGDMMTLLMKKDTLSEEATQ---FYIAETVlaiDAIHQLGFIHRDIKPDNLL-LD---AKGHVKLSDFGLCTGLKka 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 ---------------------------------GENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYT 637
Cdd:cd05627   156 hrtefyrnlthnppsdfsfqnmnskrkaetwkkNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYP 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 638 PFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd05627   236 PFC---SETPQETYRKVMNWKETLVFPPEVPISEKAKDLI 272
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
449-709 5.27e-23

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 100.99  E-value: 5.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFA---VKIIDKSKRDPSE---------------EIEIlMRYGQHPNIITLKDVFDDGRYV 510
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAikkVKIIEISNDVTKDrqlvgmcgihfttlrELKI-MNEIKHENIMGLVDVYVEGDFI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGelLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQ- 588
Cdd:PTZ00024   96 NLVMDIMASD--LKKVVDRKIrLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGI----CKIADFGLARRy 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 ----LRGENGLLLTPC----YTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGyTPFANGPNDTPEeiLLRI 654
Cdd:PTZ00024  170 gyppYSDTLSKDETMQrreeMTSKVVtlwyrAPELLMgAEKYHFAVDMWSVGCIFAELLTG-KPLFPGENEIDQ--LGRI 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 655 gngkFSLSG----GNW------------------------DNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHrDQL 706
Cdd:PTZ00024  247 ----FELLGtpneDNWpqakklplyteftprkpkdlktifPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFKS-DPL 321

                  ...
gi 1034674014 707 PND 709
Cdd:PTZ00024  322 PCD 324
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
429-711 5.47e-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: 100.14  E-value: 5.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 429 IVQINGNAAQFG-EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSkrDPSEE-------IEILMRYGQHPNIITL 500
Cdd:cd06618     2 YLTIDGKKYKADlNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRS--GNKEEnkrilmdLDVVLKSHDCPYIVKC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 501 KDVFDDGRYVYLVTDLMkgGELLDRILK--QKCFSEREASDILYVISKTVDYL-HCQGVVHRDLKPSNILyMDESAsadS 577
Cdd:cd06618    80 YGYFITDSDVFICMELM--STCLDKLLKriQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNIL-LDESG---N 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 578 IRICDFGFAKQL-------RGENgllltpCytANFVAPEVLMQQG---YDAACDIWSLGVLFYTMLAGYTPFANgpNDTP 647
Cdd:cd06618   154 VKLCDFGISGRLvdskaktRSAG------C--AAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRN--CKTE 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 648 EEILLRIGNGKF-SLSGGnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQP 711
Cdd:cd06618   224 FEVLTKILNEEPpSLPPN--EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYETAEVDVA 286
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
85-321 5.49e-23

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: 100.18  E-value: 5.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADPAQ-FELLKVLGQGSFGKVFlvrkkTGPD--AGQLYAMKVLKKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQT 161
Cdd:cd06654    16 GDPKKkYTRFEKIGQGASGTVY-----TAMDvaTGQEVAIRQMNLQQQPKKELIINEIL--VMRENKNPNIVNYLDSYLV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd06654    89 GDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQFLSAEAQSLL 321
Cdd:cd06654   168 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL--NENPLRALYLIATNGTPELQNPEKLSAI 245
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
443-699 5.51e-23

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: 101.26  E-value: 5.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI------EILMRYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGL 595
Cdd:cd05594   107 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IKITDFGLCKEGIKDGAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLrIGNGKFSLSggnwdnISDGAKD 675
Cdd:cd05594   183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRFPRT------LSPEAKS 255
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 676 LLSHMLHMDPHQRY-----TAEQILKHSW 699
Cdd:cd05594   256 LLSGLLKKDPKQRLgggpdDAKEIMQHKF 284
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
96-292 6.28e-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: 99.75  E-value: 6.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVflvRKKTGPDAGQLYAMKVLKKASLKvRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLILDFLRG 174
Cdd:cd06616    14 IGRGAFGTV---NKMLHKPSGTIMAVKRIRSTVDE-KEQKRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWICMELMDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 G-DVFTRLSKEVLFTE--EDVkfyLAELAL----ALDHL-HQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDqekk 246
Cdd:cd06616    90 SlDKFYKYVYEVLDSVipEEI---LGKIAVatvkALNYLkEELKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD---- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 247 aySFCGTVE-----YMAPEVVN----RRGHSQSADWWSYGVLMFEMLTGTLPFQG 292
Cdd:cd06616   163 --SIAKTRDagcrpYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPK 215
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
89-332 6.47e-23

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: 99.54  E-value: 6.47e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd06622     2 EIEVLDELGKGNYGSVYKVLHRP---TGVTMAMKEIR-LELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGG--DVFTRLSKEVLFTEEDVkfyLAELALALDH-----LHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd06622    78 MEYMDAGslDKLYAGGVATEGIPEDV---LRRITYAVVKglkflKEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTveYMAPEVVNRRGHSQ------SADWWSYGVLMFEMLTGTLPFQgkdrNETMNMILkAKL-------- 307
Cdd:cd06622   155 ASLAKTNIGCQS--YMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRYPYP----PETYANIF-AQLsaivdgdp 227
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 308 -GMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd06622   228 pTLPSGYSDDAQDFVAKCLNKIPNRR 253
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
449-700 7.85e-23

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: 98.99  E-value: 7.85e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIID----KSKRDPS----------EEIEiLMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd06629     9 IGKGTYGRVYLAMNATTGEMLAVKQVElpktSSDRADSrqktvvdalkSEID-TLKDLDHPNIVQYLGFEETEDYFSIFL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQ---LRG 591
Cdd:cd06629    88 EYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGIC----KISDFGISKKsddIYG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCyTANFVAPEVLM--QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd06629   164 NNGATSMQG-SVFWMAPEVIHsqGQGYSAKVDIWSLGCVVLEMLAGRRPW---SDDEAIAAMFKLGNKRSAPPVPEDVNL 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06629   240 SPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
449-649 1.06e-22

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: 99.80  E-value: 1.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDwvqtekhVFETASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05588    83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEG----HIKLTDYGMCKEGLRPGDTTSTFCG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEE 649
Cdd:cd05588   159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFdIVGSSDNPDQ 207
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
469-651 1.18e-22

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: 99.49  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDIL 541
Cdd:cd05591    23 YAIKVLKKDVILQDDDVDctmtekrILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGDLMFQIQRARKFDEPRARFYA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACD 621
Cdd:cd05591   103 AEVTLALMFLHRHGVIYRDLKLDNILLDAEG----HCKLADFGMCKEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVD 178
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1034674014 622 IWSLGVLFYTMLAGYTPF-ANGPNDTPEEIL 651
Cdd:cd05591   179 WWALGVLMYEMMAGQPPFeADNEDDLFESIL 209
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
443-698 1.21e-22

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: 98.12  E-value: 1.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII----DKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIrlpkSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLL 596
Cdd:cd08219    82 GGDLMQKIKLQrgKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNG----KVKLGDFGSARLLTSPGAYA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFSLSGGNWdniSDGAKDL 676
Cdd:cd08219   158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQGSYKPLPSHY---SYELRSL 231
                         250       260
                  ....*....|....*....|..
gi 1034674014 677 LSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd08219   232 IKQMFKRNPRSRPSATTILSRG 253
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
441-697 1.26e-22

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: 98.65  E-value: 1.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMRYgQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMvkkiamREIKMLKQL-RHENLVNLIEVFRRKKRWYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENG 594
Cdd:cd07846    80 EFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILV----SQSGVVKLCDFGFARTLAAPGE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQ-GYDAACDIWSLGVLFYTMLAGyTPFANGPNDTPE--EILLRIGN---------GKFSLS 662
Cdd:cd07846   156 VYTDYVATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTG-EPLFPGDSDIDQlyHIIKCLGNliprhqelfQKNPLF 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 663 GG--------------NWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07846   235 AGvrlpevkeveplerRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
443-699 1.56e-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: 98.32  E-value: 1.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSEEI-EI-LMRYGQHPNIITLKDVfddgryVYLVTDLMK 518
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIhlDAEEGTPSTAIrEIsLMKELKHENIVRLHDV------IHTENKLML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQ--KCFSEREASDILYVIS------KTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLR 590
Cdd:cd07836    76 VFEYMDKDLKKymDTHGVRGALDPNTVKSftyqllKGIAFCHENRVLHRDLKPQNLLI----NKRGELKLADFGLARAFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd07836   152 IPVNTFSNEVVTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLF---PGTNNEDQLLKIFRIMGTPTESTWPGI 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 670 SDGAK-------------------------DLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07836   229 SQLPEykptfpryppqdlqqlfphadplgiDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
445-639 2.05e-22

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: 97.81  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSYSVCKRCIHatTNMEFAVKiidKSKRDPSEEIE----------ILMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14145    10 LEEIIGIGGFGKVYRAIW--IGDEVAVK---AARHDPDEDISqtienvrqeaKLFAMLKHPNIIALRGVCLKEPNLCLVM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELlDRILKQKCFSEREASDILYVISKTVDYLHCQGVV---HRDLKPSNILYMDESASAD----SIRICDFGFAK 587
Cdd:cd14145    85 EFARGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKVENGDlsnkILKITDFGLAR 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 588 QLRGENGLLLTPCYTanFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd14145   164 EWHRTTKMSAAGTYA--WMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
96-332 2.11e-22

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: 97.42  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVF--LVRKKTGPDAGqlYAMKVLKKASLKVRDR--VRtkmERDILVEVNHPFIVKLHYAFQTEGkLYLILDF 171
Cdd:cd05060     3 LGHGNFGSVRkgVYLMKSGKEVE--VAVKTLKQEHEKAGKKefLR---EASVMAQLDHPCIVRLIGVCKGEP-LMLVMEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYSFC 251
Cdd:cd05060    77 APLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSR-ALGAGSDYYRAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GT----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRMLF 325
Cdd:cd05060   156 TAgrwpLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGErLPRPEECPQEIYSIMLSCW 235

                  ....*..
gi 1034674014 326 KRNPANR 332
Cdd:cd05060   236 KYRPEDR 242
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
441-677 2.28e-22

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: 99.73  E-value: 2.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEI-------EILMRyGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVghiraerDILVE-ADSLWVVKMFYSFQDKLNLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASdilYVISKTV---DYLHCQGVVHRDLKPSNILyMDesaSADSIRICDFGFAKQL- 589
Cdd:cd05628    80 MEFLPGGDMMTLLMKKDTLTEEETQ---FYIAETVlaiDSIHQLGFIHRDIKPDNLL-LD---SKGHVKLSDFGLCTGLk 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 ----------------------------------RGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAG 635
Cdd:cd05628   153 kahrtefyrnlnhslpsdftfqnmnskrkaetwkRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIG 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 636 YTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd05628   233 YPPFC---SETPQETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
449-688 2.31e-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: 2.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVK-------IIDKSKRDPSEEIEILMRYgQHPNIITLKDVfDDGRYVYLVTDL----M 517
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqelsPSDKNRERWCLEVQIMKKL-NHPNVVSARDV-PPELEKLSPNDLpllaM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 K---GGEL---LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsaDSI-RICDFGFAKQLr 590
Cdd:cd13989    79 EycsGGDLrkvLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGG--RVIyKLIDLGYAKEL- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 gENGLLLTPCY-TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngPNDTPEEILLRI--------------- 654
Cdd:cd13989   156 -DQGSLCTSFVgTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL--PNWQPVQWHGKVkqkkpehicayedlt 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 655 GNGKFSLSGGNWDNISDGAKD----LLSHMLHMDPHQR 688
Cdd:cd13989   233 GEVKFSSELPSPNHLSSILKEylesWLQLMLRWDPRQR 270
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
86-332 2.80e-22

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: 96.75  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd05059     2 DPSELTFLKELGSGQFGVVHLGKWRGKIDV----AIKMIKEGSMSEDDFIE---EAKVMMKLSHPKLVQLYGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDV--FTRLSKEVLFTEedvkfYLAELAL----ALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 239
Cdd:cd05059    75 FIVTEYMANGCLlnYLRERRGKFQTE-----QLLEMCKdvceAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAySFcGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 314
Cdd:cd05059   150 VLDDEYTS-SV-GTkfpVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGyRLYRPHLAP 227
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd05059   228 TEVYTIMYSCWHEKPEER 245
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
140-332 4.29e-22

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: 97.00  E-value: 4.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 140 ERDILVEVNHPFIVKLHYAFQTE-GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQL--GIVYRDL 216
Cdd:cd13990    54 EYEIHKSLDHPRIVKLYDVFEIDtDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIkpPIIHYDL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 217 KPENILLDEI---GHIKLTDFGLSKEsVDQEKKAYS-------FCGTVEYMAPEVVNRRGH----SQSADWWSYGVLMFE 282
Cdd:cd13990   134 KPGNILLHSGnvsGEIKITDFGLSKI-MDDESYNSDgmeltsqGAGTYWYLPPECFVVGKTppkiSSKVDVWSVGVIFYQ 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 283 MLTGTLPFqGKDRNETM----NMILKAKLGmpQF-----LSAEAQSLLRMLFKRNPANR 332
Cdd:cd13990   213 MLYGRKPF-GHNQSQEAileeNTILKATEV--EFpskpvVSSEAKDFIRRCLTYRKEDR 268
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
459-699 4.92e-22

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: 95.87  E-value: 4.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 459 RCIHATTNMEFAVKIIDKSKRdpSEEIEILMRYGQHPNIITLKDVF--DDGRYVYLVTDLmkgGELLDRILKQKCFSERE 536
Cdd:cd14022    11 RAVHLHSGEELVCKVFDIGCY--QESLAPCFCLPAHSNINQITEIIlgETKAYVFFERSY---GDMHSFVRTCKKLREEE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 537 ASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQG- 615
Cdd:cd14022    86 AARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERT--RVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGs 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 616 YDA-ACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd14022   164 YSGkAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIRRGQFNIP----ETLSPKAKCLIRSILRREPSERLTSQEI 236

                  ....*
gi 1034674014 695 LKHSW 699
Cdd:cd14022   237 LDHPW 241
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
89-344 5.14e-22

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: 96.19  E-value: 5.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFL-VRKKTGpdagqlyAMKVLKKASlkvRDRV----------RTKMERDILVEVNHPF--IVKL 155
Cdd:cd14100     1 QYQVGPLLGSGGFGSVYSgIRVADG-------APVAIKHVE---KDRVsewgelpngtRVPMEIVLLKKVGSGFrgVIRL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQTEGKLYLILDFLRG-GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTD 233
Cdd:cd14100    71 LDWFERPDSFVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FG---LSKESVDQEkkaysFCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRnetmnmILKAKLGM 309
Cdd:cd14100   151 FGsgaLLKDTVYTD-----FDGTRVYSPPEWIRfHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFF 219
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANRlgsEGVEEIKRH 344
Cdd:cd14100   220 RQRVSSECQHLIKWCLALRPSDR---PSFEDIQNH 251
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
87-319 5.53e-22

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 98.10  E-value: 5.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKV-FLVRKKTGPDAgqlyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd07880    14 PDRYRDLKQVGSGAYGTVcSALDRRTGAKV----AIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 ------YLILDFLrgGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 239
Cdd:cd07880    90 drfhdfYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SvDQEKKAYSFcgTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQ 318
Cdd:cd07880   168 T-DSEMTGYVV--TRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQ 244

                  .
gi 1034674014 319 S 319
Cdd:cd07880   245 S 245
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
464-700 6.05e-22

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 96.35  E-value: 6.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 464 TTNMEFAVKIIDKSKrdpsEEIEiLMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG---ELLDRI--LKQKCFSeREAS 538
Cdd:cd06631    37 TSDKEKAEKEYEKLQ----EEVD-LLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPGGsiaSILARFgaLEEPVFC-RYTK 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 DILyvisKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQL-----RGENGLLLTPCY-TANFVAPEVLM 612
Cdd:cd06631   111 QIL----EGVAYLHNNNVIHRDIKGNNIMLMPNGV----IKLIDFGCAKRLcinlsSGSQSQLLKSMRgTPYWMAPEVIN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 613 QQGYDAACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNGKF---SLSggnwDNISDGAKDLLSHMLHMDPHQRY 689
Cdd:cd06631   183 ETGHGRKSDIWSIGCTVFEMATGKPPWADMN---PMAAIFAIGSGRKpvpRLP----DKFSPEARDFVHACLTRDQDERP 255
                         250
                  ....*....|.
gi 1034674014 690 TAEQILKHSWI 700
Cdd:cd06631   256 SAEQLLKHPFI 266
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
87-346 6.09e-22

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: 96.30  E-value: 6.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLK---KASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd06651     6 PINWRRGKLLGQGAFGRVYLCYDV---DTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 K--LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--E 239
Cdd:cd06651    83 EktLTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAY-SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILK-----AKLGMPQFL 313
Cdd:cd06651   163 TICMSGTGIrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiatqpTNPQLPSHI 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 314 SAEAQSLLRMLF---KRNPAnrlgsegVEEIKRHLF 346
Cdd:cd06651   240 SEHARDFLGCIFveaRHRPS-------AEELLRHPF 268
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
84-332 6.22e-22

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: 97.06  E-value: 6.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  84 KADPAQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRvRTKMERDILVEVNH-PFIVKLHYAFQTE 162
Cdd:cd06618    11 KADLNDLENLGEIGSGTCGQVYKMRHKK---TGHVMAVKQMRRSGNKEENK-RILMDLDVVLKSHDcPYIVKCYGYFITD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLrgGDVFTRLSKEVL-FTEEDVkfyLAELAL----ALDHLHQL-GIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd06618    87 SDVFICMELM--STCLDKLLKRIQgPIPEDI---LGKMTVsivkALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSfCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEMLTGTLPFQGKDRN-ETMNMILK---AKLGM 309
Cdd:cd06618   162 SGRLVDSKAKTRS-AGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNeepPSLPP 240
                         250       260
                  ....*....|....*....|...
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd06618   241 NEGFSPDFCSFVDLCLTKDHRYR 263
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
89-346 7.30e-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: 96.13  E-value: 7.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRkktGPDaGQLYAMKV--LKKASLKVRDRVrtKMERDILVEVNH-PFIVKL--HYAFQTEG 163
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVL---NPK-KKIYALKRvdLEGADEQTLQSY--KNEIELLKKLKGsDRIIQLydYEVTDEDD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFlRGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEiGHIKLTDFGLSKE-- 239
Cdd:cd14131    76 YLYMVMEC-GEIDLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAiq 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 ----SVDQEkkaySFCGTVEYMAPEVVNRRGHSQ----------SADWWSYGVLMFEMLTGTLPFQgkdrnETMNMIlkA 305
Cdd:cd14131   154 ndttSIVRD----SQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQ-----HITNPI--A 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 306 KLG----------MPQFLSAEAQSLLRMLFKRNPANRLgseGVEEIKRHLF 346
Cdd:cd14131   223 KLQaiidpnheieFPDIPNPDLIDVMKRCLQRDPKKRP---SIPELLNHPF 270
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
86-290 9.13e-22

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: 96.23  E-value: 9.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFLVRK-KTGpdagQLYAMKVLkkaSLKVRDRVRTKMERDILVEVNHPFIVKLHY-AF--- 159
Cdd:cd06636    13 DPAGiFELVEVVGNGTYGQVYKGRHvKTG----QLAAIKVM---DVTEDEEEEIKLEINMLKKYSHHRNIATYYgAFikk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 ---QTEGKLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd06636    86 sppGHDDQLWLVMEFCGAGSVtdLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 235 GLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQS-----ADWWSYGVLMFEMLTGTLPF 290
Cdd:cd06636   166 GVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDAtydyrSDIWSLGITAIEMAEGAPPL 226
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
87-331 1.11e-21

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: 97.03  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKV---FLVRkktgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd07877    16 PERYQNLSPVGSGAYGSVcaaFDTK------TGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPAR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KL------YLILDfLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd07877    90 SLeefndvYLVTH-LMGADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESvDQEKKAYsfCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP-----Q 311
Cdd:cd07877   168 RHT-DDEMTGY--VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRL-VGTPgaellK 243
                         250       260
                  ....*....|....*....|....*
gi 1034674014 312 FLSAEA-----QSLLRMLfKRNPAN 331
Cdd:cd07877   244 KISSESarnyiQSLTQMP-KMNFAN 267
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
90-329 1.17e-21

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: 96.86  E-value: 1.17e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVF-LVRKKTGpdagqlyaMKV-LKK---ASLKVRDRVRTKMERDILVEVN-HPFIVKLHYAFQTE- 162
Cdd:cd07852     9 YEILKKLGKGAYGIVWkAIDKKTG--------EVVaLKKifdAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIRAEn 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GK-LYLILDFLRGgDVFTRLSKEVLfteEDV--KFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKe 239
Cdd:cd07852    81 DKdIYLVFEYMET-DLHAVIRANIL---EDIhkQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLAR- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAYSFCGTVEYMA------PEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrNETMNMILK--AKLGMP 310
Cdd:cd07852   156 SLSQLEEDDENPVLTDYVAtrwyraPEIlLGSTRYTKGVDMWSVGCILGEMLLGKPLFPG---TSTLNQLEKiiEVIGRP 232
                         250       260
                  ....*....|....*....|....*
gi 1034674014 311 ------QFLSAEAQSLLRMLFKRNP 329
Cdd:cd07852   233 saedieSIQSPFAATMLESLPPSRP 257
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
89-294 1.18e-21

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: 95.48  E-value: 1.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrkkTGPDAGQLYAMKVLKK---ASLKVRDRvRTKMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd14147     4 ELRLEEVIGIGGFGKVY-----RGSWRGELVAVKAARQdpdEDISVTAE-SVRQEARLFAMLAHPNIIALKAVCLEEPNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFT-----RLSKEVLFTeedvkfYLAELALALDHLHQLGIV---YRDLKPENILL------DEIGH--I 229
Cdd:cd14147    78 CLVMEYAAGGPLSRalagrRVPPHVLVN------WAVQIARGMHYLHCEALVpviHRDLKSNNILLlqpienDDMEHktL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 230 KLTDFGLSKESvdQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD 294
Cdd:cd14147   152 KITDFGLAREW--HKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGID 214
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
443-654 1.38e-21

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: 97.01  E-value: 1.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDwvqtekhVFEQASSNPFLVGLHSCFQTTSRLFLVIE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGL 595
Cdd:cd05617    97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVL-LDADGH---IKLTDYGMCKEGLGPGDT 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 596 LLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF---ANGPNDTPEEILLRI 654
Cdd:cd05617   173 TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQV 234
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
87-310 1.46e-21

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: 96.90  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVF-LVRKKTGPDAGqlyamkvLKKASLKVRDRV---RTKMERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd07879    14 PERYTSLKQVGSGAYGSVCsAIDKRTGEKVA-------IKKLSRPFQSEIfakRAYRELTLLKHMQHENVIGLLDVFTSA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKL------YLILDFLrggdvFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd07879    87 VSGdefqdfYLVMPYM-----QTDLQKimGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDF 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 235 GLSKeSVDQEKKAYSFcgTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKlGMP 310
Cdd:cd07879   162 GLAR-HADAEMTGYVV--TRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVT-GVP 234
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
449-699 1.50e-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: 95.90  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPS----EEIEILMRYgQHPNIITLKDVFDdGRY---VYLVT----- 514
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVrmDNERDGIPisslREITLLLNL-RHPNIVELKEVVV-GKHldsIFLVMeyceq 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLmkgGELLDRIlkQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLrGENG 594
Cdd:cd07845    93 DL---ASLLDNM--PTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGC----LKIADFGLARTY-GLPA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCY-TANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGyTPFANGPND------------TPEEillRI------ 654
Cdd:cd07845   163 KPMTPKVvTLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAH-KPLLPGKSEieqldliiqllgTPNE---SIwpgfsd 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 655 --GNGKFSLSGGNWDN-------ISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07845   239 lpLVGKFTLPKQPYNNlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
465-688 1.50e-21

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: 96.30  E-value: 1.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 465 TNMEFAVKIIDKS---KRDPSE----EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREA 537
Cdd:cd05592    19 TNQYFAIKALKKDvvlEDDDVEctmiERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNGGDLMFHIQQSGRFDEDRA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 538 SDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAK-QLRGENgLLLTPCYTANFVAPEVLMQQGY 616
Cdd:cd05592    99 RFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREG----HIKIADFGMCKeNIYGEN-KASTFCGTPDYIAPEILKGQKY 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 617 DAACDIWSLGVLFYTMLAGYTPFaNGpnDTPEEILLRIGNGKFSLSggNWdnISDGAKDLLSHMLHMDPHQR 688
Cdd:cd05592   174 NQSVDWWSFGVLLYEMLIGQSPF-HG--EDEDELFWSICNDTPHYP--RW--LTKEAASCLSLLLERNPEKR 238
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
86-365 1.55e-21

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: 95.94  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQ-FELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLkkaSLKVRDRVRTKMERDILVEVNHPFIVKLHY-AF---- 159
Cdd:cd06637     3 DPAGiFELVELVGNGTYGQVY---KGRHVKTGQLAAIKVM---DVTGDEEEEIKQEINMLKKYSHHRNIATYYgAFikkn 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 --QTEGKLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:cd06637    77 ppGMDDQLWLVMEFCGAGSVtdLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 236 LSKESVDQEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMP 310
Cdd:cd06637   157 VSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPAP 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 311 QF----LSAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLFFAnidwDKLYKREVQPPFK 365
Cdd:cd06637   235 RLkskkWSKKFQSFIESCLVKNHSQR---PSTEQLMKHPFIR----DQPNERQVRIQLK 286
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
494-695 1.58e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 98.55  E-value: 1.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDDGRYVYLVTDLMKGGELlDRILKQKC-----FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY 568
Cdd:PTZ00267  124 HFGIVKHFDDFKSDDKLLLIMEYGSGGDL-NKQIKQRLkehlpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 569 MDESAsadsIRICDFGFAKQLRGENGLLLTP--CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDt 646
Cdd:PTZ00267  203 MPTGI----IKLGDFGFSKQYSDSVSLDVASsfCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF-KGPSQ- 276
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 647 pEEILLRIGNGKFSLSGGnwdNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:PTZ00267  277 -REIMQQVLYGKYDPFPC---PVSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
449-639 1.68e-21

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: 96.22  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVEctmvekrVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05616    88 LMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEG----HIKIADFGMCKENIWDGVTTKTFCG 163
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd05616   164 TPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPF 201
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
96-348 1.74e-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: 95.01  E-value: 1.74e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFG----KVFLVRKKtgpdagQL-YAMKVLKKASLK-VRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGkLYLIL 169
Cdd:cd05115    12 LGSGNFGcvkkGVYKMRKK------QIdVAIKVLKQGNEKaVRDEMMR--EAQIMHQLDNPYIVRMIGVCEAEA-LMLVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLS-KEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE--SVDQEKK 246
Cdd:cd05115    83 EMASGGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAlgADDSYYK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRM 323
Cdd:cd05115   163 ARSAGKwPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFIEQGKrMDCPAECPPEMYALMSD 242
                         250       260
                  ....*....|....*....|....*
gi 1034674014 324 LFKRNPANRLGSEGVEEIKRHLFFA 348
Cdd:cd05115   243 CWIYKWEDRPNFLTVEQRMRTYYYS 267
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
89-332 2.05e-21

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: 94.42  E-value: 2.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIVKLHyAFQTEGK-LYL 167
Cdd:cd05148     7 EFTLERKLGSGYFGEVWEGLWKNRVRV----AIKILKSDDLLKQQDFQK--EVQALKRLRHKHLISLF-AVCSVGEpVYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS---KESVd 242
Cdd:cd05148    80 ITELMEKGSLlaFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliKEDV- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 qekkaYSFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEA 317
Cdd:cd05148   159 -----YLSSDKkipYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAGyRMPCPAKCPQEI 233
                         250
                  ....*....|....*
gi 1034674014 318 QSLLRMLFKRNPANR 332
Cdd:cd05148   234 YKIMLECWAAEPEDR 248
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
90-336 2.22e-21

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: 94.73  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd06645    13 FELIQRIGSGTYGDVYKARNVN---TGELAAIKVIKLEPGEDFAVV--QQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd06645    88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEV--VNRR-GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF-----LSAEAQSLL 321
Cdd:cd06645   168 FIGTPYWMAPEVaaVERKgGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLkdkmkWSNSFHHFV 247
                         250
                  ....*....|....*
gi 1034674014 322 RMLFKRNPANRLGSE 336
Cdd:cd06645   248 KMALTKNPKKRPTAE 262
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
449-688 2.32e-21

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: 94.90  E-value: 2.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS--KRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKriKKKKGEtmalnEKIILEKV-SSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRI--LKQKCFSEREAsdILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA------KQLRG 591
Cdd:cd05577    80 LKYHIynVGTRGFSEARA--IFYAaeIICGLEHLHNRFIVYRDLKPENILLDDHG----HVRISDLGLAvefkggKKIKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGllltpcyTANFVAPEVLMQQ-GYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSLSggnwDNI 669
Cdd:cd05577   154 RVG-------THGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrQRKEKVDKEELKRRTLEMAVEYP----DSF 222
                         250
                  ....*....|....*....
gi 1034674014 670 SDGAKDLLSHMLHMDPHQR 688
Cdd:cd05577   223 SPEARSLCEGLLQKDPERR 241
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
441-639 2.35e-21

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: 96.99  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK---SKRDPS----EEIEIlMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05621    52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKfemIKRSDSaffwEERDI-MAFANSPWVVQLFCAFQDDKYLYMV 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDrILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLrGEN 593
Cdd:cd05621   131 MEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNML-LDKYGH---LKLADFGTCMKM-DET 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 594 GLLL--TPCYTANFVAPEVLMQQG----YDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd05621   205 GMVHcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
93-347 2.45e-21

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: 95.08  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd07871    10 LDKLGEGTYATVFKGRSKL---TENLVALKEIR---LEHEEGAPCTAIREVslLKNLKHANIVTLHDIIHTERCLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGgDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd07871    84 YLDS-DLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQ----------------- 311
Cdd:cd07871   163 EVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRL-LGTPTeetwpgvtsneefrsyl 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 312 FLSAEAQSLLrmlfkrNPANRLGSEGVEEIKRHLFF 347
Cdd:cd07871   242 FPQYRAQPLI------NHAPRLDTDGIDLLSSLLLY 271
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
89-291 2.59e-21

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: 94.76  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK--L 165
Cdd:cd05038     5 HLKFIKQLGEGHFGSVELCRyDPLGDNTGEQVAVKSLQ-PSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRrsL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKesVDQ 243
Cdd:cd05038    84 RLIMEYLPSGslRDYLQRHRDQIDLKRLLLFAS-QICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK--VLP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 244 EKKAYSFCGT-----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ 291
Cdd:cd05038   161 EDKEYYYVKEpgespIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
439-697 2.59e-21

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: 94.31  E-value: 2.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYeLKEDIgvgsysvckrcihaTTNMEFAVKIIDKSKRDPSEeIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd13995    17 FGKVY-LAQDT--------------KTKKRMACKLIPVEQFKPSD-VEIQACF-RHENIAELYGALLWEETVHLFMEAGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRIlkQKCFSEREAsDILYV---ISKTVDYLHCQGVVHRDLKPSNILYMDESASadsirICDFG----------F 585
Cdd:cd13995    80 GGSVLEKL--ESCGPMREF-EIIWVtkhVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-----LVDFGlsvqmtedvyV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLRGengllltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSGGN 665
Cdd:cd13995   152 PKDLRG----------TEIYMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLEDI 221
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 666 WDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd13995   222 AQDCSPAMRELLEAALERNPNHRSSAAELLKH 253
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
439-697 2.95e-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: 93.91  E-value: 2.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKedigvgsysvCKrcihaTTNMEFAVKIIDKSKRDPS------EEIEILMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd14050    14 FGEVFKVR----------SR-----EDGKLYAVKRSRSRFRGEKdrkrklEEVERHEKLGEHPNCVRFIKAWEEKGILYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTdlmkggELLDRILKQKC-----FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesaSADSI-RICDFGFA 586
Cdd:cd14050    79 QT------ELCDTSLQQYCeethsLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL-----SKDGVcKLGDFGLV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLRGENGLLLT---PCYtanfVAPEVLmqQG-YDAACDIWSLGVlfyTML------------AGYTPFANGpnDTPEEI 650
Cdd:cd14050   148 VELDKEDIHDAQegdPRY----MAPELL--QGsFTKAADIFSLGI---TILelacnlelpsggDGWHQLRQG--YLPEEF 216
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 651 LlrigngkfslsggnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14050   217 T---------------AGLSPELRSIIKLMMDPDPERRPTAEDLLAL 248
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
89-310 2.96e-21

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: 95.83  E-value: 2.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVR----------KKTGPDAGQLYAMkvlkkaslkvrdrvRTKMERDILVEVNHPFIVKLH-- 156
Cdd:cd07849     6 RYQNLSYIGEGAYGMVCSAVhkptgqkvaiKKISPFEHQTYCL--------------RTLREIKILLRFKHENIIGILdi 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 ---YAFQTEGKLYLILDFLRGgDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd07849    72 qrpPTFESFKDVYIVQELMET-DLYKLIKTQHL-SNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKeSVDQEKKAYSF----CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLG 308
Cdd:cd07849   150 FGLAR-IADPEHDHTGFlteyVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGI-LG 227

                  ..
gi 1034674014 309 MP 310
Cdd:cd07849   228 TP 229
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
441-699 3.03e-21

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 94.88  E-value: 3.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD---PSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYLVTd 515
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDegvPSTAIrEIsLLKEMQHGNIVRLQDVVHSEKRLYLVF- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 lmkggELLDRILKQKCFS-------EREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASAdsIRICDFGFAKQ 588
Cdd:PLN00009   81 -----EYLDLDLKKHMDSspdfaknPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLL-IDRRTNA--LKLADFGLARA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIgngkFSLSG---- 663
Cdd:PLN00009  153 FGIPVRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLF---PGDSEIDELFKI----FRILGtpne 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 664 GNWDNISD-------------------------GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:PLN00009  226 ETWPGVTSlpdyksafpkwppkdlatvvptlepAGVDLLSKMLRLDPSKRITARAALEHEY 286
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
443-711 3.03e-21

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: 95.62  E-value: 3.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEIL-----MRYGQHPNIITLKDVF-----DDGRYVYL 512
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILreiklLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMkGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdesASAD-SIRICDFGFAK-QLR 590
Cdd:cd07859    82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNIL-----ANADcKLKICDFGLARvAFN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTAN--FVAPEVL--MQQGYDAACDIWSLGVLFYTMLAGyTPFANGPN-------------DTPEEILLR 653
Cdd:cd07859   156 DTPTAIFWTDYVATrwYRAPELCgsFFSKYTPAIDIWSIGCIFAEVLTG-KPLFPGKNvvhqldlitdllgTPSPETISR 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 654 IGNGK---------------FSLSGGNWDNIsdgAKDLLSHMLHMDPHQRYTAEQILKHSW---ITHRDQLPNDQP 711
Cdd:cd07859   235 VRNEKarrylssmrkkqpvpFSQKFPNADPL---ALRLLERLLAFDPKDRPTAEEALADPYfkgLAKVEREPSAQP 307
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
90-284 3.38e-21

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 96.10  E-value: 3.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDagqlyamkvlkKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPD-----------PVVLKIGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGgDVFTRLSKEVLFTEEDVKFYLAELAL-ALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDqEKKAY 248
Cdd:PHA03209  137 PHYSS-DLYTYLTKRSRPLPIDQALIIEKQILeGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVV-APAFL 214
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034674014 249 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:PHA03209  215 GLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
96-332 3.45e-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: 93.66  E-value: 3.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEgKLYLILDFLRG 174
Cdd:cd05041     3 IGRGNFGDVYRGVLK---PDNTEVAVKTCR-ETLPPDLKRKFLQEARILKQYDHPNIVKLiGVCVQKQ-PIMIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDV--FTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 252
Cdd:cd05041    78 GSLltFLRKKGARLTVKQLLQMCL-DAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDGLK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 T--VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRN 328
Cdd:cd05041   157 QipIKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQIESGyRMPAPELCPEAVYRLMLQCWAYD 236

                  ....
gi 1034674014 329 PANR 332
Cdd:cd05041   237 PENR 240
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
441-704 3.76e-21

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: 95.38  E-value: 3.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05619     5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVEctmvekrVLSLAWEHPFLTHLFCTFQTKENLFFV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRIlkQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG 591
Cdd:cd05619    85 MEYLNGGDLMFHI--QSChkFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDG----HIKIADFGMCKENML 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDtpEEIL--LRIGNGKFSlsggNWdnI 669
Cdd:cd05619   159 GDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPF-HGQDE--EELFqsIRMDNPFYP----RW--L 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 670 SDGAKDLLSHMLHMDPHQRYTAE-QILKHSWITHRD 704
Cdd:cd05619   230 EKEAKDILVKLFVREPERRLGVRgDIRQHPFFREIN 265
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
459-700 4.06e-21

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: 93.02  E-value: 4.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 459 RCIHATTNMEFAVKIIdkSKRDPSEEIEILMRYGQHPNIITLKDVF--DDGRYVYLVTDLmkgGELLDRILKQKCFSERE 536
Cdd:cd14024    11 RAEHYQTEKEYTCKVL--SLRSYQECLAPYDRLGPHEGVCSVLEVVigQDRAYAFFSRHY---GDMHSHVRRRRRLSEDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 537 ASDILYVISKTVDYLHCQGVVHRDLKpsnilymdesasadsirICDFGFAKQLRGENGLL-LTPCYTAN----------- 604
Cdd:cd14024    86 ARGLFTQMARAVAHCHQHGVILRDLK-----------------LRRFVFTDELRTKLVLVnLEDSCPLNgdddsltdkhg 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 605 ---FVAPEVL-MQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpNDT-PEEILLRIGNGKFSLSGGnwdnISDGAKDLLS 678
Cdd:cd14024   149 cpaYVGPEILsSRRSYSGkAADVWSLGVCLYTMLLGRYPF----QDTePAALFAKIRRGAFSLPAW----LSPGARCLVS 220
                         250       260
                  ....*....|....*....|..
gi 1034674014 679 HMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14024   221 CMLRRSPAERLKASEILLHPWL 242
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
86-332 4.18e-21

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: 93.77  E-value: 4.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd05114     2 NPSELTFMKELGSGLFGVVRLGKWRAQYKV----AIKAIREGAMSEEDFIE---EAKVMMKLTHPKLVQLYGVCTQQKPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFT-------RLSKEVLFTeedvkfYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd05114    75 YIVTEFMENGCLLNylrqrrgKLSRDMLLS------MCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKaySFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFL 313
Cdd:cd05114   149 YVLDDQYT--SSSGAkfpVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGhRLYRPKLA 226
                         250
                  ....*....|....*....
gi 1034674014 314 SAEAQSLLRMLFKRNPANR 332
Cdd:cd05114   227 SKSVYEVMYSCWHEKPEGR 245
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
441-704 4.29e-21

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 95.43  E-value: 4.29e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSvckRCIHATTNME----FAVKIIDKSKRDPSEEIE------ILMRYGQHPNIITLKDVFDDGRYV 510
Cdd:PTZ00426   30 EDFNFIRTLGTGSFG---RVILATYKNEdfppVAIKRFEKSKIIKQKQVDhvfserKILNYINHPFCVNLYGSFKDESYL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLR 590
Cdd:PTZ00426  107 YLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLL-LDKDGF---IKMTDFGFAKVVD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENgllLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGN-GKFslsggnwdn 668
Cdd:PTZ00426  183 TRT---YTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFyANEPLLIYQKILEGIIYfPKF--------- 250
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRY-----TAEQILKHSWITHRD 704
Cdd:PTZ00426  251 LDNNCKHLMKKLLSHDLTKRYgnlkkGAQNVKEHPWFGNID 291
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
449-696 4.76e-21

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 93.27  E-value: 4.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYS-VCKrcihAT-TNMEFAVKIIDKS--KRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLD 524
Cdd:cd14058     1 VGRGSFGvVCK----ARwRNQIVAVKIIESEseKKAFEVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RILKQKCFSEREASdilYVIS------KTVDYLHC---QGVVHRDLKPSNILYMdesASADSIRICDFGFA----KQLRG 591
Cdd:cd14058    76 VLHGKEPKPIYTAA---HAMSwalqcaKGVAYLHSmkpKALIHRDLKPPNLLLT---NGGTVLKICDFGTAcdisTHMTN 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGllltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAN--GPNdtpEEILLRIGNG-KFSLSggnwDN 668
Cdd:cd14058   150 NKG-------SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHigGPA---FRIMWAVHNGeRPPLI----KN 215
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 669 ISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14058   216 CPKPIESLMTRCWSKDPEKRPSMKEIVK 243
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
95-310 5.23e-21

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: 93.13  E-value: 5.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFlvrkkTGPDAGQLYAMKVLKKASLK----VRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd14148     1 IIGVGGFGKVY-----KGLWRGEEVAVKAARQDPDEdiavTAENVR--QEARLFWMLQHPNIIALRGVCLNPPHLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKfYLAELALALDHLHQ---LGIVYRDLKPENILLDEIGH--------IKLTDFGLSKE 239
Cdd:cd14148    74 YARGGALNRALAGKKVPPHVLVN-WAVQIARGMNYLHNeaiVPIIHRDLKSSNILILEPIEnddlsgktLKITDFGLARE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 240 SvdQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 310
Cdd:cd14148   153 W--HKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLP 221
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
88-347 6.12e-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: 94.36  E-value: 6.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlkkaslkvrdRVRTKMERD-----------ILVEVNHPFIVKLH 156
Cdd:cd07845     7 TEFEKLNRIGEGTYGIVYRARDTT---SGEIVALK-----------KVRMDNERDgipisslreitLLLNLRHPNIVELK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQteGK----LYLILDFLRGgDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKL 231
Cdd:cd07845    73 EVVV--GKhldsIFLVMEYCEQ-DLASLLdNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 232 TDFGLSKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI-------- 302
Cdd:cd07845   150 ADFGLARTYGLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIiqllgtpn 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 303 -----------LKAKLGMPQ-----------FLSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd07845   230 esiwpgfsdlpLVGKFTLPKqpynnlkhkfpWLSEAGLRLLNFLLMYDPKKRATA---EEALESSYF 293
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
86-304 6.61e-21

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: 94.15  E-value: 6.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKaslkVRDRvRTKMERDILVEVN-HPFIVKLHYAFQTEGK 164
Cdd:cd14132    16 SQDDYEIIRKIGRGKYSEVFEGINI---GNNEKVVIKVLKP----VKKK-KIKREIKILQNLRgGPNIVKLLDVVKDPQS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LY--LILDFLRGGDVFTRLSKevlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH-IKLTDFGLSkesv 241
Cdd:cd14132    88 KTpsLIFEYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA---- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 dqE----KKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLP-FQGKDRNEtmnMILK 304
Cdd:cd14132   161 --EfyhpGQEYNVrVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYD---QLVK 225
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
89-310 6.91e-21

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: 93.52  E-value: 6.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHK---ETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGG--DVFTRLSKEVLftEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd07848    79 FEYVEKNmlELLEEMPNGVP--PEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 247 AYS-FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 310
Cdd:cd07848   157 NYTeYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLP 221
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
96-290 6.92e-21

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 92.98  E-value: 6.92e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrkkTGPDAGQLYAMKVLKKASLKVRDRVrtKM---ERDILVEVNHPFIVKLHYA-FQTEGKLYLILDF 171
Cdd:cd14064     1 IGSGSFGKVY-----KGRCRNKIVAIKRYRANTYCSKSDV--DMfcrEVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHQLG--IVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKK 246
Cdd:cd14064    74 VSGGSLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRflQSLDEDNM 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 247 AYSfCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14064   154 TKQ-PGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
441-700 7.24e-21

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: 93.54  E-value: 7.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSkRDPSEEIE----ILMRYGQHPNIITL------KDVfDDGRYV 510
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPI-HDIDEEIEaeynILKALSDHPNVVKFygmyykKDV-KNGDQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRIlkqKCFSER----EASDILYVISKTV---DYLHCQGVVHRDLKPSNILYMDESAsadsIRICDF 583
Cdd:cd06638    96 WLVLELCNGGSVTDLV---KGFLKRgermEEPIIAYILHEALmglQHLHVNKTIHRDVKGNNILLTTEGG----VKLVDF 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQLRGENGLLLTPCYTANFVAPEVL-----MQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIG-NG 657
Cdd:cd06638   169 GVSAQLTSTRLRRNTSVGTPFWMAPEVIaceqqLDSTYDARCDVWSLGITAIELGDGDPPLA---DLHPMRALFKIPrNP 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 658 KFSLSGGN-WdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06638   246 PPTLHQPElW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
443-700 7.50e-21

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: 93.52  E-value: 7.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKrDPSEEIE----ILMRYGQHPNIITLKDVFDD-----GRYVYLV 513
Cdd:cd06639    24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPIS-DVDEEIEaeynILRSLPNHPNVVKFYGMFYKadqyvGGQLWLV 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGG---ELLDRILK--QKcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQ 588
Cdd:cd06639   103 LELCNGGsvtELVKGLLKcgQR-LDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVSAQ 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTPCYTANFVAPEVLM--QQ---GYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIGNGKFS--L 661
Cdd:cd06639   178 LTSARLRRNTSVGTPFWMAPEVIAceQQydySYDARCDVWSLGITAIELADGDPPLFDM---HPVKALFKIPRNPPPtlL 254
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 662 SGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06639   255 NPEKW---CRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
91-332 7.62e-21

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: 93.18  E-value: 7.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  91 ELLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd05072    10 KLVKKLGAGQFGEVWMGYYNNSTKV----AVKTLKPGTMSVQAFLE---EANLMKTLQHDKLVRLYAVVTKEEPIYIITE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFtrlskEVLFTEEDVKFYL-------AELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd05072    83 YMAKGSLL-----DFLKSDEGGKVLLpklidfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSL 320
Cdd:cd05072   158 EYTAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGyRMPRMENCPDELYDI 237
                         250
                  ....*....|..
gi 1034674014 321 LRMLFKRNPANR 332
Cdd:cd05072   238 MKTCWKEKAEER 249
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
87-310 8.56e-21

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: 94.35  E-value: 8.56e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKV---FLVRKKtgpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF---- 159
Cdd:cd07878    14 PERYQNLTPVGSGAYGSVcsaYDTRLR------QKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFtpat 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 --QTEGKLYLILDfLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd07878    88 siENFNEVYLVTN-LMGADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLA 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 238 KESvDQEKKAYsfCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07878   166 RQA-DDEMTGY--VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEV-VGTP 235
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
96-284 9.78e-21

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: 9.78e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14065     1 LGKGFFGEVYKVTHRE---TGKVMVMKELKRFD----EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHQLGIVYRDLKPENILLDEIGHIK---LTDFGLSKESVD------QEK 245
Cdd:cd14065    74 TLEELLKSMDEQLPWSQRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDektkkpDRK 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14065   154 KRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
442-700 1.02e-20

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: 93.15  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE---EIEILMRYGQHPNIITLKDVF--------DDgrYV 510
Cdd:cd06636    17 IFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEiklEINMLKKYSHHRNIATYYGAFikksppghDD--QL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQ 588
Cdd:cd06636    95 WLVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVL-LTENA---EVKLVDFGVSAQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTPCYTANFVAPEVLM-----QQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIG-NGKFSLS 662
Cdd:cd06636   171 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDM---HPMRALFLIPrNPPPKLK 247
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 663 GGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06636   248 SKKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
512-699 1.02e-20

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: 93.19  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRI--LKQKCFSEREAsdILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDesasADSIRICDFGFAK 587
Cdd:cd05605    77 LVLTIMNGGDLKFHIynMGNPGFEEERA--VFYAaeITCGLEHLHSERIVYRDLKPENILLDD----HGHVRISDLGLAV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QL------RGENGllltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFS 660
Cdd:cd05605   151 EIpegetiRGRVG-------TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrARKEKVKREEVDRRVKEDQEE 223
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 661 LSggnwDNISDGAKDLLSHMLHMDPHQR-----YTAEQILKHSW 699
Cdd:cd05605   224 YS----EKFSEEAKSICSQLLQKDPKTRlgcrgEGAEDVKSHPF 263
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
441-713 1.14e-20

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: 92.78  E-value: 1.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEdymvEIDILASC-DHPNIVKLLDAFYYENNLWILIEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILK-QKCFSEreaSDILYVISKTVD---YLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA----KQ 588
Cdd:cd06643    84 CAGGAVDAVMLElERPLTE---PQIRVVCKQTLEalvYLHENKIIHRDLKAGNILFTLDG----DIKLADFGVSakntRT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTPCYtanfVAPEVLM-----QQGYDAACDIWSLGVLFYTMlAGYTPfangPND--TPEEILLRIGNGKFS- 660
Cdd:cd06643   157 LQRRDSFIGTPYW----MAPEVVMcetskDRPYDYKADVWSLGVTLIEM-AQIEP----PHHelNPMRVLLKIAKSEPPt 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 661 -LSGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDqlpNDQPKR 713
Cdd:cd06643   228 lAQPSRW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFVSVLV---SNKPLR 275
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
90-348 1.25e-20

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: 92.26  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpdAGQLYAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGKLYLIL 169
Cdd:cd05067     9 LKLVERLGAGQFGEVWMGYYN----GHTKVAIKSLKQGSMSPDAFLA---EANLMKQLQHQRLVRLY-AVVTQEPIYIIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFtrlskEVLFTEEDVKFYL-------AELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd05067    81 EYMENGSLV-----DFLKTPSGIKLTInklldmaAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETM-NMILKAKLGMPQFLSAEAQS 319
Cdd:cd05067   156 NEYTAREGAKfPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIqNLERGYRMPRPDNCPEELYQ 235
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 320 LLRMLFKRNPANRLGSEGVEEIKRHLFFA 348
Cdd:cd05067   236 LMRLCWKERPEDRPTFEYLRSVLEDFFTA 264
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
96-332 1.28e-20

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: 91.92  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd05084     4 IGRGNFGEVFSGRLRAD---NTPVAVKSCRE-TLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRL--------SKEVLFTEEDVkfylaelALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKKA 247
Cdd:cd05084    80 DFLTFLrtegprlkVKELIRMVENA-------AAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE---EEDGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 YSFCG-----TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSL 320
Cdd:cd05084   150 YAATGgmkqiPVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQGvRLPCPENCPDEVYRL 229
                         250
                  ....*....|..
gi 1034674014 321 LRMLFKRNPANR 332
Cdd:cd05084   230 MEQCWEYDPRKR 241
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
443-698 1.35e-20

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: 92.48  E-value: 1.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYS-VCKRCIHATTNMEFAVKIIDKSKRDPS------EEIEILMR--YGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14052     2 FANVELIGSGEFSqVYKVSERVPTGKVYAVKKLKPNYAGAKdrlrrlEEVSILREltLDGHDNIVQLIDSWEYHGHLYIQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELlDRILKQ----KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQL 589
Cdd:cd14052    82 TELCENGSL-DVFLSElgllGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEG----TLKIGDFGMATVW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTPcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGP----------NDTPEEILLRIGNGKF 659
Cdd:cd14052   157 PLIRGIEREG--DREYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNGDawqklrsgdlSDAPRLSSTDLHSASS 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 660 SLSGGNWDNI-----SDGAKDLLSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd14052   235 PSSNPPPDPPnmpilSGSLDRVVRWMLSPEPDRRPTADDVLATP 278
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-688 1.37e-20

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: 92.40  E-value: 1.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-------KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemmdaKARQDCVKEIDLLKQL-NHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRIL----KQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFG----FAK 587
Cdd:cd08228    83 LADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFI----TATGVVKLGDLGlgrfFSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QLRGENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTPEEILLRIGNGKFSLSGGnwD 667
Cdd:cd08228   159 KTTAAHSLVGTPYY----MSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFY-GDKMNLFSLCQKIEQCDYPPLPT--E 231
                         250       260
                  ....*....|....*....|.
gi 1034674014 668 NISDGAKDLLSHMLHMDPHQR 688
Cdd:cd08228   232 HYSEKLRELVSMCIYPDPDQR 252
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
443-681 1.42e-20

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 95.08  E-value: 1.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK---SKRDPS----EEIEILMRyGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05624    74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKwemLKRAETacfrEERNVLVN-GDCQWITTLHYAFQDENYLYLVMD 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRILKqkcFSEREASDI--LYV--ISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRg 591
Cdd:cd05624   153 YYVGGDLLTLLSK---FEDKLPEDMarFYIgeMVLAIHSIHQLHYVHRDIKPDNVL-LDMNGH---IRLADFGSCLKMN- 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCY--TANFVAPEVL--MQQG---YDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSlsg 663
Cdd:cd05624   225 DDGTVQSSVAvgTPDYISPEILqaMEDGmgkYGPECDWWSLGVCMYEMLYGETPFyAESLVETYGKIMNHEERFQFP--- 301
                         250
                  ....*....|....*...
gi 1034674014 664 GNWDNISDGAKDLLSHML 681
Cdd:cd05624   302 SHVTDVSEEAKDLIQRLI 319
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
443-697 1.52e-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: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDpsEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd07848     3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEEN--EEVKettlrelKMLRTLKQENIVELKEAFRRRGKLYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGG--ELLDRiLKQKCFSEREASDILYVIsKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQL-RGE 592
Cdd:cd07848    81 YVEKNmlELLEE-MPNGVPPEKVRSYIYQLI-KAIHWCHKNDIVHRDIKPENLLI----SHNDVLKLCDFGFARNLsEGS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGyTPFANGPNDT--------------PEEILLRIGNGK 658
Cdd:cd07848   155 NANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDG-QPLFPGESEIdqlftiqkvlgplpAEQMKLFYSNPR 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 659 F------------SLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07848   234 FhglrfpavnhpqSLERRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNH 284
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
449-647 1.63e-20

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: 92.72  E-value: 1.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVK-----IIDKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYV------YLVTDLM 517
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKqcrqeLSPKNRERWCLEIQIMKRL-NHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRI-LKQKCFSEREAS--DILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLrgENG 594
Cdd:cd14038    81 QGGDLRKYLnQFENCCGLREGAilTLLSDISSALRYLHENRIIHRDLKPENIV-LQQGEQRLIHKIIDLGYAKEL--DQG 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 595 LLLTPCY-TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngPNDTP 647
Cdd:cd14038   158 SLCTSFVgTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL--PNWQP 209
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
89-326 1.72e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 97.12  E-value: 1.72e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014   89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF--QTEGKLY 166
Cdd:PTZ00266    14 EYEVIKKIGNGRFGEVFLVKHKR---TQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKLY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  167 LILDFLRGGDVFTRLSK-EVLF---TEEDVKFYLAELALALDHLHQLG-------IVYRDLKPENILLD----EIGHI-- 229
Cdd:PTZ00266    91 ILMEFCDAGDLSRNIQKcYKMFgkiEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLStgirHIGKIta 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  230 -----------KLTDFGLSKeSVDQEKKAYSFCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRN 296
Cdd:PTZ00266   171 qannlngrpiaKIGDFGLSK-NIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFH--KAN 247
                          250       260       270
                   ....*....|....*....|....*....|
gi 1034674014  297 ETMNMILKAKLGmPQFLSAEAQSLLRMLFK 326
Cdd:PTZ00266   248 NFSQLISELKRG-PDLPIKGKSKELNILIK 276
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
431-718 1.74e-20

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: 93.43  E-value: 1.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 431 QINGNAAQFGEVYELKEDIGVGSY-SVCKrCIHATTNMEFAVKiidKSKRDPSEEI-------EI-LMRYGQHPNIITLK 501
Cdd:cd07879     5 EVNKTVWELPERYTSLKQVGSGAYgSVCS-AIDKRTGEKVAIK---KLSRPFQSEIfakrayrELtLLKHMQHENVIGLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 502 DVF------DDGRYVYLVTDLMKGGelLDRILKQKcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNiLYMDESAsa 575
Cdd:cd07879    81 DVFtsavsgDEFQDFYLVMPYMQTD--LQKIMGHP-LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGN-LAVNEDC-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 576 dSIRICDFGFAKQLRGE-NGLLLTPCYTanfvAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFAN------------ 641
Cdd:cd07879   155 -ELKILDFGLARHADAEmTGYVVTRWYR----APEVILNwMHYNQTVDIWSVGCIMAEMLTGKTLFKGkdyldqltqilk 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 642 -----GP------NDTPE----EILLRIGNGKFSLSggnWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWITH-RDQ 705
Cdd:cd07879   230 vtgvpGPefvqklEDKAAksyiKSLPKYPRKDFSTL---FPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSfRDA 306
                         330
                  ....*....|...
gi 1034674014 706 LPNDQPKRNDVSH 718
Cdd:cd07879   307 DEETEQQPYDDSL 319
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
195-292 1.84e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.02  E-value: 1.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 195 YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG----LSKESVDQEKkaySFCGTVEYMAPE-----VVNRR 265
Cdd:NF033483  112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTTMTQTN---SVLGTVHYLSPEqarggTVDAR 188
                          90       100
                  ....*....|....*....|....*..
gi 1034674014 266 ghsqsADWWSYGVLMFEMLTGTLPFQG 292
Cdd:NF033483  189 -----SDIYSLGIVLYEMLTGRPPFDG 210
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
90-310 1.93e-20

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 92.29  E-value: 1.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKvlkkaslkvrdrvRTKMER-------------DILVEVNHPFIVKL 155
Cdd:cd07843     7 YEKLNRIEEGTYGVVYRARdKKTG----EIVALK-------------KLKMEKekegfpitslreiNILLKLQHPNIVTV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAF--QTEGKLYLILDF----LRggDVFTRLSKEvlFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHI 229
Cdd:cd07843    70 KEVVvgSNLDKIYMVMEYvehdLK--SLMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGIL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 230 KLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLG 308
Cdd:cd07843   146 KICDFGLAREYGSPLKPYTQLVVTLWYRAPELLlGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKL-LG 224

                  ..
gi 1034674014 309 MP 310
Cdd:cd07843   225 TP 226
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
447-697 1.94e-20

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: 92.18  E-value: 1.94e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYLVTdlmkggE 521
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVALKKIrldTETEGVPSTAIrEIsLLKELNHPNIVKLLDVIHTENKLYLVF------E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKqKCFSEREASDI--------LYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLrgen 593
Cdd:cd07860    80 FLHQDLK-KFMDASALTGIplpliksyLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGA----IKLADFGLARAF---- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTpCYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGN----------- 656
Cdd:cd07860   151 GVPVR-TYTHEVVtlwyrAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALF---PGDSEIDQLFRIFRtlgtpdevvwp 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 657 GKFSL-----SGGNWD---------NISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07860   227 GVTSMpdykpSFPKWArqdfskvvpPLDEDGRDLLSQMLHYDPNKRISAKAALAH 281
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
92-341 2.02e-20

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: 92.14  E-value: 2.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFL--VRKKTGPDAGQLYAMKVLKKASLkvrDRVRTKMERD--ILVEVNHPFIVKLhYAFQTEGK-LY 166
Cdd:cd05049     9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASS---PDARKDFEREaeLLTNLQHENIVKF-YGVCTEGDpLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDV--FTRL------------SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLT 232
Cdd:cd05049    85 MVFEYMEHGDLnkFLRShgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 233 DFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LG 308
Cdd:cd05049   165 DFGMSRDiySTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEVIECITQGRlLQ 244
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 309 MPQFLSAEAQSLLRMLFKRNPANRLGSEGVEEI 341
Cdd:cd05049   245 RPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKR 277
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
460-699 2.37e-20

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: 90.88  E-value: 2.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 460 CIHATTNMEFAVKIIDKSKrdpsEEIEILMRYGQHPNIITLKDVF--DDGRYVYLVTDLmkgGELLDRILKQKCFSEREA 537
Cdd:cd14023    14 QLHSGAELQCKVFPLKHYQ----DKIRPYIQLPSHRNITGIVEVIlgDTKAYVFFEKDF---GDMHSYVRSCKRLREEEA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 538 SDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQG-Y 616
Cdd:cd14023    87 ARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERT--QLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTGtY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 617 DA-ACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd14023   165 SGkSADVWSLGVMLYTLLVGRYPFH---DSDPSALFSKIRRGQFCIP----DHVSPKARCLIRSLLRREPSERLTAPEIL 237

                  ....
gi 1034674014 696 KHSW 699
Cdd:cd14023   238 LHPW 241
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
440-701 2.41e-20

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: 92.02  E-value: 2.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06644    11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEdymvEIEILATC-NHPYIVKLLGAFYWDGKLWIMIE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGEL------LDRILKqkcfsEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA--- 586
Cdd:cd06644    90 FCPGGAVdaimleLDRGLT-----EPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDG----DIKLADFGVSakn 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 -KQLRGENGLLLTPCYtanfVAPEVLMQQG-----YDAACDIWSLGVLFYTMlAGYTPFANGPNdtPEEILLRIGNGKFS 660
Cdd:cd06644   161 vKTLQRRDSFIGTPYW----MAPEVVMCETmkdtpYDYKADIWSLGITLIEM-AQIEPPHHELN--PMRVLLKIAKSEPP 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 661 --LSGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06644   234 tlSQPSKW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVS 273
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
443-700 2.77e-20

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: 91.05  E-value: 2.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNME--FAVKIIDKSKRDPSEEIEILM-RYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd14112     5 FSFGSEIFRGRFSVIVKAVDSTTETDahCAVKIFEVSDEASEAVREFESlRTLQHENVQRLIAAFKPSNFAYLVMEKLQE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 gELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdESASADSIRICDFGFAKQLRGENglLLTP 599
Cdd:cd14112    85 -DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMF--QSVRSWQVKLVDFGRAQKVSKLG--KVPV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFaNGPNDTPEEILLRIGNGKFslsggNWDNI----SDGAK 674
Cdd:cd14112   160 DGDTDWASPEFHNpETPITVQSDIWGLGVLTFCLLSGFHPF-TSEYDDEEETKENVIFVKC-----RPNLIfveaTQEAL 233
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 675 DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14112   234 RFATWALKKSPTRRMRTDEALEHRWL 259
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
443-697 2.89e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 91.71  E-value: 2.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD---PSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYLV---- 513
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEegvPSTAIrEIsLLKELQHPNIVCLEDVLMQENRLYLVfefl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 -TDLMKggeLLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLrge 592
Cdd:cd07861    82 sMDLKK---YLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGV----IKLADFGLARAF--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 nGLLLTpCYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMlAGYTPFANGpnDTPEEILLRI-----------G 655
Cdd:cd07861   152 -GIPVR-VYTHEVVtlwyrAPEVLLgSPRYSTPVDIWSIGTIFAEM-ATKKPLFHG--DSEIDQLFRIfrilgtptediW 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 656 NGKFSL----------SGGNWD----NISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07861   227 PGVTSLpdykntfpkwKKGSLRtavkNLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
469-697 3.50e-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: 91.59  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVK-IIDKSKRDPSE---EIEILMRYgQHPNIITLKD-----VFDDGRYVYLVTDLMKGGELLDRI----LKQKCFSER 535
Cdd:cd13986    28 YALKkILCHSKEDVKEamrEIENYRLF-NHPNILRLLDsqivkEAGGKKEVYLLLPYYKRGSLQDEIerrlVKGTFFPED 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 536 EASDILYVISKTVDYLH---CQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQLR----------------GENGll 596
Cdd:cd13986   107 RILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSED----DEPILMDLGSMNPARieiegrrealalqdwaAEHC-- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 ltpcyTANFVAPE---VLMQQGYDAACDIWSLGVLFYTMLAGYTPF--ANGPNDTpeeILLRIGNGKFSLSGGNwdNISD 671
Cdd:cd13986   181 -----TMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPFerIFQKGDS---LALAVLSGNYSFPDNS--RYSE 250
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd13986   251 ELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
441-687 4.37e-20

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: 93.54  E-value: 4.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK---SKRDPS----EEIEILMRyGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05623    72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKwemLKRAETacfrEERDVLVN-GDSQWITTLHYAFQDDNNLYLV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKqkcFSEREASDI----LYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQL 589
Cdd:cd05623   151 MDYYVGGDLLTLLSK---FEDRLPEDMarfyLAEMVLAIDSVHQLHYVHRDIKPDNIL-MDMNGH---IRLADFGSCLKL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RgENGLLLTPCY--TANFVAPEVL--MQQG---YDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSL 661
Cdd:cd05623   224 M-EDGTVQSSVAvgTPDYISPEILqaMEDGkgkYGPECDWWSLGVCMYEMLYGETPFyAESLVETYGKIMNHKERFQFPT 302
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 662 sggNWDNISDGAKDLLSHMLHMDPHQ 687
Cdd:cd05623   303 ---QVTDVSENAKDLIRRLICSREHR 325
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
140-336 5.37e-20

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: 90.28  E-value: 5.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 140 ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPE 219
Cdd:cd14112    50 EFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 220 NILLDEIG--HIKLTDFGlSKESVDQEKKAYSfCGTVEYMAPEVVNRRGHS--QSaDWWSYGVLMFEMLTGTLPFQG--K 293
Cdd:cd14112   129 NIMFQSVRswQVKLVDFG-RAQKVSKLGKVPV-DGDTDWASPEFHNPETPItvQS-DIWGLGVLTFCLLSGFHPFTSeyD 205
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 294 DRNETMNMILKAKLG---MPQFLSAEAQSLLRMLFKRNPANRLGSE 336
Cdd:cd14112   206 DEEETKENVIFVKCRpnlIFVEATQEALRFATWALKKSPTRRMRTD 251
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
94-332 5.44e-20

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: 90.03  E-value: 5.44e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFL-VRKKTGPdagqlYAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGK-LYLI--- 168
Cdd:cd05034     1 KKLGAGQFGEVWMgVWNGTTK-----VAVKTLKPGTMSPEAFLQ---EAQIMKKLRHDKLVQL-YAVCSDEEpIYIVtel 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 ------LDFLRGGD-VFTRLSKEVLFTeedvkfylAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd05034    72 mskgslLDYLRTGEgRALRLPQLIDMA--------AQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSfcGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAE 316
Cdd:cd05034   144 DDEYTARE--GAkfpIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERGyRMPKPPGCPDE 221
                         250
                  ....*....|....*.
gi 1034674014 317 AQSLLRMLFKRNPANR 332
Cdd:cd05034   222 LYDIMLQCWKKEPEER 237
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
90-333 6.34e-20

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: 90.02  E-value: 6.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLK--KASL-------KVRDRVRTKmerdilVEVNHPFIVKLHYAFQ 160
Cdd:cd14133     1 YEVLEVLGKGTFGQVV---KCYDLLTGEEVALKIIKnnKDYLdqsldeiRLLELLNKK------DKADKYHIVRLKDVFY 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDFLRGG-DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG--HIKLTDFGLS 237
Cdd:cd14133    72 FKNHLCIVFELLSQNlYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN------------MILKA 305
Cdd:cd14133   152 CFLTQ---RLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLAriigtigippahMLDQG 228
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 306 KLGMPQFLsaeaqSLLRMLFKRNPANRL 333
Cdd:cd14133   229 KADDELFV-----DFLKKLLEIDPKERP 251
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
442-713 6.50e-20

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: 90.93  E-value: 6.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE---EIEILMRYGQHPNIITLKDVF--------DDgrYV 510
Cdd:cd06637     7 IFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEEikqEINMLKKYSHHRNIATYYGAFikknppgmDD--QL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRI--LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQ 588
Cdd:cd06637    85 WLVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTPCYTANFVAPEVLM-----QQGYDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIG-NGKFSLS 662
Cdd:cd06637   161 LDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDM---HPMRALFLIPrNPAPRLK 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 663 GGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWIthRDQlPNDQPKR 713
Cdd:cd06637   238 SKKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI--RDQ-PNERQVR 282
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
447-700 6.58e-20

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: 89.98  E-value: 6.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFA---VKIIDKSKRDP---SEEIEILMRYgQHPNIITLKDVFDDG--RYVYLVTDLMK 518
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERqrfKQEIEILKSL-KHPNIIKFYDSWESKskKEVIFITELMT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGEL---LDRI--LKQKCFSeREASDILyvisKTVDYLHCQG--VVHRDLKPSNILYmdeSASADSIRICDFGFAKQLRG 591
Cdd:cd13983    86 SGTLkqyLKRFkrLKLKVIK-SWCRQIL----EGLNYLHTRDppIIHRDLKCDNIFI---NGNTGEVKIGDLGLATLLRQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 E--NGLLLTPcytaNFVAPEVLmQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGKF--SLsggnwD 667
Cdd:cd13983   158 SfaKSVIGTP----EFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPYSECTN--AAQIYKKVTSGIKpeSL-----S 225
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 668 NISD-GAKDLLSHMLhMDPHQRYTAEQILKHSWI 700
Cdd:cd13983   226 KVKDpELKDFIEKCL-KPPDERPSARELLEHPFF 258
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
484-700 9.15e-20

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: 91.73  E-value: 9.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 484 EIEILMrYGQHPNIITLKDVF-----DDGRYVYLVTDLMKGgELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVH 558
Cdd:cd07853    49 ELKMLC-FFKHDNVLSALDILqpphiDPFEEIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILH 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 559 RDLKPSNILYmdesASADSIRICDFGFAKQLRGENGLLLT-PCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGY 636
Cdd:cd07853   127 RDIKPGNLLV----NSNCVLKICDFGLARVEEPDESKHMTqEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 637 TPF-ANGPNDTPEEI----------------------LLRIG------NGKFSLSGGNwdniSDGAKDLLSHMLHMDPHQ 687
Cdd:cd07853   203 ILFqAQSPIQQLDLItdllgtpsleamrsacegarahILRGPhkppslPVLYTLSSQA----THEAVHLLCRMLVFDPDK 278
                         250
                  ....*....|...
gi 1034674014 688 RYTAEQILKHSWI 700
Cdd:cd07853   279 RISAADALAHPYL 291
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
91-332 1.05e-19

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: 89.79  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  91 ELLKVLGQGSFGKVFL-VRKKTGPDAGQLyAMKVLKK-ASLKVRDRVRTkmERDILVEVNHPFIVKLhYAFQTEGKLYLI 168
Cdd:cd05056     9 TLGRCIGEGQFGDVYQgVYMSPENEKIAV-AVKTCKNcTSPSVREKFLQ--EAYIMRQFDHPHIVKL-IGVITENPVWIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDV--FTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-K 245
Cdd:cd05056    85 MELAPLGELrsYLQVNKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESyY 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRM 323
Cdd:cd05056   164 KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTK 243

                  ....*....
gi 1034674014 324 LFKRNPANR 332
Cdd:cd05056   244 CWAYDPSKR 252
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
484-712 1.09e-19

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: 90.99  E-value: 1.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 484 EIEILMRYgQHPNIITLKDVFDDG--------------RYVYLVTDLMKGGelLDRILKQKCFSEREASDILYVISKTVD 549
Cdd:cd07854    52 EIKIIRRL-DHDNIVKVYEVLGPSgsdltedvgsltelNSVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 550 YLHCQGVVHRDLKPSNILYMDESAsadSIRICDFGFAKQLRGE---NGLLLTPCYTANFVAPEVLMQ-QGYDAACDIWSL 625
Cdd:cd07854   129 YIHSANVLHRDLKPANVFINTEDL---VLKIGDFGLARIVDPHyshKGYLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAA 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 626 GVLFYTMLAGYTPFA-----------------NGPNDTPEeiLLRIGNGKFSLSGGN--------WDNISDGAKDLLSHM 680
Cdd:cd07854   206 GCIFAEMLTGKPLFAgaheleqmqlilesvpvVREEDRNE--LLNVIPSFVRNDGGEprrplrdlLPGVNPEALDFLEQI 283
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1034674014 681 LHMDPHQRYTAEQILKHSWIThRDQLPNDQPK 712
Cdd:cd07854   284 LTFNPMDRLTAEEALMHPYMS-CYSCPFDEPV 314
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
449-639 1.15e-19

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: 89.28  E-value: 1.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHatTNMEFAVKiidKSKRDPSEEIEI----------LMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14148     2 IGVGGFGKVYKGLW--RGEEVAVK---AARQDPDEDIAVtaenvrqearLFWMLQHPNIIALRGVCLNPPHLCLVMEYAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELlDRILKQKCFSEREASDILYVISKTVDYLHCQGVV---HRDLKPSNILYMD----ESASADSIRICDFGFAKQLRG 591
Cdd:cd14148    77 GGAL-NRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEpienDDLSGKTLKITDFGLAREWHK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 592 ENGLLLTPCYTanFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd14148   156 TTKMSAAGTYA--WMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
443-688 1.27e-19

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: 89.96  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEdIGVGSY-SVCKRCIHATTNMeFAVKIIDKS--KRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd05607     5 YEFRV-LGKGGFgEVCAVQVKNTGQM-YACKKLDKKrlKKKSGEkmallEKEILEKV-NSPFIVSLAYAFETKTHLCLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKqkcFSER--EASDILYV---ISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQL 589
Cdd:cd05607    82 SLMNGGDLKYHIYN---VGERgiEMERVIFYsaqITCGILHLHSLKIVYRDMKPENVLLDDNG----NCRLSDLGLAVEV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGenGLLLTP-CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRI---GNGKFslsggN 665
Cdd:cd05607   155 KE--GKPITQrAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRtleDEVKF-----E 227
                         250       260
                  ....*....|....*....|...
gi 1034674014 666 WDNISDGAKDLLSHMLHMDPHQR 688
Cdd:cd05607   228 HQNFTEEAKDICRLFLAKKPENR 250
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
468-697 1.37e-19

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: 88.71  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDKSKrdpseEIEIL-MRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDrILKQkcfsEREASDILYV--- 543
Cdd:cd14059    18 EVAVKKVRDEK-----ETDIKhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYE-VLRA----GREITPSLLVdws 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 --ISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrGENGLLLTPCYTANFVAPEVLMQQGYDAACD 621
Cdd:cd14059    88 kqIASGMNYLHLHKIIHRDLKSPNVLV----TYNDVLKISDFGTSKEL-SEKSTKMSFAGTVAWMAPEVIRNEPCSEKVD 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 622 IWSLGVLFYTMLAGYTPFANGPNDTpeeILLRIGNGKFSLSGGnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14059   163 IWSFGVVLWELLTGEIPYKDVDSSA---IIWGVGSNSLQLPVP--STCPDGFKLLMKQCWNSKPRNRPSFRQILMH 233
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
89-293 1.43e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 91.44  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:PHA03207   93 QYNILSSLTPGSEGEVFVCTKH-----GDEQRKKVIVKAVTGGKTPGR---EIDILKTISHRAIINLIHAYRWKSTVCMV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS--KESVDQEKK 246
Cdd:PHA03207  165 MPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAckLDAHPDTPQ 243
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 293
Cdd:PHA03207  244 CYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGK 290
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
89-392 1.48e-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: 89.86  E-value: 1.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKvlkkaslkvrdRVRTKMERD-----------ILVEVNHPFIVKLHY 157
Cdd:cd07864     8 KFDIIGIIGEGTYGQVYKAKDK---DTGELVALK-----------KVRLDNEKEgfpitaireikILRQLNHRSVVNLKE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 158 AF----------QTEGKLYLILDFLrGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI 226
Cdd:cd07864    74 IVtdkqdaldfkKDKGAFYLVFEYM-DHDLMGLLeSGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GHIKLTDFGLSKESVDQEKKAYS-FCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKdrNETMNMILK 304
Cdd:cd07864   153 GQIKLADFGLARLYNSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQAN--QELAQLELI 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 305 AKL-GMPqflsaeaqsllrmlfkrNPANRlgsegvEEIKRHLFFANIDWDKLYKREVQPPF----KPASGKPDDTFCFDP 379
Cdd:cd07864   231 SRLcGSP-----------------CPAVW------PDVIKLPYFNTMKPKKQYRRRLREEFsfipTPALDLLDHMLTLDP 287
                         330
                  ....*....|....*
gi 1034674014 380 E--FTAKTPKDSPGL 392
Cdd:cd07864   288 SkrCTAEQALNSPWL 302
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
469-688 1.52e-19

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: 90.39  E-value: 1.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDIL 541
Cdd:cd05620    23 FAVKALKKDVVLIDDDVEctmvekrVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGDLMFHIQDKGRFDLYRATFYA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQ-LRGENGLLlTPCYTANFVAPEVLMQQGYDAAC 620
Cdd:cd05620   103 AEIVCGLQFLHSKGIIYRDLKLDNVM-LDRDGH---IKIADFGMCKEnVFGDNRAS-TFCGTPDYIAPEILQGLKYTFSV 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 621 DIWSLGVLFYTMLAGYTPFAngpNDTPEEIL--LRIGNGKFSlsggNWdnISDGAKDLLSHMLHMDPHQR 688
Cdd:cd05620   178 DWWSFGVLLYEMLIGQSPFH---GDDEDELFesIRVDTPHYP----RW--ITKESKDILEKLFERDPTRR 238
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
449-696 1.54e-19

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: 88.99  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHatTNMEFAVKIidkSKRDPSEEIEI----------LMRYGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14061     2 IGVGGFGKVYRGIW--RGEEVAVKA---ARQDPDEDISVtlenvrqearLFWMLRHPNIIALRGVCLQPPNLCLVMEYAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELlDRILKQKCFSEREASDILYVISKTVDYLHCQG---VVHRDLKPSNIL----YMDESASADSIRICDFGFAKQLrg 591
Cdd:cd14061    77 GGAL-NRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILileaIENEDLENKTLKITDFGLAREW-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF--------ANG----------PNDTPEEIllr 653
Cdd:cd14061   154 HKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYkgidglavAYGvavnkltlpiPSTCPEPF--- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 654 igngkfslsggnwdnisdgaKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14061   231 --------------------AQLMKDCWQPDPHDRPSFADILK 253
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
469-639 1.54e-19

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: 90.14  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKS---KRDPSE----EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDIL 541
Cdd:cd05587    24 YAIKILKKDviiQDDDVEctmvEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGKFKEPVAVFYA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACD 621
Cdd:cd05587   104 AEIAVGLFFLHSKGIIYRDLKLDNVM-LDAEGH---IKIADFGMCKEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKSVD 179
                         170
                  ....*....|....*...
gi 1034674014 622 IWSLGVLFYTMLAGYTPF 639
Cdd:cd05587   180 WWAYGVLLYEMLAGQPPF 197
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
436-697 1.57e-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: 89.55  E-value: 1.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKII-----DKSKRDPSEEIEILMRYgQHPNIITLKDVFD----- 505
Cdd:cd14048     1 TSRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIrlpnnELAREKVLREVRALAKL-DHPGIVRYFNAWLerppe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 506 ------DGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYV---ISKTVDYLHCQGVVHRDLKPSNILY-MDesasa 575
Cdd:cd14048    80 gwqekmDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFVCLNIfkqIASAVEYLHSKGLIHRDLKPSNVFFsLD----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 576 DSIRICDFGFAKQL-RGE---NGLLLTPCY--------TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTpfangp 643
Cdd:cd14048   155 DVVKVGDFGLVTAMdQGEpeqTVLTPMPAYakhtgqvgTRLYMSPEQIHGNQYSEKVDIFALGLILFELIYSFS------ 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 644 ndTPEE---ILLRIGNGKFSLSggnWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14048   229 --TQMErirTLTDVRKLKFPAL---FTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
93-311 1.62e-19

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: 89.45  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKtGPDAGQLYAMkVLKKASLKVRDRVRT---KMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAK-GIEEEGGETL-VLVKALQKTKDENLQsefRRELDMFRKLSHKNVVRLLGLCREAEPHYMIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDV--FTRLSKEVLFTEE----DVKFYLA---ELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd05046    88 EYTDLGDLkqFLRATKSKDEKLKppplSTKQKVAlctQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDV 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 241 VDQEkkAYSFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLGMPQ 311
Cdd:cd05046   168 YNSE--YYKLRNAlipLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELPV 240
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
90-344 1.63e-19

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: 88.86  E-value: 1.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLK---VRDRVRTKMERDILVEVNHPF--IVKLHYAFQTEGK 164
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIAD---GLPVAVKHVVKERVTewgTLNGVMVPLEIVLLKKVGSGFrgVIKLLDWYERPDG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLR-GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFG---LSKE 239
Cdd:cd14102    79 FLIVMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGsgaLLKD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEkkaysFCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRnetmnmILKAKLGMPQFLSAEAQ 318
Cdd:cd14102   159 TVYTD-----FDGTRVYSPPEWIRyHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEE------ILRGRLYFRRRVSPECQ 227
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 319 SLLRMLFKRNPANRlgsEGVEEIKRH 344
Cdd:cd14102   228 QLIKWCLSLRPSDR---PTLEQIFDH 250
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
86-332 1.72e-19

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: 88.85  E-value: 1.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFL----VRKKTgpdagqlyAMKVLKKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQT 161
Cdd:cd05112     2 DPSELTFVQEIGSGQFGLVHLgywlNKDKV--------AIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd05112    71 QAPICLVFEFMEHGCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 VDQEKKaySFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSA 315
Cdd:cd05112   151 LDDQYT--SSTGTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGfRLYKPRLAST 228
                         250
                  ....*....|....*..
gi 1034674014 316 EAQSLLRMLFKRNPANR 332
Cdd:cd05112   229 HVYEIMNHCWKERPEDR 245
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
89-332 1.75e-19

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: 90.08  E-value: 1.75e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvRKKTGPDAGQL---YAMKVLKKA-SLKVRDRVRTkmERDILVEVNHPFIVKL-----HYAF 159
Cdd:cd05108     8 EFKKIKVLGSGAFGTVY--KGLWIPEGEKVkipVAIKELREAtSPKANKEILD--EAYVMASVDNPHVCRLlgiclTSTV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGKLY---LILDFLRGGDvfTRLSKEVLFTeedvkfYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05108    84 QLITQLMpfgCLLDYVREHK--DNIGSQYLLN------WCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSFCGTV--EYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQF 312
Cdd:cd05108   156 AKLLGAEEKEYHAEGGKVpiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEISSILEKGeRLPQPPI 235
                         250       260
                  ....*....|....*....|
gi 1034674014 313 LSAEAQSLLRMLFKRNPANR 332
Cdd:cd05108   236 CTIDVYMIMVKCWMIDADSR 255
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
71-302 1.78e-19

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: 90.12  E-value: 1.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  71 EIPITHHVKegyekadpaQFELLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKvlkkaslKVRDRVRTK-------MERD 142
Cdd:cd07865     4 EFPFCDEVS---------KYEKLAKIGQGTFGEVFKARhRKTG----QIVALK-------KVLMENEKEgfpitalREIK 63
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 143 ILVEVNHPFIVKLHYAFQTE--------GKLYLILDFLRGgDVFTRLS-KEVLFTEEDVKFYLAELALALDHLHQLGIVY 213
Cdd:cd07865    64 ILQLLKHENVVNLIEICRTKatpynrykGSIYLVFEFCEH-DLAGLLSnKNVKFTLSEIKKVMKMLLNGLYYIHRNKILH 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 214 RDLKPENILLDEIGHIKLTDFGLSKE-SVDQEKKAYSFCG---TVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTL 288
Cdd:cd07865   143 RDMKAANILITKDGVLKLADFGLARAfSLAKNSQPNRYTNrvvTLWYRPPELlLGERDYGPPIDMWGAGCIMAEMWTRSP 222
                         250
                  ....*....|....
gi 1034674014 289 PFQGKDRNETMNMI 302
Cdd:cd07865   223 IMQGNTEQHQLTLI 236
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
450-688 1.79e-19

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: 89.56  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 450 GVGSYSVCKRciHATTNMeFAVKIIDKS---KRDPSE----EIEILMRYgqHPN-IITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05608    13 GFGEVSACQM--RATGKL-YACKKLNKKrlkKRKGYEgamvEKRILAKV--HSRfIVSLAYAFQTKTDLCLVMTIMNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRIL----KQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRgeNGLLL 597
Cdd:cd05608    88 LRYHIYnvdeENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDG----NVRISDLGLAVELK--DGQTK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCY--TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSLSggnwDNISDGAK 674
Cdd:cd05608   162 TKGYagTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFrARGEKVENKELKQRILNDSVTYS----EKFSPASK 237
                         250
                  ....*....|....
gi 1034674014 675 DLLSHMLHMDPHQR 688
Cdd:cd05608   238 SICEALLAKDPEKR 251
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
89-328 1.84e-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: 88.92  E-value: 1.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYLI 168
Cdd:cd14150     1 EVSMLKRIGTGSFGTVF--RGKWHGDV----AVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLskEVLFTEEDVkFYLAELA----LALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL----SKES 240
Cdd:cd14150    74 TQWCEGSSLYRHL--HVTETRFDT-MQLIDVArqtaQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLatvkTRWS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 VDQEKKAYSfcGTVEYMAPEVVNRRG---HSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAKLG--MPQFLS 314
Cdd:cd14150   151 GSQQVEQPS--GSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSNiNNRDQIIFMVGRGYLSpdLSKLSS 228
                         250
                  ....*....|....*....
gi 1034674014 315 AEAQSLLRML-----FKRN 328
Cdd:cd14150   229 NCPKAMKRLLidclkFKRE 247
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
89-284 2.18e-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: 89.16  E-value: 2.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDAgqlYAmkvLKKASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAF------- 159
Cdd:cd14048     7 DFEPIQCLGRGGFGVVFEAKNKVDDCN---YA---VKRIRLPNNELAREKVLREVraLAKLDHPGIVRYFNAWlerppeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 ----QTEGKLYLILDFLRGGDVFTRLSKEVLFTEED---VKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLT 232
Cdd:cd14048    81 wqekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 233 DFGL--------SKESVDQEKKAYSF----CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14048   161 DFGLvtamdqgePEQTVLTPMPAYAKhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
447-711 2.24e-19

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: 89.02  E-value: 2.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-----EIEILMRYGQHPNIITLKD-VFDDGRyVYLVTDLMKGG 520
Cdd:cd06617     7 EELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQkrllmDLDISMRSVDCPYTVTFYGaLFREGD-VWICMEVMDTS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 elLDRILKQ-----KCFSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYMDESasadSIRICDFGFAKQLrgENG 594
Cdd:cd06617    86 --LDKFYKKvydkgLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNG----QVKLCDFGISGYL--VDS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTP---CytANFVAPE----VLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGpnDTPEEILL--------RIGNGKF 659
Cdd:cd06617   158 VAKTIdagC--KPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPYDSW--KTPFQQLKqvveepspQLPAEKF 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 660 SLSggnwdnisdgAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQLPNDQP 711
Cdd:cd06617   234 SPE----------FQDFVNKCLKKNYKERPNYPELLQHPFFELHLSKNTDVA 275
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
86-314 2.54e-19

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: 88.40  E-value: 2.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVflvrkKTGPDAGQL-YAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK 164
Cdd:cd05113     2 DPKDLTFLKELGTGQFGVV-----KYGKWRGQYdVAIKMIKEGSMSEDEFIE---EAKVMMNLSHEKLVQLYGVCTKQRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd05113    74 IFIITEYMANGCLLNYLrEMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 244 EKKaySFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 314
Cdd:cd05113   154 EYT--SSVGSkfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGlRLYRPHLAS 227
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
430-701 2.55e-19

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: 90.47  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 430 VQINGNAAQFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDK-------SKRDPSEEIeiLMRYGQHPNIITLKD 502
Cdd:cd07876    10 VQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRpfqnqthAKRAYRELV--LLKCVNHKNIISLLN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 503 VF------DDGRYVYLVTDLMKGGelLDRILKQKCFSEReASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasad 576
Cdd:cd07876    88 VFtpqkslEEFQDVYLVMELMDAN--LCQVIHMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC---- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 577 SIRICDFGFAKQlrGENGLLLTP-CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN-DTPEEILLRI 654
Cdd:cd07876   161 TLKILDFGLART--ACTNFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHiDQWNKVIEQL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 655 GNGKFSLSGG-------------------------NWDNISDG---------AKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07876   239 GTPSAEFMNRlqptvrnyvenrpqypgisfeelfpDWIFPSESerdklktsqARDLLSKMLVIDPDKRISVDEALRHPYI 318

                  .
gi 1034674014 701 T 701
Cdd:cd07876   319 T 319
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
89-347 2.56e-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: 89.03  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAmkvLKKASLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNR---ETHEIVA---LKRVRLDDDDEgVPSSALREIclLKELKHKNIVRLYDVLHSDKKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDF----LRggDVFTRLSKEVlfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSV 241
Cdd:cd07839    75 TLVFEYcdqdLK--KYFDSCNGDI--DPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR-AF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSF-CGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLP-FQGKDRNETMNMILKAkLGMPQF------ 312
Cdd:cd07839   150 GIPVRCYSAeVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRL-LGTPTEeswpgv 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 313 ------------------------LSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd07839   229 sklpdykpypmypattslvnvvpkLNSTGRDLLQNLLVCNPVQRISA---EEALQHPYF 284
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
89-311 2.60e-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: 88.94  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRK-KTGpdaGQLYAMKvlkkaslkvRDRVRTKME-------RDILV-----EVNHPFIVKL 155
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDlKNG---GRFVALK---------RVRVQTGEEgmplstiREVAVlrhleTFEHPNVVRL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQT-----EGKLYLILDFLrGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH 228
Cdd:cd07862    70 FDVCTVsrtdrETKLTLVFEHV-DQDLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQ 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 IKLTDFGLSkesvdqekKAYSF-------CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd07862   149 IKLADFGLA--------RIYSFqmaltsvVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGK 220
                         250
                  ....*....|
gi 1034674014 302 ILKAkLGMPQ 311
Cdd:cd07862   221 ILDV-IGLPG 229
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
90-292 2.61e-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: 2.61e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlkKASLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKK---TGQIVAMK---KIRLESEEEgVPSTAIREIslLKELQHPNIVCLEDVLMQENRLY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGgDV---FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQ 243
Cdd:cd07861    76 LVFEFLSM-DLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLAR-AFGI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 244 EKKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQG 292
Cdd:cd07861   154 PVRVYTHeVVTLWYRAPEVlLGSPRYSTPVDIWSIGTIFAEMATKKPLFHG 204
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
439-697 2.86e-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: 88.32  E-value: 2.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKEDIGVGSY-SVCKrCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYgQHPNIITLKDVFDDG---------- 507
Cdd:cd14047     4 FRQDFKEIELIGSGGFgQVFK-AKHRIDGKTYAIKRVKLNNEKAEREVKALAKL-DHPNIVRYNGCWDGFdydpetsssn 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 ------RYVYLVTDLMKGGELLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIR 579
Cdd:cd14047    82 ssrsktKCLFIQMEFCEKGTLESWIEKRNgeKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG----KVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 580 ICDFGFAKQLRGENGLLLTPCyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGY-TPFANgpndtpEEILLRIGNGK 658
Cdd:cd14047   158 IGDFGLVTSLKNDGKRTKSKG-TLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCdSAFEK------SKFWTDLRNGI 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 659 FSLsggNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14047   231 LPD---IFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
88-311 3.16e-19

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: 88.63  E-value: 3.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFL-VRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKmERDILVEVNHPFIVKLhYAFQTEGKLY 166
Cdd:cd05057     7 TELEKGKVLGSGAFGTVYKgVWIPEGEKVKIPVAIKVLREETGPKANEEILD-EAYVMASVDHPHLVRL-LGICLSSQVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGG--DVFTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQE 244
Cdd:cd05057    85 LITQLMPLGclLDYVRNHRDNIGSQLLLNWCV-QIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAK-LLDVD 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 245 KKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQ 311
Cdd:cd05057   163 EKEYHAEGgkvPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGeRLPQPP 234
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
94-347 3.17e-19

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: 88.48  E-value: 3.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVflVRKktGPDAGQLYAMKVLKKASLKVRDRvrtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLIL--- 169
Cdd:cd13982     7 KVLGYGSEGTI--VFR--GTFDGRPVAVKRLLPEFFDFADR-----EVQLLRESdEHPNVIRYFCTEKDRQFLYIALelc 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 -----DFLRGGDVFtrlsKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD---EIGHIK--LTDFGLSKE 239
Cdd:cd13982    78 aaslqDLVESPRES----KLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRamISDFGLCKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 -SVDQekkaYSF------CGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTL-PFQGKDRNEtMNmILKAKLG 308
Cdd:cd13982   154 lDVGR----SSFsrrsgvAGTSGWIAPEMLSgstKRRQTRAVDIFSLGCVFYYVLSGGShPFGDKLERE-AN-ILKGKYS 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 309 MPQFLSA-----EAQSLLRMLFKRNPANRlgsEGVEEIKRHLFF 347
Cdd:cd13982   228 LDKLLSLgehgpEAQDLIERMIDFDPEKR---PSAEEVLNHPFF 268
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
96-333 3.47e-19

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: 88.48  E-value: 3.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVR-KKTGPDAGQ-LYAMKVLKKASLKVRDRVrtKMERDILVEVNHPFIVKLhYAFQTEGK-LYLILDFL 172
Cdd:cd05092    13 LGEGAFGKVFLAEcHNLLPEQDKmLVAVKALKEATESARQDF--QREAELLTVLQHQHIVRF-YGVCTEGEpLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDV--FTRL---SKEVLFTEEDVKF----------YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd05092    90 RHGDLnrFLRShgpDAKILDGGEGQAPgqltlgqmlqIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFL 313
Cdd:cd05092   170 RDiySTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGReLERPRTC 249
                         250       260
                  ....*....|....*....|
gi 1034674014 314 SAEAQSLLRMLFKRNPANRL 333
Cdd:cd05092   250 PPEVYAIMQGCWQREPQQRH 269
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
90-310 3.90e-19

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: 88.59  E-value: 3.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVL-------------KKASLkvrdrvrtkmerdiLVEVNHPFIVKLH 156
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKL---TGQLVALKEIrleheegapftaiREASL--------------LKDLKHANIVTLH 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQTEGKLYLILDFLRggdvfTRLSKEV-----LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKL 231
Cdd:cd07844    65 DIIHTKKTLTLVFEYLD-----TDLKQYMddcggGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 232 TDFGLSK-ESVdqEKKAYSF-CGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAkL 307
Cdd:cd07844   140 ADFGLARaKSV--PSKTYSNeVVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRV-L 216

                  ...
gi 1034674014 308 GMP 310
Cdd:cd07844   217 GTP 219
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
449-639 4.55e-19

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: 89.29  E-value: 4.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVEctmvekrVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPCY 601
Cdd:cd05615    98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEG----HIKIADFGMCKEHMVEGVTTRTFCG 173
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd05615   174 TPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPF 211
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
93-310 4.84e-19

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: 88.52  E-value: 4.84e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTGPDagqlyaMKVLKKASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd07873     7 LDKLGEGTYATVYKGRSKLTDN------LVALKEIRLEHEEGAPCTAIREVslLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd07873    81 YL-DKDLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSN 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 250 FCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07873   160 EVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRI-LGTP 220
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
86-290 5.39e-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: 87.61  E-value: 5.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHyAFQTEGKL 165
Cdd:cd05066     2 DASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLK-AGYTEKQRRDFLSEASIMGQFDHPNIIHLE-GVVTRSKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLIL-DFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd05066    80 VMIVtEYMENGSLDAFLRKhDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 244 EKKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPF 290
Cdd:cd05066   160 PEAAYTTRGgkiPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 210
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
443-700 5.68e-19

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: 88.37  E-value: 5.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE---EIEILMRYGQH-----PNIITLKDVFDDGRYVYLVT 514
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIRNKKRFHQQalvEVKILKHLNDNdpddkHNIVRYKDSFIFRGHLCIVF 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMkGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGFAkqlrge 592
Cdd:cd14210    95 ELL-SINLYELLKSNnfQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKS--SIKVIDFGSS------ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 ngllltpCYTANFV----------APEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDT-------------PEE 649
Cdd:cd14210   166 -------CFEGEKVytyiqsrfyrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFP-GENEEeqlacimevlgvpPKS 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 650 ILLRIGNGK-FSLSGGNWDNISDGAK----------------------DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14210   238 LIDKASRRKkFFDSNGKPRPTTNSKGkkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
449-701 5.74e-19

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: 89.52  E-value: 5.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDP----SEEIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05629     9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSemfKKDQlahvKAERDVLAE-SDSPWVVSLYYSFQDAQYLYLIMEFLPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFG----FAKQ--------- 588
Cdd:cd05629    88 LMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNIL-IDRGGH---IKLSDFGlstgFHKQhdsayyqkl 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 ---------LRGENGLLLTPCY-------------------------TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA 634
Cdd:cd05629   164 lqgksnknrIDNRNSVAVDSINltmsskdqiatwkknrrlmaystvgTPDYIAPEIFLQQGYGQECDWWSLGAIMFECLI 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 635 GYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQ--RYTAEQILKHSWIT 701
Cdd:cd05629   244 GWPPFC---SENSHETYRKIINWRETLYFPDDIHLSVEAEDLIRRLITNAENRlgRGGAHEIKSHPFFR 309
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
441-699 7.98e-19

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: 88.53  E-value: 7.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCI-HATTNMEFAVKII---DKSKRDPSEEIEILMRYGQHPN-----IITLKDVFDDGRYVY 511
Cdd:cd14214    13 ERYEIVGDLGEGTFGKVVECLdHARGKSQVALKIIrnvGKYREAARLEINVLKKIKEKDKenkflCVLMSDWFNFHGHMC 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMkgGELLDRILKQKCFSEREASDI---LYVISKTVDYLHCQGVVHRDLKPSNILYMD--------ESASAD---- 576
Cdd:cd14214    93 IAFELL--GKNTFEFLKENNFQPYPLPHIrhmAYQLCHALKFLHENQLTHTDLKPENILFVNsefdtlynESKSCEeksv 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 577 ---SIRICDFGFAKqlrGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN--------- 644
Cdd:cd14214   171 kntSIRVADFGSAT---FDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENrehlvmmek 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 645 ---DTPEEILLRIGNGKFSLSGG-NWD-NISDGAK-----------------------DLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14214   248 ilgPIPSHMIHRTRKQKYFYKGSlVWDeNSSDGRYvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRITLKEALL 327

                  ...
gi 1034674014 697 HSW 699
Cdd:cd14214   328 HPF 330
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
449-699 8.19e-19

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: 87.49  E-value: 8.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKsKRDPSEEIEILM-----------RYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd05606     2 IGRGGFGEVYGCRKADTGKMYAMKCLDK-KRIKMKQGETLAlnerimlslvsTGGDCPFIVCMTYAFQTPDKLCFILDLM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSERE----ASDILYviskTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFA-----KQ 588
Cdd:cd05606    81 NGGDLHYHLSQHGVFSEAEmrfyAAEVIL----GLEHMHNRFIVYRDLKPANIL-LDEHG---HVRISDLGLAcdfskKK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGllltpcyTANFVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSggnwD 667
Cdd:cd05606   153 PHASVG-------THGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKHEIDRMTLTMNVELP----D 221
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 668 NISDGAKDLLSHMLHMDPHQRY-----TAEQILKHSW 699
Cdd:cd05606   222 SFSPELKSLLEGLLQRDVSKRLgclgrGATEVKEHPF 258
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
89-332 8.48e-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: 87.34  E-value: 8.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRkktGPDAGQLYAMK---VLKKASLKVrdrvrTKMERDILVEV-NHPFIVKL--HYAFQTE 162
Cdd:cd14037     4 HVTIEKYLAEGGFAHVYLVK---TSNGGNRAALKrvyVNDEHDLNV-----CKREIEIMKRLsGHKNIVGYidSSANRSG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLY---LILDFLRGGDVF----TRLSKEvlFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd14037    76 NGVYevlLLMEYCKGGGVIdlmnQRLQTG--LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FG------------LSKESVDQEKKAYSfcgTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQgkdrnET 298
Cdd:cd14037   154 FGsattkilppqtkQGVTYVEEDIKKYT---TLQYRAPEMIDlyrGKPITEKSDIWALGCLLYKLCFYTTPFE-----ES 225
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 299 MNM-ILKAKLGMPQF--LSAEAQSLLRMLFKRNPANR 332
Cdd:cd14037   226 GQLaILNGNFTFPDNsrYSKRLHKLIRYMLEEDPEKR 262
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
462-688 9.54e-19

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: 87.28  E-value: 9.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 462 HATTNMEFAVK-----IIDKSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYV-----YLVTDLMKGGELLDRILK-QK 530
Cdd:cd14039    14 NQETGEKIAIKscrleLSVKNKDRWCHEIQI-MKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCSGGDLRKLLNKpEN 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 531 CFSEREaSDILYVISKT---VDYLHCQGVVHRDLKPSNILYMDESASADSiRICDFGFAKQLrgENGLLLTPCY-TANFV 606
Cdd:cd14039    93 CCGLKE-SQVLSLLSDIgsgIQYLHENKIIHRDLKPENIVLQEINGKIVH-KIIDLGYAKDL--DQGSLCTSFVgTLQYL 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 607 APEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANG----------PNDTPEEILL---RIGNGKFSLSGGNWDNIS--- 670
Cdd:cd14039   169 APELFENKSYTVTVDYWSFGTMVFECIAGFRPFLHNlqpftwhekiKKKDPKHIFAveeMNGEVRFSTHLPQPNNLCsli 248
                         250
                  ....*....|....*....
gi 1034674014 671 -DGAKDLLSHMLHMDPHQR 688
Cdd:cd14039   249 vEPMEGWLQLMLNWDPVQR 267
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
448-697 1.04e-18

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: 87.11  E-value: 1.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHATTNMEFAVKIID-KSKRDPSEEI--EI-LMRYGQHPNIITLKDVF-DDGRYVYLVTDLMKGGEL 522
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIHiDAKSSVRKQIlrELqILHECHSPYIVSFYGAFlNENNNIIICMEYMDCGSL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 lDRILKQKC-FSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRgeNGLLLTPC 600
Cdd:cd06620    92 -DKILKKKGpFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILV----NSKGQIKLCDFGVSGELI--NSIADTFV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFA-----NGPNDTPEEI---LLRIGNgKFSLSGGNWDNISDG 672
Cdd:cd06620   165 GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAgsnddDDGYNGPMGIldlLQRIVN-EPPPRLPKDRIFPKD 243
                         250       260
                  ....*....|....*....|....*
gi 1034674014 673 AKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd06620   244 LRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
82-310 1.18e-18

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: 87.44  E-value: 1.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  82 YEKADpaQFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQT 161
Cdd:cd07869     1 FGKAD--SYEKLEKLGEGSYATVYKGKSKVN---GKLVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGgDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd07869    75 KETLTLVFEYVHT-DLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 241 VDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAkLGMP 310
Cdd:cd07869   154 SVPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmKDIQDQLERIFLV-LGTP 224
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
449-688 1.23e-18

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: 87.00  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCIHATTNMeFAVKIIDKS--KRDPSE-----EIEILMRYGQHpNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd05630     8 LGKGGFgEVCACQVRATGKM-YACKKLEKKriKKRKGEamalnEKQILEKVNSR-FVVSLAYAYETKDALCLVLTLMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRI--LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA------KQLRGE 592
Cdd:cd05630    86 DLKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHG----HIRISDLGLAvhvpegQTIKGR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 593 NGllltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTP-EEI--LLRIGNGKFSlsggnwDNI 669
Cdd:cd05630   162 VG-------TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKrEEVerLVKEVPEEYS------EKF 228
                         250
                  ....*....|....*....
gi 1034674014 670 SDGAKDLLSHMLHMDPHQR 688
Cdd:cd05630   229 SPQARSLCSMLLCKDPAER 247
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
84-346 1.46e-18

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: 86.24  E-value: 1.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  84 KADPAQ-FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKkasLKVRDRVRTKMERDILV-EVNHPFIVKLHYAFQT 161
Cdd:cd06646     4 RRNPQHdYELIQRVGSGTYGDVYKARNLH---TGELAAVKIIK---LEPGDDFSLIQQEIFMVkECKHCNIVAYFGSYLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd06646    78 REKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVV---NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF-----L 313
Cdd:cd06646   158 ATIAKRKSFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPKLkdktkW 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 314 SAEAQSLLRMLFKRNPANRlgsEGVEEIKRHLF 346
Cdd:cd06646   238 SSTFHNFVKISLTKNPKKR---PTAERLLTHLF 267
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
98-333 1.57e-18

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: 85.83  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  98 QGSFGKVFLV--RKKTGPDAGQLYAMKVLKKASLKVRDRVRtkmerdilvevnHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd13995    14 RGAFGKVYLAqdTKTKKRMACKLIPVEQFKPSDVEIQACFR------------HENIAELYGALLWEETVHLFMEAGEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIkLTDFGLSKESVDQEKKAYSFCGTVE 255
Cdd:cd13995    82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 256 YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET----MNMILKAK---LGMPQFLSAEAQSLLRMLFKRN 328
Cdd:cd13995   161 YMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQApplEDIAQDCSPAMRELLEAALERN 240

                  ....*
gi 1034674014 329 PANRL 333
Cdd:cd13995   241 PNHRS 245
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
443-700 1.58e-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: 86.55  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVckrcIHATTNMEFAVKIIDKSKRDPS----------EEIEILMRYGQ--HPNIITLKDVFDDGRY- 509
Cdd:cd07863     2 YEPVAEIGVGAYGT----VYKARDPHSGHFVALKSVRVQTnedglplstvREVALLKRLEAfdHPNIVRLMDVCATSRTd 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 ----VYLVTdlmkggELLDRILKQKC-------FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSI 578
Cdd:cd07863    78 retkVTLVF------EHVDQDLRTYLdkvpppgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILV----TSGGQV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 579 RICDFGFAKQLRGEngLLLTP-CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIG- 655
Cdd:cd07863   148 KLADFGLARIYSCQ--MALTPvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFcGNSEADQLGKIFDLIGl 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 656 ------NGKFSLSGGNWD------------NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07863   226 ppeddwPRDVTLPRGAFSprgprpvqsvvpEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
449-688 1.74e-18

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: 86.59  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCIHATTNMeFAVKIIDKS--KRDPSE-----EIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd05631     8 LGKGGFgEVCACQVRATGKM-YACKKLEKKriKKRKGEamalnEKRILEKV-NSRFVVSLAYAYETKDALCLVLTIMNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRI--LKQKCFSEREAsdILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQL------R 590
Cdd:cd05631    86 DLKFHIynMGNPGFDEQRA--IFYAaeLCCGLEDLQRERIVYRDLKPENILLDDRG----HIRISDLGLAVQIpegetvR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGllltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTP-EEILLRIGNGKFSLSggnwDNI 669
Cdd:cd05631   160 GRVG-------TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKrEEVDRRVKEDQEEYS----EKF 228
                         250
                  ....*....|....*....
gi 1034674014 670 SDGAKDLLSHMLHMDPHQR 688
Cdd:cd05631   229 SEDAKSICRMLLTKNPKER 247
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
447-696 1.96e-18

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: 85.57  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFAVK-----IIDKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKtcretLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKC---------FSEREASDILYVISKtvdylHCqgvVHRDLKPSNILYMDEsasaDSIRICDFGFAKQLRG- 591
Cdd:cd05041    80 LLTFLRKKGArltvkqllqMCLDAAAGMEYLESK-----NC---IHRDLAARNCLVGEN----NVLKISDFGMSREEEDg 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ----ENGLLLTPcytANFVAPEVLMQQGYDAACDIWSLGVLFY-TMLAGYTPFANGPNDTPEEILLRigNGKFSLSGGNW 666
Cdd:cd05041   148 eytvSDGLKQIP---IKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIES--GYRMPAPELCP 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 667 DNISdgakDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd05041   223 EAVY----RLMLQCWAYDPENRPSFSEIYN 248
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
441-707 2.17e-18

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: 86.63  E-value: 2.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-------EIEILMRYgQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd06633    21 EIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEkwqdiikEVKFLQQL-KHPNTIEYKGCYLKDHTAWLV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TD--LMKGGELLDriLKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG 591
Cdd:cd06633   100 MEycLGSASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG----QVKLADFGSASIASP 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYtanfVAPEVL--MQQG-YDAACDIWSLGVL----------FYTMLAGYTPFANGPNDTPeeillrigngk 658
Cdd:cd06633   174 ANSFVGTPYW----MAPEVIlaMDEGqYDGKVDIWSLGITcielaerkppLFNMNAMSALYHIAQNDSP----------- 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 659 fSLSGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWItHRDQLP 707
Cdd:cd06633   239 -TLQSNEW---TDSFRGFVDYCLQKIPQERPSSAELLRHDFV-RRERPP 282
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
92-332 2.21e-18

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: 86.22  E-value: 2.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFLVRKK-TGPDAGQLYAMKVLKKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd05090     9 FMEELGECAFGKIYKGHLYlPGMDHAQLVAIKTLKDYN-NPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRL------SKEVLFTEED--VKFYL---------AELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd05090    88 FMNQGDLHEFLimrsphSDVGCSSDEDgtVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGM 309
Cdd:cd05090   168 LGLSREiySSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQlLPC 247
                         250       260
                  ....*....|....*....|...
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05090   248 SEDCPPRMYSLMTECWQEIPSRR 270
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
90-324 2.22e-18

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: 87.07  E-value: 2.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVL----KKASLKvrdrvRTKMERDILVEV-NHPFIVKLH-------Y 157
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITnvfsKKILAK-----RALRELKLLRHFrGHKNITCLYdmdivfpG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 158 AFQtegKLYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd07857    77 NFN---ELYLYEE-LMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KE-SVDQEKKA---YSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP-- 310
Cdd:cd07857   153 RGfSENPGENAgfmTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQV-LGTPde 231
                         250
                  ....*....|....*...
gi 1034674014 311 ----QFLSAEAQSLLRML 324
Cdd:cd07857   232 etlsRIGSPKAQNYIRSL 249
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
445-696 2.35e-18

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: 85.51  E-value: 2.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSY-SVCKRCIHATTnmeFAVKIIDKSK----RDPSEEIEILMRYGQHPNII---TLKDVFDDGRYVYLVTDL 516
Cdd:cd13979     7 LQEPLGSGGFgSVYKATYKGET---VAVKIVRRRRknraSRQSFWAELNAARLRHENIVrvlAAETGTDFASLGLIIMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRIlkqkcfseREASDILYV---------ISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAK 587
Cdd:cd13979    84 CGNGTLQQLI--------YEGSEPLPLahrilisldIARALRFCHSHGIVHLDVKPANIL-ISEQ---GVCKLCDFGCSV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QLRGENGLLLTPCY---TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNG-KFSLSG 663
Cdd:cd13979   152 KLGEGNEVGTPRSHiggTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYA---GLRQHVLYAVVAKDlRPDLSG 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 664 GNWDNISDGAKDLLSHMLHMDPHQRYTA-EQILK 696
Cdd:cd13979   229 LEDSEFGQRLRSLISRCWSAQPAERPNAdESLLK 262
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
88-302 2.41e-18

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: 85.89  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVF---LVRKKtGPDAGQLYAMKVLKK-ASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd05048     5 SAVRFLEELGEGAFGKVYkgeLLGPS-SEESAISVAIKTLKEnASPKTQQDFRR--EAELMSDLQHPNIVCLLGVCTKEQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGI----------------VYRDLKPENILLDEIG 227
Cdd:cd05048    82 PQCMLFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIaiqiaagmeylsshhyVHRDLAARNCLVGDGL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 228 HIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 302
Cdd:cd05048   162 TVKISDFGLSRDiySSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMI 239
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
86-332 2.42e-18

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: 85.54  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFL-VRKKTGPdagqlYAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQT-EG 163
Cdd:cd05068     6 DRKSLKLLRKLGSGQFGEVWEgLWNNTTP-----VAVKTLKPGTMDPEDFLR---EAQIMKKLRHPKLIQL-YAVCTlEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDVFTRLSKE--VLFTEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK--- 238
Cdd:cd05068    77 PIYIITELMKHGSLLEYLQGKgrSLQLPQLIDM-AAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARvik 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 -ESVDQEKKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMiLKAKLGMPQFLSAE 316
Cdd:cd05068   156 vEDEYEAREGAKF--PIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQ-VERGYRMPCPPNCP 232
                         250
                  ....*....|....*...
gi 1034674014 317 AQSLLRML--FKRNPANR 332
Cdd:cd05068   233 PQLYDIMLecWKADPMER 250
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
89-333 2.59e-18

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: 86.26  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrkKTGPDAGQLYAMKVLKKASLKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd14040     7 RYLLLHLLGRGGFSEVY----KAFDLYEQRYAAVKIHQLNKSWRDEKKENYhkhacrEYRIHKELDHPRIVKLYDYFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLY-LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILLDE---IGHIKLTDFGL 236
Cdd:cd14040    83 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDgtaCGEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SK------ESVDQEKKAYSFCGTVEYMAPE--VVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETM---NMIL 303
Cdd:cd14040   163 SKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqeNTIL 242
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 304 KA---KLGMPQFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd14040   243 KAtevQFPVKPVVSNEAKAFIRRCLAYRKEDRF 275
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
95-341 3.07e-18

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: 85.74  E-value: 3.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKASLKVRDRVRTKM-------------------ERDILVEVNHPFIVKL 155
Cdd:cd14000     1 LLGDGGFGSVYRASYK-----GEPVAVKIFNKHTSSNFANVPADTmlrhlratdamknfrllrqELTVLSHLHHPSIVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAfqTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELAL----ALDHLHQLGIVYRDLKPENILL-----DEI 226
Cdd:cd14000    76 LGI--GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GHIKLTDFGLSKESVDQEKKaySFCGTVEYMAPEVVNRR-GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKa 305
Cdd:cd14000   154 IIIKIADYGISRQCCRMGAK--GSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 306 klGMPQFLS-------AEAQSLLRMLFKRNPANRLGSEGVEEI 341
Cdd:cd14000   231 --GLRPPLKqyecapwPEVEVLMKKCWKENPQQRPTAVTVVSI 271
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
89-311 3.35e-18

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: 86.18  E-value: 3.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDaGQLYAMKVLKkASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAF--QTEGK 164
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKNGKD-GKEYAIKKFK-GDKEQYTGISQSACREIalLRELKHENVVSLVEVFleHADKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDF----LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----DEIGHIKLTDFGL 236
Cdd:cd07842    79 VYLLFDYaehdLWQIIKFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSFCG---TVEYMAPEVVNRRGHSQSA-DWWSYGVLMFEMLTGTLPFQGK-DRNETMNM--------IL 303
Cdd:cd07842   159 ARLFNAPLKPLADLDPvvvTIWYRAPELLLGARHYTKAiDIWAIGCIFAELLTLEPIFKGReAKIKKSNPfqrdqlerIF 238

                  ....*...
gi 1034674014 304 KAkLGMPQ 311
Cdd:cd07842   239 EV-LGTPT 245
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
95-290 3.36e-18

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: 84.97  E-value: 3.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL--DFL 172
Cdd:cd13983     8 VLGRGSFKTVY---RAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLH--QLGIVYRDLKPENILLD-EIGHIKLTDFGLSKESvdQEKKAYS 249
Cdd:cd13983    85 TSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHtrDPPIIHRDLKCDNIFINgNTGEVKIGDLGLATLL--RQSFAKS 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 250 FCGTVEYMAPEVVNrRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd13983   163 VIGTPEFMAPEMYE-EHYDEKVDIYAFGMCLLEMATGEYPY 202
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
93-332 3.54e-18

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: 86.70  E-value: 3.54e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL------Y 166
Cdd:cd07850     5 LKPIGSGAQGIVCAAYDTV---TGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKesvdqeKK 246
Cdd:cd07850    82 LVMELM---DANLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR------TA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCGTVE-----YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMP--QFLSaEAQS 319
Cdd:cd07850   153 GTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIE-QLGTPsdEFMS-RLQP 230
                         250
                  ....*....|...
gi 1034674014 320 LLRMLFKRNPANR 332
Cdd:cd07850   231 TVRNYVENRPKYA 243
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
444-724 3.67e-18

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: 85.67  E-value: 3.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 444 ELKEDIGVGSYSVCKRCIHATTNMEFAVKII----DKSK-RDPSEEIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrlelDESKfNQIIMELDILHK-AVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELlDRILKQKCFSEREASDILYVIS-KTVDYLHC----QGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrgEN 593
Cdd:cd06622    83 AGSL-DKLYAGGVATEGIPEDVLRRITyAVVKGLKFlkeeHNIIHRDVKPTNVLV----NGNGQVKLCDFGVSGNL--VA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTANFVAPEVLMQQG------YDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWD 667
Cdd:cd06622   156 SLAKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPY---PPETYANIFAQLSAIVDGDPPTLPS 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 668 NISDGAKDLLSHMLHMDPHQRYTAEQILKHSWIThrdqlpNDQPKRNDVSHVVKGAM 724
Cdd:cd06622   233 GYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV------KYKNADVDMAEWVTGAL 283
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
93-345 3.76e-18

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 86.20  E-value: 3.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKTGPDagqlyaMKVLKKASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd07872    11 LEKLGEGTYATVFKGRSKLTEN------LVALKEIRLEHEEGAPCTAIREVslLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd07872    85 YL-DKDLKQYMDDcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 FCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP-----------------Q 311
Cdd:cd07872   164 EVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRL-LGTPteetwpgissndefknyN 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 312 FLSAEAQSLLrmlfkrNPANRLGSEGVEEIKRHL 345
Cdd:cd07872   243 FPKYKPQPLI------NHAPRLDTEGIELLTKFL 270
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
61-348 3.95e-18

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: 85.84  E-value: 3.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  61 DSCHDEGVvKEIPITHHVKEGYEKAdpaQFELLKVLGQGSFGKVFLVR----KKTGPDAGQLYAMKVLK-KASLKVRDRV 135
Cdd:cd05101     1 DAPMLAGV-SEYELPEDPKWEFPRD---KLTLGKPLGEGCFGQVVMAEavgiDKDKPKEAVTVAVKMLKdDATEKDLSDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 136 RTKMERDILVEvNHPFIVKLHYAFQTEGKLYLILDFLRGGDV-----------------FTRLSKEVLfTEEDVKFYLAE 198
Cdd:cd05101    77 VSEMEMMKMIG-KHKNIINLLGACTQDGPLYVIVEYASKGNLreylrarrppgmeysydINRVPEEQM-TFKDLVSCTYQ 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 199 LALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSY 276
Cdd:cd05101   155 LARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDinNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSF 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 277 GVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRNPANR-LGSEGVEEIKRHLFFA 348
Cdd:cd05101   235 GVLMWEIFTlGGSPYPGIPVEELFKLLKEGhRMDKPANCTNELYMMMRDCWHAVPSQRpTFKQLVEDLDRILTLT 309
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
89-332 4.53e-18

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 85.35  E-value: 4.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKL---HYAFQTEGKL 165
Cdd:cd05074    10 QFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLigvSLRSRAKGRL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 ---YLILDFLRGGDVFT-----RLSKE--VLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:cd05074    90 pipMVILPFMKHGDLHTfllmsRIGEEpfTLPLQTLVRFMI-DIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 236 LSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQ 311
Cdd:cd05074   169 LSKKiySGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLIKGnRLKQPP 248
                         250       260
                  ....*....|....*....|.
gi 1034674014 312 FLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05074   249 DCLEDVYELMCQCWSPEPKCR 269
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
87-322 4.57e-18

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: 85.03  E-value: 4.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd05063     4 PSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLK-PGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGG--DVFTRlSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 244
Cdd:cd05063    83 IITEYMENGalDKYLR-DHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI-----LKAKLGMPqflSA 315
Cdd:cd05063   162 EGTYTTSGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAIndgfrLPAPMDCP---SA 238

                  ....*..
gi 1034674014 316 EAQSLLR 322
Cdd:cd05063   239 VYQLMLQ 245
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
439-696 5.00e-18

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: 84.78  E-value: 5.00e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYE--LKEDIGVGSYSVckrcihattnmEFAVKIIDKSKRDpSEEIE-----ILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd05044     8 FGEVFEgtAKDILGDGSGET-----------KVAVKTLRKGATD-QEKAEflkeaHLMSNFKHPNILKLLGVCLDNDPQY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQKC-------FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFG 584
Cdd:cd05044    76 IILELMEGGDLLSYLRAARPtaftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERVVKIGDFG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 585 FAKQL--------RGEnGLLltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFY-TMLAGYTPFangPNDTPEEILlrig 655
Cdd:cd05044   156 LARDIykndyyrkEGE-GLL-----PVRWMAPESLVDGVFTTQSDVWAFGVLMWeILTLGQQPY---PARNNLEVL---- 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 656 ngKFSLSGGNWDNISDGAKDLLSHMLH---MDPHQRYTAEQILK 696
Cdd:cd05044   223 --HFVRAGGRLDQPDNCPDDLYELMLRcwsTDPEERPSFARILE 264
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
449-644 5.28e-18

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: 84.43  E-value: 5.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEIL-----MRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG--- 520
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLkeaekMERARHSYVLPLLGVCVERRSLGLVMEYMENGslk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEReaSDILYVISKTVDYLHC--QGVVHRDLKPSNILyMDESAsadSIRICDFGFAK---------QL 589
Cdd:cd13978    81 SLLEREIQDVPWSLR--FRIIHEIALGMNFLHNmdPPLLHHDLKPENIL-LDNHF---HVKISDFGLSKlgmksisanRR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 590 RGENGLLLTPCYTanfvAPEVL--MQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN 644
Cdd:cd13978   155 RGTENLGGTPIYM----APEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAIN 207
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
93-285 5.52e-18

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: 84.94  E-value: 5.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLKKASLK-VRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK--LYLI 168
Cdd:cd05081     9 ISQLGKGNFGSVELCRyDPLGDNTGALVAVKQLQHSGPDqQRDFQR---EIQILKALHSDFIVKYRGVSYGPGRrsLRLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 247
Cdd:cd05081    86 MEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAK-LLPLDKDY 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 248 YSF----CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT 285
Cdd:cd05081   165 YVVrepgQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
96-340 5.87e-18

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: 84.47  E-value: 5.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGpdagQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQ----GLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG---------LSKESVDQEKK 246
Cdd:cd14027    77 NLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTKEEHNEQRE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFC----GTVEYMAPE---VVNRRGhSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK-----LGMPQFLS 314
Cdd:cd14027   156 VDGTAkknaGTLYYMAPEhlnDVNAKP-TEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGnrpdvDDITEYCP 234
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 315 AEAQSLLRMLFKRNPANRLGSEGVEE 340
Cdd:cd14027   235 REIIDLMKLCWEANPEARPTFPGIEE 260
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
86-302 6.01e-18

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 84.35  E-value: 6.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASlkvrdrvRTKMERDILVEV------NHPFIVKLhYAF 159
Cdd:cd05033     2 DASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGY-------SDKQRLDFLTEAsimgqfDHPNVIRL-EGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGK-LYLILDFLRGG--DVFTRLSKEVLFTEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05033    74 VTKSRpVMIVTEYMENGslDKFLRENDGKFTVTQLVGM-LRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGL 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKkAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 302
Cdd:cd05033   153 SRRLEDSEA-TYTTKGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAV 221
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
89-286 6.12e-18

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: 84.73  E-value: 6.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMK---------VLKKASLKvrdrvrtkmERDILVEVNHPFIVKLHYAF 159
Cdd:cd07847     2 KYEKLSKIGEGSYGVVFKCRNR---ETGQIVAIKkfveseddpVIKKIALR---------EIRMLKQLKHPNLVNLIEVF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGKLYLILDFLRGgDVFTRLSKEVLFTEED-VKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd07847    70 RRKRKLHLVFEYCDH-TVLNELEKNPRGVPEHlIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTG 286
Cdd:cd07847   149 ILTGPGDDYTDYVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTG 197
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
89-345 9.08e-18

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 84.39  E-value: 9.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKT---GPDAGQLYAMKVLKK-ASLK-VRDRVrTKMERDILVEvNHPFIVKLHYAFQTEG 163
Cdd:cd05053    13 RLTLGKPLGEGAFGQVVKAEAVGldnKPNEVVTVAVKMLKDdATEKdLSDLV-SEMEMMKMIG-KHKNIINLLGACTQDG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLIL---------DFLRG--------GDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI 226
Cdd:cd05053    91 PLYVVVeyaskgnlrEFLRArrppgeeaSPDDPRVPEEQL-TQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVTED 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GHIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNEtMNMIL 303
Cdd:cd05053   170 NVMKIADFGLARDihHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE-LFKLL 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 304 KA--KLGMPQFLSAEAQSLLRMLFKRNPANRLG-SEGVEEIKRHL 345
Cdd:cd05053   249 KEghRMEKPQNCTQELYMLMRDCWHEVPSQRPTfKQLVEDLDRIL 293
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
449-704 9.48e-18

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: 85.83  E-value: 9.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCiHATTNMEFAVKIIDKS---KRDPSEEIEI---LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05626     9 LGIGAFgEVCLAC-KVDTHALYAMKTLRKKdvlNRNQVAHVKAerdILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASadsIRICDFGFAKQLR----------- 590
Cdd:cd05626    88 MMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNIL-IDLDGH---IKLTDFGLCTGFRwthnskyyqkg 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 ----------------------GENGLLLTP--------CY------TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA 634
Cdd:cd05626   164 shirqdsmepsdlwddvsncrcGDRLKTLEQratkqhqrCLahslvgTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLV 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 635 GYTPFAnGPndTPEEILLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQ--RYTAEQILKHSWITHRD 704
Cdd:cd05626   244 GQPPFL-AP--TPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFSEVD 312
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
469-697 1.09e-17

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: 85.32  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIIDKSK---RDPSEEIEI---LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILY 542
Cdd:cd05610    32 YAVKVVKKADminKNMVHQVQAerdALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYIS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 543 VISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAK-QLRGE---NGLLLTPCY----------------- 601
Cdd:cd05610   112 EVALALDYLHRHGIIHRDLKPDNMLISNEG----HIKLTDFGLSKvTLNRElnmMDILTTPSMakpkndysrtpgqvlsl 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 --------------------------------TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangpND-TPE 648
Cdd:cd05610   188 isslgfntptpyrtpksvrrgaarvegerilgTPDYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPF----NDeTPQ 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 649 EILLRIGNGKFSLSGGNwDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd05610   264 QVFQNILNRDIPWPEGE-EELSVNAQNAIEILLTMDPTKRAGLKELKQH 311
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
61-327 1.15e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 85.82  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  61 DSCHDEGVVKEIPITHHVKEGYEKADpaqFELLKVLGQGSFGKVFLVRKKtgpdagqlyamKVLKKASLKVRDRVRTKME 140
Cdd:PHA03212   68 ADEDESDADASLALCAEARAGIEKAG---FSILETFTPGAEGFAFACIDN-----------KTCEHVVIKAGQRGGTATE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 141 RDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPEN 220
Cdd:PHA03212  134 AHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAEN 212
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 221 ILLDEIGHIKLTDFGLSKESVD-QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK------ 293
Cdd:PHA03212  213 IFINHPGDVCLGDFGAACFPVDiNANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFEKdgldgd 292
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 294 -DRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 327
Cdd:PHA03212  293 cDSDRQIKLIIRRSGTHPNEFPIDAQANLDEIYIG 327
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
454-699 1.22e-17

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: 83.91  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 454 YSVCKRcihaTTNMEFAVKIIDK------SKRDPSEEIEILMRyGQ-------HPNIITLKDVFDDGRY-VYLVTDLMKG 519
Cdd:cd14011    13 YNGSKK----STKQEVSVFVFEKkqleeySKRDREQILELLKR-GVkqltrlrHPRILTVQHPLEESREsLAFATEPVFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 ------GELLDRILKQKCFSEREASDI-----LYVISKTVDYLH-CQGVVHRDLKPSNIlYMDesaSADSIRICDFGFA- 586
Cdd:cd14011    88 slanvlGERDNMPSPPPELQDYKLYDVeikygLLQISEALSFLHnDVKLVHGNICPESV-VIN---SNGEWKLAGFDFCi 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 ----------KQLRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTML-AGYTPFANGPNDTPEEILLRIG 655
Cdd:cd14011   164 sseqatdqfpYFREYDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKKNSNQL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 656 NgkfSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14011   244 R---QLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
90-290 1.34e-17

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: 83.88  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTKMERDILVevNHPFIVKL-HYAFQTEGK---- 164
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLS---TGRLYALKKILCHSKEDVKEAMREIENYRLF--NHPNILRLlDSQIVKEAGgkke 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGG---DVFTRLSKE-VLFTEEDVKFYLAELALALDHLHQLGIV---YRDLKPENILLDEIGHIKLTDFGL- 236
Cdd:cd13986    77 VYLLLPYYKRGslqDEIERRLVKgTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSm 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 237 ---------SKESVDQEKKAYSFCgTVEYMAPEVVNRRGHS---QSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd13986   157 nparieiegRREALALQDWAAEHC-TMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPF 221
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
443-701 1.42e-17

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: 83.27  E-value: 1.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEdIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-------EIEILmRYGQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06607     4 EDLRE-IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEkwqdiikEVKFL-RQLRHPNTIEYKGCYLREHTAWLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 --LMKGGELLDriLKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGEN 593
Cdd:cd06607    82 ycLGSASDIVE--VHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPG----TVKLADFGSASLVCPAN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPcYtanFVAPEVL--MQQG-YDAACDIWSLGVL----------FYTMLAGYTPFANGPNDTPeeillrigngkfS 660
Cdd:cd06607   156 SFVGTP-Y---WMAPEVIlaMDEGqYDGKVDVWSLGITcielaerkppLFNMNAMSALYHIAQNDSP------------T 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 661 LSGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd06607   220 LSSGEW---SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
96-297 1.51e-17

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: 82.83  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVR-------KK---TGPDAGQLYAMK----VLKKASlkvrdrvrtkmerdilvEVNhpfiVKLHYAFQT 161
Cdd:cd14062     1 IGSGSFGTVYKGRwhgdvavKKlnvTDPTPSQLQAFKnevaVLRKTR-----------------HVN----ILLFMGYMT 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLskEVLfteeDVKFYLAEL-------ALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd14062    60 KPQLAIVTQWCEGSSLYKHL--HVL----ETKFEMLQLidiarqtAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDF 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 235 GL----SKESVDQEKKAYSfcGTVEYMAPEVVNRRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNE 297
Cdd:cd14062   134 GLatvkTRWSGSQQFEQPT--GSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
93-292 1.56e-17

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 83.86  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLkkaSLKVRDRV--RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd07870     5 LEKLGEGSYATVY---KGISRINGQLVALKVI---SMKTEEGVpfTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRggdvfTRLSKEVL-----FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd07870    79 YMH-----TDLAQYMIqhpggLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQ 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 246 KAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQG 292
Cdd:cd07870   154 TYSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
89-329 1.66e-17

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: 83.63  E-value: 1.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKAslKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 166
Cdd:cd07846     2 KYENLGLVGEGSYGMVMKCRHK---ETGQIVAIKKFLES--EDDKMVKKIAMREIkmLKQLRHENLVNLIEVFRRKKRWY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEK 245
Cdd:cd07846    77 LVFEFV-DHTVLDDLEKyPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-TLAAPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYS-FCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMpqfLSAEAQSllrm 323
Cdd:cd07846   155 EVYTdYVATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIK-CLGN---LIPRHQE---- 226

                  ....*.
gi 1034674014 324 LFKRNP 329
Cdd:cd07846   227 LFQKNP 232
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
449-639 1.86e-17

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 83.16  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRcihAT-TNMEFAVKiidKSKRDPSEEIEI----------LMRYGQHPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14146     2 IGVGGFGKVYR---ATwKGQEVAVK---AARQDPDEDIKAtaesvrqeakLFSMLRHPNIIKLEGVCLEEPNLCLVMEFA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELlDRIL--KQKCFSEREASDI--------LYVISKTVDYLHCQGVV---HRDLKPSNILYMDESASAD----SIRI 580
Cdd:cd14146    76 RGGTL-NRALaaANAAPGPRRARRIpphilvnwAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEHDDicnkTLKI 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 581 CDFGFAKQLRGENGLLLTPCYTanFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd14146   155 TDFGLAREWHRTTKMSAAGTYA--WMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
90-310 1.91e-17

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 83.73  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAmkvLKKASLKVRDR-VRTKMERDI--LVEVNH-PFIVKLHYAFQTE--G 163
Cdd:cd07837     3 YEKLEKIGEGTYGKVYKARDKN---TGKLVA---LKKTRLEMEEEgVPSTALREVslLQMLSQsIYIVRLLDVEHVEenG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 K--LYLILDFLRGG-----DVFTRLSKEVLFTEEdVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFG 235
Cdd:cd07837    77 KplLYLVFEYLDTDlkkfiDSYGRGPHNPLPAKT-IQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQKGLLKIADLG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 236 LSKESVDQEKKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07837   156 LGRAFTIPIKSYTHEIVTLWYRAPEVLLGSTHySTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRL-LGTP 230
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
92-332 1.92e-17

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: 83.86  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVflVR------KKTGPDAGQLYAMKVLK-KASLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEGK 164
Cdd:cd05099    16 LGKPLGEGCFGQV--VRaeaygiDKSRPDQTVTVAVKMLKdNATDKDLADLISEMELMKLIG-KHKNIINLLGVCTQEGP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDV-----------------FTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG 227
Cdd:cd05099    93 LYVIVEYAAKGNLreflrarrppgpdytfdITKVPEEQL-SFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 228 HIKLTDFGLSK--ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK 304
Cdd:cd05099   172 VMKIADFGLARgvHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFKLLRE 251
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 305 A-KLGMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05099   252 GhRMDKPSNCTHELYMLMRECWHAVPTQR 280
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
92-345 2.23e-17

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: 83.52  E-value: 2.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFLVR----KKTGPDAGQLYAMKVLKK-ASLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEGKLY 166
Cdd:cd05098    17 LGKPLGEGCFGQVVLAEaiglDKDKPNRVTKVAVKMLKSdATEKDLSDLISEMEMMKMIG-KHKNIINLLGACTQDGPLY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDV--FTRLSK--------------EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIK 230
Cdd:cd05098    96 VIVEYASKGNLreYLQARRppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMK 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-K 306
Cdd:cd05098   176 IADFGLARDihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKLLKEGhR 255
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 307 LGMPQFLSAEAQSLLRMLFKRNPANR-LGSEGVEEIKRHL 345
Cdd:cd05098   256 MDKPSNCTNELYMMMRDCWHAVPSQRpTFKQLVEDLDRIV 295
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
97-332 2.37e-17

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: 82.31  E-value: 2.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  97 GQGSFGKVFlvRKKTGPDAGQLYAMKVLKkaslkvrdrvrTKMERDILVEVNHPFIVKLH--------YAFQTE----GK 164
Cdd:cd14060     2 GGGSFGSVY--RAIWVSQDKEVAVKKLLK-----------IEKEAEILSVLSHRNIIQFYgaileapnYGIVTEyasyGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYlilDFLRGGDvftrlSKEVLFTEedVKFYLAELALALDHLHQ---LGIVYRDLKPENILLDEIGHIKLTDFGLSKesV 241
Cdd:cd14060    69 LF---DYLNSNE-----SEEMDMDQ--IMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASR--F 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK--AKLGMPQFLSAEAQS 319
Cdd:cd14060   137 HSHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEknERPTIPSSCPRSFAE 216
                         250
                  ....*....|...
gi 1034674014 320 LLRMLFKRNPANR 332
Cdd:cd14060   217 LMRRCWEADVKER 229
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
443-700 2.85e-17

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: 83.98  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-----ILMRYGQHPNIITLKDVF------DDGRYVY 511
Cdd:cd07874    19 YQNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRayrelVLMKCVNHKNIISLLNVFtpqkslEEFQDVY 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGelLDRILKQKCFSEReASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQlrG 591
Cdd:cd07874    99 LVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC----TLKILDFGLART--A 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTP-CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN-DTPEEILLRIGN------GKFSLSG 663
Cdd:cd07874   170 GTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYiDQWNKVIEQLGTpcpefmKKLQPTV 249
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 664 GNW-----------------DNI-----------SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07874   250 RNYvenrpkyagltfpklfpDSLfpadsehnklkASQARDLLSKMLVIDPAKRISVDEALQHPYI 314
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
92-345 2.91e-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: 82.78  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFLVR-KKTGPDAGQ-LYAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05093     9 LKRELGEGAFGKVFLAEcYNLCPEQDKiLVAVKTLKDASDNARKDFHR--EAELLTNLQHEHIVKFYGVCVEGDPLIMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDV--FTRL-----------SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05093    87 EYMKHGDLnkFLRAhgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQF 312
Cdd:cd05093   167 SRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRvLQRPRT 246
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 313 LSAEAQSLLRMLFKRNPANRLGSEGVEEIKRHL 345
Cdd:cd05093   247 CPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNL 279
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
443-699 3.06e-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: 83.13  E-value: 3.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVK-IIDKSKRD-----PSEEIEILMRYgQHPNIITLKDVF--------DDGR 508
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDgfpitALREIKILKKL-KHPNVVPLIDMAverpdkskRKRG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 509 YVYLVTDLMK---GGELLDRILKqkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGF 585
Cdd:cd07866    89 SVYMVTPYMDhdlSGLLENPSVK---LTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQG----ILKIADFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLRGE------NGLLLTPCYTANFV-----APEVLMQ-QGYDAACDIWSLGVLFYTMLAGyTPFANGPND-------- 645
Cdd:cd07866   162 ARPYDGPppnpkgGGGGGTRKYTNLVVtrwyrPPELLLGeRRYTTAVDIWGIGCVFAEMFTR-RPILQGKSDidqlhlif 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 646 ----TPEEI-------------LLRIGNGKFSLSGGNWDNISDGAkDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07866   241 klcgTPTEEtwpgwrslpgcegVHSFTNYPRTLEERFGKLGPEGL-DLLSKLLSLDPYKRLTASDALEHPY 310
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
484-697 3.34e-17

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: 82.33  E-value: 3.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 484 EIEILMRYGQHPNIITLKD-----VFDDGRYVYLVTDLMKGGELLD----RIlkQKCFSEREASDILYVISKTVDYLH-C 553
Cdd:cd14037    50 EIEIMKRLSGHKNIVGYIDssanrSGNGVYEVLLLMEYCKGGGVIDlmnqRL--QTGLTESEILKIFCDVCEAVAAMHyL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 554 QG-VVHRDLKPSNILYMDesasADSIRICDFGFA--KQLRGENGLLL-----------TPCYTAnfvaPEV--LMQ-QGY 616
Cdd:cd14037   128 KPpLIHRDLKVENVLISD----SGNYKLCDFGSAttKILPPQTKQGVtyveedikkytTLQYRA----PEMidLYRgKPI 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 617 DAACDIWSLGVLFYTMLAGYTPFANGPNdtpeeilLRIGNGKFSLSggNWDNISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14037   200 TEKSDIWALGCLLYKLCFYTTPFEESGQ-------LAILNGNFTFP--DNSRYSKRLHKLIRYMLEEDPEKRPNIYQVSY 270

                  .
gi 1034674014 697 H 697
Cdd:cd14037   271 E 271
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
348-409 3.57e-17

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 76.25  E-value: 3.57e-17
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014  348 ANIDWDKLYKREVQPPFKPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQL--FKGFSFVA 409
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGIQQepFRGFSYVF 64
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
89-333 4.06e-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: 82.80  E-value: 4.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrkKTGPDAGQLYAMKVLKKASLKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd14041     7 RYLLLHLLGRGGFSEVY----KAFDLTEQRYVAVKIHQLNKNWRDEKKENYhkhacrEYRIHKELDHPRIVKLYDYFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLY-LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILL---DEIGHIKLTDFGL 236
Cdd:cd14041    83 TDSFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SK-------ESVDQEKKAYSFCGTVEYMAPE--VVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETM---NMI 302
Cdd:cd14041   163 SKimdddsyNSVDGMELTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIlqeNTI 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 303 LKA-KLGMP--QFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd14041   243 LKAtEVQFPpkPVVTPEAKAFIRRCLAYRKEDRI 276
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
445-639 4.10e-17

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 82.00  E-value: 4.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSYSVCKRcihATTNMEF-AVKiidKSKRDPSEEIEI----------LMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd14147     7 LEEVIGIGGFGKVYR---GSWRGELvAVK---AARQDPDEDISVtaesvrqearLFAMLAHPNIIALKAVCLEEPNLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELlDRILKQKCFSEREASDILYVISKTVDYLHCQG---VVHRDLKPSNILYMDESASAD----SIRICDFGFA 586
Cdd:cd14147    81 MEYAAGGPL-SRALAGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLQPIENDDmehkTLKITDFGLA 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 587 KQLRGENGLLLTPCYTanFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd14147   160 REWHKTTQMSAAGTYA--WMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
449-704 4.72e-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: 83.19  E-value: 4.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS--KRDPSEEIEI-------LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASAdsiRICDFGFAKQLRGENGllLTP 599
Cdd:cd05633    93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHV---RISDLGLACDFSKKKP--HAS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLMQ-QGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRIGNGKFSLSggnwDNISDGAKDLLS 678
Cdd:cd05633   167 VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEIDRMTLTVNVELP----DSFSPELKSLLE 242
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 679 HMLHMDPHQRY-----TAEQILKHSWITHRD 704
Cdd:cd05633   243 GLLQRDVSKRLgchgrGAQEVKEHSFFKGID 273
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
93-310 4.82e-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: 83.01  E-value: 4.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGkvfLVRKKTGPDAGQLYAMK-VLKKASLKVRDRvRTKMERDILVEVNHPFIVKLHYAFQTEGK-LYLILD 170
Cdd:cd07856    15 LQPVGMGAFG---LVCSARDQLTGQNVAVKkIMKPFSTPVLAK-RTYRELKLLKHLRHENIISLSDIFISPLEdIYFVTE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLrGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKKAYSF 250
Cdd:cd07856    91 LL-GTDLHRLLTSRPL-EKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI---QDPQMTGY 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 251 CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07856   166 VSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITEL-LGTP 225
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
90-283 4.88e-17

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: 81.73  E-value: 4.88e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVL----KKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKR---TSEVVAIKKMsysgKQSTEKWQDIIK---EVKFLRQLRHPNTIEYKGCYLREHTA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRG--GDVFTRLSKevLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGlskeSVDQ 243
Cdd:cd06607    77 WLVMEYCLGsaSDIVEVHKK--PLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG----SASL 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 244 EKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEM 283
Cdd:cd06607   151 VCPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIEL 193
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
175-347 5.05e-17

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: 81.24  E-value: 5.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDV--FTRLSKEVlfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDeighikltDFGLSKESVDQEKKAYSFCG 252
Cdd:cd14022    69 GDMhsFVRTCKKL--REEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFK--------DEERTRVKLESLEDAYILRG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVE----------YMAPEVVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSL 320
Cdd:cd14022   139 HDDslsdkhgcpaYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCL 218
                         170       180
                  ....*....|....*....|....*..
gi 1034674014 321 LRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd14022   219 IRSILRREPSERLTS---QEILDHPWF 242
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
94-333 5.10e-17

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: 81.69  E-value: 5.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAG---QLYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd05044     1 KFLGSGAFGEVFEGTAKDILGDGsgeTKVAVKTLRKGATD-QEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKFYLAEL-ALALD------HLHQLGIVYRDLKPENILLDEIGH----IKLTDFGLSKE 239
Cdd:cd05044    80 LMEGGDLLSYLRAARPTAFTPPLLTLKDLlSICVDvakgcvYLEDMHFVHRDLAARNCLVSSKDYrervVKIGDFGLARD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 --SVDQEKKAYSFCGTVEYMAPE-VVNRRGHSQSaDWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK-AKLGMPQFLS 314
Cdd:cd05044   160 iyKNDYYRKEGEGLLPVRWMAPEsLVDGVFTTQS-DVWAFGVLMWEILTlGQQPYPARNNLEVLHFVRAgGRLDQPDNCP 238
                         250
                  ....*....|....*....
gi 1034674014 315 AEAQSLLRMLFKRNPANRL 333
Cdd:cd05044   239 DDLYELMLRCWSTDPEERP 257
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
95-332 5.21e-17

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: 82.01  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVR-KKTGPDAGQlyAMKVLKKASLKvRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL----- 167
Cdd:cd05047     2 VIGEGNFGQVLKARiKKDGLRMDA--AIKRMKEYASK-DDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLaieya 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ----ILDFLRGGDVF-------TRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05047    79 phgnLLDFLRKSRVLetdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 314
Cdd:cd05047   159 SRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPLNCD 237
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd05047   238 DEVYDLMRQCWREKPYER 255
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
444-700 5.68e-17

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: 82.79  E-value: 5.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 444 ELKEdIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE-------EIEILMRYgQHPNIITLKDVFDDGRYVYLVTD- 515
Cdd:cd06635    29 DLRE-IGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNEkwqdiikEVKFLQRI-KHPNSIEYKGCYLREHTAWLVMEy 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 -LMKGGELLDriLKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENG 594
Cdd:cd06635   107 cLGSASDLLE--VHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPG----QVKLADFGSASIASPANS 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 595 LLLTPCYtanfVAPEVL--MQQG-YDAACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIG-NGKFSLSGGNWdniS 670
Cdd:cd06635   181 FVGTPYW----MAPEVIlaMDEGqYDGKVDVWSLGITCIELAERKPPLFNM---NAMSALYHIAqNESPTLQSNEW---S 250
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 671 DGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06635   251 DYFRNFVDSCLQKIPQDRPTSEELLKHMFV 280
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
462-700 6.57e-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: 82.34  E-value: 6.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 462 HATTNMEFAVKIID---KSKRDPS---EEIeILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDrILKQKC---F 532
Cdd:cd08216    21 HKPTNTLVAVKKINlesDSKEDLKflqQEI-LTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRD-LLKTHFpegL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 533 SEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesaSADS-IRICDFGFAKQLRGENGLLLTP-CYTANFV---- 606
Cdd:cd08216    99 PELAIAFILRDVLNALEYIHSKGYIHRSVKASHILI-----SGDGkVVLSGLRYAYSMVKHGKRQRVVhDFPKSSEknlp 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 607 --APEVLMQ--QGYDAACDIWSLGVLFYTMLAGYTPFANGP---------NDTPEEIL------LRIGNGKFSLSGGNWD 667
Cdd:cd08216   174 wlSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPFSDMPatqmllekvRGTTPQLLdcstypLEEDSMSQSEDSSTEH 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 668 NISDGAKDLLSHM-------------LHMDPHQRYTAEQILKHSWI 700
Cdd:cd08216   254 PNNRDTRDIPYQRtfseafhqfvelcLQRDPELRPSASQLLAHSFF 299
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
439-657 6.96e-17

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 81.33  E-value: 6.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElkedigvGSYSvckrcihatTNMEFAVKII---DKSK-RDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd05148    19 FGEVWE-------GLWK---------NRVRVAIKILksdDLLKqQDFQKEVQALKRL-RHKHLISLFAVCSVGEPVYIIT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEREAS--DILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKqlrge 592
Cdd:cd05148    82 ELMEKGSLLAFLRSPEGQVLPVASliDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVC----KVADFGLAR----- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 593 ngLLLTPCYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNG 657
Cdd:cd05148   153 --LIKEDVYLSSdkkipykWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPY---PGMNNHEVYDQITAG 220
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
89-338 7.20e-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: 83.15  E-value: 7.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL--- 165
Cdd:cd07876    22 RYQQLKPIGSGAQG---IVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLeef 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 ---YLILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd07876    99 qdvYLVMELM---DANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMPqflSAEAQSLLR 322
Cdd:cd07876   176 NFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIE-QLGTP---SAEFMNRLQ 250
                         250
                  ....*....|....*.
gi 1034674014 323 MLFKRNPANRLGSEGV 338
Cdd:cd07876   251 PTVRNYVENRPQYPGI 266
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
89-310 7.96e-17

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: 81.55  E-value: 7.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLkkaslkvrdRVRTKME-------RDI-----LVEVNHPFIVKLH 156
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARD---PHSGHFVALKSV---------RVQTNEDglplstvREVallkrLEAFDHPNIVRLM 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQT-----EGKLYLILDFLrGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHI 229
Cdd:cd07863    69 DVCATsrtdrETKVTLVFEHV-DQDLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 230 KLTDFGLSkesvdqekKAYSF-------CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI 302
Cdd:cd07863   148 KLADFGLA--------RIYSCqmaltpvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKI 219

                  ....*...
gi 1034674014 303 LkAKLGMP 310
Cdd:cd07863   220 F-DLIGLP 226
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
92-332 8.86e-17

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: 81.21  E-value: 8.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFlvrkktgpdAGQL----YAMKVLKKaSLKVRDRVRTKMErDILVEV------NHPFIVKL-HYAFQ 160
Cdd:cd05075     4 LGKTLGEGEFGSVM---------EGQLnqddSVLKVAVK-TMKIAICTRSEME-DFLSEAvcmkefDHPNVMRLiGVCLQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 -TEGKLY----LILDFLRGGDV-----FTRLSKEVLF--TEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGH 228
Cdd:cd05075    73 nTESEGYpspvVILPFMKHGDLhsfllYSRLGDCPVYlpTQMLVKF-MTDIASGMEYLSSKNFIHRDLAARNCMLNENMN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 IKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA 305
Cdd:cd05075   152 VCVADFGLSKKiyNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQG 231
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 306 -KLGMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05075   232 nRLKQPPDCLDGLYELMSSCWLLNPKDR 259
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
449-643 8.97e-17

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: 81.02  E-value: 8.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIdKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILK 528
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKV-RLEVFRAEELMACAGL-TSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQLIKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 529 QKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdsiRICDFGFAKQLR--GENGLLLTPCY---TA 603
Cdd:cd13991    92 QGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDA---FLCDFGHAECLDpdGLGKSLFTGDYipgTE 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 604 NFVAPEVLMQQGYDAACDIWSLGVLFYTMLAG---YTPFANGP 643
Cdd:cd13991   169 THMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGchpWTQYYSGP 211
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
82-346 9.39e-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: 81.23  E-value: 9.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  82 YEKADPAQFELLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQT 161
Cdd:cd14149     6 YWEIEASEVMLSTRIGSGSFGTVY--KGKWHGDV----AVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLskEVLfteeDVKFYLAEL-------ALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd14149    79 KDNLAIVTQWCEGSSLYKHL--HVQ----ETKFQMFQLidiarqtAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 235 GLS--KESVDQEKKAYSFCGTVEYMAPEVVNRRGH---SQSADWWSYGVLMFEMLTGTLPF-QGKDRNETMNMILKAklg 308
Cdd:cd14149   153 GLAtvKSRWSGSQQVEQPTGSILWMAPEVIRMQDNnpfSFQSDVYSYGIVLYELMTGELPYsHINNRDQIIFMVGRG--- 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 309 mpqFLSAEaqslLRMLFKRNPA--NRLGSEGVEEIK--RHLF 346
Cdd:cd14149   230 ---YASPD----LSKLYKNCPKamKRLVADCIKKVKeeRPLF 264
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
89-331 9.41e-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: 82.37  E-value: 9.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVF----LVRKKtgpdagqLYAMKVLKKaslKVRDRVRTKMERDILVEVNHP------FIVKLHYA 158
Cdd:cd14226    14 RYEIDSLIGKGSFGQVVkaydHVEQE-------WVAIKIIKN---KKAFLNQAQIEVRLLELMNKHdtenkyYIVRLKRH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTEGKLYLIL--------DFLRGGDvFTRLSKEVlfteedVKFYLAELALALDHLHQ--LGIVYRDLKPENILL--DEI 226
Cdd:cd14226    84 FMFRNHLCLVFellsynlyDLLRNTN-FRGVSLNL------TRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLcnPKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 227 GHIKLTDFGLSKESvdqEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILkAK 306
Cdd:cd14226   157 SAIKIIDFGSSCQL---GQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV-EV 232
                         250       260
                  ....*....|....*....|....*
gi 1034674014 307 LGMPQFLSAEAQSLLRMLFKRNPAN 331
Cdd:cd14226   233 LGMPPVHMLDQAPKARKFFEKLPDG 257
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
89-284 9.55e-17

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 81.00  E-value: 9.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTkmerdiLVEVNHPFIVKLHYAFQTEGK---- 164
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKAKHRI---DGKTYAIKRVKLNNEKAEREVKA------LAKLDHPNIVRYNGCWDGFDYdpet 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 ------------LYLILDFLRGGDVFTRLSK----EVLFTEEDVKFYlaELALALDHLHQLGIVYRDLKPENILLDEIGH 228
Cdd:cd14047    78 sssnssrsktkcLFIQMEFCEKGTLESWIEKrngeKLDKVLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 229 IKLTDFGLSKESVDQEKKAYSFcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14047   156 VKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
149-338 9.90e-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: 80.55  E-value: 9.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 149 HPFIVKLHYAFQTEGKLYLIL--DFlrgGDV--FTRLSKEVLFTEEDVKFYlaELALALDHLHQLGIVYRDLKPENILLD 224
Cdd:cd13976    44 HPNISGVHEVIAGETKAYVFFerDH---GDLhsYVRSRKRLREPEAARLFR--QIASAVAHCHRNGIVLRDLKLRKFVFA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 225 EIGHIKLTDFGLSKESV-DQEKKAYS-FCGTVEYMAPEVVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN 300
Cdd:cd13976   119 DEERTKLRLESLEDAVIlEGEDDSLSdKHGCPAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFA 198
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034674014 301 MILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSEGV 338
Cdd:cd13976   199 KIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDI 236
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
89-332 1.05e-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: 81.22  E-value: 1.05e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPD-AGQLYAMKVLKKASLK-VRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK-- 164
Cdd:cd14205     5 HLKFLQQLGKGNFGSVEMCRYDPLQDnTGEVVAVKKLQHSTEEhLRDFER---EIEILKSLQHDNIVKYKGVCYSAGRrn 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQ 243
Cdd:cd14205    82 LRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTK-VLPQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCGTVE----YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGT----------LPFQGKDRNETMNM-----ILK 304
Cdd:cd14205   161 DKEYYKVKEPGEspifWYAPESLTESKFSVASDVWSFGVVLYELFTYIeksksppaefMRMIGNDKQGQMIVfhlieLLK 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1034674014 305 --AKLGMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd14205   241 nnGRLPRPDGCPDEIYMIMTECWNNNVNQR 270
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
449-688 1.06e-16

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: 81.94  E-value: 1.06e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCIHATTNMeFAVKIIDKS--KRDPSE-----EIEILMRYGQHpNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd05632    10 LGKGGFgEVCACQVRATGKM-YACKRLEKKriKKRKGEsmalnEKQILEKVNSQ-FVVNLAYAYETKDALCLVLTIMNGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRI--LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRgENGLLLT 598
Cdd:cd05632    88 DLKFHIynMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYG----HIRISDLGLAVKIP-EGESIRG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF-ANGPNDTPEEILLRIGNGKFSLSGgnwdNISDGAKDLL 677
Cdd:cd05632   163 RVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFrGRKEKVKREEVDRRVLETEEVYSA----KFSEEAKSIC 238
                         250
                  ....*....|.
gi 1034674014 678 SHMLHMDPHQR 688
Cdd:cd05632   239 KMLLTKDPKQR 249
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
93-332 1.12e-16

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: 81.22  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFlvRKKTGPDAGQL---YAMKVLkkaslkvRDRVRTKMERDILVE------VNHPFIVKLhYAFQTEG 163
Cdd:cd05109    12 VKVLGSGAFGTVY--KGIWIPDGENVkipVAIKVL-------RENTSPKANKEILDEayvmagVGSPYVCRL-LGICLTS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDV--FTRLSKEVLFTEeDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSV 241
Cdd:cd05109    82 TVQLVTQLMPYGCLldYVRENKDRIGSQ-DLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLAR-LL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAE 316
Cdd:cd05109   160 DIDETEYHADGgkvPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPAREIPDLLEKGeRLPQPPICTID 239
                         250
                  ....*....|....*.
gi 1034674014 317 AQSLLRMLFKRNPANR 332
Cdd:cd05109   240 VYMIMVKCWMIDSECR 255
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
444-696 1.22e-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: 80.86  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 444 ELKEDIGVGSYSvckRCIHATTNMEFAVKIIDKSkRDPSEEIE----ILMRYGQ--HPNIITLKDVFDDGRYVYLVTDLM 517
Cdd:cd14063     3 EIKEVIGKGRFG---RVHRGRWHGDVAIKLLNID-YLNEEQLEafkeEVAAYKNtrHDNLVLFMGACMDPPHLAIVTSLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesasaDSIR--ICDFGFAK-----QL 589
Cdd:cd14063    79 KGRTLYSLIHERKEkFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-------ENGRvvITDFGLFSlsgllQP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTPCYTANFVAPEVL--MQQGYDA--------ACDIWSLGVLFYTMLAGYTPFANGPndtPEEILLRIGNGKf 659
Cdd:cd14063   152 GRREDTLVIPNGWLCYLAPEIIraLSPDLDFeeslpftkASDVYAFGTVWYELLAGRWPFKEQP---AESIIWQVGCGK- 227
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 660 slsGGNWDNISDG--AKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14063   228 ---KQSLSQLDIGreVKDILMQCWAYDPEKRPTFSDLLR 263
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
443-700 1.24e-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: 82.06  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSE---EIEILM------RYGQHpNIITLKDVFDDGRYVYLV 513
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQalvEVKILDalrrkdRDNSH-NVIHMKEYFYFRNHLCIT 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMkGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadSIRICDFGfakqlrg 591
Cdd:cd14225   124 FELL-GMNLYELIKKNnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQS--SIKVIDFG------- 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 englllTPCYTANFV----------APEVLMQQGYDAACDIWSLGVLFYTMLAGYtPFANGPN------------DTPEE 649
Cdd:cd14225   194 ------SSCYEHQRVytyiqsrfyrSPEVILGLPYSMAIDMWSLGCILAELYTGY-PLFPGENeveqlacimevlGLPPP 266
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 650 ILLRIGNGK--FSLSGGNWDNISD--------GAKDL--------------LSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14225   267 ELIENAQRRrlFFDSKGNPRCITNskgkkrrpNSKDLasalktsdplfldfIRRCLEWDPSKRMTPDEALQHEWI 341
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
86-302 1.32e-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: 80.68  E-value: 1.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 165
Cdd:cd05065     2 DVSCVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLK-SGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGG--DVFTRLsKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSK---ES 240
Cdd:cd05065    81 MIITEFMENGalDSFLRQ-NDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleDD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 241 VDQEKKAYSFCGT--VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 302
Cdd:cd05065   160 TSDPTYTSSLGGKipIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDVINAI 224
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
91-332 1.48e-16

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 80.99  E-value: 1.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  91 ELLKVLGQGSFGKV-----FLVRKKtgpDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGK 164
Cdd:cd05055    38 SFGKTLGAGAFGKVveataYGLSKS---DAVMKVAVKMLK-PTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGP 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEiGHI-KLTDFGLSKESV 241
Cdd:cd05055   114 ILVITEYCCYGDLlnFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTH-GKIvKICDFGLARDIM 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKkaYSFCGT----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLGM--PQFLS 314
Cdd:cd05055   193 NDSN--YVVKGNarlpVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMaqPEHAP 270
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd05055   271 AEIYDIMKTCWDADPLKR 288
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
94-349 1.60e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 81.73  E-value: 1.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLK---VRDRVRTKM---------ERDILVEVNHPFIVKLHYAFQT 161
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTL---TGKIVAIKKVKIIEISndvTKDRQLVGMcgihfttlrELKIMNEIKHENIMGLVDVYVE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL----- 236
Cdd:PTZ00024   92 GDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLarryg 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 --------SKESVDQEKKAY-SFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAk 306
Cdd:PTZ00024  171 yppysdtlSKDETMQRREEMtSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFEL- 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 307 LGMP-----------------------------QFLSAEAQSLLRMLFKRNPANRLGSEgvEEIKRHLFFAN 349
Cdd:PTZ00024  250 LGTPnednwpqakklplyteftprkpkdlktifPNASDDAIDLLQSLLKLNPLERISAK--EALKHEYFKSD 319
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
475-695 1.61e-16

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 82.99  E-value: 1.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 475 DKSKRDPSEEIEILMrygqhpniitlkdvfddgryVYLVTDLMKGGELLDRILKQ----KCFSEREASDILYVISKTVDY 550
Cdd:PTZ00283   99 DFAKKDPRNPENVLM--------------------IALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHH 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 551 LHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQ----LRGENGLllTPCYTANFVAPEVLMQQGYDAACDIWSLG 626
Cdd:PTZ00283  159 VHSKHMIHRDIKSANILL----CSNGLVKLGDFGFSKMyaatVSDDVGR--TFCGTPYYVAPEIWRRKPYSKKADMFSLG 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 627 VLFYTMLAGYTPFaNGPNdtPEEILLRIGNGKFS-LSggnwDNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:PTZ00283  233 VLLYELLTLKRPF-DGEN--MEEVMHKTLAGRYDpLP----PSISPEMQEIVTALLSSDPKRRPSSSKLL 295
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
443-700 1.80e-16

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: 80.09  E-value: 1.80e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII-------DKSKRDPSEEIEI-LMRYGQHPNIITLKDVFDDG--RYVYL 512
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfdpespETSKEVNALECEIqLLKNLLHERIVQYYGCLRDPqeRTLSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdeSASADSIRICDFGFAKQLR-- 590
Cdd:cd06652    84 FMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL----RDSVGNVKLGDFGASKRLQti 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 -----GENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpndtpeEILLRIGNGKFSLSGGN 665
Cdd:cd06652   160 clsgtGMKSVTGTPYW----MSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA--------EFEAMAAIFKIATQPTN 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 666 WD---NISDGAKDLLSHMLhMDPHQRYTAEQILKHSWI 700
Cdd:cd06652   228 PQlpaHVSDHCRDFLKRIF-VEAKLRPSADELLRHTFV 264
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
135-334 1.81e-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: 79.71  E-value: 1.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 135 VRTKMERdiLVEVNHPFIVKLhYAFQTE-------GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLH 207
Cdd:cd14012    45 LEKELES--LKKLRHPNLVSY-LAFSIErrgrsdgWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 208 QLGIVYRDLKPENILLDEIGH---IKLTDFGLSKESVD---QEKKAYSFcgTVEYMAPEVVNRRGHSQSA-DWWSYGVLM 280
Cdd:cd14012   122 RNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDmcsRGSLDEFK--QTYWLPPELAQGSKSPTRKtDVWDLGLLF 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 281 FEMLTGTLPFQgkdRNETMNMILkaklgMPQFLSAEAQSLLRMLFKRNPANRLG 334
Cdd:cd14012   200 LQMLFGLDVLE---KYTSPNPVL-----VSLDLSASLQDFLSKCLSLDPKKRPT 245
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
470-651 1.88e-16

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 79.80  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIDK---SKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKcfsEREASDILYV--- 543
Cdd:cd05059    32 AIKMIKEgsmSEDDFIEEAKVMMKL-SHPKLVQLYGVCTKQRPIFIVTEYMANGCLLNYLRERR---GKFQTEQLLEmck 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 -ISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKqlrgengLLLTPCYTANF--------VAPEVLMQQ 614
Cdd:cd05059   108 dVCEAMEYLESNGFIHRDLAARNCLVGEQN----VVKVSDFGLAR-------YVLDDEYTSSVgtkfpvkwSPPEVFMYS 176
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034674014 615 GYDAACDIWSLGVLFYTMLA-GYTPFANGPN-DTPEEIL 651
Cdd:cd05059   177 KFSSKSDVWSFGVLMWEVFSeGKMPYERFSNsEVVEHIS 215
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
471-696 1.96e-16

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 80.38  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 471 VKIIdkSKRDPSEEI--------EILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGgELLDRILKQKCFSEREASDILY 542
Cdd:cd13980    28 VKVF--VKPDPALPLrsykqrleEIRDRLLELPNVLPFQKVIETDKAAYLIRQYVKY-NLYDRISTRPFLNLIEKKWIAF 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 543 VISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQ--LRGENGLLLT---------PCYTA--NFVAPE 609
Cdd:cd13980   105 QLLHALNQCHKRGVCHGDIKTENVLV----TSWNWVYLTDFASFKPtyLPEDNPADFSyffdtsrrrTCYIApeRFVDAL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 610 VLMQQGYD------AACDIWSLG-VLFYTMLAGYTPFangpnDTPEeiLLRIGNGKFSLSgGNWDNISD-GAKDLLSHML 681
Cdd:cd13980   181 TLDAESERrdgeltPAMDIFSLGcVIAELFTEGRPLF-----DLSQ--LLAYRKGEFSPE-QVLEKIEDpNIRELILHMI 252
                         250
                  ....*....|....*
gi 1034674014 682 HMDPHQRYTAEQILK 696
Cdd:cd13980   253 QRDPSKRLSAEDYLK 267
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
117-347 2.00e-16

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


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 79.32  E-value: 2.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 117 QLYAMKVLKKASLKVRDRVRTKMERDI--LVEVnhpfivklhyaFQTEGKLYLIL--DFlrgGDVFTRLSKEVLFTEEDV 192
Cdd:cd14023    21 LQCKVFPLKHYQDKIRPYIQLPSHRNItgIVEV-----------ILGDTKAYVFFekDF---GDMHSYVRSCKRLREEEA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 193 KFYLAELALALDHLHQLGIVYRDLKPENILL--DEIGHIKLT---DFGLSKESVDQEKKAYsfcGTVEYMAPEVVNRRG- 266
Cdd:cd14023    87 ARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsdEERTQLRLEsleDTHIMKGEDDALSDKH---GCPAYVSPEILNTTGt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 267 -HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEIKRHL 345
Cdd:cd14023   164 ySGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTA---PEILLHP 240

                  ..
gi 1034674014 346 FF 347
Cdd:cd14023   241 WF 242
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
88-341 2.20e-16

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: 80.07  E-value: 2.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLV--RKKTGpdagqlYAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGKL 165
Cdd:cd05073    11 ESLKLEKKLGAGQFGEVWMAtyNKHTK------VAVKTMKPGSMSVEAFLA---EANVMKTLQHDKLVKLH-AVVTKEPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGDVFTRLSKEVLFTEEDVKF--YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd05073    81 YIITEFMAKGSLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMiLKAKLGMPQFLSAEAQSLL 321
Cdd:cd05073   161 EYTAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRA-LERGYRMPRPENCPEELYN 239
                         250       260
                  ....*....|....*....|..
gi 1034674014 322 RML--FKRNPANRLGSEGVEEI 341
Cdd:cd05073   240 IMMrcWKNRPEERPTFEYIQSV 261
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
96-332 2.46e-16

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 79.97  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVR-KKTGPDAGQLYAMKVLKKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG--KLYLILDFL 172
Cdd:cd05079    12 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKLIMEFL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLSKEV--LFTEEDVKfYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYS- 249
Cdd:cd05079    91 PSGSLKEYLPRNKnkINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEYYTv 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 250 ---FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT--------GTL------PFQGKDRNETMNMILK--AKLGMP 310
Cdd:cd05079   169 kddLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspMTLflkmigPTHGQMTVTRLVRVLEegKRLPRP 248
                         250       260
                  ....*....|....*....|..
gi 1034674014 311 QFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05079   249 PNCPEEVYQLMRKCWEFQPSKR 270
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
175-338 2.92e-16

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 79.15  E-value: 2.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV--DQEKKAYSFCG 252
Cdd:cd14024    69 GDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPlnGDDDSLTDKHG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 TVEYMAPEVVN-RRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 330
Cdd:cd14024   149 CPAYVGPEILSsRRSYSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPA 228

                  ....*...
gi 1034674014 331 NRLGSEGV 338
Cdd:cd14024   229 ERLKASEI 236
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
85-351 3.28e-16

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: 80.45  E-value: 3.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  85 ADP------AQFELLKVLGQGSFGKVFLVR----KKTGPDAGQLYAMKVLKK-ASLKVRDRVRTKMERDILVEvNHPFIV 153
Cdd:cd05100     3 ADPkwelsrTRLTLGKPLGEGCFGQVVMAEaigiDKDKPNKPVTVAVKMLKDdATDKDLSDLVSEMEMMKMIG-KHKNII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 154 KLHYAFQTEGKLYLILDFLRGGDV-----------------FTRLSKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDL 216
Cdd:cd05100    82 NLLGACTQDGPLYVLVEYASKGNLreylrarrppgmdysfdTCKLPEEQL-TFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 217 KPENILLDEIGHIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGK 293
Cdd:cd05100   161 AARNVLVTEDNVMKIADFGLARDvhNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 294 DRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRNPANR-LGSEGVEEIKRHLFFANID 351
Cdd:cd05100   241 PVEELFKLLKEGhRMDKPANCTHELYMIMRECWHAVPSQRpTFKQLVEDLDRVLTVTSTD 300
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
443-590 3.33e-16

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: 79.42  E-value: 3.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPS--EEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMkgG 520
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQleYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLL--G 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQ--KCFSEreasdilyvisKTV-----------DYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAK 587
Cdd:cd14016    80 PSLEDLFNKcgRKFSL-----------KTVlmladqmisrlEYLHSKGYIHRDIKPENFL-MGLGKNSNKVYLIDFGLAK 147

                  ...
gi 1034674014 588 QLR 590
Cdd:cd14016   148 KYR 150
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
96-284 3.44e-16

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: 79.23  E-value: 3.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLKkaslkvrdRVRTKMERDILVEV------NHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14221     1 LGKGCFGQAI---KVTHRETGEVMVMKELI--------RFDEETQRTFLKEVkvmrclEHPNVLKFIGVLYKDKRLNFIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGG---DVFTRLSKEVLFTEEdVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-- 244
Cdd:cd14221    70 EYIKGGtlrGIIKSMDSHYPWSQR-VSF-AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKtq 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 245 ------------KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14221   148 peglrslkkpdrKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
449-700 3.98e-16

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: 79.30  E-value: 3.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSEEI-----EI-LMRYGQHPNIITLKDVFDD--GRYVYLVTDLMK 518
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVnalecEIqLLKNLRHDRIVQYYGCLRDpeEKKLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdeSASADSIRICDFGFAKQLR-------G 591
Cdd:cd06653    90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGASKRIQticmsgtG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpndtpEEILLRIgngkFSLSGGNW----- 666
Cdd:cd06653   166 IKSVTGTPYW----MSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAE------YEAMAAI----FKIATQPTkpqlp 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 667 DNISDGAKDLLSHMLhMDPHQRYTAEQILKHSWI 700
Cdd:cd06653   232 DGVSDACRDFLRQIF-VEEKRRPTAEFLLRHPFV 264
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
87-290 4.01e-16

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: 78.93  E-value: 4.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVFLvrkktGPDAGQLYAMKVLKkaslkvrDRVRTK----MERDILVEVNHPFIVKLHYAFQTE 162
Cdd:cd05039     5 KKDLKLGELIGKGEFGDVML-----GDYRGQKVAVKCLK-------DDSTAAqaflAEASVMTTLRHPNLVQLLGVVLEG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 240
Cdd:cd05039    73 NGLYIVTEYMAKGSLvdYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 241 vDQEKKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPF 290
Cdd:cd05039   153 -SSNQDGGKL--PIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
446-639 4.79e-16

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 79.33  E-value: 4.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 446 KEDIGVGSYSVCKRCIHATTNMEFAVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKD-VFDDGRyVYLVTDLMKG 519
Cdd:cd06616    11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRIrstvdEKEQKRLLMDLDVVMRSSDCPYIVKFYGaLFREGD-CWICMELMDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GelLDRILK------QKCFSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLrgE 592
Cdd:cd06616    90 S--LDKFYKyvyevlDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNIL-LDRNG---NIKLCDFGISGQL--V 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 593 NGLLLT------PcytanFVAPEVL----MQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd06616   162 DSIAKTrdagcrP-----YMAPERIdpsaSRDGYDVRSDVWSLGITLYEVATGKFPY 213
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
443-694 4.98e-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: 79.91  E-value: 4.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKiidKSKRDPSEEIEILMR--------YGQHPNIITLKD------------ 502
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPENVELALRefwalssiQRQHPNVIQLEEcvlqrdglaqrm 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 503 ----------------------VFD--DGRYVYLVTDLMKGGELLDRILKQKCfSEREASDILYVISKTVDYLHCQGVVH 558
Cdd:cd13977    79 shgssksdlylllvetslkgerCFDprSACYLWFVMEFCDGGDMNEYLLSRRP-DRQTNTSFMLQLSSALAFLHRNQIVH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 559 RDLKPSNILyMDESASADSIRICDFGFAKQLRG-----------ENGLLLTPCYTANFVAPEVlMQQGYDAACDIWSLGV 627
Cdd:cd13977   158 RDLKPDNIL-ISHKRGEPILKVADFGLSKVCSGsglnpeepanvNKHFLSSACGSDFYMAPEV-WEGHYTAKADIFALGI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 628 LFYTMLAGYTpFANGpnDTPEEI-----------------LLRIGNGKFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYT 690
Cdd:cd13977   236 IIWAMVERIT-FRDG--ETKKELlgtyiqqgkeivplgeaLLENPKLELQIPLKKKKSMNDDMKQLLRDMLAANPQERPD 312

                  ....
gi 1034674014 691 AEQI 694
Cdd:cd13977   313 AFQL 316
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
89-284 5.13e-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: 79.09  E-value: 5.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL- 167
Cdd:cd14049     7 EFEEIARLGKGGYGKVYKVRNKLD---GQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLy 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ---------ILDFLRGGDVFTRLS--KEVLFTEEDVKF---YLAELALALDHLHQLGIVYRDLKPENILLDEIG-HIKLT 232
Cdd:cd14049    84 iqmqlcelsLWDWIVERNKRPCEEefKSAPYTPVDVDVttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 233 DFGLS-----KESVDQEKKAY-------SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14049   164 DFGLAcpdilQDGNDSTTMSRlnglthtSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
474-698 5.25e-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: 78.56  E-value: 5.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 474 IDKSKRDPSE---EIEILMRYgQHPNIITL------KDVFDDGRYVYLVTDLMKGG---ELLDRILKQKCFSERE-ASDI 540
Cdd:cd14012    35 TSNGKKQIQLlekELESLKKL-RHPNLVSYlafsieRRGRSDGWKVYLLTEYAPGGslsELLDSVGSVPLDTARRwTLQL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 541 LyvisKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDFGFAKQLRGENGLL-LTPCYTANFVAPEV-LMQQGYDA 618
Cdd:cd14012   114 L----EALEYLHRNGVVHKSLHAGNVL-LDRDAGTGIVKLTDYSLGKTLLDMCSRGsLDEFKQTYWLPPELaQGSKSPTR 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 619 ACDIWSLGVLFYTMLAGYTPF--ANGPNDTPEEILLrigngkfslsggnwdniSDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14012   189 KTDVWDLGLLFLQMLFGLDVLekYTSPNPVLVSLDL-----------------SASLQDFLSKCLSLDPKKRPTALELLP 251

                  ..
gi 1034674014 697 HS 698
Cdd:cd14012   252 HE 253
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
88-296 5.27e-16

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 81.66  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFL--VRKKTGPDA---GQLYAMKVLKKASLKVRDRVR------TKMERDILV--EVNHPFIVK 154
Cdd:PHA03210  148 AHFRVIDDLPAGAFGKIFIcaLRASTEEAEarrGVNSTNQGKPKCERLIAKRVKagsraaIQLENEILAlgRLNHENILK 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 155 LHYAFQTEGKLYLI---LDFlrggDVFTRLSKEVLFTEE-----DVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI 226
Cdd:PHA03210  228 IEEILRSEANTYMItqkYDF----DLYSFMYDEAFDWKDrpllkQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCD 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 227 GHIKLTDFG----LSKESVDQEkkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTL-PFQGKDRN 296
Cdd:PHA03210  304 GKIVLGDFGtampFEKEREAFD---YGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDFcPIGDGGGK 375
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
448-699 5.92e-16

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: 78.51  E-value: 5.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHATTNMEFA-----VKIIDKSKRDP-SEEIEILmRYGQHPNII----TLKDVFDDGRYVYLVTDLM 517
Cdd:cd14033     8 EIGRGSFKTVYRGLDTETTVEVAwcelqTRKLSKGERQRfSEEVEML-KGLQHPNIVrfydSWKSTVRGHKCIILVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGEL---LDRILKQKC-FSEREASDILyvisKTVDYLH--CQGVVHRDLKPSNILYMDESASadsIRICDFGFA--KQL 589
Cdd:cd14033    87 TSGTLktyLKRFREMKLkLLQRWSRQIL----KGLHFLHsrCPPILHRDLKCDNIFITGPTGS---VKIGDLGLAtlKRA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENGLLLTPcytaNFVAPEvLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGkfsLSGGNWDNI 669
Cdd:cd14033   160 SFAKSVIGTP----EFMAPE-MYEEKYDEAVDVYAFGMCILEMATSEYPYSECQN--AAQIYRKVTSG---IKPDSFYKV 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 670 S-DGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14033   230 KvPELKEIIEGCIRTDKDERFTIQDLLEHRF 260
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
89-290 6.13e-16

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 78.48  E-value: 6.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLvrkktGPDAGQLYAMKVLKK----ASLKVRDRVRTKMERDILVEVnhpfivkLHYAFQTEGK 164
Cdd:cd05082     7 ELKLLQTIGKGEFGDVML-----GDYRGNKVAVKCIKNdataQAFLAEASVMTQLRHSNLVQL-------LGVIVEEKGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGG---DVFTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 241
Cdd:cd05082    75 LYIVTEYMAKGslvDYLRSRGRSVLGGDCLLKFSL-DVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEAS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSfcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPF 290
Cdd:cd05082   154 STQDTGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
447-658 7.52e-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: 78.52  E-value: 7.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRC----IHATTNMEFAVKIIDKSK----RDPSEEIEILmRYGQHPNIITLKDV-FDDGRY-VYLVTDL 516
Cdd:cd14205    10 QQLGKGNFGSVEMCrydpLQDNTGEVVAVKKLQHSTeehlRDFEREIEIL-KSLQHDNIVKYKGVcYSAGRRnLRLIMEY 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKcfsER--EASDILYV--ISKTVDYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQL--R 590
Cdd:cd14205    89 LPYGSLRDYLQKHK---ERidHIKLLQYTsqICKGMEYLGTKRYIHRDLATRNILVENE----NRVKIGDFGLTKVLpqD 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 591 GENGLLLTPCYTANF-VAPEVLMQQGYDAACDIWSLGVLFYTMLAgYTPFANGPndtPEEILLRIGNGK 658
Cdd:cd14205   162 KEYYKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYELFT-YIEKSKSP---PAEFMRMIGNDK 226
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
449-688 8.03e-16

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: 79.32  E-value: 8.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKS--KRDPSEEIEI-------LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKG 519
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 520 GELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLRGENGllLTP 599
Cdd:cd14223    88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANIL-LDEFG---HVRISDLGLACDFSKKKP--HAS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 600 CYTANFVAPEVLmQQG--YDAACDIWSLGVLFYTMLAGYTPFANGPNDTPEEillrIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd14223   162 VGTHGYMAPEVL-QKGvaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHE----IDRMTLTMAVELPDSFSPELRSLL 236
                         250
                  ....*....|.
gi 1034674014 678 SHMLHMDPHQR 688
Cdd:cd14223   237 EGLLQRDVNRR 247
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
86-306 8.03e-16

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: 78.65  E-value: 8.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVLGQGSFGKVF--LVRKKTGPDAgQLYAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIV---------- 153
Cdd:cd05043     4 SRERVTLSDLLQEGTFGRIFhgILRDEKGKEE-EVLVKTVKDHASEIQVTMLLQ--ESSLLYGLSHQNLLpilhvciedg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 154 ---KLHYAFQTEGKLYLildFLRGGDVFTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIK 230
Cdd:cd05043    81 ekpMVLYPYMNWGNLKL---FLQQCRLSEANNPQALSTQQLVHMAL-QIACGMSYLHRRGVIHKDIAARNCVIDDELQVK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFGLSKESV--------DQEKKAysfcgtVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNM 301
Cdd:cd05043   157 ITDNALSRDLFpmdyhclgDNENRP------IKWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDPFEMAAY 230

                  ....*
gi 1034674014 302 ILKAK 306
Cdd:cd05043   231 LKDGY 235
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
443-700 8.08e-16

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: 79.70  E-value: 8.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE-----ILMRYGQHPNIITLKDVF------DDGRYVY 511
Cdd:cd07875    26 YQNLKPIGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRayrelVLMKCVNHKNIIGLLNVFtpqkslEEFQDVY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGelLDRILKQKCFSEReASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQlrG 591
Cdd:cd07875   106 IVMELMDAN--LCQVIQMELDHER-MSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC----TLKILDFGLART--A 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTP-CYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN-DTPEEILLRIGN------------- 656
Cdd:cd07875   177 GTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDHiDQWNKVIEQLGTpcpefmkklqptv 256
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 657 -----GKFSLSGGNWDNI----------------SDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07875   257 rtyveNRPKYAGYSFEKLfpdvlfpadsehnklkASQARDLLSKMLVIDASKRISVDEALQHPYI 321
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
89-337 9.39e-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: 79.36  E-value: 9.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLV-RKKTGpdagQLYAMKVL--KK-------ASLKVRDRVRTKmERDILVEVNHpfiVKLHYA 158
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKAlDHKTN----EHVAIKIIrnKKrfhhqalVEVKILDALRRK-DRDNSHNVIH---MKEYFY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTegklYLILDF-LRGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH--IKLTD 233
Cdd:cd14225   116 FRN----HLCITFeLLGMNLYELIKKNNFqgFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVID 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGlskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQFL 313
Cdd:cd14225   192 FG---SSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEV-LGLPPPE 267
                         250       260
                  ....*....|....*....|....*.
gi 1034674014 314 SAEAQSLLRMLF--KRNPANRLGSEG 337
Cdd:cd14225   268 LIENAQRRRLFFdsKGNPRCITNSKG 293
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
441-699 9.48e-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: 78.51  E-value: 9.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYLVTdl 516
Cdd:cd07873     2 ETYIKLDKLGEGTYATVYKGRSKLTDNLVALKEIrlEHEEGAPCTAIrEVsLLKDLKHANIVTLHDIIHTEKSLTLVF-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 mkggELLDRILKQ---KCFSEREASDI---LYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLR 590
Cdd:cd07873    80 ----EYLDKDLKQyldDCGNSINMHNVklfLFQLLRGLAYCHRRKVLHRDLKPQNLLINERG----ELKLADFGLARAKS 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIgngkFSLSGG----N 665
Cdd:cd07873   152 IPTKTYSNEVVTLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLF---PGSTVEEQLHFI----FRILGTpteeT 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 666 WDNI---------------------------SDGAkDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07873   225 WPGIlsneefksynypkyradalhnhaprldSDGA-DLLSKLLQFEGRKRISAEEAMKHPY 284
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
440-700 9.48e-16

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: 79.16  E-value: 9.48e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEV----YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdKSKRDPSE----EIEILMR-------YGQHPNIITLKDVF 504
Cdd:cd14136     5 GEVyngrYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVV-KSAQHYTEaaldEIKLLKCvreadpkDPGREHVVQLLDDF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 505 D----DGRYVYLVTDLMkGGELLDRILKqkcfSEREASDILYV--ISKTV----DYLH--CqGVVHRDLKPSNILYmdes 572
Cdd:cd14136    84 KhtgpNGTHVCMVFEVL-GPNLLKLIKR----YNYRGIPLPLVkkIARQVlqglDYLHtkC-GIIHTDIKPENVLL---- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 573 aSADSIR--ICDFGFAkqlrgengllltpCYTAN----------FVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFA 640
Cdd:cd14136   154 -CISKIEvkIADLGNA-------------CWTDKhftediqtrqYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFD 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 641 --NGPNDTPE--------EILLRI-----GNGKFSL----SGGNWDNIS-------------------DGAK---DLLSH 679
Cdd:cd14136   220 phSGEDYSRDedhlaliiELLGRIprsiiLSGKYSReffnRKGELRHISklkpwpledvlvekykwskEEAKefaSFLLP 299
                         330       340
                  ....*....|....*....|.
gi 1034674014 680 MLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14136   300 MLEYDPEKRATAAQCLQHPWL 320
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
448-656 9.61e-16

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: 78.19  E-value: 9.61e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHA----TTNMEFAVKII-----DKSKRDPSEEIEIlMRYGQHPNIITLKDVFDD--GRYVYLVTDL 516
Cdd:cd05038    11 QLGEGHFGSVELCRYDplgdNTGEQVAVKSLqpsgeEQHMSDFKREIEI-LRTLDHEYIVKYKGVCESpgRRSLRLIMEY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQK---------CFSEReasdilyvISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAK 587
Cdd:cd05038    90 LPSGSLRDYLQRHRdqidlkrllLFASQ--------ICKGMEYLGSQRYIHRDLAARNILV----ESEDLVKISDFGLAK 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 588 QLRGENGLlltpcYTAN--------FVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpndTPEEILLRIGN 656
Cdd:cd05038   158 VLPEDKEY-----YYVKepgespifWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQS----PPALFLRMIGI 225
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
96-290 1.02e-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: 77.94  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVR-KKTGpdagqlyamkvLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQtEGKLYLILDFLRG 174
Cdd:cd13991    14 IGRGSFGEVHRMEdKQTG-----------FQCAVKKVRLEVFRAEELMACAGLTSPRVVPLYGAVR-EGPWVNIFMDLKE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSKEVLFTEEDVK-FYLAELALALDHLHQLGIVYRDLKPENILLDEIG-HIKLTDFGLSkESVD---QEKKAYS 249
Cdd:cd13991    82 GGSLGQLIKEQGCLPEDRAlHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHA-ECLDpdgLGKSLFT 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 250 ---FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd13991   161 gdyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
88-307 1.11e-15

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: 78.18  E-value: 1.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYL 167
Cdd:cd14151     8 GQITVGQRIGSGSFGTVY--KGKWHGDV----AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS--KESVDQE 244
Cdd:cd14151    81 VTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGS 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 245 KKAYSFCGTVEYMAPEVV---NRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAKL 307
Cdd:cd14151   161 HQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYL 227
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
96-324 1.13e-15

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: 77.92  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGPDAgqlYAMKVlkKASLKVRDRVRtkmeRDILVEVNHPFIVKLHYAFQTEG----KLYLILDF 171
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKTW---LAIKC--PPSLHVDDSER----MELLEEAKKMEMAKFRHILPVYGicsePVGLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTeeDVKFYLA-ELALALDHLHQLG--IVYRDLKPENILLDEIGHIKLTDFGLSK---ESVDQEK 245
Cdd:cd14025    75 METGSLEKLLASEPLPW--ELRFRIIhETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKdrNETMNMILKAKLGMPQFLSA-------E 316
Cdd:cd14025   153 SRDGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAGE--NNILHIMVKVVKGHRPSLSPiprqrpsE 230

                  ....*...
gi 1034674014 317 AQSLLRML 324
Cdd:cd14025   231 CQQMICLM 238
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
443-699 1.15e-15

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: 78.24  E-value: 1.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII---DKSKRDPSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYLVTdlm 517
Cdd:cd07839     2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVrldDDDEGVPSSALrEIcLLKELKHKNIVRLYDVLHSDKKLTLVF--- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 kggELLDRILKQ---KCFSEREASDI---LYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLrg 591
Cdd:cd07839    79 ---EYCDQDLKKyfdSCNGDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNG----ELKLADFGLARAF-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 enGLLLTpCYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFANGpNDTpEEILLRIgngkFSLSG-- 663
Cdd:cd07839   150 --GIPVR-CYSAEVVtlwyrPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFPG-NDV-DDQLKRI----FRLLGtp 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 664 -----------------------GNWDNI----SDGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07839   221 teeswpgvsklpdykpypmypatTSLVNVvpklNSTGRDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
492-700 1.16e-15

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: 77.58  E-value: 1.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 492 GQHPNIITLKDVFDDGRYVYLVTDL-MKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmd 570
Cdd:cd14101    64 PGHRGVIRLLDWFEIPEGFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILV-- 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 571 eSASADSIRICDFGFAKQLRGE-----NGllltpcyTANFVAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpn 644
Cdd:cd14101   142 -DLRTGDIKLIDFGSGATLKDSmytdfDG-------TRVYSPPEWILYHQYHAlPATVWSLGILLYDMVCGDIPF----- 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 645 DTPEEILlrigNGKFSLSGgnwdNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14101   209 ERDTDIL----KAKPSFNK----RVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
436-657 1.54e-15

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: 77.45  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYElkedigvGSYSVckrcihaTTnmEFAVKIIDKSKRDPSE---EIEIlMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd05068    18 SGQFGEVWE-------GLWNN-------TT--PVAVKTLKPGTMDPEDflrEAQI-MKKLRHPKLIQLYAVCTLEEPIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLDrilkqkcFSEREASDILyvISKTVD----------YLHCQGVVHRDLKPSNILYMDesasADSIRICD 582
Cdd:cd05068    81 ITELMKHGSLLE-------YLQGKGRSLQ--LPQLIDmaaqvasgmaYLESQNYIHRDLAARNVLVGE----NNICKVAD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 583 FGFAKQLRGENgllltpCYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLR 653
Cdd:cd05068   148 FGLARVIKVED------EYEAregakfpiKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPY---PGMTNAEVLQQ 218

                  ....
gi 1034674014 654 IGNG 657
Cdd:cd05068   219 VERG 222
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
443-640 1.58e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 79.69  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIeILMRYGQHPNIITLKDvfddgryvYLVTDLMKGGE- 521
Cdd:PTZ00036   68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNREL-LIMKNLNHINIIFLKD--------YYYTECFKKNEk 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 --LLDRILK---------QKCFSEREASDIL-------YVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDF 583
Cdd:PTZ00036  139 niFLNVVMEfipqtvhkyMKHYARNNHALPLflvklysYQLCRALAYIHSKFICHRDLKPQNLLI---DPNTHTLKLCDF 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 584 GFAKQLRGENGLLLTPCyTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFA 640
Cdd:PTZ00036  216 GSAKNLLAGQRSVSYIC-SRFYRAPELMLgATNYTTHIDLWSLGCIIAEMILGYPIFS 272
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
90-291 1.74e-15

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 77.63  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLKkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK--LY 166
Cdd:cd05080     6 LKKIRDLGEGHFGKVSLYCyDPTNDGTGEMVAVKALK-ADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGksLQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRLSKEVLFTEEdVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKK 246
Cdd:cd05080    85 LIMEYVPLGSLRDYLPKHSIGLAQ-LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAK-AVPEGHE 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 247 AYSFC----GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ 291
Cdd:cd05080   163 YYRVRedgdSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQ 211
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
96-284 1.89e-15

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: 77.16  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASlkvrdrvrTKMERDILVEV------NHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd14154     1 LGKGFFGQAIKVTHRE---TGEVMVMKELIRFD--------EEAQRNFLKEVkvmrslDHPNVLKFIGVLYKDKKLNLIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDV--FTRLSKEVLFTEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD----- 242
Cdd:cd14154    70 EYIPGGTLkdVLKDMARPLPWAQRVRF-AKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEerlps 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 243 ---------------QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14154   149 gnmspsetlrhlkspDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
82-283 1.93e-15

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: 78.16  E-value: 1.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  82 YEKADPAQ-FELLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVL----KKASLKVRDRVRtkmERDILVEVNHPFIVKLH 156
Cdd:cd06633    14 FYKDDPEEiFVDLHEIGHGSFGAVYFATNSH---TNEVVAIKKMsysgKQTNEKWQDIIK---EVKFLQQLKHPNTIEYK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 157 YAFQTEGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALAldHLHQLGIVYRDLKPENILLDEIGHIKLTDF 234
Cdd:cd06633    88 GCYLKDHTAWLVMEYCLGSasDLLEVHKKPLQEVEIAAITHGALQGLA--YLHSHNMIHRDIKAGNILLTEPGQVKLADF 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 235 GlskeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEM 283
Cdd:cd06633   166 G----SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDIWSLGITCIEL 213
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
441-702 1.98e-15

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: 77.39  E-value: 1.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdksKRDPSEEIE------ILMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd06645    11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVI---KLEPGEDFAvvqqeiIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQKCFSEreaSDILYVISKTVD---YLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG 591
Cdd:cd06645    88 EFCGGGSLQDIYHVTGPLSE---SQIAYVSRETLQglyYLHSKGKMHRDIKGANILLTDNG----HVKLADFGVSAQITA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQ---GYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFS----LSGG 664
Cdd:cd06645   161 TIAKRKSFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPMF---DLHPMRALFLMTKSNFQppklKDKM 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 665 NWDNisdGAKDLLSHMLHMDPHQRYTAEQILKHSWITH 702
Cdd:cd06645   238 KWSN---SFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
469-645 2.00e-15

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 77.31  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 469 FAVKIID-----KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKcfSEREAS----- 538
Cdd:cd14066    20 VAVKRLNemncaASKKEFLTELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEYMPNGSLEDRLHCHK--GSPPLPwpqrl 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 DILYVISKTVDYLHCQG---VVHRDLKPSNILyMDESASAdsiRICDFGFAK--QLRGENGLLLTPCYTANFVAPEVLMQ 613
Cdd:cd14066    97 KIAKGIARGLEYLHEECpppIIHGDIKSSNIL-LDEDFEP---KLTDFGLARliPPSESVSKTSAVKGTIGYLAPEYIRT 172
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1034674014 614 QGYDAACDIWSLGVLFYTMLAGYTPFANGPND 645
Cdd:cd14066   173 GRVSTKSDVYSFGVVLLELLTGKPAVDENREN 204
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
449-634 2.03e-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: 76.76  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGG---ELLD 524
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSFLKEVkLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGtleELLK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RILKQKCFSERE--ASDIlyviSKTVDYLHCQGVVHRDLKPSNILYMDESASADSIrICDFGFAKQL------RGENGLL 596
Cdd:cd14065    81 SMDEQLPWSQRVslAKDI----ASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAV-VADFGLAREMpdektkKPDRKKR 155
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034674014 597 LTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA 634
Cdd:cd14065   156 LTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIG 193
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
96-284 2.44e-15

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: 76.91  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14222     1 LGKGFFGQAIKVTHKA---TGKVMVMKELIRCDEETQKTFLT--EVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE----------- 244
Cdd:cd14222    76 TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKkkpppdkpttk 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 245 ---------KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14222   156 krtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
89-357 2.58e-15

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 76.53  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKaslkVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 167
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVD---GEEVAMKVESK----SQPKQVLKMEVAVLKKLqGKPHFCRLIGCGRTERYNYI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ildflrggdVFTRLSK---EVLFTEEDVKFYLA---ELAL----ALDHLHQLGIVYRDLKPENILldeIG-------HIK 230
Cdd:cd14017    74 ---------VMTLLGPnlaELRRSQPRGKFSVSttlRLGIqilkAIEDIHEVGFLHRDVKPSNFA---IGrgpsderTVY 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFGLSKESVDQEK-------KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMi 302
Cdd:cd14017   142 ILDFGLARQYTNKDGeverpprNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKlKDKEEVGKM- 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 303 lKAKLGMPQFLSAEAQSLLRMLfkrnpanrlgsegvEEIKRHLFFANIDWDKLYK 357
Cdd:cd14017   221 -KEKIDHEELLKGLPKEFFQIL--------------KHIRSLSYFDTPDYKKLHS 260
pknD PRK13184
serine/threonine-protein kinase PknD;
90-345 3.05e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 80.20  E-value: 3.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLKKaSLKVRDRVRTKMERD--ILVEVNHPFIVKLhYAFQTEGKL-Y 166
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYD---PVCSRRVALKKIRE-DLSENPLLKKRFLREakIAADLIHPGIVPV-YSICSDGDPvY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRL----SKEVLFTE----EDVKFYLA---ELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:PRK13184   79 YTMPYIEGYTLKSLLksvwQKESLSKElaekTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 236 --LSKE---------SVDQEKKAYS-------FCGTVEYMAPEVVnrRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDR 295
Cdd:PRK13184  159 aaIFKKleeedlldiDVDERNICYSsmtipgkIVGTPDYMAPERL--LGVpaSESTDIYALGVILYQMLTLSFPYRRKKG 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 296 NEtmnMILKAKLGMPQ----------FLSaeaQSLLRMLfKRNPANRLGS--EGVEEIKRHL 345
Cdd:PRK13184  237 RK---ISYRDVILSPIevapyreippFLS---QIAMKAL-AVDPAERYSSvqELKQDLEPHL 291
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
443-697 3.20e-15

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: 77.58  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCI-HATTNMEFAVKII---DKSKRDPSEEIEILMRYGQ-HPN----IITLKDVFDDGRYVYLV 513
Cdd:cd14213    14 YEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIVknvDRYREAARSEIQVLEHLNTtDPNstfrCVQMLEWFDHHGHVCIV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMkGGELLDRIlKQKCFSEREASDI---LYVISKTVDYLHCQGVVHRDLKPSNILYM--------------DESASAD 576
Cdd:cd14213    94 FELL-GLSTYDFI-KENSFLPFPIDHIrnmAYQICKSVNFLHHNKLTHTDLKPENILFVqsdyvvkynpkmkrDERTLKN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 577 S-IRICDFGFAKQLRGENGLLLTpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAN-------------- 641
Cdd:cd14213   172 PdIKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQThdskehlammeril 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 642 GPndTPEEILLRIGNGK-FSLSGGNWDNISDGAK------------------------DLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14213   249 GP--LPKHMIQKTRKRKyFHHDQLDWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLDEALK 326

                  .
gi 1034674014 697 H 697
Cdd:cd14213   327 H 327
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
89-322 3.22e-15

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: 77.51  E-value: 3.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK---- 164
Cdd:cd07859     1 RYKIQEVIGKGSYG---VVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 -LYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 243
Cdd:cd07859    78 dIYVVFE-LMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFND 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 244 EKKAY---SFCGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPqflSAEAQ 318
Cdd:cd07859   157 TPTAIfwtDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDL-LGTP---SPETI 232

                  ....
gi 1034674014 319 SLLR 322
Cdd:cd07859   233 SRVR 236
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
90-310 3.41e-15

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: 77.35  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF--------QT 161
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQI---KTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAverpdkskRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLrGGDVFTRLSKE-VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeS 240
Cdd:cd07866    87 RGSVYMVTPYM-DHDLSGLLENPsVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLAR-P 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 VDQEKKAYSFCGTVE------------YMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKL 307
Cdd:cd07866   165 YDGPPPNPKGGGGGGtrkytnlvvtrwYRPPELLlGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFK-LC 243

                  ...
gi 1034674014 308 GMP 310
Cdd:cd07866   244 GTP 246
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
468-697 3.87e-15

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: 76.25  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDKSKRDPSE-----EIEILMRYgQHPNII----------------------TLKDVFDDGryVYLVTDLMKgg 520
Cdd:cd14046    33 YYAIKKIKLRSESKNNsrilrEVMLLSRL-NHQHVVryyqawieranlyiqmeyceksTLRDLIDSG--LFQDTDRLW-- 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 elldRILKQkcfsereasdilyvISKTVDYLHCQGVVHRDLKPSNIlYMDesaSADSIRICDFGFAK------------- 587
Cdd:cd14046   108 ----RLFRQ--------------ILEGLAYIHSQGIIHRDLKPVNI-FLD---SNGNVKIGDFGLATsnklnvelatqdi 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 -----QLRGENGLLLTPCYTANFVAPEVLMQQG--YDAACDIWSLGVLFYTMLagYTPfangpnDTPEE---ILLRIGNG 657
Cdd:cd14046   166 nkstsAALGSSGDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEMC--YPF------STGMErvqILTALRSV 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 658 KFSLSGGNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14046   238 SIEFPPDFDDNKHSKQAKLIRWLLNHDPAKRPSAQELLKS 277
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
446-704 3.97e-15

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: 76.46  E-value: 3.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 446 KEDIGVGSYSVCKRCIHATTNMEFAVKIID-----KSKRDPSEEIEILMRYGQhPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd06619     6 QEILGHGNGGTVYKAYHLLTRRILAVKVIPlditvELQKQIMSELEILYKCDS-PYIIGFYGAFFVENRISICTEFMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELlDRILKqkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLrgENGLLLTPC 600
Cdd:cd06619    85 SL-DVYRK---IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLV----NTRGQVKLCDFGVSTQL--VNSIAKTYV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTP----FANGPNDTPEEILL--------RIGNGKFslsggnwdn 668
Cdd:cd06619   155 GTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPypqiQKNQGSLMPLQLLQcivdedppVLPVGQF--------- 225
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1034674014 669 iSDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRD 704
Cdd:cd06619   226 -SEKFVHFITQCMRKQPKERPAPENLMDHPFIVQYN 260
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
94-332 4.00e-15

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: 75.72  E-value: 4.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLvrkktGPDAGQL-YAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLI---- 168
Cdd:cd14203     1 VKLGQGCFGEVWM-----GTWNGTTkVAIKTLKPGTMSPEAFLE---EAQIMKKLRHDKLVQL-YAVVSEEPIYIVtefm 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 -----LDFLRGGD-VFTRLSKEVLFTeedvkfylAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 242
Cdd:cd14203    72 skgslLDFLKDGEgKYLKLPQLVDMA--------AQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 243 QE---KKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEA 317
Cdd:cd14203   144 NEytaRQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESL 221
                         250
                  ....*....|....*
gi 1034674014 318 QSLLRMLFKRNPANR 332
Cdd:cd14203   222 HELMCQCWRKDPEER 236
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
439-649 4.07e-15

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 75.81  E-value: 4.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYE--LKEDIGVgSYSVCKRCIHATTNMEFAvkiidkskrdpsEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd05085     9 FGEVYKgtLKDKTPV-AVKTCKEDLPQELKIKFL------------SEARILKQY-DHPNIVKLIGVCTQRQPIYIVMEL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQK---------CFSEREASDILYVISKtvdylHCqgvVHRDLKPSNILYMDESAsadsIRICDFGFAK 587
Cdd:cd05085    75 VPGGDFLSFLRKKKdelktkqlvKFSLDAAAGMAYLESK-----NC---IHRDLAARNCLVGENNA----LKISDFGMSR 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 588 Q----LRGENGLLLTPCytaNFVAPEVLMQQGYDAACDIWSLGVLFY-TMLAGYTPFANGPNDTPEE 649
Cdd:cd05085   143 QeddgVYSSSGLKQIPI---KWTAPEALNYGRYSSESDVWSFGILLWeTFSLGVCPYPGMTNQQARE 206
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
147-310 4.16e-15

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: 77.44  E-value: 4.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 147 VNHPFIVKLHYAFQTEGKL------YLILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPEN 220
Cdd:cd07874    73 VNHKNIISLLNVFTPQKSLeefqdvYLVMELM---DANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 221 ILLDEIGHIKLTDFGLSKeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN 300
Cdd:cd07874   150 IVVKSDCTLKILDFGLAR-TAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWN 228
                         170
                  ....*....|
gi 1034674014 301 MILKaKLGMP 310
Cdd:cd07874   229 KVIE-QLGTP 237
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
441-700 4.38e-15

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK12 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 76.77  E-value: 4.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKR----DPSEEIEILmRYGQHPNIITLKDVFDDG------- 507
Cdd:cd07864     7 DKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVrlDNEKEgfpiTAIREIKIL-RQLNHRSVVNLKEIVTDKqdaldfk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 ---RYVYLV-----TDLMKggeLLDRILKQkcFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIR 579
Cdd:cd07864    86 kdkGAFYLVfeymdHDLMG---LLESGLVH--FSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKG----QIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 580 ICDFGFAKQLRGENGLLLT-PCYTANFVAPEVLM-QQGYDAACDIWS----LGVLF-----------------YTMLAGY 636
Cdd:cd07864   157 LADFGLARLYNSEESRPYTnKVITLWYRPPELLLgEERYGPAIDVWScgciLGELFtkkpifqanqelaqlelISRLCGS 236
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 637 TPFANGPNDT---------PEEILLRIGNGKFSLsggnwdnISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd07864   237 PCPAVWPDVIklpyfntmkPKKQYRRRLREEFSF-------IPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
94-292 4.94e-15

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: 76.16  E-value: 4.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKaslkvRDRVRTKMERDI--LVEVNHP----FIVKLHYAFQTEGKLYL 167
Cdd:cd14056     1 KTIGKGRYGEVWLGKYR-----GEKVAVKIFSS-----RDEDSWFRETEIyqTVMLRHEnilgFIAADIKSTGSWTQLWL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAeLALALDHLH--------QLGIVYRDLKPENILLDEIGHIKLTDFGLS-K 238
Cdd:cd14056    71 ITEYHEHGSLYDYLQRNTLDTEEALRLAYS-AASGLAHLHteivgtqgKPAIAHRDLKSKNILVKRDGTCCIADLGLAvR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 239 ESVDQEKKAYSF---CGTVEYMAPEVVNRRGHSQS------ADWWSYGVLMFEML-----TGT-----LPFQG 292
Cdd:cd14056   150 YDSDTNTIDIPPnprVGTKRYMAPEVLDDSINPKSfesfkmADIYSFGLVLWEIArrceiGGIaeeyqLPYFG 222
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
88-305 5.02e-15

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: 77.13  E-value: 5.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMK--VLKKASlKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK- 164
Cdd:cd07854     5 SRYMDLRPLGCGSNGLVF---SAVDSDCDKRVAVKkiVLTDPQ-SVKHALR---EIKIIRRLDHDNIVKVYEVLGPSGSd 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 -------------LYLILDFLRGGdvFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIK 230
Cdd:cd07854    78 ltedvgsltelnsVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 231 LTDFGLSKeSVDQE--KKAYSFCGTVE--YMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA 305
Cdd:cd07854   156 IGDFGLAR-IVDPHysHKGYLSEGLVTkwYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILES 234
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
96-348 5.13e-15

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 76.26  E-value: 5.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLvrkktGPDAGQL-YAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLILDFLRG 174
Cdd:cd05069    20 LGQGCFGEVWM-----GTWNGTTkVAIKTLKPGTMMPEAFLQ---EAQIMKKLRHDKLVPL-YAVVSEEPIYIVTEFMGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 175 GDVFTRLSkevlftEEDVKF--------YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 246
Cdd:cd05069    91 GSLLDFLK------EGDGKYlklpqlvdMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 247 AYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRM 323
Cdd:cd05069   165 ARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKL 244
                         250       260
                  ....*....|....*....|....*
gi 1034674014 324 LFKRNPANRLGSEGVEEIKRHLFFA 348
Cdd:cd05069   245 CWKKDPDERPTFEYIQSFLEDYFTA 269
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
438-694 7.46e-15

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 75.54  E-value: 7.46e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYE----LKED--IGVgSYSVCKRCIhattnmefavkiiDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRyVY 511
Cdd:cd05056    18 QFGDVYQgvymSPENekIAV-AVKTCKNCT-------------SPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP-VW 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELlDRILKQKCFSEREASDILYV--ISKTVDYLHCQGVVHRDLKPSNILymdeSASADSIRICDFGFAKQL 589
Cdd:cd05056    83 IVMELAPLGEL-RSYLQVNKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVL----VSSPDCVKLGDFGLSRYM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 590 RGENgllltpCYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtpEEILLRIGNG-KFS 660
Cdd:cd05056   158 EDES------YYKASkgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKN---NDVIGRIENGeRLP 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 661 LSggnwDNISDGAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd05056   229 MP----PNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
96-284 7.50e-15

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: 75.20  E-value: 7.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLKKASlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14155     1 IGSGFFSEVYKVRHRT---SGQVMALKMNTLSS----NRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRL-SKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILL--DEIGHIKLT-DFGLSKE--SVDQEKKAYS 249
Cdd:cd14155    74 NLEQLLdSNEPLSWTVRVKLAL-DIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVVgDFGLAEKipDYSDGKEKLA 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034674014 250 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14155   153 VVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
89-332 8.01e-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: 74.91  E-value: 8.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrkkTGPDAGQLYAMKVLK-----KASLKvrdrvrtkmERDILVEVNHPFIVKLHYAFQTEG 163
Cdd:cd05083     7 KLTLGEIIGEGEFGAVL-----QGEYMGQKVAVKNIKcdvtaQAFLE---------ETAVMTKLQHKNLVRLLGVILHNG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 kLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsv 241
Cdd:cd05083    73 -LYIVMELMSKGNLvnFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV-- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 dQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQS 319
Cdd:cd05083   150 -GSMGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAVEKGyRMEPPEGCPPDVYS 228
                         250
                  ....*....|...
gi 1034674014 320 LLRMLFKRNPANR 332
Cdd:cd05083   229 IMTSCWEAEPGKR 241
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
95-341 8.53e-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: 74.99  E-value: 8.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFlvrkkTGPDAGQLYAMKVLKK-ASLKVrdrvrTKMERDILVEVNHPFIVKLhYAFQTEGKLyLILDFLR 173
Cdd:cd14068     1 LLGDGGFGSVY-----RAVYRGEDVAVKIFNKhTSFRL-----LRQELVVLSHLHHPSLVAL-LAAGTAPRM-LVMELAP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHQLGIVYRDLKPENILL-----DEIGHIKLTDFGLSKESVDQEKKa 247
Cdd:cd14068    69 KGSLDALLQQDNASLTRTLQHRIAlHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIK- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 248 ySFCGTVEYMAPEVVnrRG---HSQSADWWSYGVLMFEMLT-GTLPFQG-KDRNETMNMILKAKLGMP--QFLSA---EA 317
Cdd:cd14068   148 -TSEGTPGFRAPEVA--RGnviYNQQADVYSFGLLLYDILTcGERIVEGlKFPNEFDELAIQGKLPDPvkEYGCApwpGV 224
                         250       260
                  ....*....|....*....|....
gi 1034674014 318 QSLLRMLFKRNPANRLGSEGVEEI 341
Cdd:cd14068   225 EALIKDCLKENPQCRPTSAQVFDI 248
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
97-347 8.64e-15

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: 75.44  E-value: 8.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  97 GQGSFGKVFLVRKK-TGPDAGQ-LYAMKVLKKASLKVRDRVRTKMERDI--LVEVNHPFIV---------KLHYAFQTE- 162
Cdd:cd14011     5 GPGLPWKIYNGSKKsTKQEVSVfVFEKKQLEEYSKRDREQILELLKRGVkqLTRLRHPRILtvqhpleesRESLAFATEp 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 --GKLYLIL-DFLRGGDVFTRLSKEVLFTEEdVKFYLAELALALDHLHQ-LGIVYRDLKPENILLDEIGHIKLTDFGLSK 238
Cdd:cd14011    85 vfASLANVLgERDNMPSPPPELQDYKLYDVE-IKYGLLQISEALSFLHNdVKLVHGNICPESVVINSNGEWKLAGFDFCI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAYSFCG-----------TVEYMAPEVVNRRGHSQSADWWSYGVLMFEML-TGTLPFQGKDRNET----MNMI 302
Cdd:cd14011   164 SSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSykknSNQL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 303 LKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEIKRHLFF 347
Cdd:cd14011   244 RQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDA---EQLSKIPFF 285
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
422-644 8.68e-15

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 75.10  E-value: 8.68e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 422 TSANVLPIVQINGnAAQFGEVYElkedigvGSYSVCKRcihatTNMEFAVKII-----DKSKRDPSEEIEILMRYgQHPN 496
Cdd:cd05033     1 IDASYVTIEKVIG-GGEFGEVCS-------GSLKLPGK-----KEIDVAIKTLksgysDKQRLDFLTEASIMGQF-DHPN 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 497 IITLKDVFDDGRYVYLVTDLMKGGElLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdesAS 574
Cdd:cd05033    67 VIRLEGVVTKSRPVMIVTEYMENGS-LDKFLRENdgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNIL-----VN 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 575 ADSI-RICDFGFAKQLRGENgllltPCYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPN 644
Cdd:cd05033   141 SDLVcKVSDFGLSRRLEDSE-----ATYTTKggkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSN 214
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
32-310 9.78e-15

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 77.38  E-value: 9.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  32 EIVNPYEVKR----KVKVNGLKMVDEPMEEGEADSCHDEGVVKEIPIThhVKEGYEKADPAQFELLKVLGQGSFGKVFlv 107
Cdd:PTZ00036    8 EDINIYEEKNhkanKGGSGKFEMNDKKLDEEERSHNNNAGEDEDEEKM--IDNDINRSPNKSYKLGNIIGNGSFGVVY-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 108 rKKTGPDAGQLYAMK-VLKKASLKVRDRVrtkmerdILVEVNHPFIVKLHYAFQTEGK--------LYLILDFL-----R 173
Cdd:PTZ00036   84 -EAICIDTSEKVAIKkVLQDPQYKNRELL-------IMKNLNHINIIFLKDYYYTECFkkneknifLNVVMEFIpqtvhK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEV-LFTeedVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH-IKLTDFGLSKESVDQEKKAYSFC 251
Cdd:PTZ00036  156 YMKHYARNNHALpLFL---VKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYIC 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 252 GTVeYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:PTZ00036  233 SRF-YRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQV-LGTP 290
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
497-677 1.02e-14

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: 76.62  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 497 IITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESASad 576
Cdd:cd05625    63 VVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 577 sIRICDFGFAKQLR----------GEN--------------------GLLLTP-----------CY------TANFVAPE 609
Cdd:cd05625   140 -IKLTDFGLCTGFRwthdskyyqsGDHlrqdsmdfsnewgdpencrcGDRLKPlerraarqhqrCLahslvgTPNYIAPE 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 610 VLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngpNDTPEEILLRIGNGKFSLSGGNWDNISDGAKDLL 677
Cdd:cd05625   219 VLLRTGYTQLCDWWSVGVILFEMLVGQPPFL---AQTPLETQMKVINWQTSLHIPPQAKLSPEASDLI 283
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
96-360 1.12e-14

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: 75.72  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVflVRKKTGPDAGQLYAMKVL------KKASLKvrdrvrtkmERDILVEVN--------HpfIVKLHYAFQT 161
Cdd:cd14135     8 LGKGVFSNV--VRARDLARGNQEVAIKIIrnnelmHKAGLK---------ELEILKKLNdadpddkkH--CIRLLRHFEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH-IKLTDFGLSK 238
Cdd:cd14135    75 KNHLCLVFESLSMNlrEVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ESVDQEKKAY---SFcgtveYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQflsa 315
Cdd:cd14135   155 DIGENEITPYlvsRF-----YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFPK---- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 316 eaqsllRMLFKrnpaNRLGSEGVEEikrHLFFANIDWDKLYKREV 360
Cdd:cd14135   226 ------KMLRK----GQFKDQHFDE---NLNFIYREVDKVTKKEV 257
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
78-346 1.17e-14

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: 75.86  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  78 VKEGYEKADPAQ-FELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVL-KKASLKVRDRVRtkmERDILVEVNHPFIVKL 155
Cdd:cd06635    14 IAELFFKEDPEKlFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSgKQSNEKWQDIIK---EVKFLQRIKHPNSIEY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQTEGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALAldHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd06635    91 KGCYLREHTAWLVMEYCLGSasDLLEVHKKPLQEIEIAAITHGALQGLA--YLHSHNMIHRDIKAGNILLTEPGQVKLAD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGlskeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIlkAKLGMP 310
Cdd:cd06635   169 FG----SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHI--AQNESP 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 311 QFLSAEAQSLLRML----FKRNPANRLGSegvEEIKRHLF 346
Cdd:cd06635   243 TLQSNEWSDYFRNFvdscLQKIPQDRPTS---EELLKHMF 279
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
94-332 1.24e-14

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: 74.97  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKLYLI 168
Cdd:cd14204    13 KVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLlgvclEVGSQRIPKPMVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLftEEDVKF--------YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE- 239
Cdd:cd14204    93 LPFMKYGDLHSFLLRSRL--GSGPQHvplqtllkFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKi 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 -SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAE 316
Cdd:cd14204   171 ySGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLLHGhRLKQPEDCLDE 250
                         250
                  ....*....|....*.
gi 1034674014 317 AQSLLRMLFKRNPANR 332
Cdd:cd14204   251 LYDIMYSCWRSDPTDR 266
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
441-697 1.24e-14

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: 74.96  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELkEDIGVGSYSVCKRCIHATTNMEFAVKiidKSKRDPSE---------EIEILMRYGQHPNIITLKDVFDDGRYVY 511
Cdd:cd14139     1 EFLEL-EKIGVGEFGSVYKCIKRLDGCVYAIK---RSMRPFAGssneqlalhEVYAHAVLGHHPHVVRYYSAWAEDDHMI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRILKQ----KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYM-----------------D 570
Cdd:cd14139    77 IQNEYCNGGSLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIChkmqsssgvgeevsneeD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 571 ESASADSI-RICDFGFAKQLRG---ENGllltpcyTANFVAPEVLMQQ-GYDAACDIWSLGVlfytmlagytpfangpnd 645
Cdd:cd14139   157 EFLSANVVyKIGDLGHVTSINKpqvEEG-------DSRFLANEILQEDyRHLPKADIFALGL------------------ 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 646 tpeEILLRIGNGKFSLSGGNWDNISDGA------------KDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd14139   212 ---TVALAAGAEPLPTNGAAWHHIRKGNfpdvpqelpesfSSLLKNMIQPDPEQRPSATALARH 272
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
94-341 1.24e-14

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 75.22  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKV-----FLVRKKtgpDAGQLYAMKVLKKASLKVRDRVRTKmERDILVEV-NHPFIVKLHYAFQT-EGKLY 166
Cdd:cd05054    13 KPLGRGAFGKViqasaFGIDKS---ATCRTVAVKMLKEGATASEHKALMT-ELKILIHIgHHLNVVNLLGACTKpGGPLM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRL-SKEVLF-------------------------TEEDVKFYLAELALALDHLHQLGIVYRDLKPEN 220
Cdd:cd05054    89 VIVEFCKFGNLSNYLrSKREEFvpyrdkgardveeeedddelykeplTLEDLICYSFQVARGMEFLASRKCIHRDLAARN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 221 ILLDEIGHIKLTDFGLSKE---SVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRN 296
Cdd:cd05054   169 ILLSENNVVKICDFGLARDiykDPDYVRKGDARL-PLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQMD 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 297 ETMNMILK--AKLGMPQFLSAEAQSLLRMLFKRNPANRLG-SEGVEEI 341
Cdd:cd05054   248 EEFCRRLKegTRMRAPEYTTPEIYQIMLDCWHGEPKERPTfSELVEKL 295
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
147-310 1.47e-14

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: 75.85  E-value: 1.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 147 VNHPFIVKLHYAFQTEGKL------YLILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPEN 220
Cdd:cd07875    80 VNHKNIIGLLNVFTPQKSLeefqdvYIVMELM---DANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 221 ILLDEIGHIKLTDFGLSKESvdqekkAYSFCGTVE-----YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDR 295
Cdd:cd07875   157 IVVKSDCTLKILDFGLARTA------GTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDH 230
                         170
                  ....*....|....*
gi 1034674014 296 NETMNMILKaKLGMP 310
Cdd:cd07875   231 IDQWNKVIE-QLGTP 244
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
79-332 1.50e-14

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 74.72  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  79 KEGYEKADPAQFeLLKVLGQGSFGKVFlvrkKTGPDAGQLYAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLhYA 158
Cdd:cd05070     1 KDVWEIPRESLQ-LIKRLGNGQFGEVW----MGTWNGNTKVAIKTLKPGTMSPESFLE---EAQIMKKLKHDKLVQL-YA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTEGKLYLILDFLRGGD--VFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05070    72 VVSEEPIYIVTEYMSKGSllDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFL 313
Cdd:cd05070   152 ARLIEDNEYTARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPQDC 231
                         250
                  ....*....|....*....
gi 1034674014 314 SAEAQSLLRMLFKRNPANR 332
Cdd:cd05070   232 PISLHELMIHCWKKDPEER 250
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
443-639 1.69e-14

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: 74.68  E-value: 1.69e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID-------KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQifdlmdaKARADCIKEIDLLKQL-NHPNVIKYYASFIEDNELNIVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELLDRIL----KQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFG----FAK 587
Cdd:cd08229   105 LADAGDLSRMIKhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFI----TATGVVKLGDLGlgrfFSS 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 588 QLRGENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd08229   181 KTTAAHSLVGTPYY----MSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 228
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
428-697 1.72e-14

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: 74.68  E-value: 1.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 428 PIVQINGNAaqFGEVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdkskrdpsEEIEIL--MRYGQHPNIITLKDVFD 505
Cdd:cd07862     5 CVAEIGEGA--YGKVFKARDLKNGGRFVALKRVRVQTGEEGMPLSTI--------REVAVLrhLETFEHPNVVRLFDVCT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 506 DGR----------YVYLVTDLMKggeLLDRILKQKCFSErEASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASA 575
Cdd:cd07862    75 VSRtdretkltlvFEHVDQDLTT---YLDKVPEPGVPTE-TIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV----TSS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 576 DSIRICDFGFAKQLRGENGLLLTpCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAgYTPFANG------------- 642
Cdd:cd07862   147 GQIKLADFGLARIYSFQMALTSV-VVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR-RKPLFRGssdvdqlgkildv 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 643 -----PNDTPEEILLRigNGKFSLSGGN-----WDNISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd07862   225 iglpgEEDWPRDVALP--RQAFHSKSAQpiekfVTDIDELGKDLLLKCLTFNPAKRISAYSALSH 287
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
89-310 2.18e-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: 75.55  E-value: 2.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEgklylI 168
Cdd:cd07853     1 DVEPDRPIGYGAFGVVWSV---TDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPP-----H 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVL---------FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS-K 238
Cdd:cd07853    73 IDPFEEIYVVTELMQSDLhkiivspqpLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLArV 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 239 ESVDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07853   153 EEPDESKHMTQEVVTQYYRAPEIlMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDL-LGTP 224
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
96-344 2.26e-14

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: 74.48  E-value: 2.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKK-TGPDAGQ-LYAMKVLKK-ASLKVR-DRVRtkmERDILVEVNHPFIVKLhYAFQTEGK-LYLILD 170
Cdd:cd05050    13 IGQGAFGRVFQARAPgLLPYEPFtMVAVKMLKEeASADMQaDFQR---EAALMAEFDHPNIVKL-LGVCAVGKpMCLLFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFTEEDVKFYLAELA------LALDHLHQLGI----------------VYRDLKPENILLDEIGH 228
Cdd:cd05050    89 YMAYGDLNEFLRHRSPRAQCSLSHSTSSARkcglnpLPLSCTEQLCIakqvaagmaylserkfVHRDLATRNCLVGENMV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 IKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA 305
Cdd:cd05050   169 VKIADFGLSRNiySADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAHEEVIYYVRDG 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1034674014 306 K-LGMPQFLSAEAQSLLRMLFKRNPANRLGSEGVEEIKRH 344
Cdd:cd05050   249 NvLSCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQR 288
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
96-304 2.70e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 73.68  E-value: 2.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrkKTGPDAGQLYAMKVLKKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd14664     1 IGRGGAGTVY----KGVMPNGTLVAVKRLKGEGTQGGDHGFQA-EIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRL-----SKEVLFTEEDVKFYLaELALALDHLHQ---LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD-QEKK 246
Cdd:cd14664    76 SLGELLhsrpeSQPPLDWETRQRIAL-GSARGLAYLHHdcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDkDSHV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 247 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFqGKDRNETMNMILK 304
Cdd:cd14664   155 MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF-DEAFLDDGVDIVD 211
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
93-291 2.87e-14

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: 73.80  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  93 LKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKV-RDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 171
Cdd:cd14026     2 LRYLSRGAFGTVSRARHA---DWRVTVAIKCLKLDSPVGdSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTeeDVKF-----YLAELALALDHLHQLG--IVYRDLKPENILLDEIGHIKLTDFGLSK---ESV 241
Cdd:cd14026    79 MTNGSLNELLHEKDIYP--DVAWplrlrILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwrqLSI 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 242 DQEK--KAYSFCGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQ 291
Cdd:cd14026   157 SQSRssKSAPEGGTIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFE 211
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
87-302 2.93e-14

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: 73.96  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGKVF--LVRKKTGPDAGQLYAMKVLKKASLKvRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEG 163
Cdd:cd05036     5 RKNLTLIRALGQGAFGEVYegTVSGMPGDPSPLQVAVKTLPELCSE-QDEMDFLMEALIMSKFNHPNIVRCiGVCFQRLP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KlYLILDFLRGGDV--FTR-----LSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTD 233
Cdd:cd05036    84 R-FILLELMAGGDLksFLRenrprPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvAKIGD 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 234 FGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 302
Cdd:cd05036   163 FGMARDiyRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFV 234
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
494-652 3.57e-14

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 75.99  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESA 573
Cdd:NF033483   66 HPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGR 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 574 sadsIRICDFGFAKQLRGE-----NGLLltpcYTANFVAPEvlmqQ---GY-DAACDIWSLGVLFYTMLAGYTPFaNGpn 644
Cdd:NF033483  146 ----VKVTDFGIARALSSTtmtqtNSVL----GTVHYLSPE----QargGTvDARSDIYSLGIVLYEMLTGRPPF-DG-- 210

                  ....*...
gi 1034674014 645 DTPEEILL 652
Cdd:NF033483  211 DSPVSVAY 218
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
95-340 3.58e-14

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: 73.63  E-value: 3.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLKkaslkVRDRVRTKMERDILVEVN--HP----FIVKLHYAFQTEGKLYLI 168
Cdd:cd13998     2 VIGKGRFGEVWKASLK-----NEPVAVKIFS-----SRDKQSWFREKEIYRTPMlkHEnilqFIAADERDTALRTELWLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAeLALALDHLH---------QLGIVYRDLKPENILLDEIGHIKLTDFGLS-- 237
Cdd:cd13998    72 TAFHPNGSL*DYLSLHTIDWVSLCRLALS-VARGLAHLHseipgctqgKPAIAHRDLKSKNILVKNDGTCCIADFGLAvr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 -KESVDQEKKA-YSFCGTVEYMAPEV----VNRRGHS--QSADWWSYGVLMFEMLTGT-----------LPFQGKDRN-- 296
Cdd:cd13998   151 lSPSTGEEDNAnNGQVGTKRYMAPEVlegaINLRDFEsfKRVDIYAMGLVLWEMASRCtdlfgiveeykPPFYSEVPNhp 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 297 --ETMNMILKAKLGMPQFLSAEAQSL-LRMLFK-------RNPANRLGSEGVEE 340
Cdd:cd13998   231 sfEDMQEVVVRDKQRPNIPNRWLSHPgLQSLAEtieecwdHDAEARLTAQCIEE 284
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
447-699 3.67e-14

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: 73.84  E-value: 3.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD--PSEEIE--ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGel 522
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEgvPFTAIReaSLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTD-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 523 LDRILKQKCFSEREASDILYVIS--KTVDYLHCQGVVHRDLKPSNIL--YMDEsasadsIRICDFGFAKQLRgenglllT 598
Cdd:cd07870    84 LAQYMIQHPGGLHPYNVRLFMFQllRGLAYIHGQHILHRDLKPQNLLisYLGE------LKLADFGLARAKS-------I 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 599 PC--YTANFVA-----PEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFAnGPNDTPEEiLLRIGNGKFSLSGGNWDNIS 670
Cdd:cd07870   151 PSqtYSSEVVTlwyrpPDVLLgATDYSSALDIWGAGCIFIEMLQGQPAFP-GVSDVFEQ-LEKIWTVLGVPTEDTWPGVS 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 671 D----------------------------GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07870   229 KlpnykpewflpckpqqlrvvwkrlsrppKAEDLASQMLMMFPKDRISAQDALLHPY 285
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
468-644 4.09e-14

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: 73.06  E-value: 4.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDK---SKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQK-CFSEREASDILYV 543
Cdd:cd05112    30 KVAIKTIREgamSEEDFIEEAEVMMKL-SHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 ISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKqlrgengLLLTPCYTAN--------FVAPEVLMQQG 615
Cdd:cd05112   109 VCEGMAYLEEASVIHRDLAARNCLVGENQV----VKVSDFGMTR-------FVLDDQYTSStgtkfpvkWSSPEVFSFSR 177
                         170       180       190
                  ....*....|....*....|....*....|
gi 1034674014 616 YDAACDIWSLGVLFYTMLA-GYTPFANGPN 644
Cdd:cd05112   178 YSSKSDVWSFGVLMWEVFSeGKIPYENRSN 207
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
187-332 4.12e-14

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 74.27  E-value: 4.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 187 FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE---SVDQEKKAYSFCgTVEYMAPEVVN 263
Cdd:cd14207   177 LTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDiykNPDYVRKGDARL-PLKWMAPESIF 255
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 264 RRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLGM--PQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd14207   256 DKIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMraPEFATSEIYQIMLDCWQGDPNER 327
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
468-633 4.53e-14

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 73.95  E-value: 4.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDKSKRDPSEEIEI-LMRYGQHPNIITLKDVF--DDGRYVYLVTD--------LMKGGELLDRILKQKCFSERE 536
Cdd:cd07867    31 EYALKQIEGTGISMSACREIaLLRELKHPNVIALQKVFlsHSDRKVWLLFDyaehdlwhIIKFHRASKANKKPMQLPRSM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 537 ASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLL--LTP-CYTANFVAPEVLM- 612
Cdd:cd07867   111 VKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPELLLg 190
                         170       180
                  ....*....|....*....|.
gi 1034674014 613 QQGYDAACDIWSLGVLFYTML 633
Cdd:cd07867   191 ARHYTKAIDIWAIGCIFAELL 211
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
89-310 4.75e-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: 74.40  E-value: 4.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLK-------KASLKVR--DRVRtKMERDilvevNHPFIVKLHYAF 159
Cdd:cd14224    66 RYEVLKVIGKGSFGQVV---KAYDHKTHQHVALKMVRnekrfhrQAAEEIRilEHLK-KQDKD-----NTMNVIHMLESF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGKLYLILDFLrGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH--IKLTDFG 235
Cdd:cd14224   137 TFRNHICMTFELL-SMNLYELIKKNKFqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 236 lskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd14224   216 ---SSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIEL-LGMP 286
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
438-698 4.87e-14

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: 73.21  E-value: 4.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVyelkEDIGVGSYSVCKRCIHATTNMEFAVKiidKSKR----DPSEEIEILMRY-----GQHPNIITLKDVFDDGR 508
Cdd:cd14051     1 EFHEV----EKIGSGEFGSVYKCINRLDGCVYAIK---KSKKpvagSVDEQNALNEVYahavlGKHPHVVRYYSAWAEDD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 509 YVYLVTDLMKGGELLDRILKQK----CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIlYMDESASADS------- 577
Cdd:cd14051    74 HMIIQNEYCNGGSLADAISENEkageRFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI-FISRTPNPVSseeeeed 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 578 --------------IRICDFGFA---KQLRGENGllltpcyTANFVAPEVLmQQGYD--AACDIWSLGVLFYtMLAGYTP 638
Cdd:cd14051   153 fegeednpesnevtYKIGDLGHVtsiSNPQVEEG-------DCRFLANEIL-QENYShlPKADIFALALTVY-EAAGGGP 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 639 F-ANGPNDTpeeillRIGNGKFSlsggNWDNISDGAKDLLSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd14051   224 LpKNGDEWH------EIRQGNLP----PLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
95-332 5.00e-14

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 73.49  E-value: 5.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVFLVR-KKTG--PDAgqlyAMKVLKKASLKvRDRVRTKMERDILVEVN-HPFIVKLHYAFQTEGKLYLILD 170
Cdd:cd05088    14 VIGEGNFGQVLKARiKKDGlrMDA----AIKRMKEYASK-DDHRDFAGELEVLCKLGhHPNIINLLGACEHRGYLYLAIE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEVLFtEEDVKF-----------------YLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd05088    89 YAPHGNLLDFLRKSRVL-ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIAD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKESVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI-LKAKLGMPQ 311
Cdd:cd05088   168 FGLSRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpQGYRLEKPL 246
                         250       260
                  ....*....|....*....|.
gi 1034674014 312 FLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05088   247 NCDDEVYDLMRQCWREKPYER 267
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
483-650 5.25e-14

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: 72.66  E-value: 5.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 483 EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRI------LKQKCF---SEREASDILYVISKtvdylHC 553
Cdd:cd05084    43 QEARILKQY-SHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLrtegprLKVKELirmVENAAAGMEYLESK-----HC 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 554 qgvVHRDLKPSNILYMDESAsadsIRICDFGFAKQ-----LRGENGLLLTPcytANFVAPEVLMQQGYDAACDIWSLGVL 628
Cdd:cd05084   117 ---IHRDLAARNCLVTEKNV----LKISDFGMSREeedgvYAATGGMKQIP---VKWTAPEALNYGRYSSESDVWSFGIL 186
                         170       180
                  ....*....|....*....|....
gi 1034674014 629 FY-TMLAGYTPFANGPN-DTPEEI 650
Cdd:cd05084   187 LWeTFSLGAVPYANLSNqQTREAV 210
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
94-332 5.29e-14

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: 72.76  E-value: 5.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGkvfLVRKK--TGPDAGQL-YAMKVLKKASLKVRDRVRtkmerDILVEVN------HPFIVKLhYAFQTEGK 164
Cdd:cd05040     1 EKLGDGSFG---VVRRGewTTPSGKVIqVAVKCLKSDVLSQPNAMD-----DFLKEVNamhsldHPNLIRL-YGVVLSSP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSKE----VLFTEEDvkfYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeS 240
Cdd:cd05040    72 LMMVTELAPLGSLLDRLRKDqghfLISTLCD---YAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR-A 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 241 VDQEKKAY----------SFCgtveymAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA--KL 307
Cdd:cd05040   148 LPQNEDHYvmqehrkvpfAWC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKEgeRL 221
                         250       260
                  ....*....|....*....|....*
gi 1034674014 308 GMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05040   222 ERPDDCPQDIYNVMLQCWAHKPADR 246
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
449-584 5.35e-14

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: 69.39  E-value: 5.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIID----KSKRDPSEEIEILMRYGQH-PNIITLKDVFDDGRYVYLVTDLMKGGELL 523
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDdvnnEEGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 524 DRILKQkCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFG 584
Cdd:cd13968    81 AYTQEE-ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDG----NVKLIDFG 136
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
444-644 5.93e-14

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 72.59  E-value: 5.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 444 ELKEDIGVGSY-SVCKRCIHATTNMEFAVKI-------IDKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05065     7 KIEEVIGAGEFgEVCRGRLKLPGKREIFVAIktlksgyTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRPVMIITE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGElLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdesasADSIRIC---DFGFAKQLR 590
Cdd:cd05065    86 FMENGA-LDSFLRQNdgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNIL-------VNSNLVCkvsDFGLSRFLE 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 591 GENGlllTPCYTAN--------FVAPEVLMQQGYDAACDIWSLG-VLFYTMLAGYTPFANGPN 644
Cdd:cd05065   158 DDTS---DPTYTSSlggkipirWTAPEAIAYRKFTSASDVWSYGiVMWEVMSYGERPYWDMSN 217
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
96-333 7.38e-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: 72.69  E-value: 7.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKV-FLVRKKTGPDAGQLYAMKVLKKAS----------LKVRDRVRT----KMERDILVEVNHPFIVKL----- 155
Cdd:cd14067     1 LGQGGSGTViYRARYQGQPVAVKRFHIKKCKKRTdgsadtmlkhLRAADAMKNfsefRQEASMLHSLQHPCIVYLigisi 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 H---YAFQTE--GKLYLILDFLRGGDVFTRLSKEVLFTeedVKFylaELALALDHLHQLGIVYRDLKPENIL---LDEIG 227
Cdd:cd14067    81 HplcFALELAplGSLNTVLEENHKGSSFMPLGHMLTFK---IAY---QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 228 HI--KLTDFGLSKESVDQekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA 305
Cdd:cd14067   155 HIniKLSDYGISRQSFHE--GALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSKG 232
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 306 ---KLGMP---QFLSaeAQSLLRMLFKRNPANRL 333
Cdd:cd14067   233 irpVLGQPeevQFFR--LQALMMECWDTKPEKRP 264
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
441-695 7.68e-14

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: 72.36  E-value: 7.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEdIGVGSYSVCKRcihATTNMEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDVFDDGRYVyLVT 514
Cdd:cd14150     1 EVSMLKR-IGTGSFGTVFR---GKWHGDVAVKILKVTEPTPEQlqafknEMQVL-RKTRHVNILLFMGFMTRPNFA-IIT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRI-LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIlYMDESAsadSIRICDFGFA------- 586
Cdd:cd14150    75 QWCEGSSLYRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNI-FLHEGL---TVKIGDFGLAtvktrws 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 --KQLRGENGLLLtpcytanFVAPEVLMQQG---YDAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGNGKFSL 661
Cdd:cd14150   151 gsQQVEQPSGSIL-------WMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSNINNR--DQIIFMVGRGYLSP 221
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 662 SGGN-WDNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd14150   222 DLSKlSSNCPKAMKRLLIDCLKFKREERPLFPQIL 256
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
461-646 7.79e-14

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 72.90  E-value: 7.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 461 IHATTNMEFAVKIIdKSKRDPSE------EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDrILKQKCFSE 534
Cdd:cd05055    60 SKSDAVMKVAVKML-KPTAHSSErealmsELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLN-FLRRKRESF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 535 REASDIL---YVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGEN-----GLLLTPcytANFV 606
Cdd:cd05055   138 LTLEDLLsfsYQVAKGMAFLASKNCIHRDLAARNVLL----THGKIVKICDFGLARDIMNDSnyvvkGNARLP---VKWM 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 607 APEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNDT 646
Cdd:cd05055   211 APESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDS 251
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
443-651 7.84e-14

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: 73.17  E-value: 7.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKI--IDKSKRDPSEE--------IEILMRYGQHPNIITLKDVFD-DGRYVY 511
Cdd:cd14041     8 YLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDSFC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELlDRILKQ-KCFSEREASDILYVISKTVDYLH--CQGVVHRDLKPSNILYMDESASADsIRICDFGFAKQ 588
Cdd:cd14041    88 TVLEYCEGNDL-DFYLKQhKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTACGE-IKITDFGLSKI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 589 LRGEN-----GLLLTP--CYTANFVAPEVLM----QQGYDAACDIWSLGVLFYTMLAGYTPFanGPNDTPEEIL 651
Cdd:cd14041   166 MDDDSynsvdGMELTSqgAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFYQCLYGRKPF--GHNQSQQDIL 237
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
92-332 7.94e-14

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: 72.69  E-value: 7.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVF--LVRKKTGPDAGQLYAMKVLKKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05061    10 LLRELGQGSFGMVYegNARDIIKGEAETRVAVKTVNE-SASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDVFTRLSK----------EVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 239
Cdd:cd05061    89 ELMAHGDLKSYLRSlrpeaennpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMTRD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 --SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK-AKLGMPQFLSA 315
Cdd:cd05061   169 iyETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDgGYLDQPDNCPE 248
                         250
                  ....*....|....*..
gi 1034674014 316 EAQSLLRMLFKRNPANR 332
Cdd:cd05061   249 RVTDLMRMCWQFNPKMR 265
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
90-310 8.48e-14

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: 73.05  E-value: 8.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLK--KASLKvrdrvRTKMERDILVEVNHPF-------IVKLHYAFQ 160
Cdd:cd14212     1 YLVLDLLGQGTFGQVV---KCQDLKTNKLVAVKVLKnkPAYFR-----QAMLEIAILTLLNTKYdpedkhhIVRLLDHFM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 161 TEGKLYLILDFLrGGDVFtRLSKEVLF---TEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEI--GHIKLTDFG 235
Cdd:cd14212    73 HHGHLCIVFELL-GVNLY-ELLKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFG 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 236 lskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGtLP-FQGkdrNETMNMILK--AKLGMP 310
Cdd:cd14212   151 ---SACFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPlFPG---NSEYNQLSRiiEMLGMP 221
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
449-697 8.54e-14

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 72.42  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKII-------DKSKRDPSEEIEI-LMRYGQHPNIITLKDVFDD--GRYVYLVTDLMK 518
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVqfdpespETSKEVSALECEIqLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdeSASADSIRICDFGFAKQLR-------G 591
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL----RDSAGNVKLGDFGASKRLQticmsgtG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYtanfVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANgpndtpEEILLRIgnGKFSLSGGN---WDN 668
Cdd:cd06651   171 IRSVTGTPYW----MSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE------YEAMAAI--FKIATQPTNpqlPSH 238
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 669 ISDGAKDLLSHMLhMDPHQRYTAEQILKH 697
Cdd:cd06651   239 ISEHARDFLGCIF-VEARHRPSAEELLRH 266
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
449-657 9.10e-14

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: 72.04  E-value: 9.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRC-IHATTnmefAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDVFDDGRYVyLVTDLMKGGE 521
Cdd:cd14062     1 IGSGSFGTVYKGrWHGDV----AVKKLNVTDPTPSQlqafknEVAVL-RKTRHVNILLFMGYMTKPQLA-IVTQWCEGSS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRI-LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA--KQLRGENGLLLT 598
Cdd:cd14062    75 LYKHLhVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDL----TVKIGDFGLAtvKTRWSGSQQFEQ 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 599 PCYTANFVAPEVLMQQG---YDAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGNG 657
Cdd:cd14062   151 PTGSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYSHINNR--DQILFMVGRG 210
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
89-310 9.51e-14

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 72.54  E-value: 9.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGPDagqlyaMKVLKKASLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 165
Cdd:PLN00009    3 QYEKVEKIGEGTYGVVYKARDRVTNE------TIALKKIRLEQEDEgVPSTAIREIslLKEMQHGNIVRLQDVVHSEKRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLrGGDVFTRLSKEVLFTEED--VKFYLAELALALDHLHQLGIVYRDLKPENILLD-EIGHIKLTDFGLSKESVD 242
Cdd:PLN00009   77 YLVFEYL-DLDLKKHMDSSPDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLARAFGI 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 243 QEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:PLN00009  156 PVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRI-LGTP 223
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
441-699 1.00e-13

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: 72.56  E-value: 1.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRD---PS---EEIEILMRYGQHPNIITLKDV---FDDGR-YV 510
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEegvPStalREVSLLQMLSQSIYIVRLLDVehvEENGKpLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTdlmkggELLDRILKQKCFSEREAS----------DILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadSIRI 580
Cdd:cd07837    81 YLVF------EYLDTDLKKFIDSYGRGPhnplpaktiqSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKG---LLKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 581 CDFGFAKQLRgenglLLTPCYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRI 654
Cdd:cd07837   152 ADLGLGRAFT-----IPIKSYTHEIVtlwyrAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQPLF---PGDSELQQLLHI 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 655 gngkFSLSGGNWDNISDGAK----------------------------DLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07837   224 ----FRLLGTPNEEVWPGVSklrdwheypqwkpqdlsravpdlepegvDLLTKMLAYDPAKRISAKAALQHPY 292
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
440-702 1.02e-13

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: 73.12  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEV----YELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSE-EIEILMRYGQHP-----NIITLKDVFDDG 507
Cdd:cd14226     8 GEKwmdrYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIknKKAFLNQAQiEVRLLELMNKHDtenkyYIVRLKRHFMFR 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 508 RYVYLVT--------DLMK----GGELLDRILKqkcFSEREASDILYVISKTVDYLHCqgvvhrDLKPSNILYMDESASA 575
Cdd:cd14226    88 NHLCLVFellsynlyDLLRntnfRGVSLNLTRK---FAQQLCTALLFLSTPELSIIHC------DLKPENILLCNPKRSA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 576 dsIRICDFGfakqlrgenglllTPCYTAN----------FVAPEVLMQQGYDAACDIWSLGVLFYTMLAGyTPFANGPND 645
Cdd:cd14226   159 --IKIIDFG-------------SSCQLGQriyqyiqsrfYRSPEVLLGLPYDLAIDMWSLGCILVEMHTG-EPLFSGANE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 646 T-------------PEEILLR---------------------------IGNGKFSLS-------GG--------NWDNIS 670
Cdd:cd14226   223 VdqmnkivevlgmpPVHMLDQapkarkffeklpdgtyylkktkdgkkyKPPGSRKLHeilgvetGGpggrragePGHTVE 302
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1034674014 671 DGAK--DLLSHMLHMDPHQRYTAEQILKHSWITH 702
Cdd:cd14226   303 DYLKfkDLILRMLDYDPKTRITPAEALQHSFFKR 336
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
441-651 1.07e-13

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: 72.40  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKI--IDKSKRDPSEE--------IEILMRYGQHPNIITLKDVFD-DGRY 509
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELlDRILKQ-KCFSEREASDILYVISKTVDYLH--CQGVVHRDLKPSNILYMDESASADsIRICDFGFA 586
Cdd:cd14040    86 FCTVLEYCEGNDL-DFYLKQhKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGE-IKITDFGLS 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 587 KQLR----GENGLLLTP--CYTANFVAPEVLM----QQGYDAACDIWSLGVLFYTMLAGYTPFanGPNDTPEEIL 651
Cdd:cd14040   164 KIMDddsyGVDGMDLTSqgAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPF--GHNQSQQDIL 236
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
439-701 1.07e-13

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: 72.42  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEV--YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEI----LMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd07869     1 FGKAdsYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIreasLLKGLKHANIVLLHDIIHTKETLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 V-----TDLMK------GGELLDRIlkqKCFsereasdiLYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRIC 581
Cdd:cd07869    81 VfeyvhTDLCQymdkhpGGLHPENV---KLF--------LFQLLRGLSYIHQRYILHRDLKPQNLLISDTG----ELKLA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 582 DFGFAKQLRGENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFANGPN--DTPEEILLRIGN-- 656
Cdd:cd07869   146 DFGLARAKSVPSHTYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiqDQLERIFLVLGTpn 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 657 ---------------GKFSLSGGN-----WDNIS--DGAKDLLSHMLHMDPHQRYTAEQILKHSWIT 701
Cdd:cd07869   226 edtwpgvhslphfkpERFTLYSPKnlrqaWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
92-302 1.07e-13

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: 72.36  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFlVRKKTGPDAG---QLYAMKVLK-KASLKVRDRVRTK-MERDILvevNHPFIVKLHYAFQTEGKLY 166
Cdd:cd05091    10 FMEELGEDRFGKVY-KGHLFGTAPGeqtQAVAIKTLKdKAEGPLREEFRHEaMLRSRL---QHPNIVCLLGVVTKEQPMS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 167 LILDFLRGGDVFTRL--------------SKEVLFTEEDVKFY--LAELALALDHLHQLGIVYRDLKPENILLDEIGHIK 230
Cdd:cd05091    86 MIFSYCSHGDLHEFLvmrsphsdvgstddDKTVKSTLEPADFLhiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVK 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 231 LTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 302
Cdd:cd05091   166 ISDLGLFREvyAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMI 240
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
441-697 1.12e-13

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: 72.74  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCI-HATTNMEFAVKII---DKSKRDPSEEIEILMRYGQH-PN----IITLKDVFDDGRYVY 511
Cdd:cd14215    12 ERYEIVSTLGEGTFGRVVQCIdHRRGGARVALKIIknvEKYKEAARLEINVLEKINEKdPEnknlCVQMFDWFDYHGHMC 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMkGGELLDrILKQKCF---SEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYM---------------DESA 573
Cdd:cd14215    92 ISFELL-GLSTFD-FLKENNYlpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlekkrdERSV 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 574 SADSIRICDFGFAKQLRGENGLLLTpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN--------- 644
Cdd:cd14215   170 KSTAIRVVDFGSATFDHEHHSTIVS---TRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNrehlammer 246
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 645 ---DTPEEILLRIGNGKFSLSGG-NWDNISDGAK------------------------DLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd14215   247 ilgPIPSRMIRKTRKQKYFYHGRlDWDENTSAGRyvrenckplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAALK 326

                  .
gi 1034674014 697 H 697
Cdd:cd14215   327 H 327
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
481-649 1.18e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.99  E-value: 1.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 481 PSEEIE-ILMRYGQHPNIITLKDVFDDGRYVYLV-----TDLMKGGELLDRILkqkcfSEREASDILYVISKTVDYLHCQ 554
Cdd:PHA03209  102 GTTLIEaMLLQNVNHPSVIRMKDTLVSGAITCMVlphysSDLYTYLTKRSRPL-----PIDQALIIEKQILEGLRYLHAQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 555 GVVHRDLKPSNILYMDEsasaDSIRICDFGFAK-QLRGENGLLLTPCYTANfvAPEVLMQQGYDAACDIWSLGVLFYTML 633
Cdd:PHA03209  177 RIIHRDVKTENIFINDV----DQVCIGDLGAAQfPVVAPAFLGLAGTVETN--APEVLARDKYNSKADIWSAGIVLFEML 250
                         170
                  ....*....|....*.
gi 1034674014 634 AGYTPFANGPNDTPEE 649
Cdd:PHA03209  251 AYPSTIFEDPPSTPEE 266
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
463-700 1.21e-13

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: 72.36  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 463 ATTNMEFAVKIIDKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD--LMKGGELLDriLKQKCFSEREASDI 540
Cdd:cd06634    44 AIKKMSYSGKQSNEKWQDIIKEVKFLQKL-RHPNTIEYRGCYLREHTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 541 LYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLRGENGLLLTPCYtanfVAPEVL--MQQG-YD 617
Cdd:cd06634   121 THGALQGLAYLHSHNMIHRDVKAGNILLTEPGL----VKLGDFGSASIMAPANSFVGTPYW----MAPEVIlaMDEGqYD 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 618 AACDIWSLGVLFYTMLAGYTPFANGpndTPEEILLRIG-NGKFSLSGGNWdniSDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd06634   193 GKVDVWSLGITCIELAERKPPLFNM---NAMSALYHIAqNESPALQSGHW---SEYFRNFVDSCLQKIPQDRPTSDVLLK 266

                  ....
gi 1034674014 697 HSWI 700
Cdd:cd06634   267 HRFL 270
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
95-332 1.32e-13

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 72.34  E-value: 1.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  95 VLGQGSFGKVflVRKKTGPDAGQL-YAMKVLKKASLKvRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL----- 167
Cdd:cd05089     9 VIGEGNFGQV--IKAMIKKDGLKMnAAIKMLKEFASE-NDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIaieya 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ----ILDFLRGGDVFTR---LSKE----VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05089    86 pygnLLDFLRKSRVLETdpaFAKEhgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKESVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 314
Cdd:cd05089   166 SRGEEVYVKKTMGRL-PVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRMEKPRNCD 244
                         250
                  ....*....|....*...
gi 1034674014 315 AEAQSLLRMLFKRNPANR 332
Cdd:cd05089   245 DEVYELMRQCWRDRPYER 262
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
449-644 1.39e-13

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: 71.44  E-value: 1.39e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCIHATTNMEFAVKI-------IDKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGG 520
Cdd:cd05066    12 IGAGEFgEVCSGRLKLPGKREIPVAIktlkagyTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ElLDRILKQK--CFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdesasADSIRIC---DFGFAKQLRGENgl 595
Cdd:cd05066    91 S-LDAFLRKHdgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNIL-------VNSNLVCkvsDFGLSRVLEDDP-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 596 llTPCYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPN 644
Cdd:cd05066   161 --EAAYTTRggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEMSN 215
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
450-639 1.41e-13

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: 71.14  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 450 GVGSYSVCKRCIHATTNMEFAVKIIDKSKRdpseEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDrILKQ 529
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEK----EAEILSVL-SHRNIIQFYGAILEAPNYGIVTEYASYGSLFD-YLNS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 530 KCFSEREASDIL---YVISKTVDYLHCQG---VVHRDLKPSNILYmdesASADSIRICDFGfAKQLRGENgLLLTPCYTA 603
Cdd:cd14060    76 NESEEMDMDQIMtwaTDIAKGMHYLHMEApvkVIHRDLKSRNVVI----AADGVLKICDFG-ASRFHSHT-THMSLVGTF 149
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034674014 604 NFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPF 639
Cdd:cd14060   150 PWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
449-695 1.60e-13

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 71.61  E-value: 1.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCIHATTN-MEFAVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05047     3 IGEGNFgQVLKARIKKDGLrMDAAIKRMkeyasKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTV----------------DYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGF 585
Cdd:cd05047    83 LLDFLRKSRVLETDPAFAIANSTASTLssqqllhfaadvargmDYLSQKQFIHRDLAARNILVGENYVA----KIADFGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AkqlRGENGLLLTPC--YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGpndTPEEILLRIGNGkFSLS 662
Cdd:cd05047   159 S---RGQEVYVKKTMgrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGM---TCAELYEKLPQG-YRLE 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034674014 663 GGNwdNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd05047   232 KPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 262
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
92-346 1.61e-13

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: 71.97  E-value: 1.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  92 LLKVLGQGSFGKVFLVR-KKTGPDAGQ-LYAMKVLKKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 169
Cdd:cd05094     9 LKRELGEGAFGKVFLAEcYNLSPTKDKmLVAVKTLKDPTLAARKDF--QREAELLTNLQHDHIVKFYGVCGDGDPLIMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 170 DFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHQL------GIVY--------RDLKPENILLDEIGHIKLTD 233
Cdd:cd05094    87 EYMKHGDLnkFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIatqiasGMVYlasqhfvhRDLATRNCLVGANLLVKIGD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGM 309
Cdd:cd05094   167 FGMSRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIECITQGRvLER 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1034674014 310 PQFLSAEAQSLLRMLFKRNPANRLgseGVEEIKRHLF 346
Cdd:cd05094   247 PRVCPKEVYDIMLGCWQREPQQRL---NIKEIYKILH 280
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
87-310 1.78e-13

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: 72.40  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  87 PAQFELLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK-- 164
Cdd:cd07858     4 DTKYVPIKPIGRGAYG---IVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHRea 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 ---LYLILDFLRggdvfTRL-----SKEVLfTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd07858    81 fndVYIVYELMD-----TDLhqiirSSQTL-SDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 237 SKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 310
Cdd:cd07858   155 ARTTSEKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITEL-LGSP 228
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
96-348 1.78e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 71.29  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQT--EGK--LYLILDF 171
Cdd:cd14031    18 LGRGAFKTVY---KGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKkcIVLVTEL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSVDQEKKAY 248
Cdd:cd14031    95 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLMRTSFAK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 249 SFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLF 325
Cdd:cd14031   173 SVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFnkvTDPEVKEIIEGCI 251
                         250       260
                  ....*....|....*....|...
gi 1034674014 326 KRNPANRLgseGVEEIKRHLFFA 348
Cdd:cd14031   252 RQNKSERL---SIKDLLNHAFFA 271
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
441-699 1.88e-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: 71.95  E-value: 1.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSEEIE--ILMRYGQHPNIITLKDVFDDGRYVYLVTdl 516
Cdd:cd07872     6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAIRevSLLKDLKHANIVTLHDIVHTDKSLTLVF-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 mkggELLDRILKQ------KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLR 590
Cdd:cd07872    84 ----EYLDKDLKQymddcgNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERG----ELKLADFGLARAKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 GENGLLLTPCYTANFVAPEVLMQQG-YDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIGNGKFSLSGGNWDNI 669
Cdd:cd07872   156 VPTKTYSNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLF---PGSTVEDELHLIFRLLGTPTEETWPGI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 670 SDGAK--------------------------DLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07872   233 SSNDEfknynfpkykpqplinhaprldtegiELLTKFLQYESKKRISAEEAMKHAY 288
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
89-311 1.99e-13

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 71.64  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFL-VRKKTGPDAGQLYAMKVLKKASlKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGKLYL 167
Cdd:cd05110     8 ELKRVKVLGSGAFGTVYKgIWVPEGETVKIPVAIKILNETT-GPKANVEFMDEALIMASMDHPHLVRL-LGVCLSPTIQL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ILDFLRGGDV--FTRLSKEVLFTEEDVKfYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEK 245
Cdd:cd05110    86 VTQLMPHGCLldYVHEHKDNIGSQLLLN-WCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLAR-LLEGDE 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLgMPQ 311
Cdd:cd05110   164 KEYNADGgkmPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLLEKGER-LPQ 232
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
439-695 2.18e-13

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: 71.39  E-value: 2.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElKEDIGVGSYSVCKRCIHAttNMEFAVKIIdkskrdpsEEIEILMRYGQHPNII-------TLKDVFDDGRYVY 511
Cdd:cd14036    13 FAFVYE-AQDVGTGKEYALKRLLSN--EEEKNKAII--------QEINFMKKLSGHPNIVqfcsaasIGKEESDQGQAEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LV-TDLMKGG--ELLDRILKQKCFSEREASDILYVISKTVDYLHCQG--VVHRDLKPSNILYmdesASADSIRICDFGFA 586
Cdd:cd14036    82 LLlTELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLI----GNQGQIKLCDFGSA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQL---------RGENGLL---LTPCYTANFVAPEVL-MQQGY--DAACDIWSLGVLFYTMLAGYTPFANGPNdtpeeil 651
Cdd:cd14036   158 TTEahypdyswsAQKRSLVedeITRNTTPMYRTPEMIdLYSNYpiGEKQDIWALGCILYLLCFRKHPFEDGAK------- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 652 LRIGNGKFSLSGGnwDNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd14036   231 LRIINAKYTIPPN--DTQYTVFHDLIRSTLKVNPEERLSITEIV 272
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
196-333 2.41e-13

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: 71.76  E-value: 2.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 196 LAELALALDHLHQLGIVYRDLKPENILL----DEIGHIKLTDFG--LSKES----VDQEKKAYSFCGTVEYMAPEVVNRR 265
Cdd:cd14018   144 ILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGccLADDSiglqLPFSSWYVDRGGNACLMAPEVSTAV 223
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 266 G------HSQSADWWSYGVLMFEMLTGTLPF--QGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd14018   224 PgpgvviNYSKADAWAVGAIAYEIFGLSNPFygLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRV 299
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
96-332 2.50e-13

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 70.87  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLyAMKVLKKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLILDFLRGG 175
Cdd:cd05071    17 LGQGCFGEVW---MGTWNGTTRV-AIKTLKPGTMSPEAFLQ---EAQVMKKLRHEKLVQL-YAVVSEEPIYIVTEYMSKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKE---VLFTEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 252
Cdd:cd05071    89 SLLDFLKGEmgkYLRLPQLVDM-AAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 253 -TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRNP 329
Cdd:cd05071   168 fPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGyRMPCPPECPESLHDLMCQCWRKEP 247

                  ...
gi 1034674014 330 ANR 332
Cdd:cd05071   248 EER 250
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
441-698 2.58e-13

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: 70.82  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELkEDIGVGSYSVCKRCIHATTNMEFAVKIIDK------SKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd14138     6 EFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRILKQ----KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIL--------------YMDESASAD 576
Cdd:cd14138    85 EYCNGGSLADAISENyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFisrtsipnaaseegDEDEWASNK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 577 SI-RICDFGFAKQLRG---ENGllltpcyTANFVAPEVLmQQGYD--AACDIWSLGVLFYTMlAGYTPF-ANGP--NDTP 647
Cdd:cd14138   165 VIfKIGDLGHVTRVSSpqvEEG-------DSRFLANEVL-QENYThlPKADIFALALTVVCA-AGAEPLpTNGDqwHEIR 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 648 EEILLRIGNgkfslsggnwdNISDGAKDLLSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd14138   236 QGKLPRIPQ-----------VLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
90-332 2.70e-13

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: 71.03  E-value: 2.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEGKLYL- 167
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLiGVCFTASDLNKPp 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 168 ----ILDFLRGGDVFTRL-------SKEVLFTEEDVKFyLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGL 236
Cdd:cd05035    81 spmvILPFMKHGDLHSYLlysrlggLPEKLPLQTLLKF-MVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 237 SKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQF 312
Cdd:cd05035   160 SRKiySGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGnRLKQPED 239
                         250       260
                  ....*....|....*....|
gi 1034674014 313 LSAEAQSLLRMLFKRNPANR 332
Cdd:cd05035   240 CLDEVYFLMYFCWTVDPKDR 259
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
78-283 2.80e-13

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: 71.21  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  78 VKEGYEKADPAQ-FELLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVL-KKASLKVRDRVRtkmERDILVEVNHPFIVKL 155
Cdd:cd06634     4 VAELFFKDDPEKlFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSgKQSNEKWQDIIK---EVKFLQKLRHPNTIEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 156 HYAFQTEGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALAldHLHQLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd06634    81 RGCYLREHTAWLVMEYCLGSasDLLEVHKKPLQEVEIAAITHGALQGLA--YLHSHNMIHRDVKAGNILLTEPGLVKLGD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 234 FGlskeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEM 283
Cdd:cd06634   159 FG----SASIMAPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIEL 207
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
447-650 2.82e-13

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 70.45  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTN---MEFAVKIIdksKRDPSEEIEILMRYGQ---------HPNIITLKDVFDDGRyVYLVT 514
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSgkvIQVAVKCL---KSDVLSQPNAMDDFLKevnamhsldHPNLIRLYGVVLSSP-LMMVT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDRIlkqkcfseREASDILYV---------ISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGF 585
Cdd:cd05040    77 ELAPLGSLLDRL--------RKDQGHFLIstlcdyavqIANGMAYLESKRFIHRDLAARNILL----ASKDKVKIGDFGL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQLrGENglllTPCYTANF--------VAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFA--NG------------ 642
Cdd:cd05040   145 MRAL-PQN----EDHYVMQEhrkvpfawCAPESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLglNGsqilekidkege 219
                         250
                  ....*....|..
gi 1034674014 643 ----PNDTPEEI 650
Cdd:cd05040   220 rlerPDDCPQDI 231
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
439-699 3.58e-13

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: 70.81  E-value: 3.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FG--EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPSEEI-EI-LMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd07871     1 FGklETYVKLDKLGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAIrEVsLLKNLKHANIVTLHDIIHTERCLTL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTdlmkggELLDRILKQ---KC---FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFA 586
Cdd:cd07871    81 VF------EYLDSDLKQyldNCgnlMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKG----ELKLADFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLRGENGLLLTPCYTANFVAPEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEILLRIgngkFSLSGG- 664
Cdd:cd07871   151 RAKSVPTKTYSNEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMF---PGSTVKEELHLI----FRLLGTp 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 665 ---NWDNI---------------------------SDGAkDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07871   224 teeTWPGVtsneefrsylfpqyraqplinhaprldTDGI-DLLSSLLLYETKSRISAEAALRHSY 287
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
468-699 3.62e-13

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 71.24  E-value: 3.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDKSKRDPSEEIEI-LMRYGQHPNIITLKDVF--DDGRYVYLVTDLMKGGelLDRILKQKCFSERE-------- 536
Cdd:cd07868    46 DYALKQIEGTGISMSACREIaLLRELKHPNVISLQKVFlsHADRKVWLLFDYAEHD--LWHIIKFHRASKANkkpvqlpr 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 537 --ASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENGLL--LTP-CYTANFVAPEVL 611
Cdd:cd07868   124 gmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPELL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 612 M-QQGYDAACDIWSLGVLFYTMLAGYTPF------ANGPNDTPEEILLRIGNGKFSLSGGNWDNI------SDGAKD--- 675
Cdd:cd07868   204 LgARHYTKAIDIWAIGCIFAELLTSEPIFhcrqedIKTSNPYHHDQLDRIFNVMGFPADKDWEDIkkmpehSTLMKDfrr 283
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 676 -------------------------LLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07868   284 ntytncslikymekhkvkpdskafhLLQKLLTMDPIKRITSEQAMQDPY 332
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
440-699 3.69e-13

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: 70.85  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELKEDIGVGSYSVCKRCIHATTNMEFAV-----KIIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDD----GRYV 510
Cdd:cd14030    24 GRFLKFDIEIGRGSFKTVYKGLDTETTVEVAWcelqdRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQG--VVHRDLKPSNILYmdeSASADSIRICDFGFAKQ 588
Cdd:cd14030   104 VLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI---TGPTGSVKIGDLGLATL 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGE--NGLLLTPcytaNFVAPEvLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGkfsLSGGNW 666
Cdd:cd14030   181 KRASfaKSVIGTP----EFMAPE-MYEEKYDESVDVYAFGMCMLEMATSEYPYSECQN--AAQIYRRVTSG---VKPASF 250
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 667 DNIS-DGAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14030   251 DKVAiPEVKEIIEGCIRQNKDERYAIKDLLNHAF 284
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
449-693 3.73e-13

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: 70.98  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDK-SKRDPSE----EIEILMRYgQHPNIITLKDVFDD--GRYVYLVTDLMKGGE 521
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDvqmrEFEVLKKL-NHKNIVKLFAIEEEltTRHKVLVMELCPCGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 L---LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIL-YMDESASAdSIRICDFGFAKQLrGENGLLL 597
Cdd:cd13988    80 LytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQS-VYKLTDFGAAREL-EDDEQFV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 598 TPCYTANFVAPE-----VL---MQQGYDAACDIWSLGVLFYTMLAGYTPFAngPNDTP---EEILLRIGNGKFS--LSGG 664
Cdd:cd13988   158 SLYGTEEYLHPDmyeraVLrkdHQKKYGATVDLWSIGVTFYHAATGSLPFR--PFEGPrrnKEVMYKIITGKPSgaISGV 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1034674014 665 --------NWD-------NISDGAKDL----LSHMLHMDPHQRYTAEQ 693
Cdd:cd13988   236 qksengpiEWSgelpvscSLSQGLQTLltpvLANILEADQEKCWGFDQ 283
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
96-290 3.94e-13

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: 70.61  E-value: 3.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKtgpdaGQLYAMKVLKKASLKVRDRVRTKMERDI--LVEVNHPFIVKLhYAFQTEG-KLYLILDFL 172
Cdd:cd14158    23 LGEGGFGVVFKGYIN-----DKNVAVKKLAAMVDISTEDLTKQFEQEIqvMAKCQHENLVEL-LGYSCDGpQLCLVYTYM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDVFTRLS--KEVLFTEEDVKFYLAE-LALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 249
Cdd:cd14158    97 PNGSLLDRLAclNDTPPLSWHMRCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMT 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 250 --FCGTVEYMAPEVVnrRGH-SQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14158   177 erIVGTTAYMAPEAL--RGEiTPKSDIFSFGVVLLEIITGLPPV 218
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
96-284 4.36e-13

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: 69.86  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKaslkvrDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd14156     1 IGSGFFSKVYKVTHGAT---GKVMVVKIYKN------DVDQHKIVREIslLQKLSHPNIVRYLGICVKDEKLHPILEYVS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHQLGIVYRDLKPENILLDEIGHIK---LTDFGLSKESV-----DQE 244
Cdd:cd14156    72 GGCLEELLAREELPLSWREKVELAcDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGempanDPE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1034674014 245 KKaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 284
Cdd:cd14156   152 RK-LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
443-700 4.37e-13

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: 70.06  E-value: 4.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdksKRDPSEEI-----EILM-RYGQHPNIITLKDVFDDGRYVYLVTDL 516
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII---KLEPGDDFsliqqEIFMvKECKHCNIVAYFGSYLSREKLWICMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKCFSEREasdILYVISKTVD---YLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGEN 593
Cdd:cd06646    88 CGGGSLQDIYHVTGPLSELQ---IAYVCRETLQglaYLHSKGKMHRDIKGANILLTDNG----DVKLADFGVAAKITATI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPCYTANFVAPEVLMQQ---GYDAACDIWSLGVLFYTMLAGYTPFANgpndtpeeilLRIGNGKFSLSGGNWD--N 668
Cdd:cd06646   161 AKRKSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGITAIELAELQPPMFD----------LHPMRALFLMSKSNFQppK 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1034674014 669 ISDGAK------DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd06646   231 LKDKTKwsstfhNFVKISLTKNPKKRPTAERLLTHLFV 268
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
470-696 4.57e-13

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: 70.52  E-value: 4.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII--DKSKRDPSE---EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVI 544
Cdd:cd05053    47 AVKMLkdDATEKDLSDlvsEMEMMKMIGKHKNIINLLGACTQDGPLYVVVEYASKGNLREFLRARRPPGEEASPDDPRVP 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 545 SKTV----------------DYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQLRG-------ENGLLltpcy 601
Cdd:cd05053   127 EEQLtqkdlvsfayqvargmEYLASKKCIHRDLAARNVLVTED----NVMKIADFGLARDIHHidyyrktTNGRL----- 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFY-TMLAGYTPFangPNDTPEEI--LLRigngkfslSGGNWDNISDGAKDLLS 678
Cdd:cd05053   198 PVKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY---PGIPVEELfkLLK--------EGHRMEKPQNCTQELYM 266
                         250       260
                  ....*....|....*....|.
gi 1034674014 679 HML---HMDPHQRYTAEQILK 696
Cdd:cd05053   267 LMRdcwHEVPSQRPTFKQLVE 287
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
470-696 4.67e-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: 70.81  E-value: 4.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII--DKSKRDPSE---EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQK------CF------ 532
Cdd:cd05098    49 AVKMLksDATEKDLSDlisEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeyCYnpshnp 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 533 ----SEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQL-------RGENGLLltpcy 601
Cdd:cd05098   129 eeqlSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNV----MKIADFGLARDIhhidyykKTTNGRL----- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPndtPEEILlrigngKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd05098   200 PVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVP---VEELF------KLLKEGHRMDKPSNCTNELYMMM 270
                         250
                  ....*....|....*....
gi 1034674014 681 ---LHMDPHQRYTAEQILK 696
Cdd:cd05098   271 rdcWHAVPSQRPTFKQLVE 289
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
89-302 4.93e-13

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: 70.82  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVflVRKKTGPDAGQLYAMKVLKKASlKVRDRVRtkMERDILVEVNHP------FIVKLHYAFQTE 162
Cdd:cd14215    13 RYEIVSTLGEGTFGRV--VQCIDHRRGGARVALKIIKNVE-KYKEAAR--LEINVLEKINEKdpenknLCVQMFDWFDYH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 163 GKLYLILDFLrGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---------------DE 225
Cdd:cd14215    88 GHMCISFELL-GLSTFDFLKENnyLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrDE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 226 ----IGHIKLTDFGlsKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 301
Cdd:cd14215   167 rsvkSTAIRVVDFG--SATFDHEHHS-TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAM 243

                  .
gi 1034674014 302 I 302
Cdd:cd14215   244 M 244
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
470-702 4.95e-13

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: 69.63  E-value: 4.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIdksKRDPSEEIEI----LMRYGQHPNIITLKDVF-DDGRYVYLVTDLMKGGELLDrILKQKCFSEREASDILYV- 543
Cdd:cd05082    33 AVKCI---KNDATAQAFLaeasVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGSLVD-YLRSRGRSVLGGDCLLKFs 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 --ISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQLRGENGLLLTPcytANFVAPEVLMQQGYDAACD 621
Cdd:cd05082   109 ldVCEAMEYLEGNNFVHRDLAARNVLVSEDNVA----KVSDFGLTKEASSTQDTGKLP---VKWTAPEALREKKFSTKSD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 622 IWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNGkFSLSGGnwDNISDGAKDLLSHMLHMDPHQRYTAEQIlkHSWI 700
Cdd:cd05082   182 VWSFGILLWEIYSfGRVPY---PRIPLKDVVPRVEKG-YKMDAP--DGCPPAVYDVMKNCWHLDAAMRPSFLQL--REQL 253

                  ..
gi 1034674014 701 TH 702
Cdd:cd05082   254 EH 255
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
443-699 5.45e-13

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: 70.10  E-value: 5.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdkskRDPSEE------I-EI-LMRYGQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd07844     2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEI----RLEHEEgapftaIrEAsLLKDLKHANIVTLHDIIHTKKTLTLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 dlmkggELLDRILKQ---KCFSEREASDI---LYVISKTVDYLHCQGVVHRDLKPSNILYMDesasADSIRICDFGFAkq 588
Cdd:cd07844    78 ------EYLDTDLKQymdDCGGGLSMHNVrlfLFQLLRGLAYCHQRRVLHRDLKPQNLLISE----RGELKLADFGLA-- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 lRGENglLLTPCYTANFVA-----PEVLM-QQGYDAACDIWSLGVLFYTMLAGYTPF--ANGPNDTPEEILLRIG----- 655
Cdd:cd07844   146 -RAKS--VPSKTYSNEVVTlwyrpPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFpgSTDVEDQLHKIFRVLGtptee 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 656 ------------NGKFSLS-----GGNWDNISD--GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07844   223 twpgvssnpefkPYSFPFYpprplINHAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPY 285
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
436-632 7.55e-13

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: 69.23  E-value: 7.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYElkedigvGSYsvckrciHATTnmEFAVKIIDKSKRDPS---EEIEIlMRYGQHPNIITLKDVFDDGRYVYL 512
Cdd:cd05034     5 AGQFGEVWM-------GVW-------NGTT--KVAVKTLKPGTMSPEaflQEAQI-MKKLRHDKLVQLYAVCSDEEPIYI 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 513 VTDLMKGGELLD--RILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQLr 590
Cdd:cd05034    68 VTELMSKGSLLDylRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNV----CKVADFGLARLI- 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034674014 591 gENGLlltpcYTAN--------FVAPEVLMQQGYDAACDIWSLGVLFYTM 632
Cdd:cd05034   143 -EDDE-----YTARegakfpikWTAPEAALYGRFTIKSDVWSFGILLYEI 186
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
443-644 7.73e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 72.46  E-value: 7.73e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIID----KSKRDPSEEIEI-LMRYGQHPNIITLKDVFDD--GRYVYLVTD 515
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrglKEREKSQLVIEVnVMRELKHKNIVRYIDRFLNkaNQKLYILME 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  516 LMKGGELLDRIlkQKCF------SEREASDILYVISKTVDYLH-------CQGVVHRDLKPSNILYMDE-------SASA 575
Cdd:PTZ00266    95 FCDAGDLSRNI--QKCYkmfgkiEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLSTGirhigkiTAQA 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014  576 DSI------RICDFGFAKQLrGENGLLLTPCYTANFVAPEVLMQQ--GYDAACDIWSLGVLFYTMLAGYTPFANGPN 644
Cdd:PTZ00266   173 NNLngrpiaKIGDFGLSKNI-GIESMAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFHKANN 248
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
94-312 7.97e-13

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: 69.42  E-value: 7.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKASlKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEGKLYLILDFL 172
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRIT-DIEEVEQFLKEGIIMKDFSHPNVLSLlGICLPSEGSPLVVLPYM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 173 RGGDV--FTRLSKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE------ 244
Cdd:cd05058    80 KHGDLrnFIRSETHNPTVKDLIGFGL-QVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEyysvhn 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 245 KKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQF 312
Cdd:cd05058   159 HTGAKL--PVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPDVDSFDITVYLLQGrRLLQPEY 226
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
537-695 8.03e-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: 69.46  E-value: 8.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 537 ASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFA-----------KQLRGENGLLLTPCY-TAN 604
Cdd:cd14049   122 TTKILQQLLEGVTYIHSMGIVHRDLKPRNIFL---HGSDIHVRIGDFGLAcpdilqdgndsTTMSRLNGLTHTSGVgTCL 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 605 FVAPEVLMQQGYDAACDIWSLGVLfytMLAGYTPFanGPNDTPEEILLRIGNGKFSLSggnWDNISDGAKDLLSHMLHMD 684
Cdd:cd14049   199 YAAPEQLEGSHYDFKSDMYSIGVI---LLELFQPF--GTEMERAEVLTQLRNGQIPKS---LCKRWPVQAKYIKLLTSTE 270
                         170
                  ....*....|.
gi 1034674014 685 PHQRYTAEQIL 695
Cdd:cd14049   271 PSERPSASQLL 281
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
96-290 8.34e-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: 69.34  E-value: 8.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 171
Cdd:cd14032     9 LGRGSFKTVY---KGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSVDQEKKAY 248
Cdd:cd14032    86 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRASFAK 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 249 SFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14032   164 SVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPY 204
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
94-287 8.99e-13

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 69.69  E-value: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLKKAS-------LKVRDRVRtkmerdilvevNHPF---IVKLHYAFQTEG 163
Cdd:cd13981     6 KELGEGGYASVYLAKDDDEQSDGSLVALKVEKPPSiwefyicDQLHSRLK-----------NSRLresISGAHSAHLFQD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGG---DVF--TRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL--------------- 223
Cdd:cd13981    75 ESILVMDYSSQGtllDVVnkMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegeng 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 224 -DEIGhIKLTDFGLSKESVDQEKKAySF---CGTVEYMAPEVVNRRGHSQSADWwsYGV--LMFEMLTGT 287
Cdd:cd13981   155 wLSKG-LKLIDFGRSIDMSLFPKNQ-SFkadWHTDSFDCIEMREGRPWTYQIDY--FGIaaTIHVMLFGK 220
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
448-640 9.17e-13

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: 69.57  E-value: 9.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHA----TTNMEFAVKIIDKSKR-----DPSEEIEILmRYGQHPNIITLKDVFDD--GRYVYLVTDL 516
Cdd:cd05079    11 DLGEGHFGKVELCRYDpegdNTGEQVAVKSLKPESGgnhiaDLKKEIEIL-RNLYHENIVKYKGICTEdgGNGIKLIMEF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 517 MKGGELLDRILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGL 595
Cdd:cd05079    90 LPSGSLKEYLPRNKNkINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEH----QVKIGDFGLTKAIETDKEY 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 596 ------LLTPCYtanFVAPEVLMQQGYDAACDIWSLGVLFYTML----AGYTPFA 640
Cdd:cd05079   166 ytvkddLDSPVF---WYAPECLIQSKFYIASDVWSFGVTLYELLtycdSESSPMT 217
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
96-291 1.26e-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: 69.08  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTgpdagQLYAMKVLKK-ASLK---VRDRVRTKMERdiLVEVNHPFIVKLH-YAFQtEGKLYLILD 170
Cdd:cd14159     1 IGEGGFGCVYQAVMRN-----TEYAVKRLKEdSELDwsvVKNSFLTEVEK--LSRFRHPNIVDLAgYSAQ-QGNYCLIYV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 171 FLRGGDVFTRLSKEV----LFTEEDVKFYLAElALALDHLHQL--GIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVD 242
Cdd:cd14159    73 YLPNGSLEDRLHCQVscpcLSWSQRLHVLLGT-ARAIQYLHSDspSLIHGDVKSSNILLDAALNPKLGDFGLARfsRRPK 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 243 QEKKAYSFC------GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ 291
Cdd:cd14159   152 QPGMSSTLArtqtvrGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAME 206
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
89-285 1.36e-12

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: 69.29  E-value: 1.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFL-----VRKKTG--------PDAGQLYAMKVLKKaslKVRDRVRTKMERD--ILVEVNHPFIV 153
Cdd:cd05051     6 KLEFVEKLGEGQFGEVHLceangLSDLTSddfigndnKDEPVLVAVKMLRP---DASKNAREDFLKEvkIMSQLKDPNIV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 154 KLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVK-----------FYLA-ELALALDHLHQLGIVYRDLKPENI 221
Cdd:cd05051    83 RLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGASAtnsktlsygtlLYMAtQIASGMKYLESLNFVHRDLATRNC 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 222 LLDEIGHIKLTDFGLSKE--SVDQekkaYSFCGTV----EYMAPEVVNRRGHSQSADWWSYGVLMFEMLT 285
Cdd:cd05051   163 LVGPNYTIKIADFGMSRNlySGDY----YRIEGRAvlpiRWMAWESILLGKFTTKSDVWAFGVTLWEILT 228
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
470-696 1.41e-12

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: 69.66  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRI----------------LK 528
Cdd:cd05100    48 AVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLrarrppgmdysfdtckLP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 529 QKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQL-------RGENGLLltpcy 601
Cdd:cd05100   128 EEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNV----MKIADFGLARDVhnidyykKTTNGRL----- 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILlrigngKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd05100   199 PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPY---PGIPVEELF------KLLKEGHRMDKPANCTHELYMIM 269
                         250
                  ....*....|....*....
gi 1034674014 681 ---LHMDPHQRYTAEQILK 696
Cdd:cd05100   270 recWHAVPSQRPTFKQLVE 288
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
494-643 1.46e-12

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 69.59  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymde 571
Cdd:cd08227    58 HPNIVPYRATFIADNELWVVTSFMAYGSAKDLICTHfmDGMSELAIAYILQGVLKALDYIHHMGYVHRSVKASHIL---- 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 572 sASADSiRICDFGFAKQL----RGENGLLLT--PCYTAN---FVAPEVLMQ--QGYDAACDIWSLGVLFYTMLAGYTPFA 640
Cdd:cd08227   134 -ISVDG-KVYLSGLRSNLsminHGQRLRVVHdfPKYSVKvlpWLSPEVLQQnlQGYDAKSDIYSVGITACELANGHVPFK 211

                  ...
gi 1034674014 641 NGP 643
Cdd:cd08227   212 DMP 214
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
190-297 1.63e-12

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: 69.14  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 190 EDVKFYLAELALALDHLH-QLGIVYRDLKPENILLDE-IGHIKLTDFGlskESVDQEKKAYSFCGTVEYMAPEVVNRRGH 267
Cdd:cd14136   119 PLVKKIARQVLQGLDYLHtKCGIIHTDIKPENVLLCIsKIEVKIADLG---NACWTDKHFTEDIQTRQYRSPEVILGAGY 195
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1034674014 268 SQSADWWSYGVLMFEMLTGTL---PFQGKD--RNE 297
Cdd:cd14136   196 GTPADIWSTACMAFELATGDYlfdPHSGEDysRDE 230
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
440-699 1.67e-12

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: 68.59  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 440 GEVYELKEDIGVGSYSVCKRCIHATTNMEFA------VKIIDKSKRDPSEEIEILmRYGQHPNIITLKD----VFDDGRY 509
Cdd:cd14031     9 GRFLKFDIELGRGAFKTVYKGLDTETWVEVAwcelqdRKLTKAEQQRFKEEAEML-KGLQHPNIVRFYDswesVLKGKKC 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQG--VVHRDLKPSNILYmdeSASADSIRICDFGFAK 587
Cdd:cd14031    88 IVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFI---TGPTGSVKIGDLGLAT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QLRGE--NGLLLTPcytaNFVAPEvLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGkfsLSGGN 665
Cdd:cd14031   165 LMRTSfaKSVIGTP----EFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQN--AAQIYRKVTSG---IKPAS 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1034674014 666 WDNISD-GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14031   235 FNKVTDpEVKEIIEGCIRQNKSERLSIKDLLNHAF 269
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
165-335 1.75e-12

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 69.12  E-value: 1.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDvftrLSKEVLFTEEDVKF---YLAELALALDHLHQLGIVYRDLKPENILLDEIGH---IKLTDFGLSK 238
Cdd:cd13977   110 LWFVMEFCDGGD----MNEYLLSRRPDRQTntsFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLSK 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 239 ----------ESVDQEKKAYS-FCGTVEYMAPEVvnRRGH-SQSADWWSYGVLMFEM--------------LTGTLPFQG 292
Cdd:cd13977   186 vcsgsglnpeEPANVNKHFLSsACGSDFYMAPEV--WEGHyTAKADIFALGIIIWAMveritfrdgetkkeLLGTYIQQG 263
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1034674014 293 KDRNETMNMIL---KAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGS 335
Cdd:cd13977   264 KEIVPLGEALLenpKLELQIPLkkkkSMNDDMKQLLRDMLAANPQERPDA 313
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
443-705 2.17e-12

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 68.62  E-value: 2.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRdPS------EEIEILmrygqH----PNIITLKDVF-DDGRyVY 511
Cdd:cd06615     3 FEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIK-PAirnqiiRELKVL-----HecnsPYIVGFYGAFySDGE-IS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELlDRILKQkcfSEREASDILYVISKTV----DYLHCQ-GVVHRDLKPSNILYmdesASADSIRICDFGFA 586
Cdd:cd06615    76 ICMEHMDGGSL-DQVLKK---AGRIPENILGKISIAVlrglTYLREKhKIMHRDVKPSNILV----NSRGEIKLCDFGVS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 587 KQLRgeNGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTP--------FANGPNDTPEEILLRIGNGK 658
Cdd:cd06615   148 GQLI--DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeLEAMFGRPVSEGEAKESHRP 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 659 FSLSGGN----------WDNI-------------SDGAKDLLSHMLHMDPHQRYTAEQILKHSWITHRDQ 705
Cdd:cd06615   226 VSGHPPDsprpmaifelLDYIvnepppklpsgafSDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAEL 295
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
470-696 2.35e-12

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: 68.50  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII--DKSKRDPSE---EIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDI---- 540
Cdd:cd05101    60 AVKMLkdDATEKDLSDlvsEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDInrvp 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 541 ------------LYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQL-------RGENGLLltpcy 601
Cdd:cd05101   140 eeqmtfkdlvscTYQLARGMEYLASQKCIHRDLAARNVLVTENNV----MKIADFGLARDInnidyykKTTNGRL----- 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILlrigngKFSLSGGNWDNISDGAKDLLSHM 680
Cdd:cd05101   211 PVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPY---PGIPVEELF------KLLKEGHRMDKPANCTNELYMMM 281
                         250
                  ....*....|....*....
gi 1034674014 681 ---LHMDPHQRYTAEQILK 696
Cdd:cd05101   282 rdcWHAVPSQRPTFKQLVE 300
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
468-694 2.35e-12

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: 67.67  E-value: 2.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 468 EFAVKIIDK--SKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYvyLVTDLMKGGELlDRILKQK--CFSEREASDILYV 543
Cdd:cd14068    19 DVAVKIFNKhtSFRLLRQELVVLSHL-HHPSLVALLAAGTAPRM--LVMELAPKGSL-DALLQQDnaSLTRTLQHRIALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 ISKTVDYLHCQGVVHRDLKPSNILYMDESASADSI-RICDFGFAkQLRGENGlLLTPCYTANFVAPEVLMQQ-GYDAACD 621
Cdd:cd14068    95 VADGLRYLHSAMIIYRDLKPHNVLLFTLYPNCAIIaKIADYGIA-QYCCRMG-IKTSEGTPGFRAPEVARGNvIYNQQAD 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 622 IWSLGVLFYTMLAGYTPFANG---PNDTPE-EILLRIGNGKFSLSGGNWdnisDGAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd14068   173 VYSFGLLLYDILTCGERIVEGlkfPNEFDElAIQGKLPDPVKEYGCAPW----PGVEALIKDCLKENPQCRPTSAQV 245
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
439-695 2.82e-12

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 67.75  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElkediGVGsysvcKRCIHATTNMEFAVKIIDKSKRDpSEEIEIL-----MRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05032    19 FGMVYE-----GLA-----KGVVKGEPETRVAIKTVNENASM-RERIEFLneasvMKEFNCHHVVRLLGVVSTGQPTLVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRIlkQKCFSEREASDILYV------------ISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRIC 581
Cdd:cd05032    88 MELMAKGDLKSYL--RSRRPEAENNPGLGPptlqkfiqmaaeIADGMAYLAAKKFVHRDLAARNCMV----AEDLTVKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 582 DFGFAKQL-------RGENGLLltPcytANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtpEEILlr 653
Cdd:cd05032   162 DFGMTRDIyetdyyrKGGKGLL--P---VRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSN---EEVL-- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 654 igngKFSLSGGNWD---NISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd05032   232 ----KFVIDGGHLDlpeNCPDKLLELMRMCWQYNPKMRPTFLEIV 272
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
89-292 2.99e-12

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: 67.76  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 168
Cdd:cd14063     1 ELEIKEVIGKGRFGRVH--RGRWHGDV----AIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 169 LDFLRGGDVFTRL--SKEVLFTEEDVKFYLaELALALDHLHQLGIVYRDLKPENILLDEiGHIKLTDFGLSKESvdqekk 246
Cdd:cd14063    75 TSLCKGRTLYSLIheRKEKFDFNKTVQIAQ-QICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSLS------ 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 247 AYSFCGTVE-----------YMAPEVVN------RRGH----SQSADWWSYGVLMFEMLTGTLPFQG 292
Cdd:cd14063   147 GLLQPGRREdtlvipngwlcYLAPEIIRalspdlDFEEslpfTKASDVYAFGTVWYELLAGRWPFKE 213
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
206-333 3.59e-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: 67.82  E-value: 3.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 206 LHQLGIVYRDLKPENILLDEIGH-IKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEM 283
Cdd:cd13974   148 LHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYLgKPSDMWALGVVLFTM 227
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 284 LTGTLPFQGKDRNETMNMILKAKLGMPQ--FLSAEAQSLLRMLFKRNPANRL 333
Cdd:cd13974   228 LYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRL 279
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
89-332 4.15e-12

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 68.08  E-value: 4.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKV-----FLVRKKTGPDAgqlYAMKVLKKASLKVRDRVRTKmERDILVEV-NHPFIVKLHYA-FQT 161
Cdd:cd05102     8 RLRLGKVLGHGAFGKVveasaFGIDKSSSCET---VAVKMLKEGATASEHKALMS-ELKILIHIgNHLNVVNLLGAcTKP 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDV--FTRLSKEVL----------------------------------------------------- 186
Cdd:cd05102    84 NGPLMVIVEFCKYGNLsnFLRAKREGFspyrersprtrsqvrsmveavradrrsrqgsdrvasftestsstnqprqevdd 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 187 -----FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE---SVDQEKKAYSFCgTVEYMA 258
Cdd:cd05102   164 lwqspLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDiykDPDYVRKGSARL-PLKWMA 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 259 PEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK--AKLGMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd05102   243 PESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCQRLKdgTRMRAPEYATPEIYRIMLSCWHGDPKER 319
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
96-332 4.29e-12

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 67.37  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVF--LVRKKTGPDAGQLYAMKVLKKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 173
Cdd:cd05062    14 LGQGSFGMVYegIAKGVVKDEPETRVAIKTVNEAA-SMRERIEFLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIMELMT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 174 GGDVFTRL----------SKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKE--SV 241
Cdd:cd05062    93 RGDLKSYLrslrpemennPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMTRDiyET 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 242 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQS 319
Cdd:cd05062   173 DYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVLRFVMEGGlLDKPDNCPDMLFE 252
                         250
                  ....*....|...
gi 1034674014 320 LLRMLFKRNPANR 332
Cdd:cd05062   253 LMRMCWQYNPKMR 265
PTZ00284 PTZ00284
protein kinase; Provisional
89-311 4.47e-12

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 68.84  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLV--RKKTgpdagQLYAMKVLKKASLKVRD-RVRTK-MERDILVEVNHPF-IVKLHYAFQTEG 163
Cdd:PTZ00284  130 RFKILSLLGEGTFGKVVEAwdRKRK-----EYCAVKIVRNVPKYTRDaKIEIQfMEKVRQADPADRFpLMKIQRYFQNET 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLH-QLGIVYRDLKPENILL-------DEIGH------- 228
Cdd:PTZ00284  205 GHMCIVMPKYGPCLLDWIMKHGPFSHRHLAQIIFQTGVALDYFHtELHLMHTDLKPENILMetsdtvvDPVTNralppdp 284
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 --IKLTDFGlskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK 306
Cdd:PTZ00284  285 crVRICDLG---GCCDERHSRTAIVSTRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHLMEKTL 361

                  ....*
gi 1034674014 307 LGMPQ 311
Cdd:PTZ00284  362 GRLPS 366
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
89-304 4.97e-12

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: 67.73  E-value: 4.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVF----LVRKKTGpdagqlYAMKVLKKASlKVRDRVRtkMERDILVEV------NHPFIVKLHYA 158
Cdd:cd14214    14 RYEIVGDLGEGTFGKVVecldHARGKSQ------VALKIIRNVG-KYREAAR--LEINVLKKIkekdkeNKFLCVLMSDW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTEGKLYLILDFLrGGDVFTRLsKEVLFTE---EDVKFYLAELALALDHLHQLGIVYRDLKPENILLD----------- 224
Cdd:cd14214    85 FNFHGHMCIAFELL-GKNTFEFL-KENNFQPyplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynes 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 225 ---EIGHIK-----LTDFGlsKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd14214   163 kscEEKSVKntsirVADFG--SATFDHEHHT-TIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENR 239

                  ....*...
gi 1034674014 297 ETMNMILK 304
Cdd:cd14214   240 EHLVMMEK 247
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
449-647 5.07e-12

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: 66.77  E-value: 5.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIdKSKRDPS---EEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDR 525
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIY-KNDVDQHkivREISLLQKL-SHPNIVRYLGICVKDEKLHPILEYVSGGCLEEL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 526 ILKQKC-FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIrICDFGFAKQL------RGENGLLLT 598
Cdd:cd14156    79 LAREELpLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAV-VTDFGLAREVgempanDPERKLSLV 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 599 PcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTpfANgPNDTP 647
Cdd:cd14156   158 G--SAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIP--AD-PEVLP 201
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
470-696 5.38e-12

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 67.68  E-value: 5.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDI---- 540
Cdd:cd05099    48 AVKMLkdnatDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDItkvp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 541 ------------LYVISKTVDYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQL-------RGENGLLltpcy 601
Cdd:cd05099   128 eeqlsfkdlvscAYQVARGMEYLESRRCIHRDLAARNVLVTED----NVMKIADFGLARGVhdidyykKTSNGRL----- 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 602 TANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEI--LLRigngkfslSGGNWDNISDGAKDLLS 678
Cdd:cd05099   199 PVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPY---PGIPVEELfkLLR--------EGHRMDKPSNCTHELYM 267
                         250       260
                  ....*....|....*....|.
gi 1034674014 679 HM---LHMDPHQRYTAEQILK 696
Cdd:cd05099   268 LMrecWHAVPTQRPTFKQLVE 288
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
483-639 6.26e-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: 67.14  E-value: 6.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 483 EEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRIlkqKCFSE------REASDILYVISKTVDYLHCQGV 556
Cdd:cd14158    63 QEIQV-MAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDRL---ACLNDtpplswHMRCKIAQGTANGINYLHENNH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 557 VHRDLKPSNILyMDESASAdsiRICDFGFAKQLRGENGLLLTPCY--TANFVAPEVLmQQGYDAACDIWSLGVLFYTMLA 634
Cdd:cd14158   139 IHRDIKSANIL-LDETFVP---KISDFGLARASEKFSQTIMTERIvgTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIIT 213

                  ....*
gi 1034674014 635 GYTPF 639
Cdd:cd14158   214 GLPPV 218
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
443-636 6.84e-12

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 67.81  E-value: 6.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS---KRDPSEEIEILMRYGQHP----NIITLKDVFDDGRYVYLVTD 515
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHpsyARQGQIEVSILARLSTESaddyNFVRAYECFQHKNHTCLVFE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKggELLDRILKQKCFSE---REASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLrgE 592
Cdd:cd14227    97 MLE--QNLYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHV--S 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 593 NGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGY 636
Cdd:cd14227   173 KAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGW 216
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
449-639 7.89e-12

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 66.95  E-value: 7.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSY-SVCKRCIHATTN-MEFAVKII-----DKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE 521
Cdd:cd05089    10 IGEGNFgQVIKAMIKKDGLkMNAAIKMLkefasENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIAIEYAPYGN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKC----------------FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGF 585
Cdd:cd05089    90 LLDFLRKSRVletdpafakehgtastLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVS----KIADFGL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 586 AkqlRGENGLLLTPC--YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPF 639
Cdd:cd05089   166 S---RGEEVYVKKTMgrLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPY 219
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
96-235 9.56e-12

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: 63.23  E-value: 9.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFLVRKKTGPDAgqlYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 175
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIG---VAVKIGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 176 DVFTRLSKEVLFtEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFG 235
Cdd:cd13968    78 TLIAYTQEEELD-EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
448-699 1.04e-11

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: 65.87  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHATTNMEFA------VKIIDKSKRDPSEEIEILmRYGQHPNIITLKDVFDDG----RYVYLVTDLM 517
Cdd:cd14032     8 ELGRGSFKTVYKGLDTETWVEVAwcelqdRKLTKVERQRFKEEAEML-KGLQHPNIVRFYDFWESCakgkRCIVLVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRILKQKCFSEREASDILYVISKTVDYLHCQG--VVHRDLKPSNILYmdeSASADSIRICDFGFAKQLRGE--N 593
Cdd:cd14032    87 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFI---TGPTGSVKIGDLGLATLKRASfaK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 594 GLLLTPcytaNFVAPEvLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILLRIGNGkfsLSGGNWDNISDGA 673
Cdd:cd14032   164 SVIGTP----EFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQN--AAQIYRKVTCG---IKPASFEKVTDPE 233
                         250       260
                  ....*....|....*....|....*..
gi 1034674014 674 -KDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd14032   234 iKEIIGECICKNKEERYEIKDLLSHAF 260
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
484-641 1.07e-11

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: 65.63  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 484 EIEILMRYgQHPNIITLKDV-FDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYV-ISKTVDYLH--CQGVVHR 559
Cdd:cd14064    41 EVSILCRL-NHPCVIQFVGAcLDDPSQFAIVTQYVSGGSLFSLLHEQKRVIDLQSKLIIAVdVAKGMEYLHnlTQPIIHR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 560 DLKPSNILyMDESASADsirICDFG---FAKQLRGEN-----GLLLtpcytanFVAPEVLMQQG-YDAACDIWSLGVLFY 630
Cdd:cd14064   120 DLNSHNIL-LYEDGHAV---VADFGesrFLQSLDEDNmtkqpGNLR-------WMAPEVFTQCTrYSIKADVFSYALCLW 188
                         170
                  ....*....|.
gi 1034674014 631 TMLAGYTPFAN 641
Cdd:cd14064   189 ELLTGEIPFAH 199
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
443-700 1.19e-11

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: 67.08  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKR---DPSEEIEILM------RYGQHpNIITLKDVFDDGRYVYLV 513
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRfhrQAAEEIRILEhlkkqdKDNTM-NVIHMLESFTFRNHICMT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDL--MKGGELLDRIlKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASAdsIRICDFGFAKQlrg 591
Cdd:cd14224   146 FELlsMNLYELIKKN-KFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRSG--IKVIDFGSSCY--- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYtPFANGPND------------TPEEILLR------ 653
Cdd:cd14224   220 EHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGY-PLFPGEDEgdqlacmiellgMPPQKLLEtskrak 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 654 ----------------IGNGKFSLSGGN--------------WDNISDGAKD-----LLSHMLHMDPHQRYTAEQILKHS 698
Cdd:cd14224   299 nfisskgypryctvttLPDGSVVLNGGRsrrgkmrgppgskdWVTALKGCDDplfldFLKRCLEWDPAARMTPSQALRHP 378

                  ..
gi 1034674014 699 WI 700
Cdd:cd14224   379 WL 380
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
444-648 1.22e-11

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 66.62  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 444 ELKED-------IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRdPS------EEIEILMRYGQhPNIITLKDVFDDGRYV 510
Cdd:cd06650     1 ELKDDdfekiseLGAGNGGVVFKVSHKPSGLVMARKLIHLEIK-PAirnqiiRELQVLHECNS-PYIVGFYGAFYSDGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELlDRILKQKC-FSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYmdesASADSIRICDFGFAKQ 588
Cdd:cd06650    79 SICMEHMDGGSL-DQVLKKAGrIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILV----NSRGEIKLCDFGVSGQ 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRgeNGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngPNDTPE 648
Cdd:cd06650   154 LI--DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIP--PPDAKE 209
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
442-700 1.36e-11

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: 65.38  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 442 VYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSK-----------RDPSEeIEILMRYGQ-HPNIITLKDVFDDGRY 509
Cdd:cd14100     1 QYQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRvsewgelpngtRVPME-IVLLKKVGSgFRGVIRLLDWFERPDS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKG-GELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGfakq 588
Cdd:cd14100    80 FVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI---DLNTGELKLIDFG---- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 lrgeNGLLLTPCYTANF------VAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFANGPNDTPEEILLRigngkfsl 661
Cdd:cd14100   153 ----SGALLKDTVYTDFdgtrvySPPEWIRFHRYHGrSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFR-------- 220
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 662 sggnwDNISDGAKDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14100   221 -----QRVSSECQHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
96-290 1.87e-11

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: 65.46  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 171
Cdd:cd14030    33 IGRGSFKTVY---KGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSVDQEKKAY 248
Cdd:cd14030   110 MTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRASFAK 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 249 SFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14030   188 SVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPY 228
pknD PRK13184
serine/threonine-protein kinase PknD;
494-641 2.01e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 67.49  E-value: 2.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDDGRYVYLVTDLMKGgELLDRILK--------QKCFSEREAS----DILYVISKTVDYLHCQGVVHRDL 561
Cdd:PRK13184   61 HPGIVPVYSICSDGDPVYYTMPYIEG-YTLKSLLKsvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 562 KPSNILYMDESasadSIRICDFGFAKQLRGENGLLLT-------PCY-----------TANFVAPEVLMQQGYDAACDIW 623
Cdd:PRK13184  140 KPDNILLGLFG----EVVILDWGAAIFKKLEEEDLLDidvdernICYssmtipgkivgTPDYMAPERLLGVPASESTDIY 215
                         170
                  ....*....|....*...
gi 1034674014 624 SLGVLFYTMLAGYTPFAN 641
Cdd:PRK13184  216 ALGVILYQMLTLSFPYRR 233
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
436-657 2.09e-11

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: 65.00  E-value: 2.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYElkedigvGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEILMRYGQHpNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05063    15 AGEFGEVFR-------GILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHH-NIIRLEGVVTKFKPAMIITE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELlDRILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGEN 593
Cdd:cd05063    87 YMENGAL-DKYLRDHDgeFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILV----NSNLECKVSDFGLSRVLEDDP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 594 glllTPCYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtpEEILLRIGNG 657
Cdd:cd05063   162 ----EGTYTTSggkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSN---HEVMKAINDG 226
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
445-660 2.16e-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: 65.08  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSY-SVCKRCIHAttnmEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDvFDDGRYVYLVTDLM 517
Cdd:cd14151    12 VGQRIGSGSFgTVYKGKWHG----DVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNILLFMG-YSTKPQLAIVTQWC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRI-LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAK--------- 587
Cdd:cd14151    86 EGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED----LTVKIGDFGLATvksrwsgsh 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 588 QLRGENGLLLtpcytanFVAPEVLMQQG---YDAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGNGKFS 660
Cdd:cd14151   162 QFEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNR--DQIIFMVGRGYLS 228
PTZ00284 PTZ00284
protein kinase; Provisional
522-700 2.91e-11

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 66.53  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LLDRILKQKCFSEREASDILYVISKTVDYLHCQ-GVVHRDLKPSNILYMDESASAD------------SIRICDFGFAKQ 588
Cdd:PTZ00284  218 LLDWIMKHGPFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPENILMETSDTVVDpvtnralppdpcRVRICDLGGCCD 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 589 LRGENGLLLTpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPN------------DTPEEILLRIGN 656
Cdd:PTZ00284  298 ERHSRTAIVS---TRHYRSPEVVLGLGWMYSTDMWSMGCIIYELYTGKLLYDTHDNlehlhlmektlgRLPSEWAGRCGT 374
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 657 GKFSL---SGGNW-------------------DNISDGAK-DLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:PTZ00284  375 EEARLlynSAGQLrpctdpkhlariararpvrEVIRDDLLcDLIYGLLHYDRQKRLNARQMTTHPYV 441
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
465-644 3.44e-11

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


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 64.50  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 465 TNMEFAVKIIDK---SKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDrILKQKcfSEREASDIL 541
Cdd:cd05114    27 AQYKVAIKAIREgamSEEDFIEEAKVMMKL-THPKLVQLYGVCTQQKPIYIVTEFMENGCLLN-YLRQR--RGKLSRDML 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTV----DYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKqlrgengLLLTPCYTANFVA--------PE 609
Cdd:cd05114   103 LSMCQDVcegmEYLERNNFIHRDLAARNCLVNDTGV----VKVSDFGMTR-------YVLDDQYTSSSGAkfpvkwspPE 171
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1034674014 610 VLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPN 644
Cdd:cd05114   172 VFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSN 207
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
86-296 4.40e-11

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


Pssm-ID: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 64.70  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVlGQGSFGKVFLVRKKTGPDAGQlYAMKVLKKASLKVRdrvrTKMERDILVEVNHPFIVKLHYAF--QTEG 163
Cdd:cd07867     1 DLFEYEGCKV-GRGTYGHVYKAKRKDGKDEKE-YALKQIEGTGISMS----ACREIALLRELKHPNVIALQKVFlsHSDR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGgDV-----FTRLSKE----VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----DEIGHIK 230
Cdd:cd07867    75 KVWLLFDYAEH-DLwhiikFHRASKAnkkpMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 231 LTDFGLS-------KESVDQEKKAYSFCgtveYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd07867   154 IADMGFArlfnsplKPLADLDPVVVTFW----YRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED 223
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
521-700 4.43e-11

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: 63.82  E-value: 4.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadSIRICDFGfakqlrgeNGLLLTPC 600
Cdd:cd14102    91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTG---ELKLIDFG--------SGALLKDT 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTANF------VAPEVLMQQGYDA-ACDIWSLGVLFYTMLAGYTPFangpnDTPEEILlrigNGKFSLSggnwDNISDGA 673
Cdd:cd14102   160 VYTDFdgtrvySPPEWIRYHRYHGrSATVWSLGVLLYDMVCGDIPF-----EQDEEIL----RGRLYFR----RRVSPEC 226
                         170       180
                  ....*....|....*....|....*..
gi 1034674014 674 KDLLSHMLHMDPHQRYTAEQILKHSWI 700
Cdd:cd14102   227 QQLIKWCLSLRPSDRPTLEQIFDHPWM 253
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
448-639 6.42e-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: 63.44  E-value: 6.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHATTNME--FAVKIIDKSKRDPSEEIEIL-----MRYGQHPNIITLKDVFDdGRYVYLVTDLMKGG 520
Cdd:cd05116     2 ELGSGNFGTVKKGYYQMKKVVktVAVKILKNEANDPALKDELLreanvMQQLDNPYIVRMIGICE-AESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 ELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQLRGENGLLLTPC 600
Cdd:cd05116    81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYA----KISDFGLSKALRADENYYKAQT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034674014 601 ---YTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPF 639
Cdd:cd05116   157 hgkWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPY 199
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
436-657 6.59e-11

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: 63.91  E-value: 6.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYelkedigVGSYsvckrciHATTNMefAVKIIDKSKRDPSEEIEI--LMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05072    17 AGQFGEVW-------MGYY-------NNSTKV--AVKTLKPGTMSVQAFLEEanLMKTLQHDKLVRLYAVVTKEEPIYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDrILKQKCFSE---REASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQLR 590
Cdd:cd05072    81 TEYMAKGSLLD-FLKSDEGGKvllPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMC----KIADFGLARVIE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 591 GENgllltpcYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNG 657
Cdd:cd05072   156 DNE-------YTAregakfpiKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPY---PGMSNSDVMSALQRG 221
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
436-650 7.32e-11

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 63.37  E-value: 7.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYelkedigVGSYSvckrcihatTNMEFAVKIIDKSKRDPSEEIEI--LMRYGQHPNIITLKDVFDDgRYVYLV 513
Cdd:cd05067    17 AGQFGEVW-------MGYYN---------GHTKVAIKSLKQGSMSPDAFLAEanLMKQLQHQRLVRLYAVVTQ-EPIYII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDrILKQKCFSEREAS---DILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLR 590
Cdd:cd05067    80 TEYMENGSLVD-FLKTPSGIKLTINkllDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTL----SCKIADFGLARLIE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 591 GENgllltpcYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtPEEI 650
Cdd:cd05067   155 DNE-------YTAregakfpiKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTN--PEVI 214
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
90-328 7.63e-11

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: 64.34  E-value: 7.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  90 FELLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLKKASLKVRdrvRTKMERDILVEVNHPF-----IVKLHYAFQTEGK 164
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKR---GTNEIVAIKILKNHPSYAR---QGQIEVSILARLSTESaddynFVRAYECFQHKNH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIG----HIKLTDFGlske 239
Cdd:cd14227    91 TCLVFEMLEQNLYdFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFG---- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 240 SVDQEKKAY--SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKlGMPQFLSAEA 317
Cdd:cd14227   167 SASHVSKAVcsTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEYLLSA 245
                         250
                  ....*....|.
gi 1034674014 318 QSLLRMLFKRN 328
Cdd:cd14227   246 GTKTTRFFNRD 256
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
470-657 7.65e-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: 63.36  E-value: 7.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIDK---SKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILK-QKCFSEREASDILYVIS 545
Cdd:cd05113    32 AIKMIKEgsmSEDEFIEEAKVMMNL-SHEKLVQLYGVCTKQRPIFIITEYMANGCLLNYLREmRKRFQTQQLLEMCKDVC 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 546 KTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQ-LRGENGLLLTPCYTANFVAPEVLMQQGYDAACDIWS 624
Cdd:cd05113   111 EAMEYLESKQFLHRDLAARNCLVNDQGV----VKVSDFGLSRYvLDDEYTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWA 186
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1034674014 625 LGVLFYTMLA-GYTPFANGPNdtpEEILLRIGNG 657
Cdd:cd05113   187 FGVLMWEVYSlGKMPYERFTN---SETVEHVSQG 217
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
443-700 8.93e-11

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 63.78  E-value: 8.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYS-VCKRCIHATTNMEFAVKII---DKSKRDPSEEIEILMRYGQHP-----NIITLKDVFDDGRYVYLV 513
Cdd:cd14135     2 YRVYGYLGKGVFSnVVRARDLARGNQEVAIKIIrnnELMHKAGLKELEILKKLNDADpddkkHCIRLLRHFEHKNHLCLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGG--ELLDRILKQKCFSERE----ASDILYVISktvdYLHCQGVVHRDLKPSNILYmdeSASADSIRICDFGFAK 587
Cdd:cd14135    82 FESLSMNlrEVLKKYGKNVGLNIKAvrsyAQQLFLALK----HLKKCNILHADIKPDNILV---NEKKNTLKLCDFGSAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QLrGENGLllTPCYTANFV-APEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFangPNDTPEEIL--------------L 652
Cdd:cd14135   155 DI-GENEI--TPYLVSRFYrAPEIILGLPYDYPIDMWSVGCTLYELYTGKILF---PGKTNNHMLklmmdlkgkfpkkmL 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 653 RIG---------NGKF---------------------------SLSGGNWDNISDGAK------DLLSHMLHMDPHQRYT 690
Cdd:cd14135   229 RKGqfkdqhfdeNLNFiyrevdkvtkkevrrvmsdikptkdlkTLLIGKQRLPDEDRKkllqlkDLLDKCLMLDPEKRIT 308
                         330
                  ....*....|
gi 1034674014 691 AEQILKHSWI 700
Cdd:cd14135   309 PNEALQHPFI 318
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
91-313 1.06e-10

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: 63.47  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  91 ELLKVLGQGSFGK--VFLVRKKtgpDAGQLYAMKvlkKASLKVRDRVRTK-MERDILV--EVNHPFIVKLHYAFQTEGKL 165
Cdd:cd08216     1 ELLYEIGKCFKGGgvVHLAKHK---PTNTLVAVK---KINLESDSKEDLKfLQQEILTsrQLQHPNILPYVTSFVVDNDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGGdvftrlSKEVL--------FTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLS 237
Cdd:cd08216    75 YVVTPLMAYG------SCRDLlkthfpegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDQ-EKKAYSFCGTVE------YMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFqgKDRNETMNMILKAKLG 308
Cdd:cd08216   149 YSMVKHgKRQRVVHDFPKSseknlpWLSPEVLqqNLLGYNEKSDIYSVGITACELANGVVPF--SDMPATQMLLEKVRGT 226

                  ....*
gi 1034674014 309 MPQFL 313
Cdd:cd08216   227 TPQLL 231
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
96-290 1.31e-10

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: 62.71  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  96 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLKKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 171
Cdd:cd14033     9 IGRGSFKTVY---RGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 172 LRGGDVFTRLSKevlFTEEDVKF---YLAELALALDHLHQLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSVDQEK 245
Cdd:cd14033    86 MTSGTLKTYLKR---FREMKLKLlqrWSRQILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRAS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 246 KAYSFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd14033   161 FAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPY 204
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
447-640 1.48e-10

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: 62.37  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 447 EDIGVGSYSVCKRCIHATTN---MEFAVKIIDKSKRDPSEEiEIL-----MRYGQHPNIITLKDVFDdGRYVYLVTDLMK 518
Cdd:cd05060     1 KELGHGNFGSVRKGVYLMKSgkeVEVAVKTLKQEHEKAGKK-EFLreasvMAQLDHPCIVRLIGVCK-GEPLMLVMELAP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDEsasaDSIRICDFGFAKQLRGENGLllt 598
Cdd:cd05060    79 LGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNR----HQAKISDFGMSRALGAGSDY--- 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 599 pcYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFA 640
Cdd:cd05060   152 --YRAttagrwplKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYG 200
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
443-699 1.77e-10

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: 62.77  E-value: 1.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKII--DKSKRDPS----EEIEILMRYgQHPNIITLKDVFDD-----GRY-- 509
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVlmENEKEGFPitalREIKILQLL-KHENVVNLIEICRTkatpyNRYkg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 -VYLVTDLMKGGelLDRILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILymdesASADSI-RICDFGF 585
Cdd:cd07865    93 sIYLVFEFCEHD--LAGLLSNKNvkFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANIL-----ITKDGVlKLADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 586 AKQL-RGENGllLTPCYTANFV-----APEVLM-QQGYDAACDIWSLGVLFYTMLAGYtPFANGPND------------- 645
Cdd:cd07865   166 ARAFsLAKNS--QPNRYTNRVVtlwyrPPELLLgERDYGPPIDMWGAGCIMAEMWTRS-PIMQGNTEqhqltlisqlcgs 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 646 -TPE-----------EILLRIGNGKFSLSGGNWDNISD-GAKDLLSHMLHMDPHQRYTAEQILKHSW 699
Cdd:cd07865   243 iTPEvwpgvdklelfKKMELPQGQKRKVKERLKPYVKDpYALDLIDKLLVLDPAKRIDADTALNHDF 309
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
493-630 1.87e-10

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: 61.98  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 493 QHPNIITLKDVFDDGRYVYLVTDLMKGGELLD--RILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMD 570
Cdd:cd05039    58 RHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVDylRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSE 137
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 571 ESASadsiRICDFGFAK--QLRGENGLLltPcytANFVAPEVLMQQGYDAACDIWSLGVLFY 630
Cdd:cd05039   138 DNVA----KVSDFGLAKeaSSNQDGGKL--P---IKWTAPEALREKKFSTKSDVWSFGILLW 190
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
449-634 2.63e-10

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: 61.72  E-value: 2.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIEI-LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRIL 527
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANMLREVqLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQLLD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 528 KQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIrICDFGFAKQL--RGENGLLLTPCYTANF 605
Cdd:cd14155    81 SNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAV-VGDFGLAEKIpdYSDGKEKLAVVGSPYW 159
                         170       180
                  ....*....|....*....|....*....
gi 1034674014 606 VAPEVLMQQGYDAACDIWSLGVLFYTMLA 634
Cdd:cd14155   160 MAPEVLRGEPYNEKADVFSYGIILCEIIA 188
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
438-694 3.00e-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: 61.47  E-value: 3.00e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYelkedigVGSYSvckrcihATTNMefAVKIIDKSKRDPS---EEIEIlMRYGQHPNIITLKDVFDDgRYVYLVT 514
Cdd:cd14203     7 CFGEVW-------MGTWN-------GTTKV--AIKTLKPGTMSPEaflEEAQI-MKKLRHDKLVQLYAVVSE-EPIYIVT 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLDrILKQ---KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQLRG 591
Cdd:cd14203    69 EFMSKGSLLD-FLKDgegKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVC----KIADFGLARLIED 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENgllLTPCYTANF----VAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNG-KFSLSGGN 665
Cdd:cd14203   144 NE---YTARQGAKFpikwTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPY---PGMNNREVLEQVERGyRMPCPPGC 217
                         250       260
                  ....*....|....*....|....*....
gi 1034674014 666 WDNIsdgaKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd14203   218 PESL----HELMCQCWRKDPEERPTFEYL 242
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
443-633 4.07e-10

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: 61.12  E-value: 4.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKSKRDPSEEIE--ILMRYGQHPNIITLKDVFDDGRYVYLVTDLMkGG 520
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEvaVLKKLQGKPHFCRLIGCGRTERYNYIVMTLL-GP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 521 EL--LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAKQLRGENG-LLL 597
Cdd:cd14017    81 NLaeLRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERTVYILDFGLARQYTNKDGeVER 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 598 TPCYTANFVAPE----VLMQQGYDAAC--DIWSlgvLFYTML 633
Cdd:cd14017   161 PPRNAAGFRGTVryasVNAHRNKEQGRrdDLWS---WFYMLI 199
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
476-694 4.17e-10

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: 61.48  E-value: 4.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 476 KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYvyLVTDLMKGGELlDRILKQkcFSEREAS-------DILYVISKTV 548
Cdd:cd14000    52 KNFRLLRQELTVLSHL-HHPSIVYLLGIGIHPLM--LVLELAPLGSL-DHLLQQ--DSRSFASlgrtlqqRIALQVADGL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 549 DYLHCQGVVHRDLKPSNILYMD-ESASADSIRICDFGFAKQL--RGENGLLLTPcytaNFVAPEVL-MQQGYDAACDIWS 624
Cdd:cd14000   126 RYLHSAMIIYRDLKSHNVLVWTlYPNSAIIIKIADYGISRQCcrMGAKGSEGTP----GFRAPEIArGNVIYNEKVDVFS 201
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 625 LGVLFYTMLAGYTPFANGpNDTPEEillrigngkFSLSGGNWDNISD-------GAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd14000   202 FGMLLYEILSGGAPMVGH-LKFPNE---------FDIHGGLRPPLKQyecapwpEVEVLMKKCWKENPQQRPTAVTV 268
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
476-655 5.54e-10

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: 61.06  E-value: 5.54e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 476 KSKRDPSEEIEILmRYGQHPNIITLKDV-FDDGRY-VYLVTDLMKGGELLDRIlkQKCFSEREASDIL---YVISKTVDY 550
Cdd:cd05081    47 DQQRDFQREIQIL-KALHSDFIVKYRGVsYGPGRRsLRLVMEYLPSGCLRDFL--QRHRARLDASRLLlysSQICKGMEY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 551 LHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQL--RGENGLLLTPCYTANF-VAPEVLMQQGYDAACDIWSLGV 627
Cdd:cd05081   124 LGSRRCVHRDLAARNILVESEA----HVKIADFGLAKLLplDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGV 199
                         170       180
                  ....*....|....*....|....*...
gi 1034674014 628 LFYTMLAgytpFANGPNDTPEEILLRIG 655
Cdd:cd05081   200 VLYELFT----YCDKSCSPSAEFLRMMG 223
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
86-296 5.66e-10

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


Pssm-ID: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 61.61  E-value: 5.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  86 DPAQFELLKVlGQGSFGKVFLVRKKTGPDAGQlYAMKVLKKASLKVRdrvrTKMERDILVEVNHPFIVKLHYAF--QTEG 163
Cdd:cd07868    16 DLFEYEGCKV-GRGTYGHVYKAKRKDGKDDKD-YALKQIEGTGISMS----ACREIALLRELKHPNVISLQKVFlsHADR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 164 KLYLILDFLRGgDV-----FTRLSKE----VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL----DEIGHIK 230
Cdd:cd07868    90 KVWLLFDYAEH-DLwhiikFHRASKAnkkpVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVK 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 231 LTDFGLS-------KESVDQEKKAYSFCgtveYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 296
Cdd:cd07868   169 IADMGFArlfnsplKPLADLDPVVVTFW----YRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED 238
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
479-695 7.97e-10

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: 60.78  E-value: 7.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 479 RDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTV---------- 548
Cdd:cd05088    52 RDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVLETDPAFAIANSTASTLssqqllhfaa 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 549 ------DYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAK----QLRGENGLLltpcyTANFVAPEVLMQQGYDA 618
Cdd:cd05088   132 dvargmDYLSQKQFIHRDLAARNILVGENYVA----KIADFGLSRgqevYVKKTMGRL-----PVRWMAIESLNYSVYTT 202
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 619 ACDIWSLGVLFYTMLA-GYTPFANGpndTPEEILLRIGNGkFSLSGGNwdNISDGAKDLLSHMLHMDPHQRYTAEQIL 695
Cdd:cd05088   203 NSDVWSYGVLLWEIVSlGGTPYCGM---TCAELYEKLPQG-YRLEKPL--NCDDEVYDLMRQCWREKPYERPSFAQIL 274
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
88-332 9.56e-10

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 60.42  E-value: 9.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKK---ASLKVRDRVRTKMERDILVEvnHPFIVKLHYAFQTEGK 164
Cdd:cd14138     5 TEFHELEKIGSGEFGSVFKCVKRLD---GCIYAIKRSKKplaGSVDEQNALREVYAHAVLGQ--HSHVVRYYSAWAEDDH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 165 LYLILDFLRGGDVFTRLSKEV----LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILL---------------DE 225
Cdd:cd14138    80 MLIQNEYCNGGSLADAISENYrimsYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegdeDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 226 IGH----IKLTDFG-LSKESVDQEKKaysfcGTVEYMAPEVVNRR-GHSQSADWWSYGVLMFEMLTGT-LPFQGKDRNET 298
Cdd:cd14138   160 WASnkviFKIGDLGhVTRVSSPQVEE-----GDSRFLANEVLQENyTHLPKADIFALALTVVCAAGAEpLPTNGDQWHEI 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034674014 299 MNMILKAklgMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd14138   235 RQGKLPR---IPQVLSQEFLDLLKVMIHPDPERR 265
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
441-648 1.13e-09

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 60.83  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 441 EVYELKEDIGVGSYSVCKRCIHATTNMEFAVKIIDKS-----KRDPSEEIEILMRYGQhPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEikpaiRNQIIRELQVLHECNS-PYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELlDRILKQkcfSEREASDILYVIS----KTVDYLHCQ-GVVHRDLKPSNILYmdesASADSIRICDFGFAKQLR 590
Cdd:cd06649    84 HMDGGSL-DQVLKE---AKRIPEEILGKVSiavlRGLAYLREKhQIMHRDVKPSNILV----NSRGEIKLCDFGVSGQLI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034674014 591 geNGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFAngPNDTPE 648
Cdd:cd06649   156 --DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIP--PPDAKE 209
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
439-694 1.14e-09

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: 59.82  E-value: 1.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYELKedigvgsysvckrciHATTNMEFAVKIIDKSKRDPSEEIEIL-----MRYGQHPNIITLKDVFDDGryVYLV 513
Cdd:cd14025     9 FGQVYKVR---------------HKHWKTWLAIKCPPSLHVDDSERMELLeeakkMEMAKFRHILPVYGICSEP--VGLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELlDRILKQKCFSEREASDILYVISKTVDYLHCQG--VVHRDLKPSNILYMDESasadSIRICDFGFAKQLRG 591
Cdd:cd14025    72 MEYMETGSL-EKLLASEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHY----HVKISDFGLAKWNGL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 592 ENGLLL---TPCYTANFVAPEVLMQQG--YDAACDIWSLGVLFYTMLAGYTPFANGPNDTpeEILLRIGNG---KFSLSG 663
Cdd:cd14025   147 SHSHDLsrdGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFAGENNIL--HIMVKVVKGhrpSLSPIP 224
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1034674014 664 GNWDNISDGAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd14025   225 RQRPSECQQMICLMKRCWDQDPRKRPTFQDI 255
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
88-356 1.37e-09

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 60.25  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  88 AQFELLKVLGQGSFGKVFLVRKKTGpdAGQLYAMKVLKKAslkvrDRVRTKMERDILV-------EVNHPF-IVKLHYAF 159
Cdd:cd14213    12 ARYEIVDTLGEGAFGKVVECIDHKM--GGMHVAVKIVKNV-----DRYREAARSEIQVlehlnttDPNSTFrCVQMLEWF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 160 QTEGKLYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGH---------- 228
Cdd:cd14213    85 DHHGHVCIVFELLGLSTYdFIKENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYvvkynpkmkr 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 229 ---------IKLTDFGlsKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM 299
Cdd:cd14213   165 dertlknpdIKVVDFG--SATYDDEHHS-TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEHL 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 300 NMILKAKLGMPQFLSAEAQSllRMLFKRN--------PANRLGSEGVEEIKRHLFFANIDWDKLY 356
Cdd:cd14213   242 AMMERILGPLPKHMIQKTRK--RKYFHHDqldwdehsSAGRYVRRRCKPLKEFMLSQDVDHEQLF 304
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
445-660 1.41e-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: 59.66  E-value: 1.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSY-SVCKRCIHAttnmEFAVKIIDKSKRDPSE------EIEILmRYGQHPNIITLKDVFDDGRyVYLVTDLM 517
Cdd:cd14149    16 LSTRIGSGSFgTVYKGKWHG----DVAVKILKVVDPTPEQfqafrnEVAVL-RKTRHVNILLFMGYMTKDN-LAIVTQWC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 518 KGGELLDRI-LKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNIlYMDESAsadSIRICDFGFA--KQLRGENG 594
Cdd:cd14149    90 EGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNI-FLHEGL---TVKIGDFGLAtvKSRWSGSQ 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 595 LLLTPCYTANFVAPEVLMQQG---YDAACDIWSLGVLFYTMLAGYTPFANGPNDtpEEILLRIGNGKFS 660
Cdd:cd14149   166 QVEQPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGELPYSHINNR--DQIIFMVGRGYAS 232
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
439-697 1.62e-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: 59.71  E-value: 1.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElkedigvGSYsvckRCIHATTN-MEFAVKIIDKskrDPSEEIE-------ILMRYGQHPNIITLKDVFDDGRYV 510
Cdd:cd05036    19 FGEVYE-------GTV----SGMPGDPSpLQVAVKTLPE---LCSEQDEmdflmeaLIMSKFNHPNIVRCIGVCFQRLPR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGELLDRILKQKCFSEREAS----DILYV---ISKTVDYLHCQGVVHRDLKPSNILyMDESASADSIRICDF 583
Cdd:cd05036    85 FILLELMAGGDLKSFLRENRPRPEQPSSltmlDLLQLaqdVAKGCRYLEENHFIHRDIAARNCL-LTCKGPGRVAKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQL-------RGENGLLltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILlrig 655
Cdd:cd05036   164 GMARDIyradyyrKGGKAML-----PVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPY---PGKSNQEVM---- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 656 ngKFSLSGGNWD---NISDGAKDLLSHMLHMDPHQRYTAEQILKH 697
Cdd:cd05036   232 --EFVTSGGRMDppkNCPGPVYRIMTQCWQHIPEDRPNFSTILER 274
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
94-333 2.24e-09

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 59.06  E-value: 2.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRK-KTGPDagqlYAMKVLKKASLKVRdrvrtkmeRDILVEVN-------HPFIVKLHYA------- 158
Cdd:cd14036     6 RVIAEGGFAFVYEAQDvGTGKE----YALKRLLSNEEEKN--------KAIIQEINfmkklsgHPNIVQFCSAasigkee 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 159 FQTEGKLYLIL-DFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALALDHLH--QLGIVYRDLKPENILLDEIGHIKLTD 233
Cdd:cd14036    74 SDQGQAEYLLLtELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLCD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 234 FGLSKESVDQEKKAYSFC--GTVE----------YMAPEVVNRRGH---SQSADWWSYGVLMFEMLTGTLPFQ--GKDRn 296
Cdd:cd14036   154 FGSATTEAHYPDYSWSAQkrSLVEdeitrnttpmYRTPEMIDLYSNypiGEKQDIWALGCILYLLCFRKHPFEdgAKLR- 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1034674014 297 etmnmILKAKLGMPQFLSAEA--QSLLRMLFKRNPANRL 333
Cdd:cd14036   233 -----IINAKYTIPPNDTQYTvfHDLIRSTLKVNPEERL 266
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
439-696 2.74e-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: 2.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElkedigvgsySVCKRCIHATTNMEFAVKIIDKSKrDPSEEIEIL-----MRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05061    19 FGMVYE----------GNARDIIKGEAETRVAVKTVNESA-SLRERIEFLneasvMKGFTCHHVVRLLGVVSKGQPTLVV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSE----------REASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDF 583
Cdd:cd05061    88 MELMAHGDLKSYLRSLRPEAEnnpgrppptlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFT----VKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQL-------RGENGLLltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMlagyTPFANGPND--TPEEILlri 654
Cdd:cd05061   164 GMTRDIyetdyyrKGGKGLL-----PVRWMAPESLKDGVFTTSSDMWSFGVVLWEI----TSLAEQPYQglSNEQVL--- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 655 gngKFSLSGGNWD---NISDGAKDLLSHMLHMDPHQRYTAEQILK 696
Cdd:cd05061   232 ---KFVMDGGYLDqpdNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
465-639 4.46e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 59.09  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 465 TNMEFAVKIIDKSKrDPSEEIEILmRYGQHPNIITLKDVFDDGRYVYLVTDLMKGgELLDRILKQKCFSEREASDILYVI 544
Cdd:PHA03207  118 QRKKVIVKAVTGGK-TPGREIDIL-KTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLFTYVDRSGPLPLEQAITIQRRL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 545 SKTVDYLHCQGVVHRDLKPSNIlYMDESASAdsiRICDFGFAKQLRGENGlllTP-CY----TANFVAPEVLMQQGYDAA 619
Cdd:PHA03207  195 LEALAYLHGRGIIHRDVKTENI-FLDEPENA---VLGDFGAACKLDAHPD---TPqCYgwsgTLETNSPELLALDPYCAK 267
                         170       180
                  ....*....|....*....|
gi 1034674014 620 CDIWSLGVLFYTMLAGYTPF 639
Cdd:PHA03207  268 TDIWSAGLVLFEMSVKNVTL 287
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
483-650 4.63e-09

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: 58.37  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 483 EEIEILmRYGQHPNIITLKDVFDD--GRYVYLVTDLMKGGELLDRILKQKCfseREASDILYV--ISKTVDYLHCQGVVH 558
Cdd:cd05080    55 QEIDIL-KTLYHENIVKYKGCCSEqgGKSLQLIMEYVPLGSLRDYLPKHSI---GLAQLLLFAqqICEGMAYLHSQHYIH 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 559 RDLKPSNILYMDESAsadsIRICDFGFAKQLR--------GENGLllTPCYtanFVAPEVLMQQGYDAACDIWSLGVLFY 630
Cdd:cd05080   131 RDLAARNVLLDNDRL----VKIGDFGLAKAVPegheyyrvREDGD--SPVF---WYAPECLKEYKFYYASDVWSFGVTLY 201
                         170       180
                  ....*....|....*....|
gi 1034674014 631 TMLAGYTPFANGPNDTPEEI 650
Cdd:cd05080   202 ELLTHCDSSQSPPTKFLEMI 221
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
470-643 5.28e-09

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: 58.20  E-value: 5.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII-DKSKRDPSEEI---EILMRYGQHPNIITLKDVFDdGRYVYLVTDLMKGGELLDRILKQKcfSEREASDIL---Y 542
Cdd:cd05057    40 AIKVLrEETGPKANEEIldeAYVMASVDHPHLVRLLGICL-SSQVQLITQLMPLGCLLDYVRNHR--DNIGSQLLLnwcV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 543 VISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQL-RGENGLLLTPCYTA-NFVAPEVLMQQGYDAAC 620
Cdd:cd05057   117 QIAKGMSYLEEKRLVHRDLAARNVLV----KTPNHVKITDFGLAKLLdVDEKEYHAEGGKVPiKWMALESIQYRIYTHKS 192
                         170       180
                  ....*....|....*....|....
gi 1034674014 621 DIWSLGVLFYTMLA-GYTPFANGP 643
Cdd:cd05057   193 DVWSYGVTVWELMTfGAKPYEGIP 216
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
470-639 6.40e-09

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: 57.58  E-value: 6.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKII--DKSKRDPSEEIEILMRYgQHPNIITLKDV-FDDGryVYLVTDLMKGGELLDrILKQKCFSEREASDILYV--- 543
Cdd:cd05083    33 AVKNIkcDVTAQAFLEETAVMTKL-QHKNLVRLLGViLHNG--LYIVMELMSKGNLVN-FLRSRGRALVPVIQLLQFsld 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 ISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAK-QLRGENGLLLTPCYTAnfvaPEVLMQQGYDAACDI 622
Cdd:cd05083   109 VAEGMEYLESKKLVHRDLAARNILVSEDGVA----KISDFGLAKvGSMGVDNSRLPVKWTA----PEALKNKKFSSKSDV 180
                         170
                  ....*....|....*...
gi 1034674014 623 WSLGVLFYTMLA-GYTPF 639
Cdd:cd05083   181 WSYGVLLWEVFSyGRAPY 198
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
436-657 1.08e-08

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: 56.96  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 436 AAQFGEVYelkedigVGSYSvckrcihatTNMEFAVKIIDKSKRDPSEEIEI--LMRYGQHPNIITLKDVFDDgRYVYLV 513
Cdd:cd05073    21 AGQFGEVW-------MATYN---------KHTKVAVKTMKPGSMSVEAFLAEanVMKTLQHDKLVKLHAVVTK-EPIYII 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDrILKQKCFSEREAS---DILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLR 590
Cdd:cd05073    84 TEFMAKGSLLD-FLKSDEGSKQPLPkliDFSAQIAEGMAFIEQRNYIHRDLRAANILV----SASLVCKIADFGLARVIE 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 591 GENgllltpcYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNG 657
Cdd:cd05073   159 DNE-------YTAregakfpiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPY---PGMSNPEVIRALERG 224
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
449-638 1.08e-08

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: 57.14  E-value: 1.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSvckrCIHATT--NMEFAVKII--------DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMK 518
Cdd:cd14159     1 IGEGGFG----CVYQAVmrNTEYAVKRLkedseldwSVVKNSFLTEVEKLSRF-RHPNIVDLAGYSAQQGNYCLIYVYLP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 519 GGELLDRILKQK---CFSEREASDILYVISKTVDYLH-CQ-GVVHRDLKPSNILyMDESASAdsiRICDFGFAKQLR--- 590
Cdd:cd14159    76 NGSLEDRLHCQVscpCLSWSQRLHVLLGTARAIQYLHsDSpSLIHGDVKSSNIL-LDAALNP---KLGDFGLARFSRrpk 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 591 --GENGLLL---TPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTP 638
Cdd:cd14159   152 qpGMSSTLArtqTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRA 204
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
443-626 1.11e-08

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: 57.65  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 443 YELKEDIGVGSYSVCKRCIHATTNMEFAVKIIdKSK----RDPSEEIEILM--------RYGQHpnIITLKDVFDDGRYV 510
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKpayfRQAMLEIAILTllntkydpEDKHH--IVRLLDHFMHHGHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMkgGELLDRILKQKCFSEREASDILYVISKTVDYLHC---QGVVHRDLKPSNILyMDESASADsIRICDFGFAK 587
Cdd:cd14212    78 CIVFELL--GVNLYELLKQNQFRGLSLQLIRKFLQQLLDALSVlkdARIIHCDLKPENIL-LVNLDSPE-IKLIDFGSAC 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1034674014 588 QlrgENGLLLTPCYTANFVAPEVLMQQGYDAACDIWSLG 626
Cdd:cd14212   154 F---ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLG 189
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
452-708 1.20e-08

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: 56.85  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 452 GSYSVCKRCIHATTNMEFAVK-------IIDKSKRDPSEEIEILMRyGQHPNIITLKDVFDDGRYVYLVTDLMKGGELlD 524
Cdd:cd14026     8 GAFGTVSRARHADWRVTVAIKclkldspVGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGIVTEYMTNGSL-N 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RILKQK--------CFSEReasdILYVISKTVDYLHCQG--VVHRDLKPSNILYMDESasadSIRICDFGFAK------- 587
Cdd:cd14026    86 ELLHEKdiypdvawPLRLR----ILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEF----HVKIADFGLSKwrqlsis 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 588 QLRGENGLLLTPcyTANFVAPEVL---MQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNdtPEEILlrigngkFSLSGG 664
Cdd:cd14026   158 QSRSSKSAPEGG--TIIYMPPEEYepsQKRRASVKHDIYSYAIIMWEVLSRKIPFEEVTN--PLQIM-------YSVSQG 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 665 NWDNISDGAkdllshmLHMDPHQRYTAEQILKHSWITHRDQLPN 708
Cdd:cd14026   227 HRPDTGEDS-------LPVDIPHRATLINLIESGWAQNPDERPS 263
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
431-644 1.88e-08

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: 56.57  E-value: 1.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 431 QINGNAAQFGEvyELKED-IGvgsySVCKRCIHATTNME----FAVKII-DKSKRDPSEEI--EILMRYG-QHPNIITLK 501
Cdd:cd05091     2 EINLSAVRFME--ELGEDrFG----KVYKGHLFGTAPGEqtqaVAIKTLkDKAEGPLREEFrhEAMLRSRlQHPNIVCLL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 502 DVFDDGRYVYLVTDLMKGGELL-----------------DRILKqkcfSEREASDILYVISKT---VDYLHCQGVVHRDL 561
Cdd:cd05091    76 GVVTKEQPMSMIFSYCSHGDLHeflvmrsphsdvgstddDKTVK----STLEPADFLHIVTQIaagMEYLSSHHVVHKDL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 562 KPSNILYMDESasadSIRICDFGFAKQLRGEN--GLLLTPCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTP 638
Cdd:cd05091   152 ATRNVLVFDKL----NVKISDLGLFREVYAADyyKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQP 227

                  ....*.
gi 1034674014 639 FANGPN 644
Cdd:cd05091   228 YCGYSN 233
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
542-639 2.52e-08

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: 56.55  E-value: 2.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQL--------RGENGLLLtpcytaNFVAPEVLMQ 613
Cdd:cd14207   187 FQVARGMEFLSSRKCIHRDLAARNILLSENNV----VKICDFGLARDIyknpdyvrKGDARLPL------KWMAPESIFD 256
                          90       100
                  ....*....|....*....|....*..
gi 1034674014 614 QGYDAACDIWSLGVLFYTMLA-GYTPF 639
Cdd:cd14207   257 KIYSTKSDVWSYGVLLWEIFSlGASPY 283
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
449-628 2.65e-08

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: 55.98  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTN----MEFAVKIIDKSKRDPSEEIEiLMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGeLLD 524
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGevmvMKELIRFDEEAQRNFLKEVK-VMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG-TLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RILKQKC--FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTPC-- 600
Cdd:cd14154    79 DVLKDMArpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDK----TVVVADFGLARLIVEERLPSGNMSps 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 601 --------------YTA----NFVAPEVLMQQGYDAACDIWSLGVL 628
Cdd:cd14154   155 etlrhlkspdrkkrYTVvgnpYWMAPEMLNGRSYDEKVDIFSFGIV 200
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
510-651 3.72e-08

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: 55.80  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELLDRILKQKcfsEREASDILY----VISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGF 585
Cdd:cd05108    83 VQLITQLMPFGCLLDYVREHK---DNIGSQYLLnwcvQIAKGMNYLEDRRLVHRDLAARNVLV----KTPQHVKITDFGL 155
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034674014 586 AKQLRGENgllltPCYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNDTPEEIL 651
Cdd:cd05108   156 AKLLGAEE-----KEYHAEggkvpikWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEISSIL 224
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
473-708 4.00e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 56.16  E-value: 4.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 473 IIDKSKRDPSEEIEILMRYGQHPNIITLKDVFDDGRYVYLV-----TDLMkgGELLDRILKQKCfsereasDILYV---I 544
Cdd:PHA03212  121 VIKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLIlprykTDLY--CYLAAKRNIAIC-------DILAIersV 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 545 SKTVDYLHCQGVVHRDLKPSNIlYMDESASadsirIC--DFGFA--------KQLRGENGLLLTPcytanfvAPEVLMQQ 614
Cdd:PHA03212  192 LRAIQYLHENRIIHRDIKAENI-FINHPGD-----VClgDFGAAcfpvdinaNKYYGWAGTIATN-------APELLARD 258
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 615 GYDAACDIWSLGVLFYTMLAGY------------------------------TPFANGPNDTPEEILLRIGNgKFSLSGG 664
Cdd:PHA03212  259 PYGPAVDIWSAGIVLFEMATCHdslfekdgldgdcdsdrqikliirrsgthpNEFPIDAQANLDEIYIGLAK-KSSRKPG 337
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1034674014 665 N---WDNISDGAKD---LLSHMLHMDPHQRYTAEQILKHS-WITHRDQLPN 708
Cdd:PHA03212  338 SrplWTNLYELPIDleyLICKMLAFDAHHRPSAEALLDFAaFQDIPDPYPN 388
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
466-694 4.17e-08

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 55.46  E-value: 4.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 466 NMEFAVKIIDKSKRDPS---EEIEIlMRYGQHPNIITLKDVFDDgRYVYLVTDLMKGGELLDrILKQ---KCFSEREASD 539
Cdd:cd05070    33 NTKVAIKTLKPGTMSPEsflEEAQI-MKKLKHDKLVQLYAVVSE-EPIYIVTEYMSKGSLLD-FLKDgegRALKLPNLVD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 540 ILYVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLR-GENGLLLTPCYTANFVAPEVLMQQGYDA 618
Cdd:cd05070   110 MAAQVAAGMAYIERMNYIHRDLRSANILV----GNGLICKIADFGLARLIEdNEYTARQGAKFPIKWTAPEAALYGRFTI 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 619 ACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNGkFSLSGGNWDNISdgAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd05070   186 KSDVWSFGILLTELVTkGRVPY---PGMNNREVLEQVERG-YRMPCPQDCPIS--LHELMIHCWKKDPEERPTFEYL 256
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
488-645 5.19e-08

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: 54.81  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 488 LMRYGQHPNIITLKDV-FDDGRYVyLVTDLMKGGELLDRILKQKCFSEREASDILYVISKTVdYLHCQGVVHRDLKPSNI 566
Cdd:cd14027    44 MMNRLRHSRVVKLLGViLEEGKYS-LVMEYMEKGNLMHVLKKVSVPLSVKGRIILEIIEGMA-YLHGKGVIHKDLKPENI 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 567 LyMDESAsadSIRICDFGFA-------------KQLRGENGLLLTPCYTANFVAPEVL--MQQGYDAACDIWSLGVLFYT 631
Cdd:cd14027   122 L-VDNDF---HIKIADLGLAsfkmwskltkeehNEQREVDGTAKKNAGTLYYMAPEHLndVNAKPTEKSDVYSFAIVLWA 197
                         170
                  ....*....|....
gi 1034674014 632 MLAGYTPFANGPND 645
Cdd:cd14027   198 IFANKEPYENAINE 211
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
449-629 5.32e-08

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: 54.96  E-value: 5.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTN----MEFAVKIIDKSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLD 524
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGevmvMKELIRFDEETQRTFLKEVKV-MRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RI--LKQKC-FSERE--ASDIlyviSKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTP 599
Cdd:cd14221    80 IIksMDSHYpWSQRVsfAKDI----ASGMAYLHSMNIIHRDLNSHNCLVRENK----SVVVADFGLARLMVDEKTQPEGL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1034674014 600 C----------YTA----NFVAPEVLMQQGYDAACDIWSLGVLF 629
Cdd:cd14221   152 RslkkpdrkkrYTVvgnpYWMAPEMINGRSYDEKVDVFSFGIVL 195
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
445-630 6.57e-08

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: 54.78  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSY-----SVCKRCIHATTNMEFAVKII-----DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVT 514
Cdd:cd05049     9 LKRELGEGAFgkvflGECYNLEPEQDKMLVAVKTLkdassPDARKDFEREAELLTNL-QHENIVKFYGVCTEGDPLLMVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 515 DLMKGGELLD---------RILKQKCFSERE--ASDILYV---ISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRI 580
Cdd:cd05049    88 EYMEHGDLNKflrshgpdaAFLASEDSAPGEltLSQLLHIavqIASGMVYLASQHFVHRDLATRNCLV----GTNLVVKI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 581 CDFGFAKQLRGEN-----GLLLTPcytANFVAPEVLMQQGYDAACDIWSLGVLFY 630
Cdd:cd05049   164 GDFGMSRDIYSTDyyrvgGHTMLP---IRWMPPESILYRKFTTESDVWSFGVVLW 215
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
544-695 7.08e-08

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: 54.76  E-value: 7.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 ISKTVDYLHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQL---------RGENGLLltpcytaNFVAPEVLMQQ 614
Cdd:cd05043   125 IACGMSYLHRRGVIHKDIAARNCVIDDEL----QVKITDNALSRDLfpmdyhclgDNENRPI-------KWMSLESLVNK 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 615 GYDAACDIWSLGVLFYTMLA-GYTPFAngpNDTPEEILLRIGNGkFSLSGGNwdNISDGAKDLLSHMLHMDPHQRYTAEQ 693
Cdd:cd05043   194 EYSSASDVWSFGVLLWELMTlGQTPYV---EIDPFEMAAYLKDG-YRLAQPI--NCPDELFAVMACCWALDPEERPSFQQ 267

                  ..
gi 1034674014 694 IL 695
Cdd:cd05043   268 LV 269
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
470-694 7.34e-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: 54.69  E-value: 7.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIDKSKRDPS---EEIEIlMRYGQHPNIITLKDVFDDgRYVYLVTDLMKGGELLDrILKQ---KCFSEREASDILYV 543
Cdd:cd05069    40 AIKTLKPGTMMPEaflQEAQI-MKKLRHDKLVPLYAVVSE-EPIYIVTEFMGKGSLLD-FLKEgdgKYLKLPQLVDMAAQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 ISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLMQQG 615
Cdd:cd05069   117 IADGMAYIERMNYIHRDLRAANILVGDNLVC----KIADFGLARLIEDNE-------YTArqgakfpiKWTAPEAALYGR 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 616 YDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEILLRIGNG-KFSLSGGnwdnISDGAKDLLSHMLHMDPHQRYTAEQ 693
Cdd:cd05069   186 FTIKSDVWSFGILLTELVTkGRVPY---PGMVNREVLEQVERGyRMPCPQG----CPESLHELMKLCWKKDPDERPTFEY 258

                  .
gi 1034674014 694 I 694
Cdd:cd05069   259 I 259
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
465-691 8.77e-08

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: 54.09  E-value: 8.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 465 TNMEFAVKIIDKSKRDPSEEIEILMRygQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQkcFSEREASDILYVI 544
Cdd:cd05576    23 TQETFILKGLRKSSEYSRERKTIIPR--CVPNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKF--LNDKEIHQLFADL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 545 SK------------------------TVDYLHCQGVVHRDLKPSNILYMDesasADSIRICDFG----FAKQLRGEngll 596
Cdd:cd05576    99 DErlaaasrfyipeeciqrwaaemvvALDALHREGIVCRDLNPNNILLND----RGHIQLTYFSrwseVEDSCDSD---- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 597 ltpCYTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLAGYTPFANGPNDTpeeillrigNGKFSLSGGNWdnISDGAKDL 676
Cdd:cd05576   171 ---AIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHPAGI---------NTHTTLNIPEW--VSEEARSL 236
                         250
                  ....*....|....*
gi 1034674014 677 LSHMLHMDPHQRYTA 691
Cdd:cd05576   237 LQQLLQFNPTERLGA 251
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
540-638 1.60e-07

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: 53.43  E-value: 1.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 540 ILYVISKTVDYLHCQGVVHRDLKPSNILYMD-ESASADSIRICDFGFAKQL--RGENGLLLTPCYTANFVAPEVLmqqgY 616
Cdd:cd14067   119 IAYQIAAGLAYLHKKNIIFCDLKSDNILVWSlDVQEHINIKLSDYGISRQSfhEGALGVEGTPGYQAPEIRPRIV----Y 194
                          90       100
                  ....*....|....*....|..
gi 1034674014 617 DAACDIWSLGVLFYTMLAGYTP 638
Cdd:cd14067   195 DEKVDMFSYGMVLYELLSGQRP 216
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
488-639 2.49e-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: 53.09  E-value: 2.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 488 LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLDRILKQK------CFSEREAS--------DILYV---ISKTVDY 550
Cdd:cd05090    60 LMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSphsdvgCSSDEDGTvkssldhgDFLHIaiqIAAGMEY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 551 LHCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGENGLLLTP--CYTANFVAPEVLMQQGYDAACDIWSLGVL 628
Cdd:cd05090   140 LSSHFFVHKDLAARNILVGEQL----HVKISDLGLSREIYSSDYYRVQNksLLPIRWMPPEAIMYGKFSSDSDIWSFGVV 215
                         170
                  ....*....|..
gi 1034674014 629 FYTMLA-GYTPF 639
Cdd:cd05090   216 LWEIFSfGLQPY 227
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
484-654 2.55e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 53.93  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 484 EIEIL-MRYGQHPNIITLKDVFDDGRYVYLVT-----DL---MKGGEL--LDR-ILKQkcfsereASDILYVISKTVDYL 551
Cdd:PHA03210  211 ENEILaLGRLNHENILKIEEILRSEANTYMITqkydfDLysfMYDEAFdwKDRpLLKQ-------TRAIMKQLLCAVEYI 283
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 552 HCQGVVHRDLKPSNILYMDESasadSIRICDFGFAKQLRGEN-----GLLLTpcYTANfvAPEVLMQQGYDAACDIWSLG 626
Cdd:PHA03210  284 HDKKLIHRDIKLENIFLNCDG----KIVLGDFGTAMPFEKEReafdyGWVGT--VATN--SPEILAGDGYCEITDIWSCG 355
                         170       180
                  ....*....|....*....|....*...
gi 1034674014 627 VLFYTMLAGYTPFANGPNDTPEEILLRI 654
Cdd:PHA03210  356 LILLDMLSHDFCPIGDGGGKPGKQLLKI 383
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
439-639 2.60e-07

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 52.88  E-value: 2.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElKEDIGVGSYSVCKrcihattnmEFAVKIIdKSKRDPSE------EIEILMRYGQHPNIITLKDV-FDDGRYVY 511
Cdd:cd05054    20 FGKVIQ-ASAFGIDKSATCR---------TVAVKML-KEGATASEhkalmtELKILIHIGHHLNVVNLLGAcTKPGGPLM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 512 LVTDLMKGGELLDRI-LKQKCFS-----------EREASDILY--------------VISKTVDYLHCQGVVHRDLKPSN 565
Cdd:cd05054    89 VIVEFCKFGNLSNYLrSKREEFVpyrdkgardveEEEDDDELYkepltledlicysfQVARGMEFLASRKCIHRDLAARN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 566 ILYMDESAsadsIRICDFGFAKQLRGEngllltPCYTAN--------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GY 636
Cdd:cd05054   169 ILLSENNV----VKICDFGLARDIYKD------PDYVRKgdarlplkWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGA 238

                  ...
gi 1034674014 637 TPF 639
Cdd:cd05054   239 SPY 241
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
439-630 3.19e-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: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElKEDIGVGSYSVCkrcihattnMEFAVKIID-----KSKRDPSEEIEiLMRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05048    18 FGKVYK-GELLGPSSEESA---------ISVAIKTLKenaspKTQQDFRREAE-LMSDLQHPNIVCLLGVCTKEQPQCML 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASD----------------ILYVISKTVDYLHCQGVVHRDLKPSNILYMDESasadS 577
Cdd:cd05048    87 FEYMAHGDLHEFLVRHSPHSDVGVSSdddgtassldqsdflhIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGL----T 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 578 IRICDFGFAKQLrgengllltpcYTANF-------------VAPEVLMQQGYDAACDIWSLGVLFY 630
Cdd:cd05048   163 VKISDFGLSRDI-----------YSSDYyrvqsksllpvrwMPPEAILYGKFTTESDVWSFGVVLW 217
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
542-639 3.19e-07

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: 53.06  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 542 YVISKTVDYLHCQGVVHRDLKPSNILyMDESasaDSIRICDFGFAKQL--------RGENGLLLtpcytaNFVAPEVLMQ 613
Cdd:cd05102   179 FQVARGMEFLASRKCIHRDLAARNIL-LSEN---NVVKICDFGLARDIykdpdyvrKGSARLPL------KWMAPESIFD 248
                          90       100
                  ....*....|....*....|....*..
gi 1034674014 614 QGYDAACDIWSLGVLFYTMLA-GYTPF 639
Cdd:cd05102   249 KVYTTQSDVWSFGVLLWEIFSlGASPY 275
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
494-691 3.45e-07

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: 52.88  E-value: 3.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 494 HPNIITLKDVFDD---------------------------GRYVYLVtdlMKG-GELLDRILKQKCFSEREASDILYVIS 545
Cdd:cd14018    72 HPNIIRVQRAFTDsvpllpgaiedypdvlparlnpsglghNRTLFLV---MKNyPCTLRQYLWVNTPSYRLARVMILQLL 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 546 KTVDYLHCQGVVHRDLKPSNILYMDESASADSIRICDFGFAK-------QL--------RGENGLLLTPCYTANFVAPEV 610
Cdd:cd14018   149 EGVDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCCLaddsiglQLpfsswyvdRGGNACLMAPEVSTAVPGPGV 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 611 LMQqgYDAAcDIWSLGVLFYTMLAGYTPF-----ANGPNDTPEEILLRigngkfSLSggnwDNISDGAKDLLSHMLHMDP 685
Cdd:cd14018   229 VIN--YSKA-DAWAVGAIAYEIFGLSNPFyglgdTMLESRSYQESQLP------ALP----SAVPPDVRQVVKDLLQRDP 295

                  ....*.
gi 1034674014 686 HQRYTA 691
Cdd:cd14018   296 NKRVSA 301
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
449-629 3.51e-07

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: 52.25  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 449 IGVGSYSVCKRCIHATTN----MEFAVKIIDKSKRDPSEEIEIlMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGELLD 524
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGkvmvMKELIRCDEETQKTFLTEVKV-MRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 525 RILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILY-MDESASadsirICDFGFA----------------- 586
Cdd:cd14222    80 FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIkLDKTVV-----VADFGLSrliveekkkpppdkptt 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034674014 587 -KQLRGENGLLLTPCYTAN--FVAPEVLMQQGYDAACDIWSLGVLF 629
Cdd:cd14222   155 kKRTLRKNDRKKRYTVVGNpyWMAPEMLNGKSYDEKVDIFSFGIVL 200
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
464-651 3.78e-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: 52.76  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 464 TTNMEFAVKIIDKSKrDPSEEIE-----ILMRYGQHPNIITLKDVFDDGRyVYLVTDLMKGGELLDRILKQKcfsEREAS 538
Cdd:cd05110    34 TVKIPVAIKILNETT-GPKANVEfmdeaLIMASMDHPHLVRLLGVCLSPT-IQLVTQLMPHGCLLDYVHEHK---DNIGS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 DILY----VISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENGLlltpcYTAN-------FVA 607
Cdd:cd05110   109 QLLLnwcvQIAKGMMYLEERRLVHRDLAARNVLV----KSPNHVKITDFGLARLLEGDEKE-----YNADggkmpikWMA 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1034674014 608 PEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNDTPEEIL 651
Cdd:cd05110   180 LECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLL 224
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
482-639 7.46e-07

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 51.34  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 482 SEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTDLMKGGELlDRILKQKcfSEREAS-------DILYVISKTVDYLH-- 552
Cdd:cd14664    38 QAEIQTLGMI-RHRNIVRLRGYCSNPTTNLLVYEYMPNGSL-GELLHSR--PESQPPldwetrqRIALGSARGLAYLHhd 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 553 CQG-VVHRDLKPSNILyMDESASAdsiRICDFGFAKQLRGENGLLLTPCY-TANFVAPEVLMQQGYDAACDIWSLGVLFY 630
Cdd:cd14664   114 CSPlIIHRDVKSNNIL-LDEEFEA---HVADFGLAKLMDDKDSHVMSSVAgSYGYIAPEYAYTGKVSEKSDVYSYGVVLL 189

                  ....*....
gi 1034674014 631 TMLAGYTPF 639
Cdd:cd14664   190 ELITGKRPF 198
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
89-332 7.58e-07

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: 51.47  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAFQT 161
Cdd:cd14139     1 EFLELEKIGVGEFGSVYKCIKRLD---GCVYAIKRSMRPFAGSSN------EQLALHEVyahavlgHHPHVVRYYSAWAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKEV----LFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILldeIGHiKLTDFGLS 237
Cdd:cd14139    72 DDHMIIQNEYCNGGSLQDAISENTksgnHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIF---ICH-KMQSSSGV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 238 KESVDQEKKAYSFCGTV----------------------EYMAPEVVNRR-GHSQSADWWSYGvLMFEMLTGT--LPFQG 292
Cdd:cd14139   148 GEEVSNEEDEFLSANVVykigdlghvtsinkpqveegdsRFLANEILQEDyRHLPKADIFALG-LTVALAAGAepLPTNG 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1034674014 293 KDRNEtmnmILKAKL-GMPQFLSAEAQSLLRMLFKRNPANR 332
Cdd:cd14139   227 AAWHH----IRKGNFpDVPQELPESFSSLLKNMIQPDPEQR 263
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
470-655 8.11e-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: 51.50  E-value: 8.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIdKSKRDPSEEIEILMRYG-----QHPNIITLKDVFDDGRYVYLVTDLMKGGEL---LDRILKQKC-----FSERE 536
Cdd:cd05045    34 AVKML-KENASSSELRDLLSEFNllkqvNHPHVIKLYGACSQDGPLLLIVEYAKYGSLrsfLRESRKVGPsylgsDGNRN 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 537 AS-------------DIL---YVISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGFAKQLRGENGLL---- 596
Cdd:cd05045   113 SSyldnpderaltmgDLIsfaWQISRGMQYLAEMKLVHRDLAARNVLV----AEGRKMKISDFGLSRDVYEEDSYVkrsk 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034674014 597 -LTPcytANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFangPNDTPEEI--LLRIG 655
Cdd:cd05045   189 gRIP---VKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY---PGIAPERLfnLLKTG 245
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
89-224 1.04e-06

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: 50.87  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  89 QFELLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLKKASLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAFQT 161
Cdd:cd14051     1 EFHEVEKIGSGEFGSVYKCINRLD---GCVYAIKKSKKPVAGSVD------EQNALNEVyahavlgKHPHVVRYYSAWAE 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034674014 162 EGKLYLILDFLRGGDVFTRLSKE----VLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLD 224
Cdd:cd14051    72 DDHMIIQNEYCNGGSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFIS 138
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
487-639 1.20e-06

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: 50.55  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 487 ILMRYGQHPNIITLKDV-FDDGRYVYLVTDLMKGGELLDRILKQKcfSEREASDIL---YVISKTVDYLHCQGVVHRDLK 562
Cdd:cd05058    48 IIMKDFSHPNVLSLLGIcLPSEGSPLVVLPYMKHGDLRNFIRSET--HNPTVKDLIgfgLQVAKGMEYLASKKFVHRDLA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 563 PSNILyMDESASadsIRICDFGFAKQL--------RGENGLLLTpcytANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA 634
Cdd:cd05058   126 ARNCM-LDESFT---VKVADFGLARDIydkeyysvHNHTGAKLP----VKWMALESLQTQKFTTKSDVWSFGVLLWELMT 197

                  ....*.
gi 1034674014 635 -GYTPF 639
Cdd:cd05058   198 rGAPPY 203
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
148-337 1.37e-06

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


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 51.10  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 148 NHPFIVKLHYAFQTEGKLYLILDFLRGGDvftrlSKEVLFT-------EEDVKFYLAELALALDHLHQLGIVYRDLKPEN 220
Cdd:cd08227    57 NHPNIVPYRATFIADNELWVVTSFMAYGS-----AKDLICThfmdgmsELAIAYILQGVLKALDYIHHMGYVHRSVKASH 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 221 ILLDEIGHIKLTDF--GLSKESVDQEKKA------YSfCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPF 290
Cdd:cd08227   132 ILISVDGKVYLSGLrsNLSMINHGQRLRVvhdfpkYS-VKVLPWLSPEVLqqNLQGYDAKSDIYSVGITACELANGHVPF 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 291 qgKDRNETMNMILKAKLGMPQFLSAEA--QSLLRMLFKRNPANRLGSEG 337
Cdd:cd08227   211 --KDMPATQMLLEKLNGTVPCLLDTTTipAEELTMKPSRSGANSGLGES 257
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
488-657 1.48e-06

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: 50.46  E-value: 1.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 488 LMRYGQHPNIITLKDVFDDgRYVYLVTDLMKGGELLDRILKQ--KCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSN 565
Cdd:cd05071    57 VMKKLRHEKLVQLYAVVSE-EPIYIVTEYMSKGSLLDFLKGEmgKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAAN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 566 ILYMDESASadsiRICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GY 636
Cdd:cd05071   136 ILVGENLVC----KVADFGLARLIEDNE-------YTArqgakfpiKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGR 204
                         170       180
                  ....*....|....*....|.
gi 1034674014 637 TPFangPNDTPEEILLRIGNG 657
Cdd:cd05071   205 VPY---PGMVNREVLDQVERG 222
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
94-336 1.58e-06

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 50.33  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014  94 KVLGQGSFGKVFLVRKKTGpdagqLYAMKVLKK--ASLKVRDRV-RTKMERDILVEVNH--PF---IVKLHYAfqtegkl 165
Cdd:cd13980     6 KSLGSTRFLKVARARHDEG-----LVVVKVFVKpdPALPLRSYKqRLEEIRDRLLELPNvlPFqkvIETDKAA------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 166 YLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHQLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 245
Cdd:cd13980    74 YLIRQYVKY-NLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTYLPED 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 246 KAYSF-----------CgtveYMAPE----------VVNRRG--HSQSADWWSYGVLMFEMLT-GTLPFqgkdrneTMNM 301
Cdd:cd13980   153 NPADFsyffdtsrrrtC----YIAPErfvdaltldaESERRDgeLTPAMDIFSLGCVIAELFTeGRPLF-------DLSQ 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1034674014 302 ILKAKLG---MPQFLSA----EAQSLLRMLFKRNPANRLGSE 336
Cdd:cd13980   222 LLAYRKGefsPEQVLEKiedpNIRELILHMIQRDPSKRLSAE 263
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
448-639 2.42e-06

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: 49.94  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 448 DIGVGSYSVCKRCIHA--TTNMEFAVKII----DKSKRDPSEEIEILMRYGQHPNIITLKDVFDdGRYVYLVTDLMKGGE 521
Cdd:cd05115    11 ELGSGNFGCVKKGVYKmrKKQIDVAIKVLkqgnEKAVRDEMMREAQIMHQLDNPYIVRMIGVCE-AEALMLVMEMASGGP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 522 LlDRIL--KQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILYMDESASadsiRICDFGFAKQLRGENGLlltp 599
Cdd:cd05115    90 L-NKFLsgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYA----KISDFGLSKALGADDSY---- 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1034674014 600 cYTA--------NFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPF 639
Cdd:cd05115   161 -YKArsagkwplKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
510-648 2.44e-06

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: 50.02  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 510 VYLVTDLMKGGELLDRILKQKcfsEREASDILY----VISKTVDYLHCQGVVHRDLKPSNILYmdesASADSIRICDFGF 585
Cdd:cd05109    83 VQLVTQLMPYGCLLDYVRENK---DRIGSQDLLnwcvQIAKGMSYLEEVRLVHRDLAARNVLV----KSPNHVKITDFGL 155
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 586 AKQLRGENGLlltpcYTAN-------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGP-NDTPE 648
Cdd:cd05109   156 ARLLDIDETE-----YHADggkvpikWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPaREIPD 222
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
438-632 2.90e-06

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: 49.74  E-value: 2.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYELKEDigvgsysvckrcihattNMEFAVKIID-KSKRDPSEEIEI----LMRygqHPNIITL----KDVFDDGR 508
Cdd:cd13998     7 RFGEVWKASLK-----------------NEPVAVKIFSsRDKQSWFREKEIyrtpMLK---HENILQFiaadERDTALRT 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 509 YVYLVTDLMKGGELLDrILKQKCFSEREASDILYVISKTVDYLH-----CQG----VVHRDLKPSNILYMDESASAdsir 579
Cdd:cd13998    67 ELWLVTAFHPNGSL*D-YLSLHTIDWVSLCRLALSVARGLAHLHseipgCTQgkpaIAHRDLKSKNILVKNDGTCC---- 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034674014 580 ICDFGFAkqLRGENGLLLTP------CYTANFVAPEVL---MQQGYDAAC---DIWSLGVLFYTM 632
Cdd:cd13998   142 IADFGLA--VRLSPSTGEEDnanngqVGTKRYMAPEVLegaINLRDFESFkrvDIYAMGLVLWEM 204
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
470-633 4.86e-06

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: 49.19  E-value: 4.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIDkSKRDPS--EEIEI----LMRygqHPNIITL--KDVFDDGRY--VYLVTDLMKGGELLDrILKQKCFSEREASD 539
Cdd:cd14056    22 AVKIFS-SRDEDSwfRETEIyqtvMLR---HENILGFiaADIKSTGSWtqLWLITEYHEHGSLYD-YLQRNTLDTEEALR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 540 ILYVISKTVDYLHCQ--------GVVHRDLKPSNILYMDESASAdsirICDFGFAkqLRGENGLLLTP------CYTANF 605
Cdd:cd14056    97 LAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCC----IADLGLA--VRYDSDTNTIDippnprVGTKRY 170
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1034674014 606 VAPEVLMQQ-------GYDAAcDIWSLGVLFYTML 633
Cdd:cd14056   171 MAPEVLDDSinpksfeSFKMA-DIYSFGLVLWEIA 204
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
445-630 5.79e-06

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: 48.81  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSY-----SVCKRCIHATTNMEFAVKII----DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05092     9 LKWELGEGAFgkvflAECHNLLPEQDKMLVAVKALkeatESARQDFQREAELLTVL-QHQHIVRFYGVCTEGEPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELlDRILKQ-----KCFSEREA--------SDILYVISKTVD---YLHCQGVVHRDLKPSNILYMDESAsadsIR 579
Cdd:cd05092    88 YMRHGDL-NRFLRShgpdaKILDGGEGqapgqltlGQMLQIASQIASgmvYLASLHFVHRDLATRNCLVGQGLV----VK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 580 ICDFGFAKQLRGEN-----GLLLTPCytaNFVAPEVLMQQGYDAACDIWSLGVLFY 630
Cdd:cd05092   163 IGDFGMSRDIYSTDyyrvgGRTMLPI---RWMPPESILYRKFTTESDIWSFGVVLW 215
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
445-650 7.39e-06

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: 48.47  E-value: 7.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSY-----SVCKRCIHATTNMEFAVKIID----KSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05094     9 LKRELGEGAFgkvflAECYNLSPTKDKMLVAVKTLKdptlAARKDFQREAELLTNL-QHDHIVKFYGVCGDGDPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELlDRILK--------------QKCFSEREASDILYVISKTVD---YLHCQGVVHRDLKPSNILYmdesASADSI 578
Cdd:cd05094    88 YMKHGDL-NKFLRahgpdamilvdgqpRQAKGELGLSQMLHIATQIASgmvYLASQHFVHRDLATRNCLV----GANLLV 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034674014 579 RICDFGFAKQLRGEN-----GLLLTPCytaNFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTP-FANGPNDTPEEI 650
Cdd:cd05094   163 KIGDFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPwFQLSNTEVIECI 238
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
502-635 9.20e-06

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: 48.12  E-value: 9.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 502 DVFDDGRYvyLVTDLMKGGELLDRILKQKCFSEREASDIL-----YVISKTVDYLHCQGVVHRDLKPSNILYMDE----- 571
Cdd:cd13981    70 HLFQDESI--LVMDYSSQGTLLDVVNKMKNKTGGGMDEPLamfftIELLKVVEALHEVGIIHGDIKPDNFLLRLEicadw 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034674014 572 ------SASADSIRICDFGFAKQLR--GENGLLLTPCYTANFVAPEvlMQQG----YDAacDIWSLGVLFYTMLAG 635
Cdd:cd13981   148 pgegenGWLSKGLKLIDFGRSIDMSlfPKNQSFKADWHTDSFDCIE--MREGrpwtYQI--DYFGIAATIHVMLFG 219
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
424-662 1.59e-05

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: 47.46  E-value: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 424 ANVLPIVQINgnAAQFGEVYelkedigvgsysVCKRCIHATTNME--FAVKIIDKSKRDPS-----EEIEILMRYgQHPN 496
Cdd:cd05046     5 SNLQEITTLG--RGEFGEVF------------LAKAKGIEEEGGEtlVLVKALQKTKDENLqsefrRELDMFRKL-SHKN 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 497 IITLKDVFDDGRYVYLVTDLMKGGEL---------LDRILKQKCFSEREASDILYVISKTVDYLHCQGVVHRDLKPSN-I 566
Cdd:cd05046    70 VVRLLGLCREAEPHYMILEYTDLGDLkqflratksKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNcL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 567 LYMDESASADSIRICDFGFAKQLRGENGLLLTpcytANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNd 645
Cdd:cd05046   150 VSSQREVKVSLLSLSKDVYNSEYYKLRNALIP----LRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSD- 224
                         250
                  ....*....|....*..
gi 1034674014 646 tpEEILLRIGNGKFSLS 662
Cdd:cd05046   225 --EEVLNRLQAGKLELP 239
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
439-683 3.77e-05

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: 46.18  E-value: 3.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 439 FGEVYElkedigvgsySVCKRCIHATTNMEFAVKIIDKSKrDPSEEIEIL-----MRYGQHPNIITLKDVFDDGRYVYLV 513
Cdd:cd05062    19 FGMVYE----------GIAKGVVKDEPETRVAIKTVNEAA-SMRERIEFLneasvMKEFNCHHVVRLLGVVSQGQPTLVI 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 514 TDLMKGGELLDRILKQKCFSEREASDILYVISKTVD----------YLHCQGVVHRDLKPSNILYMDESasadSIRICDF 583
Cdd:cd05062    88 MELMTRGDLKSYLRSLRPEMENNPVQAPPSLKKMIQmageiadgmaYLNANKFVHRDLAARNCMVAEDF----TVKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 584 GFAKQL-------RGENGLLltpcyTANFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtpEEILlrig 655
Cdd:cd05062   164 GMTRDIyetdyyrKGGKGLL-----PVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATlAEQPYQGMSN---EQVL---- 231
                         250       260
                  ....*....|....*....|....*...
gi 1034674014 656 ngKFSLSGGNWDNiSDGAKDLLSHMLHM 683
Cdd:cd05062   232 --RFVMEGGLLDK-PDNCPDMLFELMRM 256
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
445-645 4.27e-05

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: 46.19  E-value: 4.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 445 LKEDIGVGSYS--VCKRCIHATTNME---FAVKII----DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYVYLVTD 515
Cdd:cd05093     9 LKRELGEGAFGkvFLAECYNLCPEQDkilVAVKTLkdasDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 516 LMKGGELlDRILKQ-----------KCFSEREASDILYV---ISKTVDYLHCQGVVHRDLKPSNILYMDESAsadsIRIC 581
Cdd:cd05093    88 YMKHGDL-NKFLRAhgpdavlmaegNRPAELTQSQMLHIaqqIAAGMVYLASQHFVHRDLATRNCLVGENLL----VKIG 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 582 DFGFAKQLRGEN-----GLLLTPCytaNFVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPND 645
Cdd:cd05093   163 DFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNN 229
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
470-694 1.07e-03

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: 41.74  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIdksKRDPSEEIEI-------LMRYGQHPNIITLKDVFDDGRYVYLVTDLMKGGE----LLDRILKQKCFSEREAS 538
Cdd:cd05050    39 AVKML---KEEASADMQAdfqreaaLMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAYGDlnefLRHRSPRAQCSLSHSTS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 539 D--------------ILYVISKTVD----YLHCQGVVHRDLKPSNILYMDESAsadsIRICDFGFAKQlrgengLLLTPC 600
Cdd:cd05050   116 SarkcglnplplsctEQLCIAKQVAagmaYLSERKFVHRDLATRNCLVGENMV----VKIADFGLSRN------IYSADY 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 601 YTAN--------FVAPEVLMQQGYDAACDIWSLGVLFYTMLA-GYTPFANGPNdtpEEILLRIGNGKFSlsgGNWDNISD 671
Cdd:cd05050   186 YKASendaipirWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAH---EEVIYYVRDGNVL---SCPDNCPL 259
                         250       260
                  ....*....|....*....|...
gi 1034674014 672 GAKDLLSHMLHMDPHQRYTAEQI 694
Cdd:cd05050   260 ELYNLMRLCWSKLPSDRPSFASI 282
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
544-656 1.10e-03

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: 41.53  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 544 ISKTVDYLHCQGVVHRDLKPSNILyMDESASADsirICDFGFAKQLRgeNGLLLTPCYTA----NFVAPEVLMQQGYDAA 619
Cdd:cd05075   122 IASGMEYLSSKNFIHRDLAARNCM-LNENMNVC---VADFGLSKKIY--NGDYYRQGRISkmpvKWIAIESLADRVYTTK 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034674014 620 CDIWSLGVLFYTMLA-GYTPFangPNDTPEEI--LLRIGN 656
Cdd:cd05075   196 SDVWSFGVTMWEIATrGQTPY---PGVENSEIydYLRQGN 232
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
425-652 1.15e-03

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: 41.46  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 425 NVLPIVQINGNAaQFGEVYE--LKEDIGvgsysvckrcihatTNMEFAVKIIdksKRDPSEEIEI--------LMRYGQH 494
Cdd:cd14204     7 NLLSLGKVLGEG-EFGSVMEgeLQQPDG--------------TNHKVAVKTM---KLDNFSQREIeeflseaaCMKDFNH 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 495 PNIITLKDV---FDDGRYV--YLVTDLMKGGELLDRILkqkcfSEREASDILYV-----------ISKTVDYLHCQGVVH 558
Cdd:cd14204    69 PNVIRLLGVcleVGSQRIPkpMVILPFMKYGDLHSFLL-----RSRLGSGPQHVplqtllkfmidIALGMEYLSSRNFLH 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 559 RDLKPSNILYMDESasadSIRICDFGFAKQLRG-----ENGLLLTPcytANFVAPEVLMQQGYDAACDIWSLGVLFYTML 633
Cdd:cd14204   144 RDLAARNCMLRDDM----TVCVADFGLSKKIYSgdyyrQGRIAKMP---VKWIAVESLADRVYTVKSDVWAFGVTMWEIA 216
                         250       260
                  ....*....|....*....|
gi 1034674014 634 A-GYTPFANGPNDTPEEILL 652
Cdd:cd14204   217 TrGMTPYPGVQNHEIYDYLL 236
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
438-633 1.41e-03

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: 41.55  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 438 QFGEVYeLKEDIGVGSYSVCKRCIHAT--TNMEFAVKII-----DKSKRDPSEEIEILMRYgQHPNIITLKDVFDDGRYV 510
Cdd:cd05051    17 QFGEVH-LCEANGLSDLTSDDFIGNDNkdEPVLVAVKMLrpdasKNAREDFLKEVKIMSQL-KDPNIVRLLGVCTRDEPL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 511 YLVTDLMKGGEL------------LDRILKQKCFSereASDILYV---ISKTVDYLHCQGVVHRDLKPSNILYmdesASA 575
Cdd:cd05051    95 CMIVEYMENGDLnqflqkheaetqGASATNSKTLS---YGTLLYMatqIASGMKYLESLNFVHRDLATRNCLV----GPN 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034674014 576 DSIRICDFGFAKQLrgengllltpcYTANF-------VAP-------EVLMQQgYDAACDIWSLGVLFYTML 633
Cdd:cd05051   168 YTIKIADFGMSRNL-----------YSGDYyriegraVLPirwmaweSILLGK-FTTKSDVWAFGVTLWEIL 227
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
470-644 6.41e-03

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 39.13  E-value: 6.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 470 AVKIIdKSKRDPSEEIEILMRYG------QHPNIITLKDVFDDGR------YVYLVTDLMKGGELLDRILKQKC------ 531
Cdd:cd05074    41 AVKML-KADIFSSSDIEEFLREAacmkefDHPNVIKLIGVSLRSRakgrlpIPMVILPFMKHGDLHTFLLMSRIgeepft 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034674014 532 FSEREASDILYVISKTVDYLHCQGVVHRDLKPSNILyMDESAsadSIRICDFGFAKQLRGENgLLLTPCYT---ANFVAP 608
Cdd:cd05074   120 LPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCM-LNENM---TVCVADFGLSKKIYSGD-YYRQGCASklpVKWLAL 194
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1034674014 609 EVLMQQGYDAACDIWSLGV-LFYTMLAGYTPFANGPN 644
Cdd:cd05074   195 ESLADNVYTTHSDVWAFGVtMWEIMTRGQTPYAGVEN 231
 
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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