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Conserved domains on  [gi|1958807372|ref|XP_008771565|]
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ribosomal protein S6 kinase alpha-6 isoform X1 [Rattus norvegicus]

Protein Classification

ribosomal protein S6 kinase( domain architecture ID 10144999)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
115-429 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: 712.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 274
Cdd:cd05582    81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 275 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd05582   161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 355 GS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFV 429
Cdd:cd05582   241 GAgpDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV 317
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
464-753 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: 599.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLLLTPCYT 623
Cdd:cd14091    82 LDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFGFAKQLRAENGLLMTPCYT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLH 703
Cdd:cd14091   162 ANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKMLH 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 704 MDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVLA 753
Cdd:cd14091   242 VDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVKGAVAATFRAIN 291
 
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; ...
115-429 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: 712.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 274
Cdd:cd05582    81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 275 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd05582   161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 355 GS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFV 429
Cdd:cd05582   241 GAgpDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV 317
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
464-753 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: 599.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLLLTPCYT 623
Cdd:cd14091    82 LDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFGFAKQLRAENGLLMTPCYT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLH 703
Cdd:cd14091   162 ANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKMLH 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 704 MDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVLA 753
Cdd:cd14091   242 VDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVKGAVAATFRAIN 291
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
111-368 7.70e-102

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 314.08  E-value: 7.70e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDK---KTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKAYS 270
Cdd:smart00220  77 EYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDR-NETMNMILKAKLGMPQF---LSAEAQSLLRMLF 346
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdISPEAKDLIRKLL 235
                          250       260
                   ....*....|....*....|..
gi 1958807372  347 KRNPANRLgseGVEEVKRHAFF 368
Cdd:smart00220 236 VKDPEKRL---TAEEALQHPFF 254
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
464-721 5.68e-97

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 301.37  E-value: 5.68e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerilrEIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmDESGHpdsIKICDFGFAKQLRgENGLLL 618
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDGH---VKLADFGLARQLD-PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpNDTPEEILLRIGNGRFSLSGGIWdNISRGAKDLL 698
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 1958807372  699 SHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
103-426 1.04e-88

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 282.86  E-value: 1.04e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADPAQ-----FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKAS-LKVRDRVRTKMERDILVEVNHPFIVKL 176
Cdd:PTZ00263    7 FTKPDTSSwklsdFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG 256
Cdd:PTZ00263   84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 257 LSKESVDqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSA 336
Cdd:PTZ00263  164 FAKKVPD---RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 337 EAQSLLRMLFKRNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFD--PEftakTPKDsPG 412
Cdd:PTZ00263  241 RARDLVKGLLQTDHTKRLGTlkGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkyPD----SPVD-RL 315
                         330
                  ....*....|....
gi 1958807372 413 LPASANAHQLFKGF 426
Cdd:PTZ00263  316 PPLTAAQQAEFAGF 329
Pkinase pfam00069
Protein kinase domain;
464-721 5.47e-67

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 220.96  E-value: 5.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdknilrEIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYlhsqgvvhrdlkpsnilymdesghpdsikicdfgfakqlrgeNGLL 617
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES------------------------------------------GSSL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLsggiWDNISRGAKDL 697
Cdd:pfam00069 118 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL----PSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:pfam00069 194 LKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
111-364 1.77e-61

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 214.88  E-value: 1.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLRKASLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARD---LRLGRPVALKVLRPELAAdPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-KKA 268
Cdd:COG0515    86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAE-----AQSLLR 343
Cdd:COG0515   166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDlppalDAIVLR 245
                         250       260
                  ....*....|....*....|.
gi 1958807372 344 MLFKrNPANRLGSegVEEVKR 364
Cdd:COG0515   246 ALAK-DPEERYQS--AAELAA 263
Pkinase pfam00069
Protein kinase domain;
111-368 1.77e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 206.33  E-value: 1.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHlhrlgivyrdlkpenilldeighikltdfglskesvdqEKKAYS 270
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES--------------------------------------GSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFK 347
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|.
gi 1958807372 348 RNPANRLgseGVEEVKRHAFF 368
Cdd:pfam00069 200 KDPSKRL---TATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
464-774 6.34e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 177.13  E-value: 6.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN-KRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElAADPEArerfrrEARALARL-NHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPdsiKICDFGFAKQLRGE--- 613
Cdd:COG0515    88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRV---KLIDFGIARALGGAtlt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 --NGLLLTPCYTanfvAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIWDNIS 691
Cdd:COG0515   164 qtGTVVGTPGYM----APEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---DGDSPAELLRAHLREPPPPPSELRPDLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 692 RGAKDLLSHMLHMDPHQRY-TAEQVLK--HPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVLARNQNRHPILEPVAAS 768
Cdd:COG0515   237 PALDAIVLRALAKDPEERYqSAAELAAalRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 316

                  ....*.
gi 1958807372 769 RLAQRR 774
Cdd:COG0515   317 AAAAAA 322
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
464-720 5.47e-41

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 153.43  E-value: 5.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-------RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkmkqvQHVAQEKSILMEL-SHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENgl 616
Cdd:PTZ00263   99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLL-LDNKGH---VKVTDFGFAKKVPDRT-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 lLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGgiWdnISRGAKD 696
Cdd:PTZ00263  173 -FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFF---DDTPFRIYEKILAGRLKFPN--W--FDGRARD 244
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 697 LLSHMLHMDPHQRYTA-----EQVLKHPW 720
Cdd:PTZ00263  245 LVKGLLQTDHTKRLGTlkggvADVKNHPY 273
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
216-313 9.51e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.79  E-value: 9.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 216 YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG----LSKESVDQEKkaySFCGTVEYMAPE-----VVNRR 286
Cdd:NF033483  112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTTMTQTN---SVLGTVHYLSPEqarggTVDAR 188
                          90       100
                  ....*....|....*....|....*..
gi 1958807372 287 ghsqsADWWSYGVLMFEMLTGTLPFQG 313
Cdd:NF033483  189 -----SDIYSLGIVLYEMLTGRPPFDG 210
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
515-673 6.28e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 84.85  E-value: 6.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 515 HPNIISlkeVFD---DGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMD 591
Cdd:NF033483   66 HPNIVS---VYDvgeDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-IT 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 592 ESGHpdsIKICDFGFAKQLRGE-----NGLLltpcYTANFVAPEvltqQ---GY-DAACDIWSLGVLLYTMLAGYTPFsN 662
Cdd:NF033483  142 KDGR---VKVTDFGIARALSSTtmtqtNSVL----GTVHYLSPE----QargGTvDARSDIYSLGIVLYEMLTGRPPF-D 209
                         170
                  ....*....|.
gi 1958807372 663 GpnDTPEEILL 673
Cdd:NF033483  210 G--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; ...
115-429 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: 712.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 274
Cdd:cd05582    81 GGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSFCGT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 275 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd05582   161 VEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 355 GS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQLFKGFSFV 429
Cdd:cd05582   241 GAgpDGVEEIKRHPFFATIDWNKLYRKEIKPPFKPAVSRPDDTFYFDPEFTSRTPKDSPGVPPSANAHQLFRGFSFV 317
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
464-753 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: 599.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNSVYLVTELLRGGEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLLLTPCYT 623
Cdd:cd14091    82 LDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDPESLRICDFGFAKQLRAENGLLMTPCYT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLH 703
Cdd:cd14091   162 ANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARIGSGKIDLSGGNWDHVSDSAKDLVRKMLH 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 704 MDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVLA 753
Cdd:cd14091   242 VDPSQRPTAAQVLQHPWIRNRDSLPQRQLTDPQDAALVKGAVAATFRAIN 291
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
459-752 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: 582.74  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 459 QFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14177     1 QFTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRYVYLVTELM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLLL 618
Cdd:cd14177    81 KGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLRGENGLLL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLL 698
Cdd:cd14177   161 TPCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSGKFSLSGGNWDTVSDAAKDLL 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 699 SHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVL 752
Cdd:cd14177   241 SHMLHVDPHQRYTAEQVLKHSWIACRDQLPHYQLNRQDAPHLVKGAMAATYSAL 294
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
445-784 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: 570.04  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 445 SNVLPIVQ-INGNAAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKE 523
Cdd:cd14176     1 VGVHSIVQqLHRNSIQFTDGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPTEEIEILLRYGQHPNIITLKD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 524 VFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICD 603
Cdd:cd14176    81 VYDDGKYVYVVTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNPESIRICD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 604 FGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLS 683
Cdd:cd14176   161 FGFAKQLRAENGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFSLS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 684 GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVLARNQNrhPILE 763
Cdd:cd14176   241 GGYWNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIVHWDQLPQYQLNRQDAPHLVKGAMAATYSALNRNQS--PVLE 318
                         330       340
                  ....*....|....*....|.
gi 1958807372 764 PVAASRLAQRRNMKKRTSTGL 784
Cdd:cd14176   319 PVGRSTLAQRRGIKKITSTAL 339
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
460-752 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: 532.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14178     1 FTDGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKFVYLVMELMR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLLLT 619
Cdd:cd14178    81 GGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNPESIRICDFGFAKQLRAENGLLMT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLS 699
Cdd:cd14178   161 PCYTANFVAPEVLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARIGSGKYALSGGNWDSISDAAKDIVS 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDpPQVVMEAVAAAYSVL 752
Cdd:cd14178   241 KMLHVDPHQRLTAPQVLRHPWIVNREYLSQNQLSRQD-VHLVKGAMAATYFAL 292
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
462-752 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: 532.30  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd14175     1 DGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLLLTPC 621
Cdd:cd14175    81 ELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDESGNPESLRICDFGFAKQLRAENGLLMTPC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHM 701
Cdd:cd14175   161 YTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSDAAKDLVSKM 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 702 LHMDPHQRYTAEQVLKHPWITQREQLPRHQPTSDDpPQVVMEAVAAAYSVL 752
Cdd:cd14175   241 LHVDPHQRLTAKQVLQHPWITQKDKLPQSQLNHQD-VQLVKGAMAATYSAL 290
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
114-430 1.37e-163

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: 476.13  E-value: 1.37e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLkVR---DRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05584     1 LKVLGKGGYGKVFQVRKTTGSDKGKIFAMKVLKKASI-VRnqkDTAHTKAERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd05584    80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDGTVTHT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNP 350
Cdd:cd05584   160 FCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 351 ANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSP-GLPASANAHQLFKGFS 427
Cdd:cd05584   240 SSRLGSgpGDAEEIKAHPFFRHINWDDLLAKKVEPPFKPLLQSEEDVSQFDSKFTKQTPVDSPdDSTLSESANQVFQGFT 319

                  ...
gi 1958807372 428 FVA 430
Cdd:cd05584   320 YVA 322
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
117-368 6.73e-145

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: 425.39  E-value: 6.73e-145
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd05123     1 LGKGSFGKVLLVRKK---DTGKLYAMKVLRKKEIIKRKEVeHTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTV 275
Cdd:cd05123    78 GELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTYTFCGTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 276 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLG 355
Cdd:cd05123   158 EYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLG 237
                         250
                  ....*....|...
gi 1958807372 356 SEGVEEVKRHAFF 368
Cdd:cd05123   238 SGGAEEIKAHPFF 250
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
111-430 1.82e-123

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: 373.49  E-value: 1.82e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLY 187
Cdd:cd05614     2 FELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALvqKAKTVEHTRTERNVLEHVRQsPFLVTLHYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK- 266
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKe 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPF----QGKDRNETMNMILKAKLGMPQFLSAEAQSL 341
Cdd:cd05614   162 RTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARDL 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 342 LRMLFKRNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSP-GLPASAN 418
Cdd:cd05614   242 LQKLLCKDPKKRLGAgpQGAQEIKEHPFFKGLDWEALALRKVNPPFRPSIRSELDVGNFAEEFTNLEPVYSPaGTPPSGA 321
                         330
                  ....*....|..
gi 1958807372 419 ahQLFKGFSFVA 430
Cdd:cd05614   322 --RVFQGYSFIA 331
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
464-720 1.88e-119

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: 359.87  E-value: 1.88e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd05117     2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEdeemlrREIEILKRL-DHPNIVKLYEVFEDDKNLYLVMEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDsIKICDFGFAKQLrGENGLL 617
Cdd:cd05117    81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDSP-IKIIDFGLAKIF-EEGEKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDL 697
Cdd:cd05117   159 KTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFY---GETEQELFEKILKGKYSFDSPEWKNVSEEAKDL 235
                         250       260
                  ....*....|....*....|...
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd05117   236 IKRLLVVDPKKRLTAAEALNHPW 258
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
115-429 5.69e-119

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: 361.15  E-value: 5.69e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVR-TKMERDILVEVN-HPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05570     1 KVLGKGSFGKVMLAERKK---TDELYAIKVLKKEVIIEDDDVEcTMTEKRVLALANrHPFLTGLHACFQTEDRLYFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05570    78 VNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWGGNTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05570   158 GTPDYIAPEILREQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPAR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANA--HQLFKGFSF 428
Cdd:cd05570   238 RLGCgpKGEADIKAHPFFRNIDWDKLEKKEVEPPFKPKVKSPRDTSNFDPEFTSESPRLTPVDSDLLTNidQEEFRGFSY 317

                  .
gi 1958807372 429 V 429
Cdd:cd05570   318 I 318
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
116-371 7.08e-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: 356.32  E-value: 7.08e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05583     1 VLGTGAYGKVFLVRKVGGHDAGKLYAMKVLKKATIvqKAKTAEHTMTERQVLEAVRQsPFLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV-DQEKKAYSF 271
Cdd:cd05583    81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLpGENDRAYSF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPFQGKD-RN---ETMNMILKAKLGMPQFLSAEAQSLLRML 345
Cdd:cd05583   161 CGTIEYMAPEVVRGgsDGHDKAVDWWSLGVLTYELLTGASPFTVDGeRNsqsEISKRILKSHPPIPKTFSAEAKDFILKL 240
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 346 FKRNPANRLGS--EGVEEVKRHAFFSSI 371
Cdd:cd05583   241 LEKDPKKRLGAgpRGAHEIKEHPFFKGL 268
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
115-429 3.96e-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: 348.92  E-value: 3.96e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVE-VNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05575     1 KVIGKGSFGKVLLARHK---AEGKLYAVKVLQKKAILKRNEVKHIMaERNVLLKnVKHPFLVGLHYSFQTKDKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05575    78 VNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGIEPSDTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05575   158 GTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLGS-EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQL--------F 423
Cdd:cd05575   238 RLGSgNDFLEIKNHSFFRPINWDDLEAKKIPPPFNPNVSGPLDLRNIDPEFTREPVPASVGKSADSVAVSAsvqeadnaF 317

                  ....*.
gi 1958807372 424 KGFSFV 429
Cdd:cd05575   318 DGFSYV 323
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
110-399 3.85e-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: 337.24  E-value: 3.85e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKAS-LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05580     2 DFEFLKTLGTGSFGRVRLVKHK---DSGKYYALKILKKAKiIKLKQVEHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDqekKA 268
Cdd:cd05580    79 VMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKD---RT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd05580   156 YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAKDLIKRLLVV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 349 NPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFD 399
Cdd:cd05580   236 DLTKRLGNlkNGVEDIKNHPWFAGIDWDALLQRKIPAPYVPKVRGPGDTSNFD 288
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
115-430 6.26e-109

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: 335.48  E-value: 6.26e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd05571     1 KVLGKGTFGKVILCREKA---TGELYAIKILKKEVIIAKDEVaHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 273
Cdd:cd05571    78 NGGELFFHLSRERVFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTFCG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05571   158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 354 LGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKT-----PKDSPGLPASANAHQLFKGF 426
Cdd:cd05571   238 LGGgpRDAKEIMEHPFFASINWDDLYQKKIPPPFKPQVTSETDTRYFDEEFTAESveltpPDRGDLLGLEEEERPHFEQF 317

                  ....
gi 1958807372 427 SFVA 430
Cdd:cd05571   318 SYSA 321
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
111-387 1.33e-107

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: 330.81  E-value: 1.33e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASL--KVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLY 187
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIvqKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV-DQEK 266
Cdd:cd05613    82 LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLlDENE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVN--RRGHSQSADWWSYGVLMFEMLTGTLPF----QGKDRNETMNMILKAKLGMPQFLSAEAQS 340
Cdd:cd05613   162 RAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFtvdgEKNSQAEISRRILKSEPPYPQEMSALAKD 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 341 LLRMLFKRNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05613   242 IIQRLLMKDPKKRLGCgpNGADEIKKHPFFQKINWDDLAAKKVPAPFKP 290
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
110-428 2.87e-104

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: 324.24  E-value: 2.87e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05573     2 DFEVIKVIGRGAFGEVWLVRDK---DTGQVYAMKILRKSDMLKREQIAhVRAERDILADADSPWIVRLHYAFQDEDHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 259
Cdd:cd05573    79 VMEYMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTkmnksgdre 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 -------ESVDQEKK-------------AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET 319
Cdd:cd05573   159 sylndsvNTLFQDNVlarrrphkqrrvrAYSAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVET 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 320 MNMIL--KAKLGMP--QFLSAEAQSLLRMLFKRnPANRLGSegVEEVKRHAFFSSIDWNKLykREVQPPFRPASGKPDDT 395
Cdd:cd05573   239 YSKIMnwKESLVFPddPDVSPEAIDLIRRLLCD-PEDRLGS--AEEIKAHPFFKGIDWENL--RESPPPFVPELSSPTDT 313
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1958807372 396 --FCFDPEFTAKTPKDSPGLPASANAHQL-FKGFSF 428
Cdd:cd05573   314 snFDDFEDDLLLSEYLSNGSPLLGKGKQLaFVGFTF 349
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
110-394 4.39e-103

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: 319.95  E-value: 4.39e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05574     2 HFKKIKLLGKGDVGRVYLVRLK---GTGKLFAMKVLDKEEMIKRNKVkRVLTEREILATLDHPFLPTLYASFQTSTHLCF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd05574    79 VMDYCPGGELFRLLQKqpGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSSVTPP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 -----------------------------KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd05574   159 pvrkslrkgsrrssvksieketfvaepsaRSNSFVGTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFKGSNRD 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 318 ETMNMILKAKLGMPQ--FLSAEAQSLLRMLFKRNPANRLGSE-GVEEVKRHAFFSSIDWNKLykREVQPPFRPASGKPDD 394
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 ...
115-429 7.16e-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: 7.16e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05592     1 KVLGKGSFGKVMLAELK---GTNQYFAIKALKKDVVLEDDDVECTMiERRVLaLASQHPFLTHLFCTFQTESHLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05592    78 LNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKASTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05592   158 GTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLGSEGVE--EVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSP---GLPASANAHQlFKGFS 427
Cdd:cd05592   238 RLGVPECPagDIRDHPFFKTIDWDKLERREIDPPFKPKVKSANDVSNFDPDFTMEKPVLTPvdkKLLASMDQEQ-FKGFS 316

                  ..
gi 1958807372 428 FV 429
Cdd:cd05592   317 FT 318
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
111-368 7.70e-102

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 314.08  E-value: 7.70e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDK---KTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKAYS 270
Cdd:smart00220  77 EYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQ-LDPGEKLTT 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDR-NETMNMILKAKLGMPQF---LSAEAQSLLRMLF 346
Cdd:smart00220 156 FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQlLELFKKIGKPKPPFPPPewdISPEAKDLIRKLL 235
                          250       260
                   ....*....|....*....|..
gi 1958807372  347 KRNPANRLgseGVEEVKRHAFF 368
Cdd:smart00220 236 VKDPEKRL---TAEEALQHPFF 254
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
116-428 4.53e-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: 314.51  E-value: 4.53e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd05585     1 VIGKGSFGKVMQVRKK---DTSRIYALKTIRKAHIVSRSEVtHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFIN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGT 274
Cdd:cd05585    78 GGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDDDKTNTFCGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 275 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd05585   158 PEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRL 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 355 GSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDS--PGLPASANAHQLFKGFSF 428
Cdd:cd05585   238 GYNGAQEIKNHPFFDQIDWKRLLMKKIQPPFKPAVENAIDTSNFDEEFTREKPIDSvvDDSHLSESVQQQFEGWSY 313
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
110-414 1.52e-100

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: 313.40  E-value: 1.52e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05599     2 DFEPLKVIGRGAFGEVRLVRKK---DTGHVYAMKKLRKSEMLEKEQVaHVRAERDILAEADNPWVVKLYYSFQDEENLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 268
Cdd:cd05599    79 IMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCT-GLKKSHLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSAEAQSLLRM 344
Cdd:cd05599   158 YSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIER 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 345 LFKrNPANRLGSEGVEEVKRHAFFSSIDWNKLykREVQPPFRPASGKPDDTFCFD--------PEFTAKTPKDSPGLP 414
Cdd:cd05599   238 LLC-DAEHRLGANGVEEIKSHPFFKGVDWDHI--RERPAPILPEVKSILDTSNFDefeevdlqIPSSPEAGKDSKELK 312
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
460-729 4.04e-98

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: 306.92  E-value: 4.04e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYEL---KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKnKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14092     1 FFQNYELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSR-RLDTSREVQLLRLCQGHPNIVKLHEVFQDELHTYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESgHPDSIKICDFGFAKqLRGENGL 616
Cdd:cd14092    80 LLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDED-DDAEIKIVDFGFAR-LKPENQP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVL----TQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSGGIWDNIS 691
Cdd:cd14092   158 LKTPCFTLPYAAPEVLkqalSTQGYDESCDLWSLGVILYTMLSGQVPFqSPSRNESAAEIMKRIKSGDFSFDGEEWKNVS 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLPR 729
Cdd:cd14092   238 SEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPSS 275
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
114-428 3.08e-97

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: 304.96  E-value: 3.08e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKM-ERDILVE-VNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd05604     1 LKVIGKGSFGKVLLAKRKRD---GKYYAVKVLQKKVILNRKEQKHIMaERNVLLKnVKHPFLVGLHYSFQTTDKLYFVLD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd05604    78 FVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 351
Cdd:cd05604   158 CGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQ 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 352 NRLG-SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGL---PASANAHQL----- 422
Cdd:cd05604   238 LRLGaKEDFLEIKNHPFFESINWTDLVQKKIPPPFNPNVNGPDDISNFDAEFTEEMVPYSVCVssdYSIVNASVLeadda 317

                  ....*.
gi 1958807372 423 FKGFSF 428
Cdd:cd05604   318 FVGFSY 323
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
464-721 5.68e-97

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 301.37  E-value: 5.68e-97
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKKDRerilrEIKILKKL-KHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmDESGHpdsIKICDFGFAKQLRgENGLLL 618
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILL-DEDGH---VKLADFGLARQLD-PGEKLT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpNDTPEEILLRIGNGRFSLSGGIWdNISRGAKDLL 698
Cdd:smart00220 155 TFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPG--DDQLLELFKKIGKPKPPFPPPEW-DISPEAKDLI 231
                          250       260
                   ....*....|....*....|...
gi 1958807372  699 SHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:smart00220 232 RKLLVKDPEKRLTAEEALQHPFF 254
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
114-429 7.32e-97

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: 303.93  E-value: 7.32e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVR-TKMERDILVEVNHP-FIVKLHYAFQTEGKLYLILD 191
Cdd:cd05587     1 LMVLGKGSFGKVMLAERK---GTDELYAIKILKKDVIIQDDDVEcTMVEKRVLALSGKPpFLTQLHSCFQTMDRLYFVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd05587    78 YVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFGGKTTRTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 351
Cdd:cd05587   158 CGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPA 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 352 NRLG--SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPA-SANAHQ-LFKGFS 427
Cdd:cd05587   238 KRLGcgPTGERDIKEHPFFRRIDWEKLERREIQPPFKPKIKSPRDAENFDKEFTKEPPVLTPTDKLvIMNIDQsEFEGFS 317

                  ..
gi 1958807372 428 FV 429
Cdd:cd05587   318 FV 319
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
111-430 2.27e-96

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: 302.68  E-value: 2.27e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVN---HPFIVKLHYAFQTEGKL 186
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPT---GELFAIKALKKGDIIARDEVESLMcEKRIFETVNsarHPFLVNLFACFQTPEHV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd05589    78 CFVMEYAAGGDLMMHIHEDV-FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 346
Cdd:cd05589   157 RTSTFCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 347 KRNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSP---GLPASANAHQ 421
Cdd:cd05589   237 RKNPERRLGAseRDAEDVKKQPFFRNIDWEALLARKIKPPFVPTIKSPEDVSNFDEEFTSEKPVLTPpkePRPLTEEEQA 316

                  ....*....
gi 1958807372 422 LFKGFSFVA 430
Cdd:cd05589   317 LFKDFDYVA 325
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
115-429 5.64e-96

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 301.50  E-value: 5.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKAS-LKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKCD---GKFYAVKVLQKKTiLKKKEQNHIMAERNVLLKnLKHPFLVGLHYSFQTSEKLYFVLDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05603    78 VNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05603   158 GTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLGSEG-VEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPG-----LPASANAHQLFKGF 426
Cdd:cd05603   238 RLGAKAdFLEIKNHVFFSPINWDDLYHKRITPPYNPNVAGPADLRHFDPEFTQEAVPHSVGrtpdlTASSSSSSSAFLGF 317

                  ...
gi 1958807372 427 SFV 429
Cdd:cd05603   318 SYA 320
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
115-411 2.94e-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: 300.00  E-value: 2.94e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd05595     1 KLLGKGTFGKVILVREKA---TGRYYAMKILRKEVIIAKDEVaHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 273
Cdd:cd05595    78 NGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITDGATMKTFCG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05595   158 TPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQR 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 354 LGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSP 411
Cdd:cd05595   238 LGGgpSDAKEVMEHRFFLSINWQDVVQKKLLPPFKPQVTSEVDTRYFDDEFTAQSITITP 297
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
110-428 8.53e-95

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: 298.85  E-value: 8.53e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05598     2 MFEKIKTIGVGAFGEVSLVRKK---DTNALYAMKTLRKKDVLKRNQVaHVKAERDILAEADNEWVVKLYYSFQDKENLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL---------SK 259
Cdd:cd05598    79 VMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVdqekkAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQF--LS 335
Cdd:cd05598   159 YYL-----AHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 336 AEAQSLLRMLFkRNPANRLGSEGVEEVKRHAFFSSIDWNKLykREVQPPFRPASGKPDDTFCFDP---EFTAKTPK--DS 410
Cdd:cd05598   234 PEAKDLILRLC-CDAEDRLGRNGADEIKAHPFFAGIDWEKL--RKQKAPYIPTIRHPTDTSNFDPvdpEKLRSSDEepTT 310
                         330
                  ....*....|....*....
gi 1958807372 411 PGLPASANAHQ-LFKGFSF 428
Cdd:cd05598   311 PNDPDNGKHPEhAFYEFTF 329
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
119-373 6.42e-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: 294.12  E-value: 6.42e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 119 QGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 197
Cdd:cd05579     3 RGAYGRVYLAKKKS---TGDLYAIKVIKKRDMIRKNQVdSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 198 VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK---------------ESV 262
Cdd:cd05579    80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvrrqiklsiqkkSNG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF--LSAEAQS 340
Cdd:cd05579   160 APEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpeVSDEAKD 239
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 341 LLRMLFKRNPANRLGSEGVEEVKRHAFFSSIDW 373
Cdd:cd05579   240 LISKLLTPDPEKRLGAKGIEEIKNHPFFKGIDW 272
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
117-428 5.89e-93

Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 294.09  E-value: 5.89e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEV---NHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05586     1 IGKGTFGQVYQVRKK---DTRRIYAMKVLSKKVIVAKKEVaHTIGERNILVRTaldESPFIVGLKFSFQTPTDLYLVTDY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05586    78 MSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADLTDNKTTNTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ-FLSAEAQSLLRMLFKRNP 350
Cdd:cd05586   158 GTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNP 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 351 ANRLGS-EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKD--------SPGLPA------ 415
Cdd:cd05586   238 KHRLGAhDDAVELKEHPFFADIDWDLLSKKKITPPFKPIVDSDTDVSNFDPEFTNASLLNanivpwaqRPGLPGatstpl 317
                         330
                  ....*....|...
gi 1958807372 416 SANAHQLFKGFSF 428
Cdd:cd05586   318 SPSVQANFRGFTF 330
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
106-428 3.64e-91

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: 289.61  E-value: 3.64e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 106 ADPAQFDLLKVLGQGSFGKVFLVRKKTGPdagQLYAMKVL-RKASLKVRDRVRTKMERDILVE-VNHPFIVKLHYAFQTE 183
Cdd:cd05602     4 AKPSDFHFLKVIGKGSFGKVLLARHKSDE---KFYAVKVLqKKAILKKKEEKHIMSERNVLLKnVKHPFLVGLHFSFQTT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd05602    81 DKLYFVLDYINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLR 343
Cdd:cd05602   161 PNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 344 MLFKRNPANRLG-SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGL-PASA---- 417
Cdd:cd05602   241 GLLQKDRTKRLGaKDDFTEIKNHIFFSPINWDDLINKKITPPFNPNVSGPNDLRHFDPEFTDEPVPNSIGQsPDSIlvta 320
                         330
                  ....*....|....
gi 1958807372 418 ---NAHQLFKGFSF 428
Cdd:cd05602   321 sikEAAEAFLGFSY 334
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
117-375 1.06e-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: 282.96  E-value: 1.06e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd05572     1 LGVGGFGRVELVQLKS---KGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYSFCGTV 275
Cdd:cd05572    78 GELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK-KLGSGRKTWTFCGTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 276 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN--ETMNMILKA--KLGMPQFLSAEAQSLLRMLFKRNPA 351
Cdd:cd05572   157 EYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDpmKIYNIILKGidKIEFPKYIDKNAKNLIKQLLRRNPE 236
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 352 NRLGSE--GVEEVKRHAFFSSIDWNK 375
Cdd:cd05572   237 ERLGYLkgGIRDIKKHKWFEGFDWEG 262
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
103-426 1.04e-88

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 282.86  E-value: 1.04e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADPAQ-----FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKAS-LKVRDRVRTKMERDILVEVNHPFIVKL 176
Cdd:PTZ00263    7 FTKPDTSSwklsdFEMGETLGTGSFGRVRIAKHKG---TGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG 256
Cdd:PTZ00263   84 MCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 257 LSKESVDqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSA 336
Cdd:PTZ00263  164 FAKKVPD---RTFTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 337 EAQSLLRMLFKRNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFD--PEftakTPKDsPG 412
Cdd:PTZ00263  241 RARDLVKGLLQTDHTKRLGTlkGGVADVKNHPYFHGANWDKLYARYYPAPIPVRVKSPGDTSNFEkyPD----SPVD-RL 315
                         330
                  ....*....|....
gi 1958807372 413 LPASANAHQLFKGF 426
Cdd:PTZ00263  316 PPLTAAQQAEFAGF 329
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
464-720 1.97e-88

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: 279.02  E-value: 1.97e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14003     2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIeekikrEIEIMKLL-NHPNIIKLYEVIETENKIYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGeNGLL 617
Cdd:cd14003    81 ASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENIL-LDKNGN---LKIIDFGLSNEFRG-GSLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSnGPNDtpEEILLRIGNGRFSlsggIWDNISRGAKD 696
Cdd:cd14003   156 KTFCGTPAYAAPEVLLGRKYDGpKADVWSLGVILYAMLTGYLPFD-DDND--SKLFRKILKGKYP----IPSHLSPDARD 228
                         250       260
                  ....*....|....*....|....
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14003   229 LIRRMLVVDPSKRITIEEILNHPW 252
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
110-367 2.03e-88

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: 278.97  E-value: 2.03e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKASLkvrdrVRTKMERDILVEV------NHPFIVKLHYAFQT 182
Cdd:cd14007     1 DFEIGKPLGKGKFGNVYLAReKKSG----FIVALKVISKSQL-----QKSGLEHQLRREIeiqshlRHPNILRLYGYFED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 262
Cdd:cd14007    72 KKRIYLILEYAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKaySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLL 342
Cdd:cd14007   152 SNRRK--TFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLI 229
                         250       260
                  ....*....|....*....|....*
gi 1958807372 343 RMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14007   230 SKLLQKDPSKRL---SLEQVLNHPW 251
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
115-430 4.44e-88

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: 281.03  E-value: 4.44e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05590     1 RVLGKGSFGKVMLARLK---ESGRLYAVKVLKKDVILQDDDVECTMtEKRILsLARNHPFLTQLYCCFQTPDRLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05590    78 VNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05590   158 GTPDYIAPEILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTM 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLGS---EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAK----TPKDSPGLPAsanAHQ-LFK 424
Cdd:cd05590   238 RLGSltlGGEEAILRHPFFKELDWEKLNRRQIEPPFRPRIKSREDVSNFDPDFIKEdpvlTPIEESLLPM---INQdEFR 314

                  ....*.
gi 1958807372 425 GFSFVA 430
Cdd:cd05590   315 NFSYTA 320
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
111-411 9.18e-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: 281.20  E-value: 9.18e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05593    17 FDYLKLLGKGTFGKVILVREKA---SGKYYAMKILKKEVIIAKDEVaHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAY 269
Cdd:cd05593    94 MEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDAATMK 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRN 349
Cdd:cd05593   174 TFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKD 253
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 350 PANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSP 411
Cdd:cd05593   254 PNKRLGGgpDDAKEIMRHSFFTGVNWQDVYDKKLVPPFKPQVTSETDTRYFDEEFTAQTITITP 317
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
115-429 1.33e-86

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 277.07  E-value: 1.33e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtGPDagQLYAMKVLRKASLKVRDRVRTKM-ERDILV-EVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05591     1 KVLGKGSFGKVMLAERK-GTD--EVYAIKVLKKDVILQDDDVDCTMtEKRILAlAAKHPFLTALHSCFQTKDRLFFVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05591    78 VNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGKTTTTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05591   158 GTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAK 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLG---SEGVEE-VKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANA--HQLFKGF 426
Cdd:cd05591   238 RLGcvaSQGGEDaIRQHPFFREIDWEALEQRKVKPPFKPKIKTKRDANNFDQDFTKEEPVLTPVDPAVIKQinQEEFRGF 317

                  ...
gi 1958807372 427 SFV 429
Cdd:cd05591   318 SFV 320
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
110-368 4.49e-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: 272.98  E-value: 4.49e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05578     1 HFQILRVIGKGSFGKVCIVQKK---DTKKMFAMKYMNKQKCIEKDSVRNVLnELEILQELEHPFLVNLWYSFQDEEDMYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKA 268
Cdd:cd05578    78 VVDLLLGGDLRYHLQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATK-LTDGTLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDR---NETMNMILKAKLGMPQFLSAEAQSLLRML 345
Cdd:cd05578   157 TSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRtsiEEIRAKFETASVLYPAGWSEEAIDLINKL 236
                         250       260
                  ....*....|....*....|...
gi 1958807372 346 FKRNPANRLGSegVEEVKRHAFF 368
Cdd:cd05578   237 LERDPQKRLGD--LSDLKNHPYF 257
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
111-429 4.81e-86

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: 275.72  E-value: 4.81e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtGPDagQLYAMKVLRKASLKVRDRVRTKM--ERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERK-GTD--ELYAVKILKKDVVIQDDDVECTMveKRVLALSGKPPFLTQLHSCFQTMDRLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd05616    79 VMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIWDGVTT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd05616   159 KTFCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 349 NPANRL--GSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRP-ASGKpdDTFCFDPEFTAKTPKDSPglPASANAHQL--- 422
Cdd:cd05616   239 HPGKRLgcGPEGERDIKEHAFFRYIDWEKLERKEIQPPYKPkACGR--NAENFDRFFTRHPPVLTP--PDQEVIRNIdqs 314

                  ....*...
gi 1958807372 423 -FKGFSFV 429
Cdd:cd05616   315 eFEGFSFV 322
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
111-432 9.51e-86

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: 276.14  E-value: 9.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKA---TGRYYAMKILKKEVIVAKDEVaHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLH-RLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd05594   104 MEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATM 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd05594   184 KTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKK 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 349 NPANRL--GSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAK----TPKDSPGLPASANAHQL 422
Cdd:cd05594   264 DPKQRLggGPDDAKEIMQHKFFAGIVWQDVYEKKLVPPFKPQVTSETDTRYFDEEFTAQmitiTPPDQDDSMETVDNERR 343
                         330
                  ....*....|..
gi 1958807372 423 --FKGFSFVATS 432
Cdd:cd05594   344 phFPQFSYSASA 355
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
109-401 6.08e-84

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: 268.92  E-value: 6.08e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLrkaslKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQT 182
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRIS---EHYYALKVM-----AIPEVIRLKQeqhvhnEKRVLKEVSHPFIIRLFWTEHD 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 262
Cdd:cd05612    73 QRFLYMLMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLL 342
Cdd:cd05612   153 D---RTWTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLI 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 343 RMLFKRNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFD--PE 401
Cdd:cd05612   230 KKLLVVDRTRRLGNmkNGADDVKNHRWFKSVDWDDVPQRKLKPPIVPKVSHDGDTSNFDdyPE 292
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
111-429 6.91e-83

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 267.56  E-value: 6.91e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDIL-VEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05619     7 FVLHKMLGKGSFGKVFLAELKG---TNQFFAIKALKKDVVLMDDDVECTMvEKRVLsLAWEHPFLTHLFCTFQTKENLFF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd05619    84 VMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd05619   164 STFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVR 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 349 NPANRLGSEGveEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANA--HQLFKGF 426
Cdd:cd05619   244 EPERRLGVRG--DIRQHPFFREINWEALEEREIEPPFKPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSmdQNMFRNF 321

                  ...
gi 1958807372 427 SFV 429
Cdd:cd05619   322 SFV 324
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
111-428 1.02e-82

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: 266.91  E-value: 1.02e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKAS-LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05597     3 FEILKVIGRGAFGEVAVVKLK---STEKVYAMKILNKWEmLKRAETACFREERDVLVNGDRRWITKLHYAFQDENYLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVDQEKKA 268
Cdd:cd05597    80 MDYYCGGDLLTLLSKfEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SCLKLREDGTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSF--CGTVEYMAPEVV--NRRGHSQ---SADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMP---QFLSA 336
Cdd:cd05597   159 QSSvaVGTPDYISPEILqaMEDGKGRygpECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPddeDDVSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 337 EAQSLLRMLFKRnPANRLGSEGVEEVKRHAFFSSIDWNKLykREVQPPFRPASGKPDDTFCFDPEFTA--KTPKDSPGLP 414
Cdd:cd05597   239 EAKDLIRRLICS-RERRLGQNGIDDFKKHPFFEGIDWDNI--RDSTPPYIPEVTSPTDTSNFDVDDDDlrHTDSLPPPSN 315
                         330
                  ....*....|....*
gi 1958807372 415 ASANAHQL-FKGFSF 428
Cdd:cd05597   316 AAFSGLHLpFVGFTY 330
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
110-368 3.45e-82

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: 263.69  E-value: 3.45e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05581     2 DFKFGKPLGEGSYSTVVLAKEKE---TGKEYAIKVLDKRHIIKEKKVKYvTIEKEVLSRLAHPGIVKLYYTFQDESKLYF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 259
Cdd:cd05581    79 VLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKvlgpdsspe 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 --------ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 331
Cdd:cd05581   159 stkgdadsQIAYNQARAASFVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFP 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 332 QFLSAEAQSLLRMLFKRNPANRLGS---EGVEEVKRHAFF 368
Cdd:cd05581   239 ENFPPDAKDLIQKLLVLDPSKRLGVnenGGYDELKAHPFF 278
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
460-750 5.58e-82

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: 264.59  E-value: 5.58e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYEL---KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN-KRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14179     2 FYQHYELdlkDKPLGEGSFSICRKCLHKKTNQEYAVKIVSKRmEANTQREIAALKLCEGHPNIVKLHEVYHDQLHTFLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDsIKICDFGFAKQLRGENG 615
Cdd:cd14179    82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESDNSE-IKIIDFGFARLKPPDNQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPND----TPEEILLRIGNGRFSLSGGIWDNIS 691
Cdd:cd14179   161 PLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSltctSAEEIMKKIKQGDFSFEGEAWKNVS 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLprhqptSDDP---PQVVMEAVAAAYS 750
Cdd:cd14179   241 QEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQDGSQL------SSNPlmtPDILGSSGASVHT 296
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
111-421 8.11e-82

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: 266.33  E-value: 8.11e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05629     3 FHTVKVIGKGAFGEVRLVQKK---DTGKIYAMKTLLKSEMFKKDQLaHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS----------- 258
Cdd:cd05629    80 MEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLStgfhkqhdsay 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 -------------------------------KESVDQEKK-----AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMF 302
Cdd:cd05629   160 yqkllqgksnknridnrnsvavdsinltmssKDQIATWKKnrrlmAYSTVGTPDYIAPEIFLQQGYGQECDWWSLGAIMF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 303 EMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSAEAQSLLRMLFKrNPANRLGSEGVEEVKRHAFFSSIDWNKLyk 378
Cdd:cd05629   240 ECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRRLIT-NAENRLGRGGAHEIKSHPFFRGVDWDTI-- 316
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 379 REVQPPFRPASGKPDDTFCFDPEFTAKTPkDSPGLPASANAHQ 421
Cdd:cd05629   317 RQIRAPFIPQLKSITDTSYFPTDELEQVP-EAPALKQAAPAQQ 358
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
110-365 2.10e-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: 260.53  E-value: 2.10e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARhKLTG----EKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvDQEKKA 268
Cdd:cd14003    77 VMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF-RGGSLL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 347
Cdd:cd14003   156 KTFCGTPAYAAPEVLLGRKyDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLV 235
                         250
                  ....*....|....*...
gi 1958807372 348 RNPANRLgseGVEEVKRH 365
Cdd:cd14003   236 VDPSKRI---TIEEILNH 250
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
110-365 2.28e-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: 260.87  E-value: 2.28e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKT---GEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKEsVDQEK 266
Cdd:cd05117    78 MELCTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLaskDPDSPIKIIDFGLAKI-FEEGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLL 342
Cdd:cd05117   157 KLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDspewKNVSEEAKDLI 236
                         250       260
                  ....*....|....*....|...
gi 1958807372 343 RMLFKRNPANRLgseGVEEVKRH 365
Cdd:cd05117   237 KRLLVVDPKKRL---TAAEALNH 256
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
110-399 6.68e-81

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: 260.80  E-value: 6.68e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14209     2 DFDRIKTLGTGSFGRVMLVRHKET---GNYYAMKILDKQKVvKLKQVEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdqEKKA 268
Cdd:cd14209    79 VMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRV---KGRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd14209   156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 349 NPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFD 399
Cdd:cd14209   236 DLTKRFGNlkNGVNDIKNHKWFATTDWIAIYQRKVEAPFIPKLKGPGDTSNFD 288
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
115-429 1.15e-80

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: 261.03  E-value: 1.15e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM--ERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05620     1 KVLGKGSFGKVLLAELK---GKGEYFAVKALKKDVVLIDDDVECTMveKRVLALAWENPFLTHLYCTFQTKEHLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd05620    78 LNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRASTFC 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd05620   158 GTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTR 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 353 RLGSEGveEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDS---PGLPASANaHQLFKGFSFV 429
Cdd:cd05620   238 RLGVVG--NIRGHPFFKTINWTALEKRELDPPFKPKVKSPSDYSNFDREFLSEKPRLSysdKNLIDSMD-QSAFAGFSFI 314
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
111-429 2.50e-80

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: 260.71  E-value: 2.50e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKA---TGDIYAMKVLKKSETLAQEEVSFfEEERDIMAKANSPWITKLQYAFQDSENLYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVDQEKKA 268
Cdd:cd05601    80 MEYHPGGDLLSLLSRyDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG-SAAKLSSDKTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSF--CGTVEYMAPEV---VNRRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSA 336
Cdd:cd05601   159 TSKmpVGTPDYIAPEVltsMNGGSkgtYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMnfKKFLKFPEdpKVSE 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 337 EAQSLLRMLFKrNPANRLGSEGveeVKRHAFFSSIDWNKLykREVQPPFRPASGKPDDTFCFDpEFTAKtpKDSPGLPAS 416
Cdd:cd05601   239 SAVDLIKGLLT-DAKERLGYEG---LCCHPFFSGIDWNNL--RQTVPPFVPTLTSDDDTSNFD-EFEPK--KTRPSYENF 309
                         330
                  ....*....|....*....
gi 1958807372 417 ANAHQL------FKGFSFV 429
Cdd:cd05601   310 NKSKGFsgkdlpFVGFTFT 328
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
111-431 5.12e-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: 260.31  E-value: 5.12e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHP-FIVKLHYAFQTEGKLYL 188
Cdd:cd05615    12 FNFLMVLGKGSFGKVMLAERKG---SDELYAIKILKKDVVIQDDDVECTMvEKRVLALQDKPpFLTQLHSCFQTVDRLYF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd05615    89 VMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGVTT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd05615   169 RTFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTK 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 349 NPANRL--GSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRP-ASGKPDDTfcFDPEFTAKTPK-DSPGLPASANAHQL-F 423
Cdd:cd05615   249 HPAKRLgcGPEGERDIREHAFFRRIDWDKLENREIQPPFKPkVCGKGAEN--FDKFFTRGQPVlTPPDQLVIANIDQAdF 326

                  ....*...
gi 1958807372 424 KGFSFVAT 431
Cdd:cd05615   327 EGFSYVNP 334
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
110-428 1.69e-79

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


Pssm-ID: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 260.35  E-value: 1.69e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVR-TKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05600    12 DFQILTQVGQGGYGSVFLARKK---DTGEICALKIMKKKVLFKLNEVNhVLTERDILTTTNSPWLVKLLYAFQDPENVYL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK-- 266
Cdd:cd05600    89 AMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGLASGTLSPKKie 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 -----------------------------------KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd05600   169 smkirleevkntafleltakerrniyramrkedqnYANSVVGSPDYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPF 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 312 QGKDRNETMNMIL--KAKLGMPQF--------LSAEAQSLLRMLFKrNPANRLGSegVEEVKRHAFFSSIDWNKLYKReV 381
Cdd:cd05600   249 SGSTPNETWANLYhwKKTLQRPVYtdpdlefnLSDEAWDLITKLIT-DPQDRLQS--PEQIKNHPFFKNIDWDRLREG-S 324
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 382 QPPFRPASGKPDDTFCFDpEFTAKTPKDS-------------PGLPASANAHQ-LFKGFSF 428
Cdd:cd05600   325 KPPFIPELESEIDTSYFD-DFNDEADMAKykdvhekqkslegSGKNGGDNGNRsLFVGFTF 384
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
115-429 3.62e-78

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: 255.04  E-value: 3.62e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVR---DRVRTkmERDIL-VEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05588     1 RVIGRGSYAKVLMVELKK---TKRIYAMKVIKKELVNDDediDWVQT--EKHVFeTASNHPFLVGLHSCFQTESRLFFVI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd05588    76 EFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTST 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ--GKDRNETMN-------MILKAKLGMPQFLSAEAQSL 341
Cdd:cd05588   156 FCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDivGSSDNPDQNtedylfqVILEKPIRIPRSLSVKAASV 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 342 LRMLFKRNPANRLG---SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASAN 418
Cdd:cd05588   236 LKGFLNKNPAERLGchpQTGFADIQSHPFFRTIDWEQLEQKQVTPPYKPRIESERDLENFDPQFTNEPVQLTPDDPDVIE 315
                         330
                  ....*....|...
gi 1958807372 419 A--HQLFKGFSFV 429
Cdd:cd05588   316 KidQSEFEGFEYV 328
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
464-720 8.47e-78

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 251.48  E-value: 8.47e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEhmienEVAILRRV-KHPNIVQLIEEYDTDTELYLVMELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRgenGLLL 618
Cdd:cd14095    81 KGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLKLADFGLATEVK---EPLF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLL 698
Cdd:cd14095   158 TVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFR-SPDRDQEELFDLILAGEFEFLSPYWDNISDSAKDLI 236
                         250       260
                  ....*....|....*....|..
gi 1958807372 699 SHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14095   237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
464-720 1.58e-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: 248.06  E-value: 1.58e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN----KRDPSE-EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKalkgKEDSLEnEIAVLRKI-KHPNIVQLLDIYESKSHLYLVMELV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdeSGHPDS-IKICDFGFAKQlrGENGLL 617
Cdd:cd14083    84 TGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYY--SPDEDSkIMISDFGLSKM--EDSGVM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgPNDTpeEILLRIGNGRFSLSGGIWDNISRGAKDL 697
Cdd:cd14083   160 STACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYD-ENDS--KLFAQILKAEYEFDSPYWDDISDSAKDF 236
                         250       260
                  ....*....|....*....|...
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14083   237 IRHLMEKDPNKRYTCEQALEHPW 259
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
462-721 2.26e-76

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: 248.87  E-value: 2.26e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDI-GIGSYSVCKRCIHSASNMEFAVKIIDK----NKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14090     1 DLYKLTGELlGEGAYASVQTCINLYTGKEYAVKIIEKhpghSRSRVFREVETLHQCQGHPNILQLIEYFEDDERFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILymdeSGHPDSI---KICDFGFAKQLRGE 613
Cdd:cd14090    81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENIL----CESMDKVspvKICDFDLGSGIKLS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGL--------LLTPCYTANFVAPEVL---TQQG--YDAACDIWSLGVLLYTMLAGYTPFSN--GPN----------DTP 668
Cdd:cd14090   157 STSmtpvttpeLLTPVGSAEYMAPEVVdafVGEAlsYDKRCDLWSLGVILYIMLCGYPPFYGrcGEDcgwdrgeacqDCQ 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 669 EEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14090   237 ELLFHSIQEGEYEFPEKEWSHISAEAKDLISHLLVRDASQRYTAEQVLQHPWV 289
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
460-721 5.69e-76

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: 248.25  E-value: 5.69e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYE--LKED-IGIGSYSVCKRCIHSASNMEFAVKIIDKN-KRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14180     1 FFQCYEldLEEPaLGEGSFSVCRKCRHRQSGQEYAVKIISRRmEANTQREVAALRLCQSHPNIVALHEVLHDQYHTYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDES-GHPdsIKICDFGFAKqLRGEN 614
Cdd:cd14180    81 ELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESdGAV--LKVIDFGFAR-LRPQG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GL-LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSN----GPNDTPEEILLRIGNGRFSLSGGIWDN 689
Cdd:cd14180   158 SRpLQTPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSkrgkMFHNHAADIMHKIKEGDFSLEGEAWKG 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 690 ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14180   238 VSEEAKDLVRGLLTVDPAKRLKLSELRESDWL 269
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
117-387 6.63e-76

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: 247.06  E-value: 6.63e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd05577     1 LGRGGFGEVCACQVK---ATGKMYACKKLDKKRIKKKKGETMALnEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKAYSFCG 273
Cdd:cd05577    78 GDLKYHIYNvgTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVE-FKGGKKIKGRVG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQ----GKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd05577   157 THGYMAPEVLqKEVAYDFSVDWFALGCMLYEMIAGRSPFRqrkeKVDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 349 NPANRLGSEG--VEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05577   237 DPERRLGCRGgsADEVKEHPFFRSLNWQRLEAGMLEPPFVP 277
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
116-387 2.42e-75

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: 245.81  E-value: 2.42e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNH----PFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05606     1 IIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGETLALnERIMLSLVSTggdcPFIVCMTYAFQTPDKLCFIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQEKKAYS 270
Cdd:cd05606    78 DLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF--SKKKPHA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPF---QGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 346
Cdd:cd05606   156 SVGTHGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFrqhKTKDKHEIDRMTLTMNVELPDSFSPELKSLLEGLL 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 347 KRNPANRLGSE--GVEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05606   236 QRDVSKRLGCLgrGATEVKEHPFFKGVDWQQVYLQKYPPPLIP 278
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
114-374 3.30e-75

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: 244.70  E-value: 3.30e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVR-TKMERDIL-VEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd05611     1 LKPISKGAFGSVYLAKKRS---TGDYFAIKVLKKSDMIAKNQVTnVKAERAIMmIQGESPYVAKLYYSFQSKDYLYLVME 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSkESVDQEKKAYSF 271
Cdd:cd05611    78 YLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS-RNGLEKRHNKKF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 347
Cdd:cd05611   157 VGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRLLC 236
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 348 RNPANRLGSEGVEEVKRHAFFSSIDWN 374
Cdd:cd05611   237 MDPAKRLGANGYQEIKSHPFFKSINWD 263
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
460-720 4.57e-75

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: 244.57  E-value: 4.57e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------------EIEILMRYGQHPNIISLKEVFDD 527
Cdd:cd14093     1 FYAKYEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITGEKSSEneaeelreatrrEIEILRQVSGHPNIIELHDVFES 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 528 GKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFA 607
Cdd:cd14093    81 PTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNL----NVKISDFGFA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQLrGENGLLLTPCYTANFVAPEVL------TQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndTPEEILLR-IGNGRF 680
Cdd:cd14093   157 TRL-DEGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWH----RKQMVMLRnIMEGKY 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 681 SLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14093   232 EFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPF 271
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
108-429 5.67e-75

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: 247.29  E-value: 5.67e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKAS-LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd05596    25 AEDFDVIKVIGRGAFGEVQLVRHKS---TKKVYAMKLLSKFEmIKRSDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKeVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEK 266
Cdd:cd05596   102 YMVMDYMPGGDLVNLMSN-YDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCMK-MDKDG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYS--FCGTVEYMAPEVVNRRGH----SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--KAKLGMP--QFLSA 336
Cdd:cd05596   180 LVRSdtAVGTPDYISPEVLKSQGGdgvyGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMnhKNSLQFPddVEISK 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 337 EAQSLLRMlFKRNPANRLGSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPAS 416
Cdd:cd05596   260 DAKSLICA-FLTDREVRLGRNGIEEIKAHPFFKNDQWTWDNIRETVPPVVPELSSDIDTSNFDDIEEDETPEETFPVPKA 338
                         330
                  ....*....|....
gi 1958807372 417 ANAHQL-FKGFSFV 429
Cdd:cd05596   339 FVGNHLpFVGFTYS 352
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
110-373 2.30e-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: 243.08  E-value: 2.30e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05609     1 DFETIKLISNGAYGAVYLVRHR---ETRQRFAMKKINKQNLILRNQIqQVFVERDILTFAENPFVVSMYCSFETKRHLCM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 259
Cdd:cd05609    78 VMEYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKiglmslttn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ---ESVDQEKKAYS---FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ- 332
Cdd:cd05609   158 lyeGHIEKDTREFLdkqVCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEg 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 333 --FLSAEAQSLLRMLFKRNPANRLGSEGVEEVKRHAFFSSIDW 373
Cdd:cd05609   238 ddALPDDAQDLITRLLQQNPLERLGTGGAEEVKQHPFFQDLDW 280
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
111-429 1.15e-73

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: 244.16  E-value: 1.15e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPdagQLYAMKVLRKASLKVRDRVR-TKMERDILVEVN-HPFIVKLHYAFQTEGKLYL 188
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKND---QIYAMKVVKKELVHDDEDIDwVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd05617    94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN-------MILKAKLGMPQFLSAEAQSL 341
Cdd:cd05617   174 STFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNtedylfqVILEKPIRIPRFLSVKASHV 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 342 LRMLFKRNPANRLGSE---GVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAK----TPKDSPGLP 414
Cdd:cd05617   254 LKGFLNKDPKERLGCQpqtGFSDIKSHTFFRSIDWDLLEKKQVTPPFKPQITDDYGLENFDTQFTSEpvqlTPDDEDVIK 333
                         330
                  ....*....|....*
gi 1958807372 415 ASANAHqlFKGFSFV 429
Cdd:cd05617   334 RIDQSE--FEGFEYI 346
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
111-387 2.66e-70

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: 232.25  E-value: 2.66e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRD-RVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05605     2 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKRKgEAMALNEKQILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 267
Cdd:cd05605    79 LTIMNGGDLKFHIYNmgNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVE-IPEGET 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 343
Cdd:cd05605   158 IRGRVGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARkekvKREEVDRRVKEDQEEYSEKFSEEAKSICS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 344 MLFKRNPANRLG--SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05605   238 QLLQKDPKTRLGcrGEGAEDVKSHPFFKSINFKRLEAGLLEPPFVP 283
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
464-720 3.61e-70

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: 231.41  E-value: 3.61e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YEL-KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRdPSEEIEILMRYGQHPNIISLKEVF----DDGKYVYLVTDLM 538
Cdd:cd14089     2 YTIsKQVLGLGINGKVLECFHKKTGEKFALKVLRDNPK-ARREVELHWRASGCPHIVRIIDVYentyQGRKCLLVVMECM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDSI-KICDFGFAKQLRGeNG 615
Cdd:cd14089    81 EGGELFSRIQERADsaFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKG--PNAIlKLTDFGFAKETTT-KK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGA 694
Cdd:cd14089   158 SLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKKRIRNGQYEFPNPEWSNVSEEA 237
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14089   238 KDLIRGLLKTDPSERLTIEEVMNHPW 263
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
462-729 1.28e-69

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: 230.65  E-value: 1.28e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK--RDPSEEIEI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14166     3 ETFIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPlsRDSSLENEIaVLKRIKHENIVTLEDIYESTTHYYLVMQLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYM--DESGhpdSIKICDFGFAKQlrGENGL 616
Cdd:cd14166    83 SGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLtpDENS---KIMITDFGLSKM--EQNGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKD 696
Cdd:cd14166   158 MSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY---EETESRLFEKIKEGYYEFESPFWDDISESAKD 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWITQREQLPR 729
Cdd:cd14166   235 FIRHLLEKNPSKRYTCEKALSHPWIIGNTALHR 267
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
111-428 1.33e-69

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: 233.41  E-value: 1.33e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05627     4 FESLKVIGRGAFGEVRLVQKK---DTGHIYAMKILRKADMLEKEQVaHIRAERDILVEADGAWVVKMFYSFQDKRNLYLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL------------ 257
Cdd:cd05627    81 MEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLctglkkahrtef 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 ------------------SKESVDQEKK-----AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 314
Cdd:cd05627   161 yrnlthnppsdfsfqnmnSKRKAETWKKnrrqlAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 315 DRNETMNMILKAKLGM---PQFLSAEAQSLLRMLFKRNPANRLGSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASgk 391
Cdd:cd05627   241 TPQETYRKVMNWKETLvfpPEVPISEKAKDLILRFCTDAENRIGSNGVEEIKSHPFFEGVDWEHIRERPAAIPIEIKS-- 318
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958807372 392 PDDTFCFD--PEFTAKTPKDSPGLPASANAHQLFKGFSF 428
Cdd:cd05627   319 IDDTSNFDdfPESDILQPAPNTTEPDYKSKDWVFLNYTY 357
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
111-429 1.02e-68

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 231.07  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKASLKVRDRVR-TKMERDILVEV-NHPFIVKLHYAFQTEGKLY 187
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRlKKTE----RIYAMKVVKKELVNDDEDIDwVQTEKHVFEQAsNHPFLVGLHSCFQTESRLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 267
Cdd:cd05618    98 FVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDT 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ--GKDRNETMN-------MILKAKLGMPQFLSAEA 338
Cdd:cd05618   178 TSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDivGSSDNPDQNtedylfqVILEKQIRIPRSLSVKA 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 339 QSLLRMLFKRNPANRLG---SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAK----TPKDSP 411
Cdd:cd05618   258 ASVLKSFLNKDPKERLGchpQTGFADIQGHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDSQFTNEpvqlTPDDDD 337
                         330
                  ....*....|....*...
gi 1958807372 412 GLPASANAHqlFKGFSFV 429
Cdd:cd05618   338 IVRKIDQSE--FEGFEYI 353
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
459-721 1.06e-68

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: 227.66  E-value: 1.06e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 459 QFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK------------RDPSEEIEILMRYgQHPNIISLKEVFD 526
Cdd:cd14084     3 ELRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrreinkpRNIETEIEILKKL-SHPCIIKIEDFFD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 527 DGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPdSIKICDFGF 606
Cdd:cd14084    82 AEDDYYIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEEC-LIKITDFGL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLrGENGLLLTPCYTANFVAPEVLT---QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTP--EEILlrigNGRFS 681
Cdd:cd14084   161 SKIL-GETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSlkEQIL----SGKYT 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 682 LSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14084   236 FIPKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
85-432 2.33e-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: 231.44  E-value: 2.33e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  85 RREDLVKEI-----PITQHVKEGYEKADpaQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRK-ASLKVRDRVRT 158
Cdd:cd05624    45 RRDKYVSEFlewakPFTQLVKEMQLHRD--DFEIIKVIGRGAFGEVAVVKMKN---TERIYAMKILNKwEMLKRAETACF 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 159 KMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDL 237
Cdd:cd05624   120 REERNVLVNGDCQWITTLHYAFQDENYLYLVMDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDI 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 238 KPENILLDEIGHIKLTDFG----LSKESVDQEKKAysfCGTVEYMAPEVVNRR-----GHSQSADWWSYGVLMFEMLTGT 308
Cdd:cd05624   200 KPDNVLLDMNGHIRLADFGsclkMNDDGTVQSSVA---VGTPDYISPEILQAMedgmgKYGPECDWWSLGVCMYEMLYGE 276
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 309 LPFQGKDRNETMNMIL--KAKLGMPQFL---SAEAQSLL-RMLFKRNpaNRLGSEGVEEVKRHAFFSSIDWNKLykREVQ 382
Cdd:cd05624   277 TPFYAESLVETYGKIMnhEERFQFPSHVtdvSEEAKDLIqRLICSRE--RRLGQNGIEDFKKHAFFEGLNWENI--RNLE 352
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 383 PPFRPASGKPDDTFCFD-PEFTAKTPKDSPglPAS----ANAHQLFKGFSFVATS 432
Cdd:cd05624   353 APYIPDVSSPSDTSNFDvDDDVLRNPEILP--PSShtgfSGLHLPFVGFTYTTES 405
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
464-726 6.15e-68

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: 226.15  E-value: 6.15e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDkNKRDPSEEIEILMRYG------QHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14086     3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIIN-TKKLSARDHQKLEREAricrllKHPNIVRLHDSISEEGFHYLVFDL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPdSIKICDFGFAKQLRGEN--- 614
Cdd:cd14086    82 VTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKGA-AVKLADFGLAIEVQGDQqaw 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 -GLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRG 693
Cdd:cd14086   161 fGFAGTPGY----LSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFW---DEDQHRLYAQIKAGAYDYPSPEWDTVTPE 233
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQ 726
Cdd:cd14086   234 AKDLINQMLTVNPAKRITAAEALKHPWICQRDR 266
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
464-720 2.66e-67

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 223.29  E-value: 2.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI---EILM-RYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMiesEILIiKSLSHPNIVKLFEVYETEKEIYLILEYVR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGEnglLLT 619
Cdd:cd14185    82 GGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVTGP---IFT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLS 699
Cdd:cd14185   159 VCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRS-PERDQEELFQIIQLGHYEFLPPYWDNISEAAKDLIS 237
                         250       260
                  ....*....|....*....|.
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14185   238 RLLVVDPEKRYTAKQVLQHPW 258
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
109-412 4.38e-67

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 227.20  E-value: 4.38e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05626     1 SMFVKIKTLGIGAFGEVCLACKV---DTHALYAMKTLRKKDVLNRNQVaHVKAERDILAEADNEWVVKLYYSFQDKDNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL---------- 257
Cdd:cd05626    78 FVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgfrwthns 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 ------------SKESVD-------------------------QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVL 300
Cdd:cd05626   158 kyyqkgshirqdSMEPSDlwddvsncrcgdrlktleqratkqhQRCLAHSLVGTPNYIAPEVLLRKGYTQLCDWWSVGVI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 301 MFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQ--FLSAEAQSLLRMLFKrNPANRLGSEGVEEVKRHAFFSSIDWNKL 376
Cdd:cd05626   238 LFEMLVGQPPFLAPTPTETQLKVInwENTLHIPPqvKLSPEAVDLITKLCC-SAEERLGRNGADDIKAHPFFSEVDFSSD 316
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1958807372 377 YKRevQP-PFRPASGKPDDTFCFDPEFTAKTPKDSPG 412
Cdd:cd05626   317 IRT--QPaPYVPKISHPMDTSNFDPVEEESPWNDASG 351
Pkinase pfam00069
Protein kinase domain;
464-721 5.47e-67

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 220.96  E-value: 5.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKdknilrEIKILKKL-NHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYlhsqgvvhrdlkpsnilymdesghpdsikicdfgfakqlrgeNGLL 617
Cdd:pfam00069  80 VEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES------------------------------------------GSSL 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLsggiWDNISRGAKDL 697
Cdd:pfam00069 118 TTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPEL----PSNLSEEAKDL 193
                         250       260
                  ....*....|....*....|....
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:pfam00069 194 LKKLLKKDPSKRLTATQALQHPWF 217
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
110-353 5.82e-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: 222.34  E-value: 5.82e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRK---SDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRL----SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd08215    78 MEYADGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEAQSLLRM 344
Cdd:cd08215   158 DLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNS 237

                  ....*....
gi 1958807372 345 LFKRNPANR 353
Cdd:cd08215   238 MLQKDPEKR 246
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
462-721 9.36e-67

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: 223.08  E-value: 9.36e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEF-AVKIIDK-----NKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKY 530
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVPLRNTGKPvAIKVVRKadlssDNLKGSSRANILkevqiMKRLSHPNIVKLLDFQESDEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILY--------------------- 589
Cdd:cd14096    81 YYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkadddetk 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 590 MDE--------SGHPDSIKICDFGFAKQLRGENglLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFS 661
Cdd:cd14096   161 VDEgefipgvgGGGIGIVKLADFGLSKQVWDSN--TKTPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFPPFY 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 662 NgpnDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14096   239 D---ESIETLTEKISRGDYTFLSPWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
111-399 1.99e-66

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: 225.30  E-value: 1.99e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05628     3 FESLKVIGRGAFGEVRLVQKK---DTGHVYAMKILRKADMLEKEQVgHIRAERDILVEADSLWVVKMFYSFQDKLNLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL------------ 257
Cdd:cd05628    80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkahrtef 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 ------------------SKESVDQEKK-----AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 314
Cdd:cd05628   160 yrnlnhslpsdftfqnmnSKRKAETWKRnrrqlAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPPFCSE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 315 DRNETMNMILKAKLGM---PQFLSAEAQSLLRMLFKRNPANRLGSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASgk 391
Cdd:cd05628   240 TPQETYKKVMNWKETLifpPEVPISEKAKDLILRFCCEWEHRIGAPGVEEIKTNPFFEGVDWEHIRERPAAIPIEIKS-- 317

                  ....*...
gi 1958807372 392 PDDTFCFD 399
Cdd:cd05628   318 IDDTSNFD 325
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
462-721 2.35e-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: 221.05  E-value: 2.35e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKEtsienEIAVLHKI-KHPNIVALDDIYESGGHLYLIMQ 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILY--MDESghpDSIKICDFGFAKqLRGEN 614
Cdd:cd14167    82 LVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYysLDED---SKIMISDFGLSK-IEGSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgPNDTpeEILLRIGNGRFSLSGGIWDNISRGA 694
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDA--KLFEQILKAEYEFDSPYWDDISDSA 234
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14167   235 KDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
462-720 2.75e-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: 220.67  E-value: 2.75e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEhlienEVSILRRV-KHPNIIMLIEEMDTPAELYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGEngl 616
Cdd:cd14184    80 LVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVCEYPDGTKSLKLGDFGLATVVEGP--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKD 696
Cdd:cd14184   157 LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRS-ENNLQEDLFDQILLGKLEFPSPYWDNITDSAKE 235
                         250       260
                  ....*....|....*....|....
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14184   236 LISHMLQVNVEARYTAEQILSHPW 259
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
464-722 3.79e-65

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: 217.34  E-value: 3.79e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-RDPSE------EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQlQKSGLehqlrrEIEI-QSHLRHPNILRLYGYFEDKKRIYLILE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrgENGL 616
Cdd:cd14007    81 YAPNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENIL-LGSNGE---LKLADFGWSVHA--PSNR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSlsggIWDNISRGAKD 696
Cdd:cd14007   155 RKTFCGTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPPF---ESKSHQETYKRIQNVDIK----FPSSVSPEAKD 227
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14007   228 LISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
110-438 6.49e-65

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: 220.32  E-value: 6.49e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEV----NHPFIVKLHYAFQTEGK 185
Cdd:cd05633     6 DFSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQE 265
Cdd:cd05633    83 LCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDF--SK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPF---QGKDRNETMNMILKAKLGMPQFLSAEAQSL 341
Cdd:cd05633   161 KKPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTVNVELPDSFSPELKSL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 342 LRMLFKRNPANRLGSE--GVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDpeFTAKTPKDSPGLPASANA 419
Cdd:cd05633   241 LEGLLQRDVSKRLGCHgrGAQEVKEHSFFKGIDWQQVYLQKYPPPLIPPRGEVNAADAFD--IGSFDEEDTKGIKLLDSD 318
                         330
                  ....*....|....*....
gi 1958807372 420 HQLFKGFSFVatsIAEEYK 438
Cdd:cd05633   319 QELYKNFPLV---ISERWQ 334
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
77-433 1.31e-64

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: 221.43  E-value: 1.31e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  77 DEGEPVFCRREDLVKEI-----PITQHVKEgyEKADPAQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRK-ASL 150
Cdd:cd05623    37 DECSNSPLRREKNILEYlewakPFTSKVKQ--MRLHKEDFEILKVIGRGAFGEVAVVKLK---NADKVFAMKILNKwEML 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 151 KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHR 229
Cdd:cd05623   112 KRAETACFREERDVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQ 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 230 LGIVYRDLKPENILLDEIGHIKLTDFG----LSKESVDQEKKAysfCGTVEYMAPEVVN-----RRGHSQSADWWSYGVL 300
Cdd:cd05623   192 LHYVHRDIKPDNILMDMNGHIRLADFGsclkLMEDGTVQSSVA---VGTPDYISPEILQamedgKGKYGPECDWWSLGVC 268
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 301 MFEMLTGTLPFQGKDRNETMNMIL--KAKLGMPQFL---SAEAQSLLRMLFKRNpANRLGSEGVEEVKRHAFFSSIDWNK 375
Cdd:cd05623   269 MYEMLYGETPFYAESLVETYGKIMnhKERFQFPTQVtdvSENAKDLIRRLICSR-EHRLGQNGIEDFKNHPFFVGIDWDN 347
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 376 LykREVQPPFRPASGKPDDTFCFDPEftAKTPKDSPGLP-----ASANAHQLFKGFSFVATSI 433
Cdd:cd05623   348 I--RNCEAPYIPEVSSPTDTSNFDVD--DDCLKNCETMPppthtAFSGHHLPFVGFTYTSSCV 406
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
110-405 1.52e-64

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: 219.37  E-value: 1.52e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05610     5 EFVIVKPISRGAFGKVYLGRKK---NNSKLYAVKVVKKADMINKNMVhQVQAERDALALSKSPFIVHLYYSLQSANNVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE--- 265
Cdd:cd05610    82 VMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRElnm 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 ------------KKAYS--------------------------------------FCGTVEYMAPEVVNRRGHSQSADWW 295
Cdd:cd05610   162 mdilttpsmakpKNDYSrtpgqvlslisslgfntptpyrtpksvrrgaarvegerILGTPDYLAPELLLGKPHGPAVDWW 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 296 SYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP---QFLSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAFFSSID 372
Cdd:cd05610   242 ALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKR---AGLKELKQHPLFHGVD 318
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1958807372 373 WNKLYKREvqPPFRPASGKPDDTFCFDPEFTAK 405
Cdd:cd05610   319 WENLQNQT--MPFIPQPDDETDTSYFEARNNAQ 349
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
464-721 2.16e-64

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: 215.48  E-value: 2.16e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDP---SEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd14087     3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGRevcESELNVLRRV-RHTNIIQLIEVFETKERVYMVMELATG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDeSGHPDSIKICDFGFAKQLR-GENGLLLT 619
Cdd:cd14087    82 GELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYH-PGPDSKIMITDFGLASTRKkGPNCLMKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLS 699
Cdd:cd14087   161 TCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFD---DDNRTRLYRQILRAKYSYSGEPWPSVSNLAKDFID 237
                         250       260
                  ....*....|....*....|..
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14087   238 RLLTVNPGERLSATQALKHPWI 259
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
460-723 4.68e-64

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: 215.16  E-value: 4.68e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID---KNKRDPSE----------EIEILMRYGQHPNIISLKEVFD 526
Cdd:cd14182     1 FYEKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDitgGGSFSPEEvqelreatlkEIDILRKVSGHPNIIQLKDTYE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 527 DGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGF 606
Cdd:cd14182    81 TNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDM----NIKLTDFGF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLrGENGLLLTPCYTANFVAPEVL------TQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndTPEEILLR-IGNGR 679
Cdd:cd14182   157 SCQL-DPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWH----RKQMLMLRmIMSGN 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 680 FSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd14182   232 YQFGSPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
470-720 6.66e-64

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: 213.67  E-value: 6.66e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKII---DKNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDR 546
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKFIpkrDKKKEAVLREISI-LNQLQHPRIIQLHEAYESPTELVLILELCSGGELLDR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 547 ILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDsIKICDFGFAKQLRGEnGLLLTPCYTANF 626
Cdd:cd14006    80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENIL-LADRPSPQ-IKIIDFGLARKLNPG-EELKEIFGTPEF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 627 VAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDP 706
Cdd:cd14006   157 VAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFL---GEDDQETLANISACRVDFSEEYFSSVSQEAKDFIRKLLVKEP 233
                         250
                  ....*....|....
gi 1958807372 707 HQRYTAEQVLKHPW 720
Cdd:cd14006   234 RKRPTAQEALQHPW 247
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
460-722 8.69e-64

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: 215.07  E-value: 8.69e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK--NKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14085     1 LEDFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKtvDKKIVRTEIGVLLRL-SHPNIIKLKEIFETPTEISLVLEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDS-IKICDFGFAKQLRGENgL 616
Cdd:cd14085    80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPA--PDApLKIADFGLSKIVDQQV-T 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRIGNGRFSLSGGIWDNISRGAKD 696
Cdd:cd14085   157 MKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGD--QYMFKRILNCDYDFVSPWWDDVSLNAKD 234
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14085   235 LVKKLIVLDPKKRLTTQQALQHPWVT 260
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
457-720 1.91e-63

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: 213.68  E-value: 1.91e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 457 AAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID------------KNKRDPSEEIEILMRYGQHPNIISLKEV 524
Cdd:cd14181     5 AKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlspeqleEVRSSTLKEIHILRQVSGHPSIITLIDS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 525 FDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDF 604
Cdd:cd14181    85 YESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENIL-LDDQLH---IKLSDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 605 GFAKQLrGENGLLLTPCYTANFVAPEVL------TQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndTPEEILLR-IGN 677
Cdd:cd14181   161 GFSCHL-EPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWH----RRQMLMLRmIME 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 678 GRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14181   236 GRYQFSSPEWDDRSSTVKDLISRLLVVDPEIRLTAEQALQHPF 278
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
111-426 2.33e-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: 214.91  E-value: 2.33e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEV----NHPFIVKLHYAFQTEGKL 186
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKA---DTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQEK 266
Cdd:cd14223    79 SFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDF--SKK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRR-GHSQSADWWSYGVLMFEMLTGTLPF---QGKDRNETMNMILKAKLGMPQFLSAEAQSLL 342
Cdd:cd14223   157 KPHASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLRGHSPFrqhKTKDKHEIDRMTLTMAVELPDSFSPELRSLL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 343 RMLFKRNPANRLG--SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDpeFTAKTPKDSPGLPASANAH 420
Cdd:cd14223   237 EGLLQRDVNRRLGcmGRGAQEVKEEPFFRGLDWQMVFLQKYPPPLIPPRGEVNAADAFD--IGSFDEEDTKGIKLLESDQ 314

                  ....*.
gi 1958807372 421 QLFKGF 426
Cdd:cd14223   315 ELYRNF 320
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
461-729 2.64e-63

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: 213.21  E-value: 2.64e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14169     2 NSVYELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKEamvenEIAVLRRI-NHENIVSLEDIYESPTHLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdESGHPDS-IKICDFGFAKQlrGEN 614
Cdd:cd14169    81 ELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLY--ATPFEDSkIMISDFGLSKI--EAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgPNDTpeEILLRIGNGRFSLSGGIWDNISRGA 694
Cdd:cd14169   157 GMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYD-ENDS--ELFNQILKAEYEFDSPYWDDISESA 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLPR 729
Cdd:cd14169   234 KDFIRHLLERDPEKRFTCEQALQHPWISGDTALDR 268
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
464-721 2.76e-63

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: 212.81  E-value: 2.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNME--FAVKIIDKnKRDPSE--------EIEILMRYgQHPNIISLKEVFDDGKYVYL 533
Cdd:cd14080     2 YRLGKTIGEGSYSKVKLAEYTKSGLKekVACKIIDK-KKAPKDflekflprELEILRKL-RHPNIIQVYSIFERGSKVFI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGE 613
Cdd:cd14080    80 FMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENIL-LDSNNN---VKLSDFGFARLCPDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLL--TPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFsngpNDTPEEILLRIGNGR---FSLSGgiw 687
Cdd:cd14080   156 DGDVLskTFCGSAAYAAPEILQGIPYDPkKYDIWSLGVILYIMLCGSMPF----DDSNIKKMLKDQQNRkvrFPSSV--- 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 688 DNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14080   229 KKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
109-400 3.08e-63

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: 216.84  E-value: 3.08e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05625     1 SMFVKIKTLGIGAFGEVCLARKV---DTKALYATKTLRKKDVLLRNQVaHVKAERDILAEADNEWVVRLYYSFQDKDNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL---------- 257
Cdd:cd05625    78 FVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthds 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 ---------SKESVD----------------------------QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVL 300
Cdd:cd05625   158 kyyqsgdhlRQDSMDfsnewgdpencrcgdrlkplerraarqhQRCLAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 301 MFEMLTGTLPFQGKDRNETMNMILKAKLGM---PQF-LSAEAQSLLRMLFkRNPANRLGSEGVEEVKRHAFFSSIDWNKL 376
Cdd:cd05625   238 LFEMLVGQPPFLAQTPLETQMKVINWQTSLhipPQAkLSPEASDLIIKLC-RGPEDRLGKNGADEIKAHPFFKTIDFSSD 316
                         330       340
                  ....*....|....*....|....
gi 1958807372 377 YkREVQPPFRPASGKPDDTFCFDP 400
Cdd:cd05625   317 L-RQQSAPYIPKITHPTDTSNFDP 339
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
464-720 4.94e-63

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: 211.88  E-value: 4.94e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-------RDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14663     2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQvaregmvEQIKREIAI-MKLLRHPNIVELHEVMATKTKIFFVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGF---AKQLRGE 613
Cdd:cd14663    81 LVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLL-LDEDGN---LKISDFGLsalSEQFRQD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 nGLLLTPCYTANFVAPEVLTQQGYD-AACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGgiWdnISR 692
Cdd:cd14663   157 -GLLHTTCGTPNYVAPEVLARRGYDgAKADIWSCGVILFVLLAGYLPFD---DENLMALYRKIMKGEFEYPR--W--FSP 228
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14663   229 GAKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
464-721 1.23e-62

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: 210.57  E-value: 1.23e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEI-LMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14081     3 YRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESvlmkvEREIaIMKLIEHPNVLKLYDVYENKKYLYLVLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKqLRGENGLL 617
Cdd:cd14081    83 VSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLL-LDEKN---NIKIADFGMAS-LQPEGSLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYD-AACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSlsggIWDNISRGAKD 696
Cdd:cd14081   158 ETSCGSPHYACPEVIKGEKYDgRKADIWSCGVILYALLVGALPFD---DDNLRQLLEKVKRGVFH----IPHFISPDAQD 230
                         250       260
                  ....*....|....*....|....*
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14081   231 LLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
470-720 4.54e-62

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: 208.91  E-value: 4.54e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNK-------RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEiikrkevEHTLNERNILERV-NHPFIVKLHYAFQTEEKLYLVLDYVPGGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASnvLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTP 620
Cdd:cd05123    80 LFSHLSKEGRFPEERAR--FYAaeIVLALEYLHSLGIIYRDLKPENIL-LDSDGH---IKLTDFGLAKELSSDGDRTYTF 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSggiwDNISRGAKDLLSH 700
Cdd:cd05123   154 CGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPF---YAENRKEIYEKILKSPLKFP----EYVSPEAKSLISG 226
                         250       260
                  ....*....|....*....|...
gi 1958807372 701 MLHMDPHQRYT---AEQVLKHPW 720
Cdd:cd05123   227 LLQKDPTKRLGsggAEEIKAHPF 249
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
470-721 9.96e-62

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: 208.56  E-value: 9.96e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNK--------------RDPSE----EIEIlMRYGQHPNIISLKEVFDD--GK 529
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRlrkrregkndrgkiKNALDdvrrEIAI-MKKLDHPNIVRLYEVIDDpeSD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 530 YVYLVTDLMKGGELLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFA 607
Cdd:cd14008    80 KLYLVLEYCEGGPVMELDSGDRvpPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLL-LTADGT---VKISDFGVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQLRGENGLLLTPCYTANFVAPEVLT--QQGYDA-ACDIWSLGVLLYTMLAGYTPFsNGpnDTPEEILLRIGNGRFSLsg 684
Cdd:cd14008   156 EMFEDGNDTLQKTAGTPAFLAPELCDgdSKTYSGkAADIWALGVTLYCLVFGRLPF-NG--DNILELYEAIQNQNDEF-- 230
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 685 GIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14008   231 PIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
111-387 1.52e-61

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 208.72  E-value: 1.52e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05630     2 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKRKGEAMALnEKQILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 267
Cdd:cd05630    79 LTLMNGGDLKFHIYHmgQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVH-VPEGQT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 343
Cdd:cd05630   158 IKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRkkkiKREEVERLVKEVPEEYSEKFSPQARSLCS 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 344 MLFKRNPANRLGSEG--VEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05630   238 MLLCKDPAERLGCRGggAREVKEHPLFKKLNFKRLGAGMLEPPFKP 283
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
111-364 1.77e-61

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 214.88  E-value: 1.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLRKASLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARD---LRLGRPVALKVLRPELAAdPEARERFRREARALARLNHPNIVRVYDVGEEDGRPYLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-KKA 268
Cdd:COG0515    86 MEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATlTQT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAE-----AQSLLR 343
Cdd:COG0515   166 GTVVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPSELRPDlppalDAIVLR 245
                         250       260
                  ....*....|....*....|.
gi 1958807372 344 MLFKrNPANRLGSegVEEVKR 364
Cdd:COG0515   246 ALAK-DPEERYQS--AAELAA 263
Pkinase pfam00069
Protein kinase domain;
111-368 1.77e-61

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 206.33  E-value: 1.77e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHR---DTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHlhrlgivyrdlkpenilldeighikltdfglskesvdqEKKAYS 270
Cdd:pfam00069  78 EYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLES--------------------------------------GSSLTT 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFK 347
Cdd:pfam00069 120 FVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLK 199
                         250       260
                  ....*....|....*....|.
gi 1958807372 348 RNPANRLgseGVEEVKRHAFF 368
Cdd:pfam00069 200 KDPSKRL---TATQALQHPWF 217
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
458-722 9.23e-61

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 206.00  E-value: 9.23e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 458 AQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVY 532
Cdd:cd14183     2 ASISERYKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKEhmiqnEVSILRRV-KHPNIVLLIEEMDMPTELY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLrg 612
Cdd:cd14183    81 LVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATVV-- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 eNGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNDTPEEILLRIGNGRFSLSGGIWDNISR 692
Cdd:cd14183   159 -DGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPF-RGSGDDQEVLFDQILMGQVDFPSPYWDNVSD 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14183   237 SAKELITMMLQVDVDQRYSALQVLEHPWVN 266
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
110-365 1.00e-60

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 205.72  E-value: 1.00e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKaSLKVRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTK---TGESVAIKIIDK-EQVAREGMVEQIKREIAImkLLRHPNIVELHEVMATKTKIF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS--KESVDQE 265
Cdd:cd14663    77 FVMELVTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalSEQFRQD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRM 344
Cdd:cd14663   157 GLLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKR 236
                         250       260
                  ....*....|....*....|.
gi 1958807372 345 LFKRNPANRLgseGVEEVKRH 365
Cdd:cd14663   237 ILDPNPSTRI---TVEQIMAS 254
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
95-428 1.06e-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: 207.16  E-value: 1.06e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  95 ITQHVKEGYEKADpaQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASL-KVRDRVRTKMERDILVEVNHPFI 173
Cdd:cd05621    40 IVNKIRELQMKAE--DYDVVKVIGRGAFGEVQLVRHKA---SQKVYAMKLLSKFEMiKRSDSAFFWEERDIMAFANSPWV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 174 VKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLT 253
Cdd:cd05621   115 VQLFCAFQDDKYLYMVMEYMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 254 DFGLSKEsVDQEKKAY--SFCGTVEYMAPEVVNRRG----HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL--K 325
Cdd:cd05621   194 DFGTCMK-MDETGMVHcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKIMdhK 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 326 AKLGMPQ--FLSAEAQSLLrMLFKRNPANRLGSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFT 403
Cdd:cd05621   273 NSLNFPDdvEISKHAKNLI-CAFLTDREVRLGRNGVEEIKQHPFFRNDQWNWDNIRETAAPVVPELSSDIDTSNFDDIED 351
                         330       340
                  ....*....|....*....|....*.
gi 1958807372 404 AKTPKDSPGLPASANAHQL-FKGFSF 428
Cdd:cd05621   352 DKGDVETFPIPKAFVGNQLpFVGFTY 377
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
117-365 1.10e-59

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: 201.34  E-value: 1.10e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd00180     1 LGKGSFGKVYKARDKET---GKKVAVKVIPKEKLK-KLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAYSFCG 273
Cdd:cd00180    77 SLKDLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdlDSDDSLLKTTGGTT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMltgtlpfqgkdrnetmnmilkaklgmpqflsAEAQSLLRMLFKRNPANR 353
Cdd:cd00180   157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKR 205
                         250
                  ....*....|..
gi 1958807372 354 LgseGVEEVKRH 365
Cdd:cd00180   206 P---SAKELLEH 214
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
462-721 1.18e-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: 203.72  E-value: 1.18e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDI-GIGSYSVCKRCIHSASNMEFAVKIIDK----NKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14173     1 DVYQLQEEVlGEGAYARVQTCINLITNKEYAVKIIEKrpghSRSRVFREVEMLYQCQGHRNVLELIEFFEEEDKFYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILymdeSGHPDSI---KICDF--GFAKQLR 611
Cdd:cd14173    81 KMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENIL----CEHPNQVspvKICDFdlGSGIKLN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENG-----LLLTPCYTANFVAPEVLTQQG-----YDAACDIWSLGVLLYTMLAGYTPF-----SNGPNDTPEE------ 670
Cdd:cd14173   157 SDCSpistpELLTPCGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIMLSGYPPFvgrcgSDCGWDRGEAcpacqn 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 671 -ILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14173   237 mLFESIQEGKYEFPEKDWAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
111-399 1.29e-59

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 205.60  E-value: 1.29e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTG--PDAgqlyAMKVLRKASLKVRDRV-RTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:PTZ00426   32 FNFIRTLGTGSFGRVILATYKNEdfPPV----AIKRFEKSKIIKQKQVdHVFSERKILNYINHPFCVNLYGSFKDESYLY 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdqEKK 267
Cdd:PTZ00426  108 LVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV---DTR 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 347
Cdd:PTZ00426  185 TYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLS 264
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 348 RNPANRLGS--EGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFD 399
Cdd:PTZ00426  265 HDLTKRYGNlkKGAQNVKEHPWFGNIDWVSLLHKNVEVPYKPKYKNVFDSSNFE 318
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
460-721 1.57e-59

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: 202.58  E-value: 1.57e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYEL-KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYGQHPNIISLKEVFDDGKYVY 532
Cdd:cd14106     5 INEVYTVeSTPLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDcrneilHEIAVLELCKDCPRVVNLHEVYETRSELI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDsIKICDFGFAKQL-R 611
Cdd:cd14106    85 LILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFPLGD-IKLCDFGISRVIgE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GEN--GLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDN 689
Cdd:cd14106   164 GEEirEILGTPDY----VAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFG---GDDKQETFLNISQCNLDFPEELFKD 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 690 ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14106   237 VSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
111-387 2.76e-59

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: 202.92  E-value: 2.76e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05631     2 FRHYRVLGKGGFGEVCACQVRA---TGKMYACKKLEKKRIKKRKGEAMALnEKRILEKVNSRFVVSLAYAYETKDALCLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 267
Cdd:cd05631    79 LTIMNGGDLKFHIYNmgNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQ-IPEGET 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 343
Cdd:cd05631   158 VRGRVGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRkervKREEVDRRVKEDQEEYSEKFSEDAKSICR 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 344 MLFKRNPANRLG--SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05631   238 MLLTKNPKERLGcrGNGAAGVKQHPIFKNINFKRLEANMLEPPFCP 283
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
115-368 4.48e-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: 201.24  E-value: 4.48e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLRKASLKvRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd14099     7 KFLGKGGFAKCYEV---TDMSTGKVYAGKVVPKSSLT-KPKQREKLKSEIKIhrSLKHPNIVKFHDCFEDEENVYILLEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd14099    83 CSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL--SAEAQSLLRMLFKRN 349
Cdd:cd14099   163 GTPNYIAPEVLEKkKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHLsiSDEAKDLIRSMLQPD 242
                         250
                  ....*....|....*....
gi 1958807372 350 PANRLgseGVEEVKRHAFF 368
Cdd:cd14099   243 PTKRP---SLDEILSHPFF 258
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
111-399 2.58e-58

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: 200.97  E-value: 2.58e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05632     4 FRQYRVLGKGGFGEVCACQVRA---TGKMYACKRLEKKRIKKRKGESMALnEKQILEKVNSQFVVNLAYAYETKDALCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 267
Cdd:cd05632    81 LTIMNGGDLKFHIYNmgNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVK-IPEGES 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLR 343
Cdd:cd05632   160 IRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRkekvKREEVDRRVLETEEVYSAKFSEEAKSICK 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 344 MLFKRNPANRLG--SEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPasgKPDDTFCFD 399
Cdd:cd05632   240 MLLTKDPKQRLGcqEEGAGEVKRHPFFRNMNFKRLEAGMLDPPFVP---DPRAVYCKD 294
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
115-368 5.60e-58

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: 198.13  E-value: 5.60e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd06606     6 ELLGKGSFGSVYLaLNLDTG----ELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAYSF 271
Cdd:cd06606    82 PGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrlAEIATGEGTKSL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF-QGKDRNETMNMILKAKLG--MPQFLSAEAQSLLRMLFKR 348
Cdd:cd06606   162 RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWsELGNPVAALFKIGSSGEPppIPEHLSEEAKDFLRKCLQR 241
                         250       260
                  ....*....|....*....|
gi 1958807372 349 NPANRLgseGVEEVKRHAFF 368
Cdd:cd06606   242 DPKKRP---TADELLQHPFL 258
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
462-721 7.75e-58

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: 198.84  E-value: 7.75e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYEL--KEDIGIGSYSVCKRCIHSASNMEFAVKI-IDKNKrdPSEEIEILMRYGQHPNIISLKEVFDDG---------- 528
Cdd:cd14171     4 EEYEVnwTQKLGTGISGPVRVCVKKSTGERFALKIlLDRPK--ARTEVRLHMMCSGHPNIVQIYDVYANSvqfpgesspr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 KYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDS-IKICDFGFA 607
Cdd:cd14171    82 ARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNS--EDApIKLCDFGFA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQlrgENGLLLTPCYTANFVAPEVL-----------------TQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDT-P 668
Cdd:cd14171   160 KV---DQGDLMTPQFTPYYVAPQVLeaqrrhrkersgiptspTPYTYDKSCDMWSLGVIIYIMLCGYPPFySEHPSRTiT 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 669 EEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14171   237 KDMKRKIMTGSYEFPEEEWSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
460-726 9.90e-58

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: 198.92  E-value: 9.90e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK---------RDPSEEIEILMRYgQHPNIISLKEVFDDGKY 530
Cdd:cd14094     1 FEDVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsspglstEDLKREASICHML-KHPHIVELLETYSSDGM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGELLDRILKKK----CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMD-ESGHPdsIKICDFG 605
Cdd:cd14094    80 LYMVFEFMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLASkENSAP--VKLGGFG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndTPEEILLRIGNGRFSLSGG 685
Cdd:cd14094   158 VAIQLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYG----TKERLFEGIIKGKYKMNPR 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 686 IWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQ 726
Cdd:cd14094   234 QWSHISESAKDLVRRMLMLDPAERITVYEALNHPWIKERDR 274
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
464-720 1.28e-57

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: 197.31  E-value: 1.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK-----NKRDP---SEEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14098     2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKrkvagNDKNLqlfQREINILKSL-EHPGIVRLIDWYEDDQHIYLVM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDSIKICDFGFAKqLRGENG 615
Cdd:cd14098    81 EYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDD--PVIVKISDFGLAK-VIHTGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQ------GYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDN 689
Cdd:cd14098   158 FLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFD---GSSQLPVEKRIRKGRYTQPPLVDFN 234
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 690 ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14098   235 ISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
464-721 1.58e-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: 197.95  E-value: 1.58e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDI-GIGSYSVCKRCIHSASNMEFAVKIIDKN----KRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14174     3 YRLTDELlGEGAYAKVQGCVSLQNGKEYAVKIIEKNaghsRSRVFREVETLYQCQGNKNILELIEFFEDDTRFYLVFEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDSIKICDFGFAKQLRGENGL-- 616
Cdd:cd14174    83 RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENIL-CESPDKVSPVKICDFDLGSGVKLNSACtp 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 -----LLTPCYTANFVAPEVL---TQQG--YDAACDIWSLGVLLYTMLAGYTPFSN--GPN---DTPE-------EILLR 674
Cdd:cd14174   162 ittpeLTTPCGSAEYMAPEVVevfTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGhcGTDcgwDRGEvcrvcqnKLFES 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 675 IGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14174   242 IQEGKYEFPDKDWSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
470-719 2.60e-57

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: 194.80  E-value: 2.60e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS-----EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELL 544
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKLleellREIEILKKL-NHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYT 623
Cdd:cd00180    80 DLLkENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENIL-LDSDGT---VKLADFGLAKDLDSDDSLLKTTGGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 AN--FVAPEVLTQQGYDAACDIWSLGVLLYTMlagytpfsngpndtpeeillrigngrfslsggiwdnisRGAKDLLSHM 701
Cdd:cd00180   156 TPpyYAPPELLGGRYYGPKVDIWSLGVILYEL--------------------------------------EELKDLIRRM 197
                         250
                  ....*....|....*...
gi 1958807372 702 LHMDPHQRYTAEQVLKHP 719
Cdd:cd00180   198 LQYDPKKRPSAKELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
110-364 3.30e-57

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: 196.27  E-value: 3.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRkASLKVRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLL---GRPVAIKVLR-PELAEDEEFRERFLReaRALARLSHPNIVRVYDVGEDDGRPY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK-ESVDQEK 266
Cdd:cd14014    77 IVMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARaLGDSGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL-GMPQFLSAEAQSL---- 341
Cdd:cd14014   157 QTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPpPPSPLNPDVPPALdaii 236
                         250       260
                  ....*....|....*....|...
gi 1958807372 342 LRMLfKRNPANRLGSegVEEVKR 364
Cdd:cd14014   237 LRAL-AKDPEERPQS--AAELLA 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
110-368 5.35e-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: 195.55  E-value: 5.35e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLRKASLkVRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKL 186
Cdd:cd14081     2 PYRLGKTLGKGQTGLVKLaKHCVTG----QKVAIKIVNKEKL-SKESVLMKVEREIAIMklIEHPNVLKLYDVYENKKYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSkeSVDQE- 265
Cdd:cd14081    77 YLVLEYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMA--SLQPEg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRM 344
Cdd:cd14081   155 SLLETSCGSPHYACPEVIkGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRR 234
                         250       260
                  ....*....|....*....|....
gi 1958807372 345 LFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14081   235 MLEVNPEKRI---TIEEIKKHPWF 255
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
99-428 9.47e-57

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 199.85  E-value: 9.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  99 VKEGYEKADpaQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASL-KVRDRVRTKMERDILVEVNHPFIVKLH 177
Cdd:cd05622    65 IRDLRMKAE--DYEVVKVIGRGAFGEVQLVRHKS---TRKVYAMKLLSKFEMiKRSDSAFFWEERDIMAFANSPWVVQLF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 YAFQTEGKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05622   140 YAFQDDRYLYMVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGT 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 S-KESVDQEKKAYSFCGTVEYMAPEVVNRRG----HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK--LGM 330
Cdd:cd05622   219 CmKMNKEGMVRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKnsLTF 298
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 331 PQ--FLSAEAQSLLrMLFKRNPANRLGSEGVEEVKRHAFFSSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPK 408
Cdd:cd05622   299 PDdnDISKEAKNLI-CAFLTDREVRLGRNGVEEIKRHLFFKNDQWAWETLRDTVAPVVPDLSSDIDTSNFDDLEEDKGEE 377
                         330       340
                  ....*....|....*....|.
gi 1958807372 409 DSPGLPASANAHQL-FKGFSF 428
Cdd:cd05622   378 ETFPIPKAFVGNQLpFVGFTY 398
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
457-721 1.74e-56

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 195.65  E-value: 1.74e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 457 AAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK---RDPSEEIEI-LMRYGQHPNIISLKEVFDDGKYVY 532
Cdd:cd14168     5 VEDIKKIFEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKAlkgKESSIENEIaVLRKIKHENIVALEDIYESPNHLY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESgHPDSIKICDFGFAKqLRG 612
Cdd:cd14168    85 LVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQD-EESKIMISDFGLSK-MEG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgPNDTpeEILLRIGNGRFSLSGGIWDNISR 692
Cdd:cd14168   163 KGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYD-ENDS--KLFEQILKADYEFDSPYWDDISD 239
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14168   240 SAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
117-368 3.40e-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: 193.54  E-value: 3.40e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLK-------VRDRVRTKMER-----DILVEVNHPFIVKLHYAF--QT 182
Cdd:cd14008     1 LGRGSFGKVKLALDT---ETGQLYAIKIFNKSRLRkrregknDRGKIKNALDDvrreiAIMKKLDHPNIVRLYEVIddPE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSkE 260
Cdd:cd14008    78 SDKLYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVS-E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAYSFC-GTVEYMAPEV--VNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL--GMPQFL 334
Cdd:cd14008   157 MFEDGNDTLQKTaGTPAFLAPELcdGDSKTySGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDefPIPPEL 236
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 335 SAEAQSLLRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14008   237 SPELKDLLRRMLEKDPEKRI---TLKEIKEHPWV 267
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
111-387 4.65e-56

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: 193.97  E-value: 4.65e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05607     4 FYEFRVLGKGGFGEVCAVQVKN---TGQMYACKKLDKKRLKKKSGEKMALlEKEILEKVNSPFIVSLAYAFETKTHLCLV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKK 267
Cdd:cd05607    81 MSLMNGGDLKYHIYNvgERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVE-VKEGKP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILK--AKLGMPQFlSAEAQSL 341
Cdd:cd05607   160 ITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHkekvSKEELKRRTLEdeVKFEHQNF-TEEAKDI 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 342 LRMLFKRNPANRLGS-EGVEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05607   239 CRLFLAKKPENRLGSrTNDDDPRKHEFFKSINFPRLEAGLIDPPFVP 285
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
470-721 9.81e-56

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: 191.67  E-value: 9.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE----EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD 545
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREdvrnEIEI-MNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKKKcFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdSIKICDFGFAKQLrGENGLLLTPCYT 623
Cdd:cd14103    80 RVVDDD-FELTERDCILFMrqICEGVQYMHKQGILHLDLKPENILCVSRTGN--QIKIIDFGLARKY-DPDKKLKVLFGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTqqgYDA---ACDIWSLGVLLYTMLAGYTPFSnGPNDTpeEILLRIGNGRFSLSGGIWDNISRGAKDLLSH 700
Cdd:cd14103   156 PEFVAPEVVN---YEPisyATDMWSVGVICYVLLSGLSPFM-GDNDA--ETLANVTRAKWDFDDEAFDDISDEAKDFISK 229
                         250       260
                  ....*....|....*....|.
gi 1958807372 701 MLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14103   230 LLVKDPRKRMSAAQCLQHPWL 250
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
464-721 3.91e-55

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: 190.46  E-value: 3.91e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK-------NKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14099     3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPKssltkpkQREKLKSEIKI-HRSLKHPNIVKFHDCFEDEENVYILLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGL 616
Cdd:cd14099    82 LCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLF-LDENMN---VKIGDFGLAARLEYDGER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIwdNISRGAK 695
Cdd:cd14099   158 KKTLCGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLLVGKPPFE---TSDVKETYKRIKKNEYSFPSHL--SISDEAK 232
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14099   233 DLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
114-387 5.06e-55

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: 191.25  E-value: 5.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05608     6 FRVLGKGGFGEVSACQMRA---TGKLYACKKLNKKRLKKRKGYEGAMvEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd05608    83 MNGGDlryhIYNVDEENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKT 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK----DRNETMNMILKAKLGMPQFLSAEAQSLLRM 344
Cdd:cd05608   163 KGYAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFRARgekvENKELKQRILNDSVTYSEKFSPASKSICEA 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 345 LFKRNPANRLGSE--GVEEVKRHAFFSSIDWNKLYKREVQPPFRP 387
Cdd:cd05608   243 LLAKDPEKRLGFRdgNCDGLRTHPFFRDINWRKLEAGILPPPFVP 287
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
461-721 1.16e-54

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: 189.43  E-value: 1.16e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYEL-KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRdPSEEIEILMRYGQHPNIISLKEVFDD---GKYVYL-VT 535
Cdd:cd14172     2 TDDYKLsKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPK-ARREVEHHWRASGGPHIVHILDVYENmhhGKRCLLiIM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKK--KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDsIKICDFGFAKQLRGE 613
Cdd:cd14172    81 ECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAV-LKLTDFGFAKETTVQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLlTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSGGIWDNISR 692
Cdd:cd14172   160 NALQ-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFySNTGQAISPGMKRRIRMGQYGFPNPEWAEVSE 238
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14172   239 EAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
464-721 1.78e-54

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: 188.78  E-value: 1.78e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFqevrcMKLVQHPNVVRLYEVIDTQTKLYLILELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdSIKICDFGFAKQLR-GENgl 616
Cdd:cd14074    85 DGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQG---LVKLTDFGFSNKFQpGEK-- 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNGpNDTpeEILLRIGNGRFSLSggiwDNISRGAK 695
Cdd:cd14074   160 LETSCGSLAYSAPEILLGDEYDApAVDIWSLGVILYMLVCGQPPFQEA-NDS--ETLTMIMDCKYTVP----AHVSPECK 232
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14074   233 DLIRRMLIRDPKKRASLEEIENHPWL 258
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
464-721 1.92e-54

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: 188.85  E-value: 1.92e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIE---ILMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKASrrgvsrEDIErevSILRQVLHPNIITLHDVFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLrgEN 614
Cdd:cd14105    87 LELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFGLAHKI--ED 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLL-TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRG 693
Cdd:cd14105   165 GNEFkNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVNYDFDDEYFSNTSEL 241
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14105   242 AKDFIRQLLVKDPRKRMTIQESLRHPWI 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
464-721 3.71e-54

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 187.41  E-value: 3.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI--EI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESIlnEIaILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDrILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGlLL 618
Cdd:cd05122    82 GSLKD-LLKNTNktLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANIL-LTSDGE---VKLIDFGLSAQLSDGKT-RN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFSLSGGIWdnISRGAKDL 697
Cdd:cd05122   156 TFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYS---ELPPMKALFLIAtNGPPGLRNPKK--WSKEFKDF 230
                         250       260
                  ....*....|....*....|....
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd05122   231 LKKCLQKDPEKRPTAEQLLKHPFI 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
111-368 4.64e-54

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 187.41  E-value: 4.64e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05122     2 FEILEKIGKGGFGVVYKARhKKTG----QIVAIKKINLESKEKKESILN--EIAILKKCKHPNIVKYYGSYLKKDELWIV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsVDQEKKA 268
Cdd:cd05122    76 MEFCSGGSLKDLLkNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQ-LSDGKTR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK---AKLGMPQFLSAEAQSLLRML 345
Cdd:cd05122   155 NTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATngpPGLRNPKKWSKEFKDFLKKC 234
                         250       260
                  ....*....|....*....|...
gi 1958807372 346 FKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd05122   235 LQKDPEKRP---TAEQLLKHPFI 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
464-720 1.89e-53

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: 185.55  E-value: 1.89e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-------EIEILmRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14079     4 YILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDmeekirrEIQIL-KLFRHPHIIRLYEVIETPTDIFMVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDesgHPDSIKICDFGFAKQLR-GEng 615
Cdd:cd14079    83 YVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLL-LD---SNMNVKIADFGLSNIMRdGE-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPF--SNGPNdtpeeILLRIGNGRFSLSggiwDNISR 692
Cdd:cd14079   157 FLKTSCGSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPFddEHIPN-----LFKKIKSGIYTIP----SHLSP 227
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14079   228 GARDLIKRMLVVDPLKRITIPEIRQHPW 255
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
117-354 3.73e-53

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 184.39  E-value: 3.73e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASlkvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14006     1 LGRGRFGVVKRCIEKA---TGREFAAKFIPKRD---KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG--HIKLTDFGLSKEsVDQEKKAYSFCGT 274
Cdd:cd14006    75 ELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARK-LNPGEELKEIFGT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 275 VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG----MPQFLSAEAQSLLRMLFKRNP 350
Cdd:cd14006   154 PEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDfseeYFSSVSQEAKDFIRKLLVKEP 233

                  ....
gi 1958807372 351 ANRL 354
Cdd:cd14006   234 RKRP 237
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
470-721 7.44e-53

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 184.26  E-value: 7.44e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE----EIEI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELL 544
Cdd:cd06606     8 LGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEElealEREIrILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRGENGL--LLTPCY 622
Cdd:cd06606    88 SLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANIL-VDSDG---VVKLADFGCAKRLAEIATGegTKSLRG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLRIGNGrfSLSGGIWDNISRGAKDLLSHML 702
Cdd:cd06606   164 TPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSELGN--PVAALFKIGSS--GEPPPIPEHLSEEAKDFLRKCL 239
                         250
                  ....*....|....*....
gi 1958807372 703 HMDPHQRYTAEQVLKHPWI 721
Cdd:cd06606   240 QRDPKKRPTADELLQHPFL 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
113-368 8.87e-53

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: 183.92  E-value: 8.87e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVrKKTGPDAGQLYAMKVLRKAslKVRDRVRTKM---ERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14080     4 LGKTIGEGSYSKVKLA-EYTKSGLKEKVACKIIDKK--KAPKDFLEKFlprELEILRKLRHPNIIQVYSIFERGSKVFIF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAY 269
Cdd:cd14080    81 MEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 S--FCGTVEYMAPEVVnrRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP---QFLSAEAQSL 341
Cdd:cd14080   161 SktFCGSAAYAAPEIL--QGipyDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECKDL 238
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 342 LRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14080   239 IDQLLEPDPTKRA---TIEEILNHPWL 262
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
462-721 1.03e-52

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: 184.07  E-value: 1.03e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK----------NKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYV 531
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKrrtkssrrgvSREDIEREVSILKEI-QHPNVITLHEVYENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLR 611
Cdd:cd14194    84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKID 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GEN---GLLLTPcytaNFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWD 688
Cdd:cd14194   164 FGNefkNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANVSAVNYEFEDEYFS 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14194   237 NTSALAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
462-721 1.86e-52

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: 183.52  E-value: 1.86e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILmRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14097     1 KIYTFGRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSavklleREVDIL-KHVNHAHIIHLEEVFETPKRMYLVM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILY---MDESGHPDSIKICDFGFA--KQL 610
Cdd:cd14097    80 ELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssIIDNNDKLNIKVTDFGLSvqKYG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTpCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNGRFSLSGGIWDNI 690
Cdd:cd14097   160 LGEDMLQET-CGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAK---SEEKLFEEIRKGDLTFTQSVWQSV 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 691 SRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14097   236 SDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
117-357 3.92e-52

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: 182.04  E-value: 3.92e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14009     1 IGRGSFATVWKGRHK---QTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKeSVDQEKKAYSFCG 273
Cdd:cd14009    78 DLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFAR-SLQPASMAETLCG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFKRN 349
Cdd:cd14009   157 SPLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSDAVIPfpiaAQLSPDCKDLLRRLLRRD 236

                  ....*...
gi 1958807372 350 PANRLGSE 357
Cdd:cd14009   237 PAERISFE 244
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
470-729 4.76e-52

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: 183.70  E-value: 4.76e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRdPSEEIEILMRYGQHPNIISLKEVFDD----GKYVYLVTDLMKGGELLD 545
Cdd:cd14170    10 LGLGINGKVLQIFNKRTQEKFALKMLQDCPK-ARREVELHWRASQCPHIVRIVDVYENlyagRKCLLIVMECLDGGELFS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKK--KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdeSGHPDSI-KICDFGFAKQLRGENGLLlTPCY 622
Cdd:cd14170    89 RIQDRgdQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYT--SKRPNAIlKLTDFGFAKETTSHNSLT-TPCY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHM 701
Cdd:cd14170   166 TPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFySNHGLAISPGMKTRIRMGQYEFPNPEWSEVSEEVKMLIRNL 245
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 702 LHMDPHQRYTAEQVLKHPWITQREQLPR 729
Cdd:cd14170   246 LKTEPTQRMTITEFMNHPWIMQSTKVPQ 273
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
462-720 4.84e-52

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: 182.15  E-value: 4.84e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID--KNKRDPSEEI--EI-LMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14069     1 EDWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDmkRAPGDCPENIkkEVcIQKMLSHKNVVRFYGHRREGEFQYLFLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESghpDSIKICDFGFAKQLR--GEN 614
Cdd:cd14069    81 YASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLL-LDEN---DNLKISDFGLATVFRykGKE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFSNgPNDTPEEILLRIGNGRFSLsgGIWDNISRG 693
Cdd:cd14069   157 RLLNKMCGTLPYVAPELLAKKKYRAEpVDVWSCGIVLFAMLAGELPWDQ-PSDSCQEYSDWKENKKTYL--TPWKKIDTA 233
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14069   234 ALSLLRKILTENPNKRITIEDIKKHPW 260
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
464-720 5.18e-52

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: 182.78  E-value: 5.18e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKIIKLKQVEhvlnekrILSEV-RHPFIVNLLGSFQDDRNLYMVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASnvLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGEN 614
Cdd:cd05580    82 YVPGGELFSLLRRSGRFPNDVAK--FYAaeVVLALEYLHSLDIVYRDLKPENLL-LDSDGH---IKITDFGFAKRVKDRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 gllLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILlrigNGRFSLSggiwDNISRG 693
Cdd:cd05580   156 ---YTLCGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYPPFfDENPMKIYEKIL----EGKIRFP----SFFDPD 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 694 AKDLLSHMLHMDPHQRY-----TAEQVLKHPW 720
Cdd:cd05580   225 AKDLIKRLLVVDLTKRLgnlknGVEDIKNHPW 256
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
115-366 6.43e-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: 182.21  E-value: 6.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVR--------DRVRTKMErdILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14084    12 RTLGSGACGEVKLAYDKS---TCKKVAIKIINKRKFTIGsrreinkpRNIETEIE--ILKKLSHPCIIKIEDFFDAEDDY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKeSVD 263
Cdd:cd14084    87 YIVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSK-ILG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM-NMILKAKL--GMPQF--LS 335
Cdd:cd14084   166 ETSLMKTLCGTPTYLAPEVLRsfgTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMSLkEQILSGKYtfIPKAWknVS 245
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 336 AEAQSLLRMLFKRNPANRLgseGVEEVKRHA 366
Cdd:cd14084   246 EEAKDLVKKMLVVDPSRRP---SIEEALEHP 273
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
464-721 9.52e-52

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 181.05  E-value: 9.52e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEEnlkkiyREVQI-MKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRgENGLL 617
Cdd:cd14071    81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLL-LDANM---NIKIADFGFSNFFK-PGELL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFsNGPndTPEEILLRIGNGRFSlsggIWDNISRGAKD 696
Cdd:cd14071   156 KTWCGSPPYAAPEVFEGKEYEGPqLDIWSLGVVLYVLVCGALPF-DGS--TLQTLRDRVLSGRFR----IPFFMSTDCEH 228
                         250       260
                  ....*....|....*....|....*
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14071   229 LIRRMLVLDPSKRLTIEQIKKHKWM 253
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
110-355 1.42e-51

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: 180.66  E-value: 1.42e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd08530     1 DFKVLKKLGKGSYGSVYKVKRLSD---NQVYALKEVNLGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLCIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEV----LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKesVDQE 265
Cdd:cd08530    78 MEYAPFGDLSKLISKRKkkrrLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISK--VLKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEAQSLLRM 344
Cdd:cd08530   156 NLAKTQIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPpIPPVYSQDLQQIIRS 235
                         250
                  ....*....|.
gi 1958807372 345 LFKRNPANRLG 355
Cdd:cd08530   236 LLQVNPKKRPS 246
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
464-721 2.45e-51

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: 179.89  E-value: 2.45e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK--RD-PSEEIEI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKAlgDDlPRVKTEIeALKNLSHQHICRLYHVIETDNKIFMVLEYCP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGF-AKQLRGENGLLL 618
Cdd:cd14078    85 GGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLL-LDEDQN---LKLIDFGLcAKPKGGMDHHLE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGY-DAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGgiWdnISRGAKDL 697
Cdd:cd14078   161 TCCGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALLCGFLPFD---DDNVMALYRKIQSGKYEEPE--W--LSPSSKLL 233
                         250       260
                  ....*....|....*....|....
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14078   234 LDQMLQVDPKKRITVKELLNHPWV 257
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
111-361 3.26e-51

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 179.77  E-value: 3.26e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLK---VRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14116     7 FEIGRPLGKGKFGNVYLAREK---QSKFILALKVLFKAQLEkagVEHQLRREVE--IQSHLRHPNILRLYGYFHDATRVY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 267
Cdd:cd14116    82 LILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSRRT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 aySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 347
Cdd:cd14116   162 --TLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLK 239
                         250
                  ....*....|....
gi 1958807372 348 RNPANRLGSEGVEE 361
Cdd:cd14116   240 HNPSQRPMLREVLE 253
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
464-721 1.09e-50

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: 178.66  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEI---LMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd14195     7 YEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSrrgvsrEEIERevnILREIQHPNIITLHDIFENKTDVVLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGEN 614
Cdd:cd14195    87 LELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAHKIEAGN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 ---GLLLTPcytaNFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNIS 691
Cdd:cd14195   167 efkNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GETKQETLTNISAVNYDFDEEYFSNTS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14195   240 ELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
459-721 2.04e-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: 177.84  E-value: 2.04e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 459 QFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIE---ILMRYGQHPNIISLKEVFDDGK 529
Cdd:cd14196     2 KVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASrrgvsrEEIErevSILRQVLHPNIITLHDVYENRT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 530 YVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQ 609
Cdd:cd14196    82 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LrgENGLLLTPCY-TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWD 688
Cdd:cd14196   162 I--EDGVEFKNIFgTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFL---GDTKQETLANITAVSYDFDEEFFS 236
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14196   237 HTSELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
111-354 2.74e-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: 177.13  E-value: 2.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14095     2 YDIGRVIGDGNFAVVKECRDKAT---DKEYALKIIDKAKCKGKEHM-IENEVAILRRVKHPNIVQLIEEYDTDTELYLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG----HIKLTDFGLSKESVDQek 266
Cdd:cd14095    78 ELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKEP-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 kAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN--ETMNMILKAKLGMP----QFLSAEAQS 340
Cdd:cd14095   156 -LFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILLCGFPPFRSPDRDqeELFDLILAGEFEFLspywDNISDSAKD 234
                         250
                  ....*....|....
gi 1958807372 341 LLRMLFKRNPANRL 354
Cdd:cd14095   235 LISRMLVVDPEKRY 248
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
470-720 2.96e-50

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: 176.64  E-value: 2.96e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKlqenleSEIAILKSI-KHPNIVRLYDVQKTEDFIYLVLEYCAGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDSIKICDFGFAKQLRgENGLLLTPCYT 623
Cdd:cd14009    80 SQYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLL-LSTSGDDPVLKIADFGFARSLQ-PASMAETLCGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNdtPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLH 703
Cdd:cd14009   158 PLYMAPEILQFQKYDAKADLWSVGAILFEMLVGKPPF-RGSN--HVQLLRNIERSDAVIPFPIAAQLSPDCKDLLRRLLR 234
                         250
                  ....*....|....*..
gi 1958807372 704 MDPHQRYTAEQVLKHPW 720
Cdd:cd14009   235 RDPAERISFEEFFAHPF 251
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
464-721 5.57e-50

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: 175.89  E-value: 5.57e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS---EEIEILMRYG---QHPNIISLKEVFDD--GKYVYLVT 535
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFRHPKaalREIKLLKHLNdveGHPNIVKLLDVFEHrgGNHLCLVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMkgGELLDRILKK--KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdSIKICDFGFAKQLRge 613
Cdd:cd05118    81 ELM--GMNLYELIKDypRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELG---QLKLADFGLARSFT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 nglllTPCYTANFV-----APEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFS-NGPNDTPEEILLRIGNGRFslsggi 686
Cdd:cd05118   154 -----SPPYTPYVAtrwyrAPEVlLGAKPYGSSIDIWSLGCILAELLTGRPLFPgDSEVDQLAKIVRLLGTPEA------ 222
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 687 wdnisrgaKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd05118   223 --------LDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
464-716 8.51e-50

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 175.85  E-value: 8.51e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14014     2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEfrerflrEARALARL-SHPNIVRVYDVGEDDGRPYIVME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmDESGHpdsIKICDFGFAKQLrGENGL 616
Cdd:cd14014    81 YVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL-TEDGR---VKLTDFGIARAL-GDSGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTP--CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIWDNISRGA 694
Cdd:cd14014   156 TQTGsvLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPF---DGDSPAAVLAKHLQEAPPPPSPLNPDVPPAL 232
                         250       260
                  ....*....|....*....|...
gi 1958807372 695 KDLLSHMLHMDPHQRY-TAEQVL 716
Cdd:cd14014   233 DAIILRALAKDPEERPqSAAELL 255
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
109-353 1.30e-49

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: 175.47  E-value: 1.30e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLrkaSLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGK 185
Cdd:cd06623     1 SDLERVKVLGQGSSGVVYKVRhKPTG----KIYALKKI---HVDGDEEFRKQLLRElkTLRSCESPYVVKCYGAFYKEGE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHR-LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 264
Cdd:cd06623    74 ISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGISKVLENT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL-----SAEAQ 339
Cdd:cd06623   154 LDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPSLpaeefSPEFR 233
                         250
                  ....*....|....
gi 1958807372 340 SLLRMLFKRNPANR 353
Cdd:cd06623   234 DFISACLQKDPKKR 247
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
464-720 1.47e-49

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: 175.87  E-value: 1.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK------NKRDP-SEEIEILMRYGqHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKrhiikeKKVKYvTIEKEVLSRLA-HPGIVKLYYTFQDESKLYFVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGL 616
Cdd:cd05581    82 YAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENIL-LDEDMH---IKITDFGTAKVLGPDSSP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTP-----------------CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTpeEILLRIGNGR 679
Cdd:cd05581   158 ESTKgdadsqiaynqaraasfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKPPFR-GSNEY--LTFQKIVKLE 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 680 FSLSggiwDNISRGAKDLLSHMLHMDPHQR------YTAEQVLKHPW 720
Cdd:cd05581   235 YEFP----ENFPPDAKDLIQKLLVLDPSKRlgvnenGGYDELKAHPF 277
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
464-721 1.61e-49

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: 174.96  E-value: 1.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd08215     2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlsnmseKEREEALNEVKLLSKL-KHPNIVKYYESFEENGKLCIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKC----FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGE 613
Cdd:cd08215    81 ADGGDLAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIF-LTKDGV---VKLGDFGISKVLEST 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNdtPEEILLRIGNGRFSlsgGIWDNISRG 693
Cdd:cd08215   157 TDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPF-EANN--LPALVYKIVKGQYP---PIPSQYSSE 230
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08215   231 LRDLVNSMLQKDPEKRPSANEILSSPFI 258
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
464-720 3.90e-49

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: 174.02  E-value: 3.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKnKRDPSE--------EIEIlMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSK-KKAPEDylqkflprEIEV-IKGLKHPNLICFYEAIETTSRVYIIM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK-QLRGEN 614
Cdd:cd14162    80 ELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLL-LDKNNN---LKITDFGFARgVMKTKD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 G---LLLTPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNG-RFSLSggiwDN 689
Cdd:cd14162   156 GkpkLSETYCGSYAYASPEILRGIPYDPfLSDIWSMGVVLYTMVYGRLPFD---DSNLKVLLKQVQRRvVFPKN----PT 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 690 ISRGAKDLLSHMLHMDPhQRYTAEQVLKHPW 720
Cdd:cd14162   229 VSEECKDLILRMLSPVK-KRITIEEIKRDPW 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
464-721 4.32e-48

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: 170.98  E-value: 4.32e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDP------SEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14075     4 YRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQktqrllSREISSMEKL-HHPNIIRLYEVVETLSKLHLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENgLL 617
Cdd:cd14075    83 ASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYAS----NNCVKVGDFGFSTHAKRGE-TL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGY-DAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISRGAKD 696
Cdd:cd14075   158 NTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMVTGVMPFR---AETVAKLKKCILEGTYTIP----SYVSEPCQE 230
                         250       260
                  ....*....|....*....|....*
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14075   231 LIRGILQPVPSDRYSIDEIKNSEWL 255
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
464-774 6.34e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 177.13  E-value: 6.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN-KRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:COG0515     9 YRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElAADPEArerfrrEARALARL-NHPNIVRVYDVGEEDGRPYLVME 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPdsiKICDFGFAKQLRGE--- 613
Cdd:COG0515    88 YVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANIL-LTPDGRV---KLIDFGIARALGGAtlt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 --NGLLLTPCYTanfvAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIWDNIS 691
Cdd:COG0515   164 qtGTVVGTPGYM----APEQARGEPVDPRSDVYSLGVTLYELLTGRPPF---DGDSPAELLRAHLREPPPPPSELRPDLP 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 692 RGAKDLLSHMLHMDPHQRY-TAEQVLK--HPWITQREQLPRHQPTSDDPPQVVMEAVAAAYSVLARNQNRHPILEPVAAS 768
Cdd:COG0515   237 PALDAIVLRALAKDPEERYqSAAELAAalRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 316

                  ....*.
gi 1958807372 769 RLAQRR 774
Cdd:COG0515   317 AAAAAA 322
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
459-721 8.11e-48

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: 170.59  E-value: 8.11e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 459 QFSEAYELKEDiGIGSYSVCKRcihsasnmeFAVKIIDKNKRDPSEEIEILmRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14088    13 EFCEIFRAKDK-TTGKLYTCKK---------FLKRDGRKVRKAAKNEINIL-KMVKHPNILQLVDVFETRKEYFIFLELA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHpDSIKICDFGFAKQlrgENGLLL 618
Cdd:cd14088    82 TGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRLKN-SKIVISDFHLAKL---ENGLIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEE-----ILLRIGNGRFSLSGGIWDNISRG 693
Cdd:cd14088   158 EPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEnhdknLFRKILAGDYEFDSPYWDDISQA 237
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14088   238 AKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
111-359 8.55e-48

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: 170.13  E-value: 8.55e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVrtkMERDILV--EVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHW---NENQEYAMKIIDKSKLKGKEDM---IESEILIikSLSHPNIVKLFEVYETEKEIYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFGLSKESVdq 264
Cdd:cd14185    76 ILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 eKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN--ETMNMIlkaKLGMPQFL-------S 335
Cdd:cd14185   154 -GPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGFPPFRSPERDqeELFQII---QLGHYEFLppywdniS 229
                         250       260
                  ....*....|....*....|....
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd14185   230 EAAKDLISRLLVVDPEKRYTAKQV 253
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
470-720 1.27e-47

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: 169.71  E-value: 1.27e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPSEEI----EILMRyGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRhivQTRQQEHIfsekEILEE-CNSPFIVKLYRTFKDKKYLYMLMEYCLGGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGlLLTPCY 622
Cdd:cd05572    80 LWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLL-LDSNGY---VKLVDFGFAKKLGSGRK-TWTFCG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTP----EEILLRIGNGRFSlsggiwDNISRGAKDLL 698
Cdd:cd05572   155 TPEYVAPEIILNKGYDFSVDYWSLGILLYELLTGRPPFG-GDDEDPmkiyNIILKGIDKIEFP------KYIDKNAKNLI 227
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 699 SHMLHMDPHQRY-----TAEQVLKHPW 720
Cdd:cd05572   228 KQLLRRNPEERLgylkgGIRDIKKHKW 254
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
110-368 1.82e-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: 1.82e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGK-LY 187
Cdd:cd14069     2 DWDLVQTLGEGAFGEVFLaVNRNTE----EAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRF-YGHRREGEfQY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSkeSV----D 263
Cdd:cd14069    77 LFLEYASGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLA--TVfrykG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK----AKLGMPQFLSAEA 338
Cdd:cd14069   155 KERLLNKMCGTLPYVAPELLAKKKyRAEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKenkkTYLTPWKKIDTAA 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 339 QSLLRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14069   235 LSLLRKILTENPNKRI---TIEDIKKHPWY 261
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
464-721 1.94e-47

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: 168.94  E-value: 1.94e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSvckrCIHSASNME----FAVKIIDKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYL 533
Cdd:cd06627     2 YQLGDLIGRGAFG----SVYKGLNLNtgefVAIKQISLEKIPKSDlksvmgEIDLLKKL-NHPNIVKYIGSVKTKDSLYI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGE 613
Cdd:cd06627    77 ILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDG----LVKLADFGVATKLNEV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRfslSGGIWDNISRG 693
Cdd:cd06627   153 EKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYY---DLQPMAALFRIVQDD---HPPLPENISPE 226
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06627   227 LRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
117-353 3.03e-47

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: 168.10  E-value: 3.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd13999     1 IGSGSFGEVYKGKWR-----GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTV 275
Cdd:cd13999    76 SLYDLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVVGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 276 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD-RNETMNMILKAKL-----GMPQFLSaeaqSLLRMLFKRN 349
Cdd:cd13999   156 RWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSpIQIAAAVVQKGLRppippDCPPELS----KLIKRCWNED 231

                  ....
gi 1958807372 350 PANR 353
Cdd:cd13999   232 PEKR 235
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
110-353 3.47e-47

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 168.34  E-value: 3.47e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVR-DRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIER---ATGREVAIKSIKKDKIEDEqDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 268
Cdd:cd14073    79 VMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSN-LYSKDKLL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSaEAQSLLRMLFK 347
Cdd:cd14073   158 QTFCGSPLYASPEIVNGTPyQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIRWMLT 236

                  ....*.
gi 1958807372 348 RNPANR 353
Cdd:cd14073   237 VNPKRR 242
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
464-722 1.86e-46

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: 166.23  E-value: 1.86e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-KNKRDPSEEIEI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd06614     2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRlRKQNKELIINEIlIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGE----NGL 616
Cdd:cd06614    82 SLTDIItQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILL----SKDGSVKLADFGFAAQLTKEkskrNSV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPcYtanFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFSLSGGiwDNISRGAK 695
Cdd:cd06614   158 VGTP-Y---WMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYL---EEPPLRALFLITtKGIPPLKNP--EKWSPEFK 228
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd06614   229 DFLNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
114-353 2.30e-46

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


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 166.14  E-value: 2.30e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd08218     5 IKKIGEGSFGKALLVKSKE---DGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd08218    82 DGGDLYKRINAQrgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVELARTC 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ-GKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNP 350
Cdd:cd08218   162 IGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEaGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRNP 241

                  ...
gi 1958807372 351 ANR 353
Cdd:cd08218   242 RDR 244
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
111-384 2.95e-46

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: 166.19  E-value: 2.95e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLkVRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14117     8 FDIGRPLGKGKFGNVYLAREK---QSKFIVALKVLFKSQI-EKEGVEHQLRREIEIQshLRHPNILRLYNYFHDRKRIYL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKa 268
Cdd:cd14117    84 ILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRR- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 ySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd14117   163 -TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRY 241
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958807372 349 NPANRLGSEGVEEvkrHAffssidWNKLYKREVQPP 384
Cdd:cd14117   242 HPSERLPLKGVME---HP------WVKANSRRVLPP 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
110-368 3.89e-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: 165.79  E-value: 3.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpDaGQLYAMKVLRKASLKVRDRvrtKM---ERDILVEVNHPFIVKLHYAF--QTEG 184
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKS--D-GKILVWKEIDYGKMSEKEK---QQlvsEVNILRELKHPNIVRYYDRIvdRANT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGGD---VFTRLSKEVLFTEED-VKFYLAELALALDHLHRLG-----IVYRDLKPENILLDEIGHIKLTDF 255
Cdd:cd08217    75 TLYIVMEYCEGGDlaqLIKKCKKENQYIPEEfIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 256 GLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNEtmnMILKAKLGM----P 331
Cdd:cd08217   155 GLARVLSHDSSFAKTYVGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELCALHPPFQAANQLE---LAKKIKEGKfpriP 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 332 QFLSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAFF 368
Cdd:cd08217   232 SRYSSELNEVIKSMLNVDPDKR---PSVEELLQLPLI 265
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
111-368 4.00e-46

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: 165.10  E-value: 4.00e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRkasLKVRDRVRTKMERDILVEVN----HPFIVKLHYAF--QTEG 184
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDK---VTGEKVAIKKIK---NDFRHPKAALREIKLLKHLNdvegHPNIVKLLDVFehRGGN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI-GHIKLTDFGLSKESV 262
Cdd:cd05118    75 HLCLVFELM-GMNLYELIKDyPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARSFT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKkaYSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMPQFLsaeaqSL 341
Cdd:cd05118   154 SPPY--TPYVATRWYRAPEVLLGaKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVR-LLGTPEAL-----DL 225
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 342 LRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd05118   226 LSKMLKYDPAKRI---TASQALAHPYF 249
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
110-367 5.38e-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: 165.54  E-value: 5.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKAS-LKVRDRVRTkmerdiLVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14010     1 NYVLYDEIGRGKHSVVYKGRRKG---TIEFVAIKCVDKSKrPEVLNEVRL------THELKHPNVLKFYEWYETSNHLWL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--------- 259
Cdd:cd14010    72 VVEYCTGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARregeilkel 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 -------ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA-----K 327
Cdd:cd14010   152 fgqfsdeGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNEdppppP 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 328 LGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAF 367
Cdd:cd14010   232 PKVSSKPSPDFKSLLKGLLEKDPAKRLSW---DELVKHPF 268
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
490-722 7.90e-46

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: 165.08  E-value: 7.90e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIdkNKRDPSE---------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLdRILKK-KCFSEQEAS 559
Cdd:cd05579    21 YAIKVI--KKRDMIRknqvdsvlaERNILSQA-QNPFVVKLYYSFQGKKNLYLVMEYLPGGDLY-SLLENvGALDEDVAR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 NVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK-------------------QLRGENGLLLTP 620
Cdd:cd05579    97 IYIAEIVLALEYLHSHGIIHRDLKPDNIL-IDANGH---LKLTDFGLSKvglvrrqiklsiqkksngaPEKEDRRIVGTP 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGpnDTPEEILLRIGNGRFSlsggiW---DNISRGAKDL 697
Cdd:cd05579   173 DY----LAPEILLGQGHGKTVDWWSLGVILYEFLVGIPPF-HA--ETPEEIFQNILNGKIE-----WpedPEVSDEAKDL 240
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 698 LSHMLHMDPHQR---YTAEQVLKHPWIT 722
Cdd:cd05579   241 ISKLLTPDPEKRlgaKGIEEIKNHPFFK 268
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
464-721 1.11e-45

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: 164.10  E-value: 1.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-------RDP-----SEEIEIL--MRYGQHPNIISLKEVFDDGK 529
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERilvdtwvRDRklgtvPLEIHILdtLNKRSHPNIVKLLDFFEDDE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 530 YVYLVTDLMKGG-ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK 608
Cdd:cd14004    82 FYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVI-LDGNGT---IKLIDFGSAA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 QLrgENGLLLTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFSNgpndtPEEIL---LRIGNGrfslsg 684
Cdd:cd14004   158 YI--KSGPFDTFVGTIDYAAPEVLRGNPYGGKeQDIWALGVLLYTLVFKENPFYN-----IEEILeadLRIPYA------ 224
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 685 giwdnISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14004   225 -----VSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
464-720 1.27e-45

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 163.91  E-value: 1.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKII---DKNKRDPSEEIEILMRYGqHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIplrSSTRARAFQERDILARLS-HRRLTCLLDQFETRKTLILILELCSS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdesgHP--DSIKICDFGFAKQLRGENgLLL 618
Cdd:cd14107    83 EELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMV----SPtrEDIKICDFGFAQEITPSE-HQF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDtpEEILLRIGNGRFSLSGGIWDNISRGAKDLL 698
Cdd:cd14107   158 SKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFA-GEND--RATLLNVAEGVVSWDTPEITHLSEDAKDFI 234
                         250       260
                  ....*....|....*....|..
gi 1958807372 699 SHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14107   235 KRVLQPDPEKRPSASECLSHEW 256
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
110-367 1.59e-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: 163.58  E-value: 1.59e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14002     2 NYHVLELIGEGSFGKVYKGRRK---YTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAY 269
Cdd:cd14002    79 TEYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRN 349
Cdd:cd14002   158 SIKGTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKD 237
                         250
                  ....*....|....*...
gi 1958807372 350 PANRLGSEGVEEvkrHAF 367
Cdd:cd14002   238 PSKRLSWPDLLE---HPF 252
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
464-721 2.48e-45

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: 162.94  E-value: 2.48e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-RDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14073     3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKiEDEQDmvrirrEIEIMSSL-NHPHIIRIYEVFENKDKIVIVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAkQLRGENGL 616
Cdd:cd14073    82 YASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENIL-LDQNG---NAKIADFGLS-NLYSKDKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFsNGPNDTpeeILLR-IGNGRF----SLSggiwdni 690
Cdd:cd14073   157 LQTFCGSPLYASPEIVNGTPYQGPeVDCWSLGVLLYTLVYGTMPF-DGSDFK---RLVKqISSGDYreptQPS------- 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 691 srGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14073   226 --DASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
464-721 9.29e-45

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: 161.87  E-value: 9.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK--RDPSE-----EIEILMRYgQHPNIISLKEVFD--DGKyVYLV 534
Cdd:cd14165     3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKapDDFVEkflprELEILARL-NHKSIIKTYEIFEtsDGK-VYIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQL-RGE 613
Cdd:cd14165    81 MELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDF----NIKLTDFGFSKRClRDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NG---LLLTPCYTANFVAPEVLTQQGYDAAC-DIWSLGVLLYTMLAGYTPFsngpNDTPEEILLRIGNG---RFSLSggi 686
Cdd:cd14165   157 NGrivLSKTFCGSAAYAAPEVLQGIPYDPRIyDIWSLGVILYIMVCGSMPY----DDSNVKKMLKIQKEhrvRFPRS--- 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 687 wDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14165   230 -KNLTSECKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
462-721 2.20e-44

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: 160.99  E-value: 2.20e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS-----EEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSmdelrKEIQA-MSQCNHPNVVSYYTSFVVGDELWLVMP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLD---RILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFA------ 607
Cdd:cd06610    80 LLSGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNIL-LGEDG---SVKIADFGVSaslatg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 --KQLRGENGLLLTPCYtanfVAPEVLTQ-QGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIGNGRFSL-- 682
Cdd:cd06610   156 gdRTRKVRKTFVGTPCW----MAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYP---PMKVLMLTLQNDPPSle 228
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 683 SGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06610   229 TGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
111-367 3.45e-44

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: 159.89  E-value: 3.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVF---TGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDV-KFYLAELALALDHLHRLGIVYRDLKPENILLDE-IGHIKLTDFGLSKeSVDQEKKA 268
Cdd:cd14074    82 ELGDGGDMYDYIMKHENGLNEDLaRKYFRQIVSAISYCHKLHVVHRDLKPENVVFFEkQGLVKLTDFGFSN-KFQPGEKL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVnrRGHSQSA---DWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRML 345
Cdd:cd14074   161 ETSCGSLAYSAPEIL--LGDEYDApavDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRM 238
                         250       260
                  ....*....|....*....|..
gi 1958807372 346 FKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14074   239 LIRDPKKRA---SLEEIENHPW 257
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-383 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 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLkVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRS---TGKLYALKCIKKSPL-SRD---SSLENEIAVlkRIKHENIVTLEDIYESTTHYYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKesVDQE 265
Cdd:cd14166    78 VMQLVSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSK--MEQN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETmNMILKAKLGMPQF-------LSAEA 338
Cdd:cd14166   156 GIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFY--EETES-RLFEKIKEGYYEFespfwddISESA 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANRLGSegvEEVKRHAFfssIDWNKLYKREVQP 383
Cdd:cd14166   233 KDFIRHLLEKNPSKRYTC---EKALSHPW---IIGNTALHRDIYP 271
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
460-721 6.50e-44

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: 159.72  E-value: 6.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELK--EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd14197     5 FQERYSLSpgRELGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDcrmeiiHEIAVLELAQANPWVINLHEVYETASEM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRIL--KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDsIKICDFGFAKQ 609
Cdd:cd14197    85 ILVLEYAAGGEIFNQCVadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLGD-IKIVDFGLSRI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRGENGL---LLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGI 686
Cdd:cd14197   164 LKNSEELreiMGTPEY----VAPEILSYEPISTATDMWSIGVLAYVMLTGISPFL---GDDKQETFLNISQMNVSYSEEE 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 687 WDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14197   237 FEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
110-365 7.29e-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: 7.29e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVflvrKKTGPDAGQLYAMKVLRKASLK-VRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14161     4 RYEFLETLGKGTYGRV----KKARDSSGRLVAIKSIRKDRIKdEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 268
Cdd:cd14161    80 VMEYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSN-LYNQDKFL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSaEAQSLLRMLFK 347
Cdd:cd14161   159 QTYCGSPLYASPEIVNGRPYIgPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLM 237
                         250
                  ....*....|....*...
gi 1958807372 348 RNPANRlgsEGVEEVKRH 365
Cdd:cd14161   238 VNPERR---ATLEDVASH 252
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-353 8.02e-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: 159.07  E-value: 8.02e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14083     5 YEFKEVLGTGAFSEVVLAEDKA---TGKLVAIKCIDKKALKGKE---DSLENEIAVlrKIKHPNIVQLLDIYESKSHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL---LDEIGHIKLTDFGLSKesVDQE 265
Cdd:cd14083    79 VMELVTGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK--MEDS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLgmpQF-------LSAEA 338
Cdd:cd14083   157 GVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAEY---EFdspywddISDSA 233
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd14083   234 KDFIRHLMEKDPNKR 248
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
465-726 9.84e-44

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: 158.91  E-value: 9.84e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSYSVCKRCIHSASNMEFAVKII----DKNKRDP-SEEIEILMRyGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd06623     4 ERVKVLGQGSSGVVYKVRHKPTGKIYALKKIhvdgDEEFRKQlLRELKTLRS-CESPYVVKCYGAFYKEGEISIVLEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLrgENGLLL 618
Cdd:cd06623    83 GGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLI----NSKGEVKIADFGISKVL--ENTLDQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCY--TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNG-RFSLSGGIWdniSRGAK 695
Cdd:cd06623   157 CNTFvgTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGpPPSLPAEEF---SPEFR 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWITQREQ 726
Cdd:cd06623   234 DFISACLQKDPKKRPSAAELLQHPFIKKADN 264
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
462-721 1.19e-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: 158.49  E-value: 1.19e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS-------EEIEILMRYgQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAgmvqrvrNEVEIHCQL-KHPSILELYNYFEDSNYVYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELlDRILK--KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRG 612
Cdd:cd14186    80 LEMCHNGEM-SRYLKnrKKPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNM----NIKIADFGLATQLKM 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISR 692
Cdd:cd14186   155 PHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFD---TDTVKNTLNKVVLADYEMP----AFLSR 227
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14186   228 EAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
110-353 1.20e-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: 158.60  E-value: 1.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLR--KASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVN---SDQKYAMKEIRlpKSSSAVED---SRKEAVLLAKMKHPNIVAFKESFEADGHLY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTR--LSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd08219    75 IVMEYCDGGDLMQKikLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrNETMNMILKAKLG----MPQFLSAEAQSL 341
Cdd:cd08219   155 AYACTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQA---NSWKNLILKVCQGsykpLPSHYSYELRSL 231
                         250
                  ....*....|..
gi 1958807372 342 LRMLFKRNPANR 353
Cdd:cd08219   232 IKQMFKRNPRSR 243
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
469-722 1.21e-43

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: 159.06  E-value: 1.21e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-----------------------RDPSE----EIEILMRYgQHPNIISL 521
Cdd:cd14118     1 EIGKGSYGIVKLAYNEEDNTLYAMKILSKKKllkqagffrrppprrkpgalgkpLDPLDrvyrEIAILKKL-DHPNVVKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 522 KEVFDD--GKYVYLVTDLMKGGELLdRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsI 599
Cdd:cd14118    80 VEVLDDpnEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLL-LGDDGH---V 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 600 KICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYD---AACDIWSLGVLLYTMLAGYTPF------------SNGP 664
Cdd:cd14118   155 KIADFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKfsgKALDIWAMGVTLYCFVFGRCPFeddhilglhekiKTDP 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 665 NDTPEEIllrigngrfslsggiwdNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14118   235 VVFPDDP-----------------VVSEQLKDLILRMLDKNPSERITLPEIKEHPWVT 275
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
470-717 1.26e-43

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: 158.08  E-value: 1.26e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMefAVKIIDKNKRDPS------EEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd13999     1 IGSGSFGEVYKGKWRGTDV--AIKKLKVEDDNDEllkefrREVSI-LSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKK-CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd13999    78 YDLLHKKKiPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNIL-LDENFT---VKIADFGLSRIKNSTTEKMTGVVG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLRIGNGrfsLSGGIWDNISRGAKDLLSHML 702
Cdd:cd13999   154 TPRWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEVPFKELSP--IQIAAAVVQKG---LRPPIPPDCPPELSKLIKRCW 228
                         250
                  ....*....|....*
gi 1958807372 703 HMDPHQRYTAEQVLK 717
Cdd:cd13999   229 NEDPEKRPSFSEIVK 243
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
103-368 1.43e-43

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 158.67  E-value: 1.43e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADPAQfdllkVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVN-------HPFIV 174
Cdd:cd14093     2 YAKYEPKE-----ILGRGVSSTVRrCIEKETG----QEFAVKIIDITGEKSSENEAEELREATRREIEilrqvsgHPNII 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 175 KLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd14093    73 ELHDVFESPTFIFLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGLSKEsVDQEKKAYSFCGTVEYMAPEVV------NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK- 327
Cdd:cd14093   153 FGFATR-LDEGEKLRELCGTPGYLAPEVLkcsmydNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKy 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 328 -LGMPQF--LSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14093   232 eFGSPEWddISDTAKDLISKLLVVDPKKRLTA---EEALEHPFF 272
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
117-357 1.53e-43

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: 157.77  E-value: 1.53e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd14103     1 LGRGKFGTVYrCVEKATG----KELAAKFIKCRKAKDREDVR--NEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSKE--VLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIGH-IKLTDFGLSKEsVDQEKKAYSF 271
Cdd:cd14103    75 GELFERVVDDdfEL-TERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARK-YDPDKKLKVL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK--LGMPQF--LSAEAQSLLRMLFK 347
Cdd:cd14103   153 FGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKwdFDDEAFddISDEAKDFISKLLV 232
                         250
                  ....*....|
gi 1958807372 348 RNPANRLGSE 357
Cdd:cd14103   233 KDPRKRMSAA 242
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
464-721 2.38e-43

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: 157.42  E-value: 2.38e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSvcKRCI--HSASNMEFAVKIIDKNK-------RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05578     2 FQILRVIGKGSFG--KVCIvqKKDTKKMFAMKYMNKQKciekdsvRNVLNELEILQEL-EHPFLVNLWYSFQDEEDMYMV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASnvLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRg 612
Cdd:cd05578    79 VDLLLGGDLRYHLQQKVKFSEETVK--FYIceIVLALDYLHSKNIIHRDIKPDNIL-LDEQGH---VHITDFNIATKLT- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEIL-LRIGNGRFSLSGgiWdniS 691
Cdd:cd05578   152 DGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGKRPYEIHSRTSIEEIRaKFETASVLYPAG--W---S 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 692 RGAKDLLSHMLHMDPHQRY-TAEQVLKHPWI 721
Cdd:cd05578   227 EEAIDLINKLLERDPQKRLgDLSDLKNHPYF 257
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
110-357 2.64e-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: 158.74  E-value: 2.64e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14086     2 EYDLKEELGKGAFS---VVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd14086    79 FDLVTGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEAQSLL 342
Cdd:cd14086   159 AWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLI 238
                         250
                  ....*....|....*
gi 1958807372 343 RMLFKRNPANRLGSE 357
Cdd:cd14086   239 NQMLTVNPAKRITAA 253
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
115-359 2.71e-43

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 159.44  E-value: 2.71e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKaslkvrdRVRTKMERDI----LVEvNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14179    13 KPLGEGSFS---ICRKCLHKKTNQEYAVKIVSK-------RMEANTQREIaalkLCE-GHPNIVKLHEVYHDQLHTFLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQEKK 267
Cdd:cd14179    82 ELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPPDNQP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET----MNMILKAKLGMPQF-------LSA 336
Cdd:cd14179   162 LKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDKSLTctsaEEIMKKIKQGDFSFegeawknVSQ 241
                         250       260
                  ....*....|....*....|...
gi 1958807372 337 EAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd14179   242 EAKDLIQGLLTVDPNKRIKMSGL 264
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
115-396 4.75e-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: 158.62  E-value: 4.75e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKaslkvrdRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14092    12 EALGDGSFS---VCRKCVHKKTGQEFAVKIVSR-------RLDTSREVQLLRLCqGHPNIVKLHEVFQDELHTYLVMELL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQEKKAyS 270
Cdd:cd14092    82 RGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQPLK-T 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRR----GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNE-TMNMILKAKLGMPQF-------LSAEA 338
Cdd:cd14092   161 PCFTLPYAAPEVLKQAlstqGYDESCDLWSLGVILYTMLSGQVPFQSPSRNEsAAEIMKRIKSGDFSFdgeewknVSSEA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 339 QSLLRMLFKRNPANRLgseGVEEVKRHaffssiDWNKLYKREVQPPFR-----PASGKPDDTF 396
Cdd:cd14092   241 KSLIQGLLTVDPSKRL---TMSELRNH------PWLQGSSSPSSTPLMtpgvlSSSAAAVSTA 294
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
110-353 5.50e-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: 156.66  E-value: 5.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpDAGQLyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKS--DSEHC-VIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHI-KLTDFGLSKESVDQEK 266
Cdd:cd08225    78 MEYCDGGDLMKRINRQrgVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSME 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG--MPQFlSAEAQSLLRM 344
Cdd:cd08225   158 LAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApiSPNF-SRDLRSLISQ 236

                  ....*....
gi 1958807372 345 LFKRNPANR 353
Cdd:cd08225   237 LFKVSPRDR 245
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
117-367 6.09e-43

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: 156.34  E-value: 6.09e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKV-----FLVRKKTgpdagqlyAMKVLRKAslKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14075    10 LGSGNFSQVklgihQLTKEKV--------AIKILDKT--KLDQKTQRLLSREIssMEKLHHPNIIRLYEVVETLSKLHLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvDQEKKAY 269
Cdd:cd14075    80 MEYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHA-KRGETLN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVV---NRRGHsqSADWWSYGVLMFEMLTGTLPFqgkdRNETM----NMILKAKLGMPQFLSAEAQSLL 342
Cdd:cd14075   159 TFCGSPPYAAPELFkdeHYIGI--YVDIWALGVLLYFMVTGVMPF----RAETVaklkKCILEGTYTIPSYVSEPCQELI 232
                         250       260
                  ....*....|....*....|....*
gi 1958807372 343 RMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14075   233 RGILQPVPSDRY---SIDEIKNSEW 254
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
110-353 7.93e-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: 157.60  E-value: 7.93e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvRKKTGPDAGQLYAMKVLRKASLKvrDRVRTKMERD-ILVEVN------HPFIVKLHYAFQT 182
Cdd:cd14096     2 NYRLINKIGEGAFSNVY--KAVPLRNTGKPVAIKVVRKADLS--SDNLKGSSRAnILKEVQimkrlsHPNIVKLLDFQES 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL------------------- 243
Cdd:cd14096    78 DEYYYIVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkaddd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 244 ---LDE-----------IGHIKLTDFGLSKESVDQEKKaySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTL 309
Cdd:cd14096   158 etkVDEgefipgvggggIGIVKLADFGLSKQVWDSNTK--TPCGTVGYTAPEVVKDERYSKKVDMWALGCVLYTLLCGFP 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 310 PFQGKDRNETMNMILKaklGMPQFL-------SAEAQSLLRMLFKRNPANR 353
Cdd:cd14096   236 PFYDESIETLTEKISR---GDYTFLspwwdeiSKSAKDLISHLLTVDPAKR 283
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
115-368 8.10e-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: 156.24  E-value: 8.10e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14189     7 RLLGKGGFARCY---EMTDLATNKTYAVKVIPHSRVaKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKaySF 271
Cdd:cd14189    84 SRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAArlEPPEQRKK--TI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 351
Cdd:cd14189   162 CGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPG 241
                         250
                  ....*....|....*..
gi 1958807372 352 NRLgseGVEEVKRHAFF 368
Cdd:cd14189   242 DRL---TLDQILEHEFF 255
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
464-720 1.01e-42

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: 158.60  E-value: 1.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPS----EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05573     3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSdmlKREQIahvrAERDILADA-DSPWIVRLHYAFQDEDHLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLR--GEN 614
Cdd:cd05573    82 YMPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNIL-LDADGH---IKLADFGLCTKMNksGDR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLL---------------------------TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDT 667
Cdd:cd05573   158 ESYLndsvntlfqdnvlarrrphkqrrvraySAVGTPDYIAPEVLRGTGYGPECDWWSLGVILYEMLYGFPPFY---SDS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 668 PEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLhMDPHQRYT-AEQVLKHPW 720
Cdd:cd05573   235 LVETYSKIMNWKESLVFPDDPDVSPEAIDLIRRLL-CDPEDRLGsAEEIKAHPF 287
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-357 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 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14167     5 YDFREVLGTGAFSEVVLAEEKR---TQKLVAIKCIAKKALEGKE---TSIENEIAVlhKIKHPNIVALDDIYESGGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL---LDEIGHIKLTDFGLSKESvDQE 265
Cdd:cd14167    79 IMQLVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIE-GSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA--KLGMPQF--LSAEAQSL 341
Cdd:cd14167   158 SVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAeyEFDSPYWddISDSAKDF 237
                         250
                  ....*....|....*.
gi 1958807372 342 LRMLFKRNPANRLGSE 357
Cdd:cd14167   238 IQHLMEKDPEKRFTCE 253
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
109-356 1.12e-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: 155.77  E-value: 1.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKaslKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14087     1 AKYDIKALIGRGSFSRVVRVEHRV---TRQPYAIKMIET---KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYM 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGL-SKESVDQ 264
Cdd:cd14087    75 VMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLaSTRKKGP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM-PQF---LSAEAQS 340
Cdd:cd14087   155 NCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsGEPwpsVSNLAKD 234
                         250
                  ....*....|....*.
gi 1958807372 341 LLRMLFKRNPANRLGS 356
Cdd:cd14087   235 FIDRLLTVNPGERLSA 250
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
464-720 1.18e-42

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: 156.80  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILM------RYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14209     3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKVVKLKQVEHTLnekrilQAINFPFLVKLEYSFKDNSNLYMVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENgll 617
Cdd:cd14209    83 VPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLL-IDQQGY---IKVTDFGFAKRVKGRT--- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGiwdnISRGAKDL 697
Cdd:cd14209   156 WTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF---ADQPIQIYEKIVSGKVRFPSH----FSSDLKDL 228
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 698 LSHMLHMDPHQRY-----TAEQVLKHPW 720
Cdd:cd14209   229 LRNLLQVDLTKRFgnlknGVNDIKNHKW 256
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
461-721 1.21e-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: 155.93  E-value: 1.21e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID----KNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14191     1 SDFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKaysaKEKENIRQEISI-MNCLHHPKLVQCVDAFEEKANIVMVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpDSIKICDFGFAKQLRGEnG 615
Cdd:cd14191    80 MVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTG--TKIKLIDFGLARRLENA-G 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTpeEILLRIGNGRFSLSGGIWDNISRGAK 695
Cdd:cd14191   157 SLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFM-GDNDN--ETLANVTSATWDFDDEAFDEISDDAK 233
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14191   234 DFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
110-353 1.30e-42

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: 155.37  E-value: 1.30e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVL---TGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAy 269
Cdd:cd14072    78 MEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLD- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd14072   157 TFCGSPPYAAPELFQgKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVL 236

                  ....*
gi 1958807372 349 NPANR 353
Cdd:cd14072   237 NPSKR 241
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
100-368 2.80e-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: 155.51  E-value: 2.80e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 100 KEGYEKADPAQfdllkVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLR----KASLKVRDRVR--TKMERDILVEV-NHPF 172
Cdd:cd14181     6 KEFYQKYDPKE-----VIGRGVSS---VVRRCVHRHTGQEFAVKIIEvtaeRLSPEQLEEVRssTLKEIHILRQVsGHPS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 173 IVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKL 252
Cdd:cd14181    78 IITLIDSYESSTFIFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 253 TDFGLSKEsVDQEKKAYSFCGTVEYMAPEVV------NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA 326
Cdd:cd14181   158 SDFGFSCH-LEPGEKLRELCGTPGYLAPEILkcsmdeTHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEG 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 327 K--LGMPQF--LSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14181   237 RyqFSSPEWddRSSTVKDLISRLLVVDPEIRLTA---EQALQHPFF 279
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
464-721 2.94e-42

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: 154.60  E-value: 2.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14072     2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSslqklfREVRI-MKILNHPNIVKLFEVIETEKTLYLVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGlL 617
Cdd:cd14072    81 ASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLL-LDADMN---IKIADFGFSNEFTPGNK-L 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFsNGPNdtPEEILLRIGNGRFSlsggIWDNISRGAKD 696
Cdd:cd14072   156 DTFCGSPPYAAPELFQGKKYDGPeVDVWSLGVILYTLVSGSLPF-DGQN--LKELRERVLRGKYR----IPFYMSTDCEN 228
                         250       260
                  ....*....|....*....|....*
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14072   229 LLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
470-719 3.33e-42

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: 154.47  E-value: 3.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIID------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd08530     8 LGKGSYGSVYKVKRLSDNQVYALKEVNlgslsqKEREDSVNEIRLLASV-NHPNIIRYKEAFLDGNRLCIVMEYAPFGDL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILK----KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRgeNGLLLT 619
Cdd:cd08530    87 SKLISKrkkkRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSA----GDLVKIGDLGISKVLK--KNLAKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLsggIWDNISRGAKDLLS 699
Cdd:cd08530   161 QIGTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRPPFE---ARTMQELRYKVCRGKFPP---IPPVYSQDLQQIIR 234
                         250       260
                  ....*....|....*....|
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHP 719
Cdd:cd08530   235 SLLQVNPKKRPSCDKLLQSP 254
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
117-354 8.93e-42

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: 153.47  E-value: 8.93e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLRK---ASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14097     9 LGQGSFGVVI---EATHKETQTKWAIKKINRekaGSSAVKLLER---EVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL--------DEIgHIKLTDFGLS--KESVD 263
Cdd:cd14097    83 EDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnnDKL-NIKVTDFGLSvqKYGLG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 qEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQ 339
Cdd:cd14097   162 -EDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTqsvwQSVSDAAK 240
                         250
                  ....*....|....*
gi 1958807372 340 SLLRMLFKRNPANRL 354
Cdd:cd14097   241 NVLQQLLKVDPAHRM 255
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
111-367 1.06e-41

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: 153.09  E-value: 1.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRK-KTGPDAgqlyAMKVL-RKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14186     3 FKVLNLLGKGSFACVYRARSlHTGLEV----AIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVfTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd14186    79 VLEMCHNGEM-SRYLKNRKkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLF 346
Cdd:cd14186   158 KHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLL 237
                         250       260
                  ....*....|....*....|.
gi 1958807372 347 KRNPANRLgseGVEEVKRHAF 367
Cdd:cd14186   238 RKNPADRL---SLSSVLDHPF 255
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
115-368 1.15e-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: 152.81  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDrVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd14079     8 KTLGVGSFGKVKLAEHEL---TGHKVAVKILNRQKIKSLD-MEEKIRREIqiLKLFRHPHIIRLYEVIETPTDIFMVMEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSfC 272
Cdd:cd14079    84 VSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKTS-C 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQS-ADWWSYGVLMFEMLTGTLPFqgkDRNETMNMILKAKLGM---PQFLSAEAQSLLRMLFKR 348
Cdd:cd14079   163 GSPNYAAPEVISGKLYAGPeVDVWSCGVILYALLCGSLPF---DDEHIPNLFKKIKSGIytiPSHLSPGARDLIKRMLVV 239
                         250       260
                  ....*....|....*....|
gi 1958807372 349 NPANRLgseGVEEVKRHAFF 368
Cdd:cd14079   240 DPLKRI---TIPEIRQHPWF 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
111-354 1.73e-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: 1.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14078     5 YELHETIGSGGFAKVKLATHIL---TGEKVAIKIMDKKALG-DDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRL-SKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL-SKESVDQEKKA 268
Cdd:cd14078    81 EYCPGGELFDYIvAKDRL-SEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGGMDHHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQS-ADWWSYGVLMFEMLTGTLPFqgkDRNETMNM---ILKAKLGMPQFLSAEAQSLLRM 344
Cdd:cd14078   160 ETCCGSPAYAAPELIQGKPYIGSeADVWSMGVLLYALLCGFLPF---DDDNVMALyrkIQSGKYEEPEWLSPSSKLLLDQ 236
                         250
                  ....*....|
gi 1958807372 345 LFKRNPANRL 354
Cdd:cd14078   237 MLQVDPKKRI 246
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
464-720 1.81e-41

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: 152.23  E-value: 1.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKR-DPSEEIEIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd14662     2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLKiDENVQREIInHRSLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPdSIKICDFGFAK------QLRGENG 615
Cdd:cd14662    82 ELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSPAP-RLKICDFGYSKssvlhsQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 lllTPCYtanfVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNgPNDtPEEI---LLRIGNGRFSLSGGIwdNIS 691
Cdd:cd14662   160 ---TPAY----IAPEVLSRKEYDGkVADVWSCGVTLYVMLVGAYPFED-PDD-PKNFrktIQRIMSVQYKIPDYV--RVS 228
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14662   229 QDCRHLLSRIFVANPAKRITIPEIKNHPW 257
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
464-722 2.00e-41

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: 153.20  E-value: 2.00e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK--------------------------RDPSE----EIEILMRYg 513
Cdd:cd14199     4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKlmrqagfprrppprgaraapegctqpRGPIErvyqEIAILKKL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 514 QHPNIISLKEVFDDGK--YVYLVTDLMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMD 591
Cdd:cd14199    83 DHPNVVKLVEVLDDPSedHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLL-VG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 592 ESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVL--TQQGYDA-ACDIWSLGVLLYTMLAGYTPFSngpndtp 668
Cdd:cd14199   161 EDGH---IKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLseTRKIFSGkALDVWAMGVTLYCFVFGQCPFM------- 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 669 EEILLRIGNGRFSLSGGIWD--NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14199   231 DERILSLHSKIKTQPLEFPDqpDISDDLKDLLFRMLDKNPESRISVPEIKLHPWVT 286
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
468-720 2.06e-41

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: 152.06  E-value: 2.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEF-AVKIIDKNKRDPS------EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd14121     1 EKLGSGTYATVYKAYRKSGAREVvAVKCVSKSSLNKAstenllTEIELLKKL-KHPHIVELKDFQWDEEHIYLIMEYCSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdeSGHPDSIKICDFGFAK---------QLR 611
Cdd:cd14121    80 GDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLS--SRYNPVLKLADFGFAQhlkpndeahSLR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GenglllTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGR-FSLSGGIwdNI 690
Cdd:cd14121   158 G------SPLY----MAPEMILKKKYDARVDLWSVGVILYECLFGRAPFA---SRSFEELEEKIRSSKpIEIPTRP--EL 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 691 SRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14121   223 SADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
460-721 2.14e-41

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: 152.44  E-value: 2.14e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDP-SEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14113     5 FDSFYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKlmKRDQvTHELGVLQSL-QHPQLVGLLDTFETPTSYILVLE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDSIKICDFGFAKQLRGE--- 613
Cdd:cd14113    84 MADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENIL-VDQSLSKPTIKLADFGDAVQLNTTyyi 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPcytaNFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRG 693
Cdd:cd14113   163 HQLLGSP----EFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFL---DESVEETCLNICRLDFSFPDDYFKGVSQK 235
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14113   236 AKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
461-721 2.45e-41

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: 152.03  E-value: 2.45e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSY-SVCKrCIHSASNMEFAVKIIDKNKRDPSEEIEI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd06612     2 EEVFDILEKLGEGSYgSVYK-AIHKETGQVVAIKVVPVEEDLQEIIKEIsILKQCDSPYIVKYYGSYFKNTDLWIVMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENG-- 615
Cdd:cd06612    81 GAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNIL-LNEEGQ---AKLADFGVSGQLTDTMAkr 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 --LLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIGNgRFSLSGGIWDNISRG 693
Cdd:cd06612   157 ntVIGTPFW----MAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIH---PMRAIFMIPN-KPPPTLSDPEKWSPE 228
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06612   229 FNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
111-353 2.47e-41

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 151.80  E-value: 2.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVD---GRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd08529    79 EYAENGDLHSLIKSQRgrPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRMLFK 347
Cdd:cd08529   159 QTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKyPPISASYSQDLSQLIDSCLT 238

                  ....*.
gi 1958807372 348 RNPANR 353
Cdd:cd08529   239 KDYRQR 244
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
110-353 4.12e-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: 4.12e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVflvRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMER--DILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14098     1 KYQIIDRLGSGTFAEV---KKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQReiNILKSLEHPGIVRLIDWYEDDQHIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG--HIKLTDFGLSKeSVDQE 265
Cdd:cd14098    78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAK-VIHTG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRR------GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL----S 335
Cdd:cd14098   157 TFLVTFCGTMAYLAPEILMSKeqnlqgGYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPLVdfniS 236
                         250
                  ....*....|....*...
gi 1958807372 336 AEAQSLLRMLFKRNPANR 353
Cdd:cd14098   237 EEAIDFILRLLDVDPEKR 254
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
464-721 4.19e-41

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: 151.20  E-value: 4.19e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKII----DKNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERATGNNFAAKFImtphESDKETVRKEIQI-MNQLHHPKLINLHDAFEDDNEMVLILEFLS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKK-CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlyMDESGHPDSIKICDFGFAKQLRGENGLLL 618
Cdd:cd14114    83 GGELFERIAAEHyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENI--MCTTKRSNEVKLIDFGLATHLDPKESVKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDtpEEILLRIGNGRFSLSGGIWDNISRGAKDLL 698
Cdd:cd14114   161 TTG-TAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFA-GEND--DETLRNVKSCDWNFDDSAFSGISEEAKDFI 236
                         250       260
                  ....*....|....*....|...
gi 1958807372 699 SHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14114   237 RKLLLADPNKRMTIHQALEHPWL 259
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
464-720 5.47e-41

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 153.43  E-value: 5.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-------RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREilkmkqvQHVAQEKSILMEL-SHPFIVNMMCSFQDENRVYFLLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENgl 616
Cdd:PTZ00263   99 FVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLL-LDNKGH---VKVTDFGFAKKVPDRT-- 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 lLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGgiWdnISRGAKD 696
Cdd:PTZ00263  173 -FTLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFF---DDTPFRIYEKILAGRLKFPN--W--FDGRARD 244
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 697 LLSHMLHMDPHQRYTA-----EQVLKHPW 720
Cdd:PTZ00263  245 LVKGLLQTDHTKRLGTlkggvADVKNHPY 273
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
110-365 8.10e-41

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: 151.63  E-value: 8.10e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVrtkmerDILVEV-NHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14091     1 EYEIKEEIGKGSYSVCKRCIHKA---TGKEYAVKIIDKSKRDPSEEI------EILLRYgQHPNIITLRDVYDDGNSVYL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL-DEIGH---IKLTDFGLSKESVDQ 264
Cdd:cd14091    72 VTELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYaDESGDpesLRICDFGFAKQLRAE 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFqGKDRNETMNMILKaKLGMPQF---------LS 335
Cdd:cd14091   152 NGLLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGYTPF-ASGPNDTPEVILA-RIGSGKIdlsggnwdhVS 229
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSegvEEVKRH 365
Cdd:cd14091   230 DSAKDLVRKMLHVDPSQRPTA---AQVLQH 256
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
464-721 1.42e-40

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: 150.71  E-value: 1.42e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PS---EEIEILMRYgQHPNIISLKEVFDDGKYVYLV--- 534
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegiPStalREISLLKEL-KHPNIVKLLDVIHTENKLYLVfey 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 --TDLMKggeLLDRILKKkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRg 612
Cdd:cd07829    80 cdQDLKK---YLDKRPGP--LPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLL-INRDG---VLKLADFGLARAFG- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 englLLTPCYTANFV-----APEVL-TQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIgngrFSLSG-- 684
Cdd:cd07829   150 ----IPLRTYTHEVVtlwyrAPEILlGSKHYSTAVDIWSVGCIFAELITGKPLF---PGDSEIDQLFKI----FQILGtp 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 685 --GIWDNISR-------------------------GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd07829   219 teESWPGVTKlpdykptfpkwpkndlekvlprldpEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
115-368 1.89e-40

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: 149.39  E-value: 1.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKvRDRVRTKMERDILVE--VNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd14188     7 KVLGKGGFAKCY---EMTDLTTNKVYAAKIIPHSRVS-KPHQREKIDKEIELHriLHHKHVVQFYHYFEDKENIYILLEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFC 272
Cdd:cd14188    83 CSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTIC 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd14188   163 GTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPED 242
                         250
                  ....*....|....*.
gi 1958807372 353 RlgsEGVEEVKRHAFF 368
Cdd:cd14188   243 R---PSLDEIIRHDFF 255
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
117-311 1.96e-40

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: 149.76  E-value: 1.96e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgPDAGQLYAMKVLRKASL-----KVRDRVRTkmERDILVEVNHPFIVKLHYAFQTE-GKLYLIL 190
Cdd:cd13994     1 IGKGATSVVRIVTKKN-PRSGVLYAVKEYRRRDDeskrkDYVKRLTS--EYIISSKLHHPNIVKVLDLCQDLhGKWCLVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS-KESVDQEKKAY 269
Cdd:cd13994    78 EYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAeVFGMPAEKESP 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 270 SF---CGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd13994   158 MSaglCGSEPYMAPEVFTSGSYDgRAVDVWSCGIVLFALFTGRFPW 203
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
490-720 2.14e-40

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: 151.40  E-value: 2.14e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDK-----NKRDPSE---EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNV 561
Cdd:cd05584    27 FAMKVLKKasivrNQKDTAHtkaERNILEAV-KHPFIVDLHYAFQTGGKLYLILEYLSGGELFMHLEREGIFMEDTACFY 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 562 LYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAAC 641
Cdd:cd05584   106 LAEITLALGHLHSLGIIYRDLKPENIL-LDAQGH---VKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILTRSGHGKAV 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 642 DIWSLGVLLYTMLAGYTPFSnGPN--DTPEEILlrigNGRFSLSggiwDNISRGAKDLLSHMLHMDPHQRY-----TAEQ 714
Cdd:cd05584   182 DWWSLGALMYDMLTGAPPFT-AENrkKTIDKIL----KGKLNLP----PYLTNEARDLLKKLLKRNVSSRLgsgpgDAEE 252

                  ....*.
gi 1958807372 715 VLKHPW 720
Cdd:cd05584   253 IKAHPF 258
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
464-723 2.70e-40

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: 151.14  E-value: 2.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSY-SVCKrCIHSASNMEFAVKIIDKNKRDPSE------EIEILmRYGQHPNIISLKEVF-----DDGKYV 531
Cdd:cd07834     2 YELLKPIGSGAYgVVCS-AYDKRTGRKVAIKKISNVFDDLIDakrilrEIKIL-RHLKHENIIGLLDILrppspEEFNDV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMkggEL-LDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQ 609
Cdd:cd07834    80 YIVTELM---ETdLHKVIKsPQPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNC----DLKICDFGLARG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRG-ENGLLLTPcytanFV------APEV-LTQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPN------------DTP- 668
Cdd:cd07834   153 VDPdEDKGFLTE-----YVvtrwyrAPELlLSSKKYTKAIDIWSVGCIFAELLTR-KPLFPGRDyidqlnlivevlGTPs 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 669 EEILLRIGNGRF-----SLS-------GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd07834   227 EEDLKFISSEKArnylkSLPkkpkkplSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQ 293
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
120-368 2.71e-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: 149.23  E-value: 2.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 120 GSFGKVFLVRKktgPDAGQLYAMKVLRKASLKVRDRvRTKMERDIlvevnhPFIVKLHYAFQTEGKLYLILDFLRGGDVF 199
Cdd:cd05576    10 GVIDKVLLVMD---TRTQETFILKGLRKSSEYSRER-KTIIPRCV------PNMVCLRKYIISEESVFLVLQHAEGGKLW 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 200 TRLSKEV-------LFT---------------EEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05576    80 SYLSKFLndkeihqLFAdlderlaaasrfyipEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDqekkaySFCG-TVE--YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ----GKDRNETMNmilkaklgM 330
Cdd:cd05576   160 WSEVED------SCDSdAIEnmYCAPEVGGISEETEACDWWSLGALLFELLTGKALVEchpaGINTHTTLN--------I 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 331 PQFLSAEAQSLLRMLFKRNPANRLGS--EGVEEVKRHAFF 368
Cdd:cd05576   226 PEWVSEEARSLLQQLLQFNPTERLGAgvAGVEDIKSHPFF 265
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
464-723 3.20e-40

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: 149.32  E-value: 3.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-KNKRDPSEEI--EILMRYGQH-PNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd06609     3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDlEEAEDEIEDIqqEIQFLSQCDsPYITKYYGSFLKGSKLWIIMEYCG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRgengllLT 619
Cdd:cd06609    83 GGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEG----DVKLADFGVSGQLT------ST 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYTANFV------APEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRI-GNGRFSLSGgiwDNISR 692
Cdd:cd06609   152 MSKRNTFVgtpfwmAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLS---DLHPMRVLFLIpKNNPPSLEG---NKFSK 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06609   226 PFKDFVELCLNKDPKERPSAKELLKHKFIKK 256
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
111-368 4.18e-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: 148.65  E-value: 4.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd06605     3 LEYLGELGEGNGGVVSKVRHRP---SGQIMAVKVIR-LEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDvFTRLSKEVLFTEEDvkfYLAELALA----LDHLH-RLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQe 265
Cdd:cd06605    79 EYMDGGS-LDKILKEVGRIPER---ILGKIAVAvvkgLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDS- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 kKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI--LKAKLGMP------QFLSAE 337
Cdd:cd06605   154 -LAKTFVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPSMMIFelLSYIVDEPppllpsGKFSPD 232
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 338 AQSLLRMLFKRNPANRlgsEGVEEVKRHAFF 368
Cdd:cd06605   233 FQDFVSQCLQKDPTER---PSYKELMEHPFI 260
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
470-720 5.82e-40

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: 147.80  E-value: 5.82e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDK--NKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRI 547
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKDVAVKFVSKkmKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 548 LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDSIKICDFGFAKQLRGE---NGLLLTPcyta 624
Cdd:cd14115    81 MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLL-IDLRIPVPRVKLIDLEDAVQISGHrhvHHLLGNP---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 625 NFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHM 704
Cdd:cd14115   156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFL---DESKEETCINVCRVDFSFPDEYFGDVSQAARDFINVILQE 232
                         250
                  ....*....|....*.
gi 1958807372 705 DPHQRYTAEQVLKHPW 720
Cdd:cd14115   233 DPRRRPTAATCLQHPW 248
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
468-720 6.44e-40

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: 147.94  E-value: 6.44e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGg 541
Cdd:cd14082     9 EVLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQesqlrnEVAILQQL-SHPGVVNLECMFETPERVFVVMEKLHG- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRIL--KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPdSIKICDFGFAKQLrGENGLLLT 619
Cdd:cd14082    87 DMLEMILssEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPFP-QVKLCDFGFARII-GEKSFRRS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngpnDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLS 699
Cdd:cd14082   165 VVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF-----NEDEDINDQIQNAAFMYPPNPWKEISPDAIDLIN 239
                         250       260
                  ....*....|....*....|.
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14082   240 NLLQVKMRKRYSVDKSLSHPW 260
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
490-720 6.72e-40

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: 148.01  E-value: 6.72e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVL 562
Cdd:cd05611    24 FAIKVLKKSDMIAKNQVTnvkaeraIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGGDCASLIKTLGGLPEDWAKQYI 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK--QLRGENGLLLTpcyTANFVAPEVLTQQGYDAA 640
Cdd:cd05611   104 AEVVLGVEDLHQRGIIHRDIKPENLL-IDQTGH---LKLTDFGLSRngLEKRHNKKFVG---TPDYLAPETILGVGDDKM 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 641 CDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTA---EQVLK 717
Cdd:cd05611   177 SDWWSLGCVIFEFLFGYPPFHAE---TPDAVFDNILSRRINWPEEVKEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKS 253

                  ...
gi 1958807372 718 HPW 720
Cdd:cd05611   254 HPF 256
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
110-353 7.03e-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: 147.97  E-value: 7.03e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKV--LRKASlkVRDRVRTKMERDILVEVNHPFIVKLHYAFQTE-GKL 186
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRD---RKQYVIKKlnLKNAS--KRERKAAEQEAKLLSKLKHPNIVSYKESFEGEdGFL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLS--KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 264
Cdd:cd08223    76 YIVMGFCEGGDLYTRLKeqKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL-GMPQFLSAEAQSLLR 343
Cdd:cd08223   156 SDMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIK 235
                         250
                  ....*....|
gi 1958807372 344 MLFKRNPANR 353
Cdd:cd08223   236 AMLHQDPEKR 245
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
464-721 7.27e-40

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: 148.23  E-value: 7.27e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSAS-NMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14202     4 FSRKDLIGHGAFAVVFKGRHKEKhDLEVAVKCINKKNLAKSQtllgkEIKILKEL-KHENIVALYDFQEIANSVYLVMEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESG---HPDSI--KICDFGFAKQLRG 612
Cdd:cd14202    83 CNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGGrksNPNNIriKIADFGFARYLQN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 eNGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRfSLSGGIWDNISR 692
Cdd:cd14202   163 -NMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQ---ASSPQDLRLFYEKNK-SLSPNIPRETSS 237
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14202   238 HLRQLLLGLLQRNQKDRMDFDEFFHHPFL 266
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
111-365 8.47e-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: 8.47e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDAgqlYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTE---VAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAyS 270
Cdd:cd14071    79 EYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLK-T 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRN 349
Cdd:cd14071   158 WCGSPPYAAPEVFEgKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLD 237
                         250
                  ....*....|....*.
gi 1958807372 350 PANRLgseGVEEVKRH 365
Cdd:cd14071   238 PSKRL---TIEQIKKH 250
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
115-354 8.57e-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: 147.88  E-value: 8.57e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKaslkvrdRVRTKMER-DILVEV-------NHPFIVKLHYAFQTEGKL 186
Cdd:cd14106    14 TPLGRGKFA---VVRKCIHKETGKEYAAKFLRK-------RRRGQDCRnEILHEIavlelckDCPRVVNLHEVYETRSEL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKeSVD 263
Cdd:cd14106    84 ILILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISR-VIG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL----SAEAQ 339
Cdd:cd14106   163 EGEEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEELfkdvSPLAI 242
                         250
                  ....*....|....*
gi 1958807372 340 SLLRMLFKRNPANRL 354
Cdd:cd14106   243 DFIKRLLVKDPEKRL 257
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
110-353 8.60e-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: 147.37  E-value: 8.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd06627     1 NYQLGDLIGRGAFGSVY---KGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAY 269
Cdd:cd06627    78 LEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDEN 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK-AKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:cd06627   158 SVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELLTGNPPYYDLQPMAALFRIVQdDHPPLPENISPELRDFLLQCFQK 237

                  ....*
gi 1958807372 349 NPANR 353
Cdd:cd06627   238 DPTLR 242
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
470-720 9.53e-40

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: 147.40  E-value: 9.53e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNK--RDPS------EEIEILMRYgQHPNIISLKEVFDD---GKyVYLVTDLM 538
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKlrRIPNgeanvkREIQILRRL-NHRNVIKLVDVLYNeekQK-LYMVMEYC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGG--ELLDRILKKKcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLR--GEN 614
Cdd:cd14119    79 VGGlqEMLDSAPDKR-LPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTD----GTLKISDFGVAEALDlfAED 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDA--ACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISR 692
Cdd:cd14119   154 DTCTTSQGSPAFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTTGKYPFE---GDNIYKLFENIGKGEYTIP----DDVDP 226
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14119   227 DLQDLLRGMLEKDPEKRFTIEQIRQHPW 254
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
464-722 1.43e-39

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: 147.86  E-value: 1.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PSE---EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd07832     2 YKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEggiPNQalrEIKALQACQGHPYVVKLRDVFPHGTGFVLVFEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGelLDRILK--KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENG 615
Cdd:cd07832    82 MLSS--LSEVLRdeERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLL-ISSTGV---LKIADFGLARLFSEEDP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTP-CYTANFVAPEVL-TQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPND------------TPEE-------ILLR 674
Cdd:cd07832   156 RLYSHqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNG-SPLFPGENDieqlaivlrtlgTPNEktwpeltSLPD 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 675 IGNGRFSLSGGI-WDNI----SRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd07832   235 YNKITFPESKGIrLEEIfpdcSPEAIDLLKGLLVYNPKKRLSAEEALRHPYFF 287
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
462-721 1.45e-39

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: 146.63  E-value: 1.45e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEIlMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKElrnlrqEIEI-LRKLNHPNIIEMLDSFETKKEFVVVT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGgELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrGENG 615
Cdd:cd14002    80 EYAQG-ELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNIL-IGKGGV---VKLCDFGFARAM-SCNT 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLL-----TPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndtpeeillrigNGRFSLSGGI---- 686
Cdd:cd14002   154 LVLtsikgTPLY----MAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYT--------------NSIYQLVQMIvkdp 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 687 --W-DNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14002   216 vkWpSNMSPEFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
115-353 1.56e-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: 146.89  E-value: 1.56e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVflvRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd14070     8 RKLGEGSFAKV---REGLHAVTGEKVAIKVIDKKKAKKDSYVTKNLRREgrIQQMIRHPNITQLLDILETENSYYLVMEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAYS 270
Cdd:cd14070    85 CPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNcaGILGYSDPFST 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD---RNETMNMILKAKLGMPQFLSAEAQSLLRMLFK 347
Cdd:cd14070   165 QCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPfslRALHQKMVDKEMNPLPTDLSPGAISFLRSLLE 244

                  ....*.
gi 1958807372 348 RNPANR 353
Cdd:cd14070   245 PDPLKR 250
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
461-720 1.83e-39

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: 146.59  E-value: 1.83e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID---KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14108     1 TDYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvraKKKTSARRELALLAEL-DHKSIVRFHDAFEKRRVVIIVTEL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGgELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDSIKICDFGFAKQLR-GEngl 616
Cdd:cd14108    80 CHE-ELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQK--TDQVRICDFGNAQELTpNE--- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 lltPCY----TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDtpEEILLRIGNGRFSLSGGIWDNISR 692
Cdd:cd14108   154 ---PQYckygTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFV-GEND--RTTLMNIRNYNVAFEESMFKDLCR 227
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 693 GAKDLLSHMLHMDpHQRYTAEQVLKHPW 720
Cdd:cd14108   228 EAKGFIIKVLVSD-RLRPDAEETLEHPW 254
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
464-722 2.60e-39

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: 147.02  E-value: 2.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK---------RDPS---------------------EEIEILMRYg 513
Cdd:cd14200     2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKllkqygfprRPPPrgskaaqgeqakplaplervyQEIAILKKL- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 514 QHPNIISLKEVFDDGKY--VYLVTDLMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMD 591
Cdd:cd14200    81 DHVNIVKLIEVLDDPAEdnLYMVFDLLRKGPVME-VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 592 EsGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVL--TQQGYDA-ACDIWSLGVLLYTMLAGYTPF-------- 660
Cdd:cd14200   160 D-GH---VKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLsdSGQSFSGkALDVWAMGVTLYCFVYGKCPFidefilal 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 661 ----SNGPNDTPEEillrigngrfslsggiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14200   236 hnkiKNKPVEFPEE-----------------PEISEELKDLILKMLDKNPETRITVPEIKVHPWVT 284
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
111-354 3.31e-39

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: 146.48  E-value: 3.31e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDR--VRTKMERD--ILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14105     7 YDIGEELGSGQFAVVKKCREKS---TGLEYAAKFIKKRRSKASRRgvSREDIEREvsILRQVLHPNIITLHDVFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDE----IGHIKLTDFGLSKESV 262
Cdd:cd14105    84 VLILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDknvpIPRIKLIDFGLAHKIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 D-QEKKaySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFL----SAE 337
Cdd:cd14105   164 DgNEFK--NIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDEYfsntSEL 241
                         250
                  ....*....|....*..
gi 1958807372 338 AQSLLRMLFKRNPANRL 354
Cdd:cd14105   242 AKDFIRQLLVKDPRKRM 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
464-720 3.71e-39

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 145.90  E-value: 3.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKR-DPSEEIEIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd14665     2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEKiDENVQREIInHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPdSIKICDFGFAK------QLRGENG 615
Cdd:cd14665    82 ELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTL-LDGSPAP-RLKICDFGYSKssvlhsQPKSTVG 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 lllTPCYtanfVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFSNgPNDTPE--EILLRIGNGRFSLSGGIwdNISR 692
Cdd:cd14665   160 ---TPAY----IAPEVLLKKEYDGKiADVWSCGVTLYVMLVGAYPFED-PEEPRNfrKTIQRILSVQYSIPDYV--HISP 229
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14665   230 ECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
109-369 5.63e-39

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 145.80  E-value: 5.63e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14169     3 SVYELKEKLGEGAFSEVVLAQER---GSQRLVALKCIPKKALRGKEAM-VENEIAVLRRINHENIVSLEDIYESPTHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD---EIGHIKLTDFGLSKesVDQE 265
Cdd:cd14169    79 AMELVTGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSK--IEAQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA--KLGMPQF--LSAEAQSL 341
Cdd:cd14169   157 GMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAeyEFDSPYWddISESAKDF 236
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 342 LRMLFKRNPANRLgseGVEEVKRHAFFS 369
Cdd:cd14169   237 IRHLLERDPEKRF---TCEQALQHPWIS 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
468-721 8.53e-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: 144.72  E-value: 8.53e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIID----KNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14192    10 EVLGGGRFGQVHKCTELSTGLTLAAKIIKvkgaKEREEVKNEINI-MNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKcFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdSIKICDFGFAKQLRGENGLLLTpC 621
Cdd:cd14192    89 FDRITDES-YQLTELDAILFTrqICEGVHYLHQHYILHLDLKPENILCVNSTGN--QIKIIDFGLARRYKPREKLKVN-F 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHM 701
Cdd:cd14192   165 GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFL---GETDAETMNNIVNCKWDFDAEAFENLSEEAKDFISRL 241
                         250       260
                  ....*....|....*....|
gi 1958807372 702 LHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14192   242 LVKEKSCRMSATQCLKHEWL 261
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
464-721 9.93e-39

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: 144.93  E-value: 9.93e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASN-----MEFAVKIIDKNK-RDPSEEIEI-----LMRYGQHPNIISLKEVFDDGKYVY 532
Cdd:cd14076     3 YILGRTLGEGEFGKVKLGWPLPKAnhrsgVQVAIKLIRRDTqQENCQTSKImreinILKGLTHPNIVRLLDVLKTKKYIG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESghpDSIKICDFGFAKQLRG 612
Cdd:cd14076    83 IVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLL-LDKN---RNLVITDFGFANTFDH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENG-LLLTPCYTANFVAPE-VLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDN 689
Cdd:cd14076   159 FNGdLMSTSCGSPCYAAPElVVSDSMYAGrKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRLYRYICNTPLIFPEY 238
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 690 ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14076   239 VTPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
468-721 1.66e-38

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: 143.90  E-value: 1.66e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIID----KNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14193    10 EILGGGRFGQVHKCEEKSSGLKLAAKIIKarsqKEKEEVKNEIEV-MNQLNHANLIQLYDAFESRNDIVLVMEYVDGGEL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKcFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdSIKICDFGFAKQLRGENGLLLTpC 621
Cdd:cd14193    89 FDRIIDEN-YNLTELDTILFIkqICEGIQYMHQMYILHLDLKPENILCVSREAN--QVKIIDFGLARRYKPREKLRVN-F 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTpeEILLRIGNGRFSLSGGIWDNISRGAKDLLSHM 701
Cdd:cd14193   165 GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFL-GEDDN--ETLNNILACQWDFEDEEFADISEEAKDFISKL 241
                         250       260
                  ....*....|....*....|
gi 1958807372 702 LHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14193   242 LIKEKSWRMSASEALKHPWL 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
115-358 1.95e-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: 143.95  E-value: 1.95e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVflvRKKTGPDAGQLYAMKVLRKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14192    10 EVLGGGRFGQV---HKCTELSTGLTLAAKIIKVKGAKEREEV--KNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIGH-IKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd14192    85 GGELFDRITDESYqLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGNqIKIIDFGLARRYKPREKLKVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 cGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 347
Cdd:cd14192   165 -GTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLV 243
                         250
                  ....*....|.
gi 1958807372 348 RNPANRLGSEG 358
Cdd:cd14192   244 KEKSCRMSATQ 254
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
113-353 2.90e-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: 143.07  E-value: 2.90e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  113 LLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLRK-ASLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:smart00221   3 LGKKLGEGAFGEVYKGTlKGKGDGKEVEVAVKTLKEdASEQQIEEFL--REARIMRKLDHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  191 DFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVDQEKK 267
Cdd:smart00221  81 EYMPGGDLldYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDlYDDDYYK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRML 345
Cdd:smart00221 161 VKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPYPGMSNAEVLEYLKKGYrLPKPPNCPPELYKLMLQC 240

                   ....*...
gi 1958807372  346 FKRNPANR 353
Cdd:smart00221 241 WAEDPEDR 248
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
470-721 3.44e-38

Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 143.22  E-value: 3.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHS--ASNMEFAVKIIdkNKRDPSE-----------EIEILMRYgQHPNIIslkEVFD-----DGKYV 531
Cdd:cd13994     1 IGKGATSVVRIVTKKnpRSGVLYAVKEY--RRRDDESkrkdyvkrltsEYIISSKL-HHPNIV---KVLDlcqdlHGKWC 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 yLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLR 611
Cdd:cd13994    75 -LVMEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENIL-LDEDGV---LKLTDFGTAEVFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGllLTPCYTAN------FVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNgPNDTPEEILLRIGNGRFSLSG 684
Cdd:cd13994   150 MPAE--KESPMSAGlcgsepYMAPEVFTSGSYDGrAVDVWSCGIVLFALFTGRFPWRS-AKKSDSAYKAYEKSGDFTNGP 226
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 685 --GIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd13994   227 yePIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
110-327 3.63e-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: 143.41  E-value: 3.63e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPdaGQLYAMKVLRKASLKVRdrvRTKMERD-----ILVEVN-------HPFIVKLH 177
Cdd:cd08528     1 EYAVLELLGSGAFGCVYKVRKKSNG--QTLLALKEINMTNPAFG---RTEQERDksvgdIISEVNiikeqlrHPNIVRYY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 YAFQTEGKLYLILDFLRG---GDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHR-LGIVYRDLKPENILLDEIGHIKL 252
Cdd:cd08528    76 KTFLENDRLYIVMELIEGaplGEHFSSLkEKNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTI 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 253 TDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK 327
Cdd:cd08528   156 TDFGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAE 230
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
464-721 3.74e-38

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: 142.79  E-value: 3.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSaSNMEFAVKIIDKNK-RDPSE------EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14161     5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRiKDEQDllhirrEIEI-MSSLNHPHIISVYEVFENSSKIVIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRGENgL 616
Cdd:cd14161    83 YASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENIL-LDANG---NIKIADFGLSNLYNQDK-F 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFSNGPNDTpeeILLRIGNGRFSLSGGIWDnisrgAK 695
Cdd:cd14161   158 LQTYCGSPLYASPEIVNGRPYIGPeVDSWSLGVLLYILVHGTMPFDGHDYKI---LVKQISSGAYREPTKPSD-----AC 229
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14161   230 GLIRWLLMVNPERRATLEDVASHWWV 255
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
110-311 5.01e-38

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 142.40  E-value: 5.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd06612     4 VFDILEKLGEGSYGSVYKAIHK---ETGQVVAIKVVPVEE----DLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGG---DVFTRLSKEvlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd06612    77 MEYCGAGsvsDIMKITNKT--LTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMA 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd06612   155 KRNTVIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPY 199
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
467-721 5.35e-38

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: 142.75  E-value: 5.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 467 KEDIGIGSYSVCKRCIHSASNMEFAVKIIdkNKRDPSE------EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd14190     9 KEVLGGGKFGKVHTCTEKRTGLKLAAKVI--NKQNSKDkemvllEIQV-MNQLNHRNLIQLYEAIETPNEIVLFMEYVEG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdSIKICDFGFAKQLRGENGLLLT 619
Cdd:cd14190    86 GELFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGH--QVKIIDFGLARRYNPREKLKVN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 pCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTpeEILLRIGNGRFSLSGGIWDNISRGAKDLLS 699
Cdd:cd14190   164 -FGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFL-GDDDT--ETLNNVLMGNWYFDEETFEHVSDEAKDFVS 239
                         250       260
                  ....*....|....*....|..
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14190   240 NLIIKERSARMSATQCLKHPWL 261
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
464-721 9.21e-38

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


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 142.20  E-value: 9.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-------KNKRDPSEEIEI-----------LMRYGQHPNIISLKEVF 525
Cdd:cd14077     3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPrasnaglKKEREKRLEKEIsrdirtireaaLSSLLNHPHICRLRDFL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 526 DDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFG 605
Cdd:cd14077    83 RTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENIL-ISKSG---NIKIIDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAKQLRGENgLLLTPCYTANFVAPEVLTQQGYDAA-CDIWSLGVLLYTMLAGYTPFsngpNDTPEEIL-LRIGNGRFSLS 683
Cdd:cd14077   159 LSNLYDPRR-LLRTFCGSLYFAAPELLQAQPYTGPeVDVWSFGVVLYVLVCGKVPF----DDENMPALhAKIKKGKVEYP 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 684 ggiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14077   234 ----SYLSSECKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
117-358 1.22e-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: 141.35  E-value: 1.22e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDagQLYAMKVLRKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14120     1 IGHGAFAVVFKGRHRKKPD--LPVAIKCITKKNLSKSQNLLGK-EIKILKELSHENVVALLDCQETSSSVYLVMEYCNGG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG---------HIKLTDFGLSKeSVDQEKK 267
Cdd:cd14120    78 DLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFAR-FLQDGMM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRM 344
Cdd:cd14120   157 AATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQAQTPQELKAFYEKNANLRPNIpsgTSPALKDLLLG 236
                         250
                  ....*....|....
gi 1958807372 345 LFKRNPANRLGSEG 358
Cdd:cd14120   237 LLKRNPKDRIDFED 250
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
110-367 1.23e-37

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: 142.00  E-value: 1.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKV--LRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd06609     2 LFTLLERIGKGSFGEVYKGIdKRTN----QVVAIKVidLEEAEDEIEDIQQ---EIQFLSQCDSPYITKYYGSFLKGSKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTrLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd06609    75 WIIMEYCGGGSVLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA---KLGMPQFlSAEAQSLLR 343
Cdd:cd06609   154 KRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNnppSLEGNKF-SKPFKDFVE 232
                         250       260
                  ....*....|....*....|....
gi 1958807372 344 MLFKRNPANRLGSegvEEVKRHAF 367
Cdd:cd06609   233 LCLNKDPKERPSA---KELLKHKF 253
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
462-722 1.26e-37

Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 141.63  E-value: 1.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS-------EEIEIlMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd14116     5 EDFEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAgvehqlrREVEI-QSHLRHPNILRLYGYFHDATRVYLI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAkqLRGEN 614
Cdd:cd14116    84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLL----GSAGELKIADFGWS--VHAPS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISRGA 694
Cdd:cd14116   158 SRRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLVGKPPFE---ANTYQETYKRISRVEFTFP----DFVTEGA 230
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14116   231 RDLISRLLKHNPSQRPMLREVLEHPWIT 258
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
470-719 1.33e-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: 141.35  E-value: 1.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSA-SNMEFAVKIID-----KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITkknlsKSQNLLGKEIKILKEL-SHENVVALLDCQETSSSVYLVMEYCNGGDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDS-----IKICDFGFAKQLRGeNGLLL 618
Cdd:cd14120    80 ADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGRKPSpndirLKIADFGFARFLQD-GMMAA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRfSLSGGIWDNISRGAKDLL 698
Cdd:cd14120   159 TLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAPFQ---AQTPQELKAFYEKNA-NLRPNIPSGTSPALKDLL 234
                         250       260
                  ....*....|....*....|.
gi 1958807372 699 SHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14120   235 LGLLKRNPKDRIDFEDFFSHP 255
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
464-721 1.71e-37

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 140.90  E-value: 1.71e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKnKRDPSE--------EIEILMRYgQHPNIISLKEVFD--DGKyVYL 533
Cdd:cd14163     2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDK-SGGPEEfiqrflprELQIVERL-DHKNIIHVYEMLEsaDGK-IYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpdSIKICDFGFAKQL-RG 612
Cdd:cd14163    79 VMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-----TLKLTDFGFAKQLpKG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNgpNDTPeEILLRIGNGrFSLSGGIwdNIS 691
Cdd:cd14163   154 GRELSQTFCGSTAYAAPEVLQGVPHDSrKGDIWSMGVVLYVMLCAQLPFDD--TDIP-KMLCQQQKG-VSLPGHL--GVS 227
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14163   228 RTCQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
483-719 2.06e-37

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 142.74  E-value: 2.06e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 483 HSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSE 555
Cdd:cd05570    16 RKKTDELYAIKVLKKEVIIEDDDVEctmtekrVLALANRHPFLTGLHACFQTEDRLYFVMEYVNGGDLMFHIQRARRFTE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 556 QEAsnVLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLT 633
Cdd:cd05570    96 ERA--RFYAaeICLALQFLHERGIIYRDLKLDNVL-LDAEGH---IKIADFGMCKEGIWGGNTTSTFCGTPDYIAPEILR 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 634 QQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSlsggIWDNISRGAKDLLSHMLHMDPHQR---- 709
Cdd:cd05570   170 EQDYGFSVDWWALGVLLYEMLAGQSPF---EGDDEDELFEAILNDEVL----YPRWLSREAVSILKGLLTKDPARRlgcg 242
                         250
                  ....*....|.
gi 1958807372 710 -YTAEQVLKHP 719
Cdd:cd05570   243 pKGEADIKAHP 253
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
462-720 3.28e-37

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


Pssm-ID: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 141.30  E-value: 3.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKiidKNKRDPSEEI-------EI-LMRYGQHPNIISLKEVFDDGKYVYL 533
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIK---KFKESEDDEDvkktalrEVkVLRQLRHENIVNLKEAFRRKGRLYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGG--ELLDRilKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLR 611
Cdd:cd07833    78 VFEYVERTllELLEA--SPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENIL-VSESG---VLKLCDFGFARALT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPcYTAN--FVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGyTPFSNGPND--------------TPEEILLR 674
Cdd:cd07833   152 ARPASPLTD-YVATrwYRAPELLVgDTNYGKPVDVWAIGCIMAELLDG-EPLFPGDSDidqlyliqkclgplPPSHQELF 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 675 IGNGRFslSGGIWDNI--------------SRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07833   230 SSNPRF--AGVAFPEPsqpeslerrypgkvSSPALDFLKACLRMDPKERLTCDELLQHPY 287
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
113-367 3.40e-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: 140.66  E-value: 3.40e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKV--------LRKASLKVRDR-----VRTKMERDILVEVNHPFIVKLHYA 179
Cdd:cd14077     5 FVKTIGAGSMGKVKLAKHIR---TGEKCAIKIiprasnagLKKEREKRLEKeisrdIRTIREAALSSLLNHPHICRLRDF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd14077    82 LRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSN 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 eSVDQEKKAYSFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEA 338
Cdd:cd14077   162 -LYDPRRLLRTFCGSLYFAAPELLQAQPYTgPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSEC 240
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14077   241 KSLISRMLVVDPKKRA---TLEQVLNHPW 266
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
117-365 3.48e-37

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: 140.15  E-value: 3.48e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRtkmERDILVEVN-HPFIVKLH-YAFQTEGKLYLILDFLR 194
Cdd:cd13987     1 LGEGTYGKVLLAVHKG---SGTKMALKFVPKPSTKLKDFLR---EYNISLELSvHPHIIKTYdVAFETEDYYVFAQEYAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL--DEIGHIKLTDFGLSKeSVDQEKKAYSfc 272
Cdd:cd13987    75 YGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTR-RVGSTVKRVS-- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHS-----QSADWWSYGVLMFEMLTGTLPFQ---GKDRNETMNM-ILKAKLGMP--QF--LSAEAQ 339
Cdd:cd13987   152 GTIPYTAPEVCEAKKNEgfvvdPSIDVWAFGVLLFCCLTGNFPWEkadSDDQFYEEFVrWQKRKNTAVpsQWrrFTPKAL 231
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 340 SLLRMLFKRNPaNRLGSegVEEVKRH 365
Cdd:cd13987   232 RMFKKLLAPEP-ERRCS--IKEVFKY 254
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
460-721 3.94e-37

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: 140.44  E-value: 3.94e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYEL-KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKR------DPSEEIEILMRYGQHPNIISLKEVFDDGKYVY 532
Cdd:cd14198     5 FNNFYILtSKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRgqdcraEILHEIAVLELAKSNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKK--KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDsIKICDFGFAKQL 610
Cdd:cd14198    85 LILEYAAGGEIFNLCVPDlaEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYPLGD-IKIVDFGMSRKI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 rGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtpEEILLRIGNGRFSLSGGIWDNI 690
Cdd:cd14198   164 -GHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDN---QETFLNISQVNVDYSEETFSSV 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 691 SRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14198   240 SQLATDFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
464-721 4.49e-37

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: 140.06  E-value: 4.49e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI--EIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd06647     9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYLAG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENGLLLTP 620
Cdd:cd06647    89 GSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRSTM 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFSLSGGiwDNISRGAKDLLS 699
Cdd:cd06647   164 VGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQNP--EKLSAIFRDFLN 238
                         250       260
                  ....*....|....*....|..
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06647   239 RCLEMDVEKRGSAKELLQHPFL 260
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
117-361 4.61e-37

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: 141.55  E-value: 4.61e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKaslkvrdRVRTKMERDI----LVEvNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd14180    14 LGEGSFS---VCRKCRHRQSGQEYAVKIISR-------RMEANTQREVaalrLCQ-SHPNIVALHEVLHDQYHTYLVMEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGLSKESVDQEKKAY 269
Cdd:cd14180    83 LRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLRPQGSRPLQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN-------ETMNMILKAKLGMP----QFLSAEA 338
Cdd:cd14180   163 TPCFTLQYAAPELFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKmfhnhaaDIMHKIKEGDFSLEgeawKGVSEEA 242
                         250       260
                  ....*....|....*....|...
gi 1958807372 339 QSLLRMLFKRNPANRLGSEGVEE 361
Cdd:cd14180   243 KDLVRGLLTVDPAKRLKLSELRE 265
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
110-359 4.81e-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: 139.78  E-value: 4.81e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14184     2 KYKIGKVIGDGNFA---VVKECVERSTGKEFALKIIDKAKCCGKEHL-IENEVSILRRVKHPNIIMLIEEMDTPAELYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFGLSKESvdqE 265
Cdd:cd14184    78 MELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVV---E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD--RNETMNMILKAKLGMPQ----FLSAEAQ 339
Cdd:cd14184   155 GPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPSpywdNITDSAK 234
                         250       260
                  ....*....|....*....|
gi 1958807372 340 SLLRMLFKRNPANRLGSEGV 359
Cdd:cd14184   235 ELISHMLQVNVEARYTAEQI 254
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
464-722 5.79e-37

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: 140.65  E-value: 5.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05612     3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAipevirlKQEQHVHNEKRVLKEV-SHPFIIRLFWTEHDQRFLYMLME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENgl 616
Cdd:cd05612    82 YVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENIL-LDKEGH---IKLTDFGFAKKLRDRT-- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 lLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISRGAKD 696
Cdd:cd05612   156 -WTLCGTPEYLAPEVIQSKGHNKAVDWWALGILIYEMLVGYPPFF---DDNPFGIYEKILAGKLEFP----RHLDLYAKD 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 697 LLSHMLHMDPHQRY-----TAEQVLKHPWIT 722
Cdd:cd05612   228 LIKKLLVVDRTRRLgnmknGADDVKNHRWFK 258
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
462-721 5.86e-37

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: 139.57  E-value: 5.86e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYEL-KEDIGIGSYSVCKRCIHSASNMEFAVKIIdknKRDPS--EEIEIlMRYGQHPNIISLKEVFDD-GKYVYLVTDL 537
Cdd:cd14109     3 ELYEIgEEDEKRAAQGAPFHVTERSTGRNFLAQLR---YGDPFlmREVDI-HNSLDHPNIVQMHDAYDDeKLAVTVIDNL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRIL--KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghpDSIKICDFGFAKQLrgENG 615
Cdd:cd14109    79 ASTIELVRDNLlpGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD-----DKLKLADFGQSRRL--LRG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCY-TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNDTpeEILLRIGNGRFSLSGGIWDNISRGA 694
Cdd:cd14109   152 KLTTLIYgSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPF-LGDNDR--ETLTNVRSGKWSFDSSPLGNISDDA 228
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14109   229 RDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
115-356 6.33e-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: 139.67  E-value: 6.33e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMerDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14190    10 EVLGGGKFGKVHTCTEKR---TGLKLAAKVINKQNSKDKEMVLLEI--QVMNQLNHRNLIQLYEAIETPNEIVLFMEYVE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL-DEIGH-IKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd14190    85 GGELFERIVDEDYhLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvNRTGHqVKIIDFGLARRYNPREKLKVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 cGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 347
Cdd:cd14190   165 -GTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDeetfEHVSDEAKDFVSNLII 243

                  ....*....
gi 1958807372 348 RNPANRLGS 356
Cdd:cd14190   244 KERSARMSA 252
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
117-354 6.51e-37

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: 139.35  E-value: 6.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDagQLYAMKVLRKASLK--VRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14121     3 LGSGTYATVYKAYRKSGAR--EVVAVKCVSKSSLNkaSTENLLTEIE--LLKKLKHPHIVELKDFQWDEEHIYLIMEYCS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDV--FTRlSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG--HIKLTDFGLSKeSVDQEKKAYS 270
Cdd:cd14121    79 GGDLsrFIR-SRRTL-PESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQ-HLKPNDEAHS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK-LGMPQF--LSAEAQSLLRMLFK 347
Cdd:cd14121   156 LRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTRpeLSADCRDLLLRLLQ 235

                  ....*..
gi 1958807372 348 RNPANRL 354
Cdd:cd14121   236 RDPDRRI 242
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
464-720 6.66e-37

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: 139.98  E-value: 6.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSY-SVCKRCIHSASNMeFAVKIIDKNKRDPSE-----EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd07830     1 YKVIKQLGDGTFgSVYLARNKETGEL-VAIKKMKKKFYSWEEcmnlrEVKSLRKLNEHPNIVKLKEVFRENDELYFVFEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGgELLDRIL--KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGEng 615
Cdd:cd07830    80 MEG-NLYQLMKdrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSG----PEVVKIADFGLAREIRSR-- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 llltPCYTAnFV------APEVLTQQG-YDAACDIWSLGVL---LYTMlagyTPFSNGPNDTPEeiLLRIgngrFSLSG- 684
Cdd:cd07830   153 ----PPYTD-YVstrwyrAPEILLRSTsYSSPVDIWALGCImaeLYTL----RPLFPGSSEIDQ--LYKI----CSVLGt 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 685 ---GIWD--------------------------NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07830   218 ptkQDWPegyklasklgfrfpqfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPY 282
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
110-367 7.25e-37

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: 139.13  E-value: 7.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKAsLKVRDRVrtkmERDIL--VEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNK---ETKELVAVKYIERG-LKIDENV----QREIInhRSLRHPNIIRFKEVVLTPTHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD--EIGHIKLTDFGLSKESVDQE 265
Cdd:cd14662    73 IVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVLHS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAySFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQGKD--RN--ETMNMILKAKLGMPQF--LSAEA 338
Cdd:cd14662   153 QPK-STVGTPAYIAPEVLSRKEYDgKVADVWSCGVTLYVMLVGAYPFEDPDdpKNfrKTIQRIMSVQYKIPDYvrVSQDC 231
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14662   232 RHLLSRIFVANPAKRI---TIPEIKNHPW 257
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-369 7.72e-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: 140.57  E-value: 7.72e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDrvrTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLAEERA---TGKLFAVKCIPKKALKGKE---SSIENEIAVlrKIKHENIVALEDIYESPNHLYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESVDQE 265
Cdd:cd14168    86 VMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSfCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA--KLGMPQF--LSAEAQSL 341
Cdd:cd14168   166 VMSTA-CGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyEFDSPYWddISDSAKDF 244
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 342 LRMLFKRNPANRlgsEGVEEVKRHAFFS 369
Cdd:cd14168   245 IRNLMEKDPNKR---YTCEQALRHPWIA 269
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
464-723 7.73e-37

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: 139.61  E-value: 7.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS---EEIEILmRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd14104     2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVlvkKEISIL-NIARHRNILRLHESFESHEELVMIFEFISG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdSIKICDFGFAKQLR-GEN-GLL 617
Cdd:cd14104    81 VDIFERITTARFeLNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGS--YIKIIEFGQSRQLKpGDKfRLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDL 697
Cdd:cd14104   159 YT---SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFE---AETNQQTIENIRNAEYAFDDEAFKNISIEALDF 232
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd14104   233 VDRLLVKERKSRMTAQEALNHPWLKQ 258
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
117-365 8.41e-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: 139.42  E-value: 8.41e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVR----------------DRVRTKMER-----DILVEVNHPFIVK 175
Cdd:cd14118     2 IGKGSYGIVKLAYNE---EDNTLYAMKILSKKKLLKQagffrrppprrkpgalGKPLDPLDRvyreiAILKKLDHPNVVK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 176 LHYAFQ--TEGKLYLILDFLRGGDVFtRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLT 253
Cdd:cd14118    79 LVEVLDdpNEDNLYMVFELVDKGAVM-EVPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 254 DFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQS---ADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM 330
Cdd:cd14118   158 DFGVSNEFEGDDALLSSTAGTPAFMAPEALSESRKKFSgkaLDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVF 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 331 PQ--FLSAEAQSLLRMLFKRNPANRLgseGVEEVKRH 365
Cdd:cd14118   238 PDdpVVSEQLKDLILRMLDKNPSERI---TLPEIKEH 271
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
107-375 1.02e-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: 139.78  E-value: 1.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLR-KASLKVRDRVrtkMERDILVEVNHPFIVKLHYAFQTEG 184
Cdd:cd06644     9 DPNEvWEIIGELGDGAFGKVYKAKNK---ETGALAAAKVIEtKSEEELEDYM---VEIEILATCNHPYIVKLLGAFYWDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06644    83 KLWIMIEFCPGGAVdAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVV-----NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK---LGMPQFLS 335
Cdd:cd06644   163 TLQRRDSFIGTPYWMAPEVVmcetmKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWS 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSEGVEEvkrHAFFSSIDWNK 375
Cdd:cd06644   243 MEFRDFLKTALDKHPETRPSAAQLLE---HPFVSSVTSNR 279
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
115-367 1.30e-36

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: 138.69  E-value: 1.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLvrkKTGPDAGQLYAMKVLRKASL-KVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd06632     6 QLLGSGSFGSVYE---GFNGDTGDFFAVKEVSLVDDdKKSRESVKQLEQEIalLSKLRHPNIVQYYGTEREEDNLYIFLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQeKKAYSF 271
Cdd:cd06632    83 YVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF-SFAKSF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRR--GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL--GMPQFLSAEAQSLLRMLFK 347
Cdd:cd06632   162 KGSPYWMAPEVIMQKnsGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGElpPIPDHLSPDAKDFIRLCLQ 241
                         250       260
                  ....*....|....*....|
gi 1958807372 348 RNPANRlgsEGVEEVKRHAF 367
Cdd:cd06632   242 RDPEDR---PTASQLLEHPF 258
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
117-368 1.33e-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: 1.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVflvRKKTGPDAGQLYAMKVL--RKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQT-EGKLYLILDFL 193
Cdd:cd14165     9 LGEGSYAKV---KSAYSERLKCNVAIKIIdkKKAPDDFVEKFLPR-ELEILARLNHKSIIKTYEIFETsDGKVYIVMELG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV-DQEKK---AY 269
Cdd:cd14165    85 VQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCLrDENGRivlSK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVnrRGHS---QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ--FLSAEAQSLLRM 344
Cdd:cd14165   165 TFCGSAAYAAPEVL--QGIPydpRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPRskNLTSECKDLIYR 242
                         250       260
                  ....*....|....*....|....
gi 1958807372 345 LFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14165   243 LLQPDVSQRL---CIDEVLSHPWL 263
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
462-721 1.65e-36

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: 138.03  E-value: 1.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII---DKNKRDPSEEIEILmRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14111     3 KPYTFLDEKARGRFGVIRRCRENATGKNFPAKIVpyqAEEKQGVLQEYEIL-KSLHHERIMALHEAYITPRYLVLIAEFC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLrgeNGLLL 618
Cdd:cd14111    82 SGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNL----NAIKIVDFGSAQSF---NPLSL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCY----TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSlSGGIWDNISRGA 694
Cdd:cd14111   155 RQLGrrtgTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFE---DQDPQETEAKILVAKFD-AFKLYPNVSQSA 230
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14111   231 SLFLKKVLSSYPWSRPTTKDCFAHAWL 257
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
464-720 1.70e-36

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: 138.58  E-value: 1.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVC-----KRCIHSasnmeFAVKIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14010     2 YVLYDEIGRGKHSVVykgrrKGTIEF-----VAIKCVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK---------- 608
Cdd:cd14010    77 TGGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNIL-LDGNGT---LKLSDFGLARregeilkelf 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 ----------QLRGENGLLLTPCYTAnfvaPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNG 678
Cdd:cd14010   153 gqfsdegnvnKVSKKQAKRGTPYYMA----PELFQGGVHSFASDLWALGCVLYEMFTGKPPFV---AESFTELVEKILNE 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 679 RF-SLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP-W 720
Cdd:cd14010   226 DPpPPPPKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPfW 269
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
103-368 1.80e-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: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADPAQfdllkVLGQGSFGkvfLVRKKTGPDAGQLYAMKVL------RKASLKVRD-RVRTKMERDILVEVN-HPFIV 174
Cdd:cd14182     2 YEKYEPKE-----ILGRGVSS---VVRRCIHKPTRQEYAVKIIditgggSFSPEEVQElREATLKEIDILRKVSgHPNII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 175 KLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd14182    74 QLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGLSKEsVDQEKKAYSFCGTVEYMAPEVV------NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA-- 326
Cdd:cd14182   154 FGFSCQ-LDPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGny 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 327 KLGMPQF--LSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14182   233 QFGSPEWddRSDTVKDLISRFLVVQPQKRYTA---EEALAHPFF 273
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
113-353 1.91e-36

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: 138.01  E-value: 1.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFL-VRKKTGPDAGQLYAMKVLRKASlkvRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:pfam07714   3 LGEKLGEGAFGEVYKgTLKGEGENTKIKVAVKTLKEGA---DEEEREDFLEEASImkKLDHPNIVKLLGVCTQGEPLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDV--FTRLSKEVLFTEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKesvDQEKK 267
Cdd:pfam07714  80 TEYMPGGDLldFLRKHKRKLTLKDLLSM-ALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR---DIYDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGT-----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQS 340
Cdd:pfam07714 156 DYYRKRGggklpIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGYrLPQPENCPDELYD 235
                         250
                  ....*....|...
gi 1958807372 341 LLRMLFKRNPANR 353
Cdd:pfam07714 236 LMKQCWAYDPEDR 248
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
111-354 2.02e-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: 138.10  E-value: 2.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14114     4 YDILEELGTGAFGVVHRCTERA---TGNNFAAKFIMTPHESDKETVRK--EIQIMNQLHHPKLINLHDAFEDDNEMVLIL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKE-VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD--EIGHIKLTDFGLSKEsVDQEKK 267
Cdd:cd14114    79 EFLSGGELFERIAAEhYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATH-LDPKES 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLR 343
Cdd:cd14114   158 VKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDdsafSGISEEAKDFIR 237
                         250
                  ....*....|.
gi 1958807372 344 MLFKRNPANRL 354
Cdd:cd14114   238 KLLLADPNKRM 248
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
113-353 2.18e-36

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 137.66  E-value: 2.18e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  113 LLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLRK-ASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:smart00219   3 LGKKLGEGAFGEVYKGKlKGKGGKKKVEVAVKTLKEdASEQQIEEFLR--EARIMRKLDHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  191 DFLRGGDV--FTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVDQEKK 267
Cdd:smart00219  81 EYMEGGDLlsYLRKNRPKL-SLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDlYDDDYYR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRML 345
Cdd:smart00219 160 KRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEYLKNGYrLPQPPNCPPELYDLMLQC 239

                   ....*...
gi 1958807372  346 FKRNPANR 353
Cdd:smart00219 240 WAEDPEDR 247
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
113-353 2.29e-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: 138.25  E-value: 2.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVRK-KTGpdagQLYAMKVLRKASLKVRD----RVRTKM-ERDILVEV-NHPFIVKLHYAFQTEGK 185
Cdd:cd13993     4 LISPIGEGAYGVVYLAVDlRTG----RKYAIKCLYKSGPNSKDgndfQKLPQLrEIDLHRRVsRHPNIITLHDVFETEVA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFT--RLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI-GHIKLTDFGLSKesv 262
Cdd:cd13993    80 IYIVLEYCPNGDLFEaiTENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLAT--- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 dQEKKAYSF-CGTVEYMAPEVVNRRGHSQ------SADWWSYGVLMFEMLTGTLPFQ--GKDRNETMNMILKAKLGMPQF 333
Cdd:cd13993   157 -TEKISMDFgVGSEFYMAPECFDEVGRSLkgypcaAGDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPNLFDVI 235
                         250       260
                  ....*....|....*....|..
gi 1958807372 334 L--SAEAQSLLRMLFKRNPANR 353
Cdd:cd13993   236 LpmSDDFYNLLRQIFTVNPNNR 257
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
111-354 2.73e-36

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: 137.84  E-value: 2.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDR--VRTKMERD--ILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14194     7 YDTGEELGSGQFAVVKKCREKS---TGLQYAAKFIKKRRTKSSRRgvSREDIEREvsILKEIQHPNVITLHEVYENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG----HIKLTDFGLSKEsV 262
Cdd:cd14194    84 ILILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFGLAHK-I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEA 338
Cdd:cd14194   163 DFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeyfsNTSALA 242
                         250
                  ....*....|....*.
gi 1958807372 339 QSLLRMLFKRNPANRL 354
Cdd:cd14194   243 KDFIRRLLVKDPKKRM 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
110-367 3.33e-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: 137.42  E-value: 3.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKAslkvrDRVRTKMERDIL--VEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQ---TKELVAVKYIERG-----EKIDENVQREIInhRSLRHPNIVRFKEVILTPTHLA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD--EIGHIKLTDFGLSKESV--D 263
Cdd:cd14665    73 IVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDgsPAPRLKICDFGYSKSSVlhS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKkaySFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEMLTGTLPFQG----KDRNETMNMILKAKLGMPQF--LSA 336
Cdd:cd14665   153 QPK---STVGTPAYIAPEVLLKKEYDgKIADVWSCGVTLYVMLVGAYPFEDpeepRNFRKTIQRILSVQYSIPDYvhISP 229
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 337 EAQSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14665   230 ECRHLISRIFVADPATRI---TIPEIRNHEW 257
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
115-370 3.64e-36

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: 137.37  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLRKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14187    13 RFLGKGGFAKCYEI---TDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL-SKESVDQEKKAySFC 272
Cdd:cd14187    90 RRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLaTKVEYDGERKK-TLC 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd14187   169 GTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTA 248
                         250
                  ....*....|....*...
gi 1958807372 353 RlgsEGVEEVKRHAFFSS 370
Cdd:cd14187   249 R---PTINELLNDEFFTS 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
107-378 4.62e-36

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: 137.57  E-value: 4.62e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQF-DLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLR-KASLKVRDRVrtkMERDILVEVNHPFIVKLHYAFQTEG 184
Cdd:cd06611     2 NPNDIwEIIGELGDGAFGKVYKAQHKE---TGLFAAAKIIQiESEEELEDFM---VEIDILSECKHPNIVGLYEAYFYEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06611    76 KLWILIEFCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPfqgkdRNET--MNMILK------AKLGM 330
Cdd:cd06611   156 TLQKRDTFIGTPYWMAPEVVAcetfkDNPYDYKADIWSLGITLIELAQMEPP-----HHELnpMRVLLKilksepPTLDQ 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 331 PQFLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFFSSIDWNKLYK 378
Cdd:cd06611   231 PSKWSSSFNDFLKSCLVKDPDDRPTA---AELLKHPFVSDQSDNKAIK 275
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
459-739 4.66e-36

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: 139.42  E-value: 4.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 459 QFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK------NKRDPSEEIEILmRYGQHPNIISLKEVF------D 526
Cdd:cd07855     2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNafdvvtTAKRTLRELKIL-RHFKHDNIIAIRDILrpkvpyA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 527 DGKYVYLVTDLMKGGelLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFG 605
Cdd:cd07855    81 DFKDVYVVLDLMESD--LHHIIHsDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLL-VNENCE---LKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAKQLRG---ENGLLLTPcYTAN--FVAPEV-LTQQGYDAACDIWSLGVLLYTMLaGYTPFSNGPN-------------D 666
Cdd:cd07855   155 MARGLCTspeEHKYFMTE-YVATrwYRAPELmLSLPEYTQAIDMWSVGCIFAEML-GRRQLFPGKNyvhqlqliltvlgT 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 667 TPEEILLRIGNGRF--------SLSGGIWDNISRGAK----DLLSHMLHMDPHQRYTAEQVLKHPWITQreqlpRHQPts 734
Cdd:cd07855   233 PSQAVINAIGADRVrryiqnlpNKQPVPWETLYPKADqqalDLLSQMLRFDPSERITVAEALQHPFLAK-----YHDP-- 305

                  ....*
gi 1958807372 735 DDPPQ 739
Cdd:cd07855   306 DDEPD 310
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
115-368 5.73e-36

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: 136.72  E-value: 5.73e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLR--KASLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd06625     6 KLLGQGAFGQVYLCYDA---DTGRELAVKQVEidPINTEASKEVKAlECEIQLLKNLQHERIVQYYGCLQDEKSLSIFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKKAY 269
Cdd:cd06625    83 YMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKrlQTICSSTGMK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILK-----AKLGMPQFLSAEAQSLLRM 344
Cdd:cd06625   163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWA---EFEPMAAIFKiatqpTNPQLPPHVSEDARDFLSL 239
                         250       260
                  ....*....|....*....|....
gi 1958807372 345 LFKRNPANRlgsEGVEEVKRHAFF 368
Cdd:cd06625   240 IFVRNKKQR---PSAEELLSHSFV 260
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
111-368 7.40e-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: 136.27  E-value: 7.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKAslKVRDRVRTK-MERDILV--EVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYSTK---HKCKVAIKIVSKK--KAPEDYLQKfLPREIEVikGLKHPNLICFYEAIETTSRVY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK---ESVDQ 264
Cdd:cd14162    77 IIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgvmKTKDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKK-AYSFCGTVEYMAPEVVnrRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMP--QFLSAEA 338
Cdd:cd14162   157 KPKlSETYCGSYAYASPEIL--RGipyDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQR-RVVFPknPTVSEEC 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 339 QSLL-RML---FKRNPanrlgsegVEEVKRHAFF 368
Cdd:cd14162   234 KDLIlRMLspvKKRIT--------IEEIKRDPWF 259
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
464-721 7.67e-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: 7.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-RDPSEEIEILMRYGQ------HPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd14070     4 YLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKKKaKKDSYVTKNLRREGRiqqmirHPNITQLLDILETENSYYLVME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESghpDSIKICDFGFAKQLRGENGL 616
Cdd:cd14070    84 LCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLL-LDEN---DNIKLIDFGLSNCAGILGYS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 --LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTpEEILLRIGNGRFS-LSGGiwdnISRG 693
Cdd:cd14070   160 dpFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSL-RALHQKMVDKEMNpLPTD----LSPG 234
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 694 AKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14070   235 AISFLRSLLEPDPLKRPNIKQALANRWL 262
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
116-359 9.29e-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: 137.16  E-value: 9.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMErdILVEV-NHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14090     9 LLGEGAYASVQTCINLY---TGKEYAVKIIEKHPGHSRSRVFREVE--TLHQCqGHPNILQLIEYFEDDERFYLVFEKMR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL---LDEIGHIKLTDFGLSKESVDQEKKA--- 268
Cdd:cd14090    84 GGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKLSSTSMtpv 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 -----YSFCGTVEYMAPEVVNR-RGHSQS----ADWWSYGVLMFEMLTGTLPFQGK-------DRNET----MNMILKA- 326
Cdd:cd14090   164 ttpelLTPVGSAEYMAPEVVDAfVGEALSydkrCDLWSLGVILYIMLCGYPPFYGRcgedcgwDRGEAcqdcQELLFHSi 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 327 KLGMPQF-------LSAEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd14090   244 QEGEYEFpekewshISAEAKDLISHLLVRDASQRYTAEQV 283
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
100-353 1.08e-35

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 141.69  E-value: 1.08e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 100 KEGYEKADPAQ--FDLLKVLGQGSFGKVFLVRKKTGPdagqlyAMKVLRKASLKVRDRVRT--KMERDILVEVNHPFIVK 175
Cdd:PTZ00267   56 EEVPESNNPREhmYVLTTLVGRNPTTAAFVATRGSDP------KEKVVAKFVMLNDERQAAyaRSELHCLAACDHFGIVK 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 176 LHYAFQTEGKLYLILDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIK 251
Cdd:PTZ00267  130 HFDDFKSDDKLLLIMEYGSGGDlnkqIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIK 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 252 LTDFGLSKESVDQEK--KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG 329
Cdd:PTZ00267  210 LGDFGFSKQYSDSVSldVASSFCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYD 289
                         250       260
                  ....*....|....*....|....*
gi 1958807372 330 -MPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:PTZ00267  290 pFPCPVSSGMKALLDPLLSKNPALR 314
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
461-737 1.18e-35

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: 138.21  E-value: 1.18e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKiidknKRDPSE----------EIEILMRYgQHPNIISLKEV-----F 525
Cdd:cd07849     4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIK-----KISPFEhqtyclrtlrEIKILLRF-KHENIIGILDIqrpptF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 526 DDGKYVYLVTDLMKGGelLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFG 605
Cdd:cd07849    78 ESFKDVYIVQELMETD--LYKLIKTQHLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNC----DLKICDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAK--QLRGENGLLLTPcYTAN--FVAPEV-LTQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPN------------DTP 668
Cdd:cd07849   152 LARiaDPEHDHTGFLTE-YVATrwYRAPEImLNSKGYTKAIDIWSVGCILAEMLSN-RPLFPGKDylhqlnlilgilGTP 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 669 -EEILLRIGNGRF-----SL---SGGIWD----NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQlPRHQPTSD 735
Cdd:cd07849   230 sQEDLNCIISLKArnyikSLpfkPKVPWNklfpNADPKALDLLDKMLTFNPHKRITVEEALAHPYLEQYHD-PSDEPVAE 308

                  ..
gi 1958807372 736 DP 737
Cdd:cd07849   309 EP 310
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
464-719 1.26e-35

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: 136.86  E-value: 1.26e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEIlMRYGQHPNIISLKEVF------DDGKYVYLVTDL 537
Cdd:cd14137     6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDKRYKNRELQI-MRRLKHPNIVKLKYFFyssgekKDEVYLNLVMEY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MkgGELLDRILKKKCFSEQEASNVL-----YVITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdsIKICDFGFAKQL-R 611
Cdd:cd14137    85 M--PETLYRVIRHYSKNKQTIPIIYvklysYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGV---LKLCDFGSAKRLvP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLlltpCY--TANFVAPE-VLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRI----G-------- 676
Cdd:cd14137   160 GEPNV----SYicSRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLF---PGESSVDQLVEIikvlGtptreqik 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 677 --NG-----RFSLSGGI-WDNISRG-----AKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14137   233 amNPnytefKFPQIKPHpWEKVFPKrtppdAIDLLSKILVYNPSKRLTALEALAHP 288
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
115-353 1.28e-35

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: 135.89  E-value: 1.28e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd06626     6 NKIGEGTFGKVYTA---VNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ-----EKKAY 269
Cdd:cd06626    83 EGTLEELLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNtttmaPGEVN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDrNETMNMIlkaKLGM---PQF-----LSAEA 338
Cdd:cd06626   163 SLVGTPAYMAPEVITgnkGEGHGRAADIWSLGCVVLEMATGKRPWSELD-NEWAIMY---HVGMghkPPIpdslqLSPEG 238
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd06626   239 KDFLSRCLESDPKKR 253
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
115-356 1.51e-35

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: 135.43  E-value: 1.51e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14193    10 EILGGGRFGQVHKCEEKS---SGLKLAAKIIKARSQKEKEEV--KNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL--DEIGHIKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd14193    85 GGELFDRIIDENYnLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLARRYKPREKLRVNF 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 cGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 347
Cdd:cd14193   165 -GTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEdeefADISEEAKDFISKLLI 243

                  ....*....
gi 1958807372 348 RNPANRLGS 356
Cdd:cd14193   244 KEKSWRMSA 252
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
107-375 1.52e-35

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: 136.31  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQF-DLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLrkaSLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEG 184
Cdd:cd06643     2 NPEDFwEIVGELGDGAFGKVYKAQNK---ETGILAAAKVI---DTKSEEELEDYMvEIDILASCDHPNIVKLLDAFYYEN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06643    76 NLWILIEFCAGGAVdAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVV-----NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK---LGMPQFLS 335
Cdd:cd06643   156 TLQRRDSFIGTPYWMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWS 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSegvEEVKRHAFFSSIDWNK 375
Cdd:cd06643   236 PEFKDFLRKCLEKNVDARWTT---SQLLQHPFVSVLVSNK 272
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
463-721 1.59e-35

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: 135.75  E-value: 1.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 463 AYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILmRYGQHPNIISL--KEVFDDGKYVYLV 534
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEkqqlvsEVNIL-RELKHPNIVRYydRIVDRANTTLYIV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELldRILKKKC------FSEQEASNVLYVITKTVEYLH-----SQGVVHRDLKPSNIlYMDESGHpdsIKICD 603
Cdd:cd08217    80 MEYCEGGDL--AQLIKKCkkenqyIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANI-FLDSDNN---VKLGD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 604 FGFAKQLRGENGL----LLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNDtpEEILLRIGNGR 679
Cdd:cd08217   154 FGLARVLSHDSSFaktyVGTPYY----MSPELLNEQSYDEKSDIWSLGCLIYELCALHPPF-QAANQ--LELAKKIKEGK 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 680 FSlsgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08217   227 FP---RIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
470-709 1.62e-35

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 137.45  E-value: 1.62e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPSEEI----EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05575     3 IGKGSFGKVLLARHKAEGKLYAVKVLQKKailKRNEVKHImaerNVLLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd05575    83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENIL-LDSQGH---VVLTDFGLCKEGIEPSDTTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpNDTPE---EIL---LRIGngrfslsggiwDNISRGAKD 696
Cdd:cd05575   159 TPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFYS--RDTAEmydNILhkpLRLR-----------TNVSPSARD 225
                         250
                  ....*....|...
gi 1958807372 697 LLSHMLHMDPHQR 709
Cdd:cd05575   226 LLEGLLQKDRTKR 238
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
515-720 1.68e-35

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: 137.36  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 515 HPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASnvlYVITKTV---EYLHSQGVVHRDLKPSNILyMD 591
Cdd:cd05599    60 NPWVVKLYYSFQDEENLYLIMEFLPGGDMMTLLMKKDTLTEEETR---FYIAETVlaiESIHKLGYIHRDIKPDNLL-LD 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 592 ESGHpdsIKICDFGFAKQLRGENgLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEI 671
Cdd:cd05599   136 ARGH---IKLSDFGLCTGLKKSH-LAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEMLIGYPPFC---SDDPQET 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 672 LLRIGNGRFSLSGGIWDNISRGAKDLLSHMLhMDPHQR---YTAEQVLKHPW 720
Cdd:cd05599   209 CRKIMNWRETLVFPPEVPISPEAKDLIERLL-CDAEHRlgaNGVEEIKSHPF 259
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
111-353 1.72e-35

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 135.20  E-value: 1.72e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKV---DGCLYAVKKSKKPFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYIQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGG---DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG----LSKESV 262
Cdd:cd13997    79 MELCENGslqDALEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGlatrLETSGD 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEkkaysfcGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGT-LPFQGKDRNEtmnmILKAKLGMP--QFLSAEA 338
Cdd:cd13997   159 VEE-------GDSRYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEpLPRNGQQWQQ----LRQGKLPLPpgLVLSQEL 227
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd13997   228 TRLLKVMLDPDPTRR 242
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
115-357 1.87e-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: 135.45  E-value: 1.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASlKVRDrVRTKMERDILV---EVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd14197    15 RELGRGKFA---VVRKCVEKDSGKEFAAKFMRKRR-KGQD-CRMEIIHEIAVlelAQANPWVINLHEVYETASEMILVLE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRL--SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDE---IGHIKLTDFGLSKeSVDQEK 266
Cdd:cd14197    90 YAAGGEIFNQCvaDREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSespLGDIKIVDFGLSR-ILKNSE 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLL 342
Cdd:cd14197   169 ELREIMGTPEYVAPEILSYEPISTATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSeeefEHLSESAIDFI 248
                         250
                  ....*....|....*
gi 1958807372 343 RMLFKRNPANRLGSE 357
Cdd:cd14197   249 KTLLIKKPENRATAE 263
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
110-353 1.90e-35

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: 135.24  E-value: 1.90e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd08222     1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLS----KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEiGHIKLTDFGLSKESVDQE 265
Cdd:cd08222    81 TEYCEGGDLDDKISeykkSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRILMGTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL-GMPQFLSAEAQSLLRM 344
Cdd:cd08222   160 DLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSR 239

                  ....*....
gi 1958807372 345 LFKRNPANR 353
Cdd:cd08222   240 MLNKDPALR 248
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
464-736 1.99e-35

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 137.06  E-value: 1.99e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN-------KRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSetlaqeeVSFFEEERDI-MAKANSPWITKLQYAFQDSENLYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDriLKKKC---FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrGE 613
Cdd:cd05601    82 YHPGGDLLS--LLSRYddiFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENIL-IDRTGH---IKLADFGSAAKL-SS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLT--PCYTANFVAPEVLT------QQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGG 685
Cdd:cd05601   155 DKTVTSkmPVGTPDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEMLYGKTPFT---EDTVIKTYSNIMNFKKFLKFP 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 686 IWDNISRGAKDLLSHMLhMDPHQRYTAEQVLKHP------WITQREQLPRHQPT--SDD 736
Cdd:cd05601   232 EDPKVSESAVDLIKGLL-TDAKERLGYEGLCCHPffsgidWNNLRQTVPPFVPTltSDD 289
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
111-367 2.02e-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: 135.47  E-value: 2.02e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDR--VRTKMER--DILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14196     7 YDIGEELGSGQFAIVKKCREKS---TGLEYAAKFIKKRQSRASRRgvSREEIERevSILRQVLHPNIITLHDVYENRTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENI-LLDE---IGHIKLTDFGLSKESV 262
Cdd:cd14196    84 VLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKnipIPHIKLIDFGLAHEIE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM-PQFLSAE---A 338
Cdd:cd14196   164 DGVEFKNIF-GTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFdEEFFSHTselA 242
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14196   243 KDFIRKLLVKETRKRL---TIQEALRHPW 268
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
116-354 2.19e-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: 135.35  E-value: 2.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLvrkktGPDA--GQLYAMK--VLRKASLKVRDRVRT-----KMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd06628     7 LIGSGSFGSVYL-----GMNAssGELMAVKqvELPSVSAENKDRKKSmldalQREIALLRELQHENIVQYLGSSSDANHL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE------ 260
Cdd:cd06628    82 NIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKleansl 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRnetMNMILK----AKLGMPQFLSA 336
Cdd:cd06628   162 STKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQ---MQAIFKigenASPTIPSNISS 238
                         250       260
                  ....*....|....*....|...
gi 1958807372 337 EAQSLLRMLF-----KRNPANRL 354
Cdd:cd06628   239 EARDFLEKTFeidhnKRPTADEL 261
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
490-740 2.58e-35

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 136.60  E-value: 2.58e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKN---KRDP----SEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLdRILKK---KCFSEQEAS 559
Cdd:cd05574    29 FAMKVLDKEemiKRNKvkrvLTEREILATL-DHPFLPTLYASFQTSTHLCFVMDYCPGGELF-RLLQKqpgKRLPEEVAR 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 NVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQL----------------RGENGLLLTPCY- 622
Cdd:cd05574   107 FYAAEVLLALEYLHLLGFVYRDLKPENIL-LHESGH---IMLTDFDLSKQSsvtpppvrkslrkgsrRSSVKSIEKETFv 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 ------------TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDtpEEILLRIGNGRFSLSGGIwdNI 690
Cdd:cd05574   183 aepsarsnsfvgTEEYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTTPFK-GSNR--DETFSNILKKELTFPESP--PV 257
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 691 SRGAKDLLSHMLHMDPHQR----YTAEQVLKHPWITQ-REQLPRHQPtsddPPQV 740
Cdd:cd05574   258 SSEAKDLIRKLLVKDPSKRlgskRGASEIKRHPFFRGvNWALIRNMT----PPII 308
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
470-722 3.22e-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: 134.68  E-value: 3.22e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN-------KRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllkphqKEKMSMEIAI-HRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd14187    94 LLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDM----EVKIGDFGLATKVEYDGERKKTLCG 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSlsggIWDNISRGAKDLLSHML 702
Cdd:cd14187   170 TPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLLVGKPPFE---TSCLKETYLRIKKNEYS----IPKHINPVAASLIQKML 242
                         250       260
                  ....*....|....*....|
gi 1958807372 703 HMDPHQRYTAEQVLKHPWIT 722
Cdd:cd14187   243 QTDPTARPTINELLNDEFFT 262
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
113-367 3.84e-35

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 134.53  E-value: 3.84e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFL--VRKKTGPDAGQLYAMKVLRKASLKVRDRVrTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14076     5 LGRTLGEGEFGKVKLgwPLPKANHRSGVQVAIKLIRRDTQQENCQT-SKIMREIniLKGLTHPNIVRLLDVLKTKKYIGI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVDQEKK 267
Cdd:cd14076    84 VLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfDHFNGDL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRG--HSQSADWWSYGVLMFEMLTGTLPF-------QGKDRNETMNMILKAKLGMPQFLSAEA 338
Cdd:cd14076   164 MSTSCGSPCYAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFdddphnpNGDNVPRLYRYICNTPLIFPEYVTPKA 243
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14076   244 RDLLRRILVPNPRKRI---RLSAIMRHAW 269
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
462-721 4.38e-35

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: 134.28  E-value: 4.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII---DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd14110     3 KTYAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIpykPEDKQLVLREYQVLRRL-SHPRIAQLHSAYLSPRHLVLIEELC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENGLLL 618
Cdd:cd14110    82 SGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITE----KNLLKIVDLGNAQPFNQGKVLMT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPC-YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSgGIWDNISRGAKDL 697
Cdd:cd14110   158 DKKgDYVETMAPELLEGQGAGPQTDIWAIGVTAFIMLSADYPVS---SDLNWERDRNIRKGKVQLS-RCYAGLSGGAVNF 233
                         250       260
                  ....*....|....*....|....
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14110   234 LKSTLCAKPWGRPTASECLQNPWL 257
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
111-354 7.46e-35

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: 133.59  E-value: 7.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14191     4 YDIEERLGSGKFGQVFrLVEKKTK----KVWAGKFFKAYSAKEKENIRQEIS--IMNCLHHPKLVQCVDAFEEKANIVMV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIG-HIKLTDFGLSK--ESVDQ 264
Cdd:cd14191    78 LEMVSGGELFERIIDEDFeLTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARrlENAGS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYsfcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQS 340
Cdd:cd14191   158 LKVLF---GTPEFVAPEVINYEPIGYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDdeafDEISDDAKD 234
                         250
                  ....*....|....
gi 1958807372 341 LLRMLFKRNPANRL 354
Cdd:cd14191   235 FISNLLKKDMKARL 248
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
120-370 8.01e-35

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 133.44  E-value: 8.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 120 GSFGKVFLVRKKtgpDAGQLYamkvlrkaslkVRDRVRTKMERDILVEV-----NHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:PHA03390   27 GKFGKVSVLKHK---PTQKLF-----------VQKIIKAKNFNAIEPMVhqlmkDNPNFIKLYYSVTTLKGHVLIMDYIK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDE-IGHIKLTDFGLSK----ESVDQekkay 269
Cdd:PHA03390   93 DGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLCDYGLCKiigtPSCYD----- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 sfcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNE-----TMNMILKAKLGMPQFLSAEAQSLLRM 344
Cdd:PHA03390  168 ---GTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFK-EDEDEeldleSLLKRQQKKLPFIKNVSKNANDFVQS 243
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 345 LFKRNPANRLGSegVEEVKRHAFFSS 370
Cdd:PHA03390  244 MLKYNINYRLTN--YNEIIKHPFLKI 267
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
115-353 9.67e-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: 133.05  E-value: 9.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLkvrDRVRTKMERDILV--EVNHPFIVKLhYAFQTE-GKLYLILD 191
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDAS---ESERKDFLKEARVmkKLGHPNVVRL-LGVCTEeEPLYLVME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVL---------FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsV 262
Cdd:cd00192    77 YMEGGDLLDFLRKSRPvfpspepstLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRD-I 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK-AKLGMPQFLSAE 337
Cdd:cd00192   156 YDDDYYRKKTGGklpIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSNEEVLEYLRKgYRLPKPENCPDE 235
                         250
                  ....*....|....*.
gi 1958807372 338 AQSLLRMLFKRNPANR 353
Cdd:cd00192   236 LYELMLSCWQLDPEDR 251
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
464-721 1.21e-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: 133.21  E-value: 1.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIH-SASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14201     8 YSRKDLVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKSQillgkEIKILKEL-QHENIVALYDVQEMPNSVFLVMEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDS-----IKICDFGFAKQLRg 612
Cdd:cd14201    87 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSvsgirIKIADFGFARYLQ- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRfSLSGGIWDNISR 692
Cdd:cd14201   166 SNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQ---ANSPQDLRMFYEKNK-NLQPSIPRETSP 241
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14201   242 YLADLLLGLLQRNQKDRMDFEAFFSHPFL 270
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
111-357 1.21e-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: 133.19  E-value: 1.21e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRkasLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd13996     8 FEEIELLGSGGFGSVYKVRNKVD---GVTYAIKKIR---LTEKSSASEKVLREVkaLAKLNHPNIVRYYTAWVEEPPLYI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYL---AELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLTDFGLSKESVDQ 264
Cdd:cd13996    82 QMELCEGGTLRDWIDRRNSSSKNDRKLALelfKQILKGVSYIHSKGIVHRDLKPSNIFLDnDDLQVKIGDFGLATSIGNQ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAY--------------SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLtgtLPFQ-GKDRNETMNMILKAKLg 329
Cdd:cd13996   162 KRELNnlnnnnngntsnnsVGIGTPLYASPEQLDGENYNEKADIYSLGIILFEML---HPFKtAMERSTILTDLRNGIL- 237
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 330 mPQFLSA----EAQSLLRMLfKRNPANRLGSE 357
Cdd:cd13996   238 -PESFKAkhpkEADLIQSLL-SKNPEERPSAE 267
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
470-712 2.26e-34

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: 133.94  E-value: 2.26e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN----KRDPSE---EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05603     3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKKtilkKKEQNHimaERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd05603    83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENIL-LDCQGH---VVLTDFGLCKEGMEPEETTSTFCG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEIL---LRIGNGRfslsggiwdniSRGAKDLL 698
Cdd:cd05603   159 TPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLYGLPPFySRDVSQMYDNILhkpLHLPGGK-----------TVAACDLL 227
                         250
                  ....*....|....
gi 1958807372 699 SHMLHMDPHQRYTA 712
Cdd:cd05603   228 QGLLHKDQRRRLGA 241
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
451-739 2.28e-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: 2.28e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 451 VQINGNAAQFSEAYELKEDIGIGSY-SVCKrCIHSASNMEFAVKIIDKnkrdPSEEIEI---------LMRYGQHPNIIS 520
Cdd:cd07851     4 QELNKTVWEVPDRYQNLSPVGSGAYgQVCS-AFDTKTGRKVAIKKLSR----PFQSAIHakrtyrelrLLKHMKHENVIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 521 LKEVF------DDGKYVYLVTDLMkgGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESg 594
Cdd:cd07851    79 LLDVFtpasslEDFQDVYLVTHLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDC- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 595 hpdSIKICDFGFAKQLRGE-NGLLLTPCYTanfvAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPND----- 666
Cdd:cd07851   156 ---ELKILDFGLARHTDDEmTGYVATRWYR----APEImLNWMHYNQTVDIWSVGCIMAELLTGKTLFpGSDHIDqlkri 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 667 -----TP-EEILLRIGNGR---------------FSlsgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITqre 725
Cdd:cd07851   229 mnlvgTPdEELLKKISSESarnyiqslpqmpkkdFK---EVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLA--- 302
                         330
                  ....*....|....
gi 1958807372 726 qlPRHQPTsDDPPQ 739
Cdd:cd07851   303 --EYHDPE-DEPVA 313
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
111-368 2.80e-34

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: 132.66  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKmERDILVEVN-HPFIVKLHYAFQTEGKLYLI 189
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNK---ETGELVAIKKMKKKFYSWEECMNLR-EVKSLRKLNeHPNIVKLKEVFRENDELYFV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGgDVF--TRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvdQEKK 267
Cdd:cd07830    77 FEYMEG-NLYqlMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI--RSRP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AY-SFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQGkdRNET--MNMI-----------------LKA 326
Cdd:cd07830   154 PYtDYVSTRWYRAPEILLRSTsYSSPVDIWALGCIMAELYTLRPLFPG--SSEIdqLYKIcsvlgtptkqdwpegykLAS 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 327 KLG--MPQFL-----------SAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07830   232 KLGfrFPQFAptslhqlipnaSPEAIDLIKDMLRWDPKKRPTA---SQALQHPYF 283
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
470-732 3.04e-34

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: 133.59  E-value: 3.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI------EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd05595     3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVahtvteSRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYT 623
Cdd:cd05595    83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLM-LDKDGH---IKITDFGLCKEGITDGATMKTFCGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLrIGNGRFSlsggiwDNISRGAKDLLSHMLH 703
Cdd:cd05595   159 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELIL-MEEIRFP------RTLSPEAKSLLAGLLK 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 704 MDPHQRY-----TAEQVLKHP------W--ITQREQLPRHQP 732
Cdd:cd05595   232 KDPKQRLgggpsDAKEVMEHRfflsinWqdVVQKKLLPPFKP 273
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
115-365 3.76e-34

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: 131.64  E-value: 3.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKaSLKVRDRVRTKMERDilvevNHPFIVKLH--YA--FQTEGKLYLI 189
Cdd:cd14089     7 QVLGLGINGKVLeCFHKKTG----EKFALKVLRD-NPKARREVELHWRAS-----GCPHIVRIIdvYEntYQGRKCLLVV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGLSKEsVDQ 264
Cdd:cd14089    77 MECMEGGELFSRIQEraDSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKE-TTT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMILKAKLGMPQF---------LS 335
Cdd:cd14089   156 KKSLQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKKRIRNGQYefpnpewsnVS 234
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 336 AEAQSLLRMLFKRNPANRLgseGVEEVKRH 365
Cdd:cd14089   235 EEAKDLIRGLLKTDPSERL---TIEEVMNH 261
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
464-737 7.18e-34

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: 133.07  E-value: 7.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVK-IID--KNKRDPSE---EIEILMRYGQHPNIISLKEVF--DDGKYVYLVT 535
Cdd:cd07852     9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDafRNATDAQRtfrEIMFLQELNDHPNIIKLLNVIraENDKDIYLVF 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGelLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLR---- 611
Cdd:cd07852    89 EYMETD--LHAVIRANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNIL-LNSDCR---VKLADFGLARSLSqlee 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPcYTAN--FVAPEVL-TQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPN--DTPEEILLRIGN--------- 677
Cdd:cd07852   163 DDENPVLTD-YVATrwYRAPEILlGSTRYTKGVDMWSVGCILGEMLLG-KPLFPGTStlNQLEKIIEVIGRpsaediesi 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 678 ---------------GRFSLSgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQreqlpRHQPtSDDP 737
Cdd:cd07852   241 qspfaatmleslppsRPKSLD-ELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVAQ-----FHNP-ADEP 308
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
110-368 7.24e-34

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 131.68  E-value: 7.24e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlRKASLKVRDRVRTKMERDI--LVEVN-HPFIVKLHYAFQTEGKL 186
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRE---TGETVALK--KVALRKLEGGIPNQALREIkaLQACQgHPYVVKLRDVFPHGTGF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLrGGDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd07832    76 VLVFEYM-LSSLSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEED 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSF-CGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQF---------- 333
Cdd:cd07832   155 PRLYSHqVATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRT-LGTPNEktwpeltslp 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 334 ---------------------LSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07832   234 dynkitfpeskgirleeifpdCSPEAIDLLKGLLVYNPKKRLSA---EEALRHPYF 286
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
470-725 7.67e-34

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: 130.93  E-value: 7.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKrDPSE------EIEILMRyGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd06605     9 LGEGNGGVVSKVRHRPSGQIMAVKVIRLEI-DEALqkqilrELDVLHK-CNSPYIVGFYGAFYSEGDISICMEYMDGGSL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 lDRILKK-KCFSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLrgENGLLLTPC 621
Cdd:cd06605    87 -DKILKEvGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNIL-VNSRG---QVKLCDFGVSGQL--VDSLAKTFV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSN---GPNDTPEEILLRIGNGRF-SLSGGIWdniSRGAKDL 697
Cdd:cd06605   160 GTRSYMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYPPpnaKPSMMIFELLSYIVDEPPpLLPSGKF---SPDFQDF 236
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWITQRE 725
Cdd:cd06605   237 VSQCLQKDPTERPSYKELMEHPFIKRYE 264
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
110-354 9.42e-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: 130.52  E-value: 9.42e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPDAGqlYAMKVLRKASLKVRDRVRTKmERDILVEVNHPFIVKLhYAFQT-EGKLYL 188
Cdd:cd14202     3 EFSRKDLIGHGAFAVVFKGRHKEKHDLE--VAVKCINKKNLAKSQTLLGK-EIKILKELKHENIVAL-YDFQEiANSVYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG---------HIKLTDFGLSK 259
Cdd:cd14202    79 VMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGFAR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 eSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL---GMPQFLSA 336
Cdd:cd14202   159 -YLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSlspNIPRETSS 237
                         250
                  ....*....|....*...
gi 1958807372 337 EAQSLLRMLFKRNPANRL 354
Cdd:cd14202   238 HLRQLLLGLLQRNQKDRM 255
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
464-721 1.35e-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: 129.98  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS-------EEIEILMRYgQHPNIISLKEVFD-DGKYVYLVt 535
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfvqkflpRELSILRRV-NHPNIVQMFECIEvANGRLYIV- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 dlMKGGE--LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdeSGHPDSIKICDFGFAKQLRGE 613
Cdd:cd14164    80 --MEAAAtdLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILL---SADDRKIKIADFGFARFVEDY 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFsngpNDTPEEILLRIGNGRFSLSGgiwDNISR 692
Cdd:cd14164   155 PELSTTFCGSRAYTPPEVILGTPYDPkKYDVWSLGVVLYVMVTGTMPF----DETNVRRLRLQQRGVLYPSG---VALEE 227
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14164   228 PCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
505-728 1.63e-33

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: 129.98  E-value: 1.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKP 584
Cdd:cd14117    56 EIEI-QSHLRHPNILRLYNYFHDRKRIYLILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKP 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 585 SNILYmdesGHPDSIKICDFGF---AKQLRGEnglllTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFS 661
Cdd:cd14117   135 ENLLM----GYKGELKIADFGWsvhAPSLRRR-----TMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVGMPPFE 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 662 NGPNDTPEEILLRIgNGRFSLSggiwdnISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI--TQREQLP 728
Cdd:cd14117   206 SASHTETYRRIVKV-DLKFPPF------LSDGSRDLISKLLRYHPSERLPLKGVMEHPWVkaNSRRVLP 267
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
117-314 1.69e-33

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: 129.88  E-value: 1.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd13978     1 LGSGGFGTVSKARHV---SWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHRL--GIVYRDLKPENILLDEIGHIKLTDFGLSK-----ESVDQEKKA 268
Cdd:cd13978    78 SLKSLLEREIQDVPWSLRFRIIhEIALGMNFLHNMdpPLLHHDLKPENILLDNHFHVKISDFGLSKlgmksISANRRRGT 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 269 YSFCGTVEYMAPEV---VNRRGHSQSaDWWSYGVLMFEMLTGTLPFQGK 314
Cdd:cd13978   158 ENLGGTPIYMAPEAfddFNKKPTSKS-DVYSFAIVIWAVLTRKEPFENA 205
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
481-720 1.72e-33

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: 131.32  E-value: 1.72e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 481 CIHSASNMEFAVKIIDKNKRDPSEEIE------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFS 554
Cdd:cd05571    14 CREKATGELYAIKILKKEVIIAKDEVAhtltenRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGELFFHLSRERVFS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 555 EQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQ 634
Cdd:cd05571    94 EDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLL-LDKDGH---IKITDFGLCKEEISYGATTKTFCGTPEYLAPEVLED 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 635 QGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLrIGNGRFSlsggiwDNISRGAKDLLSHMLHMDPHQRY---- 710
Cdd:cd05571   170 NDYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELIL-MEEVRFP------STLSPEAKSLLAGLLKKDPKKRLgggp 242
                         250
                  ....*....|.
gi 1958807372 711 -TAEQVLKHPW 720
Cdd:cd05571   243 rDAKEIMEHPF 253
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
470-721 1.83e-33

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: 129.48  E-value: 1.83e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE----EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD 545
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKKMDLRKQQRREllfnEVVI-MRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKKKCFSEQEASNVLYVItKTVEYLHSQGVVHRDLKPSNILYMdesgHPDSIKICDFGFAKQLRGE----NGLLLTPC 621
Cdd:cd06648    94 IVTHTRMNEEQIATVCRAVL-KALSFLHSQGVIHRDIKSDSILLT----SDGRVKLSDFGFCAQVSKEvprrKSLVGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTAnfvaPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIgngRFSLSGGIWD--NISRGAKDLLS 699
Cdd:cd06648   169 WMA----PEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEP---PLQAMKRI---RDNEPPKLKNlhKVSPRLRSFLD 238
                         250       260
                  ....*....|....*....|..
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06648   239 RMLVRDPAQRATAAELLNHPFL 260
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
110-365 2.15e-33

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 130.74  E-value: 2.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRT---KMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14094     4 VYELCEVIGKGPFS---VVRRCIHRETGQQFAVKIVDVAKFTSSPGLSTedlKREASICHMLKHPHIVELLETYSSDGML 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSK 259
Cdd:cd14094    81 YMVFEFMDGADlcfeIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKdRNETMNMILKAKLGM--PQF--LS 335
Cdd:cd14094   161 QLGESGLVAGGRVGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGCLPFYGT-KERLFEGIIKGKYKMnpRQWshIS 239
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 336 AEAQSLLRMLFKRNPANRLgseGVEEVKRH 365
Cdd:cd14094   240 ESAKDLVRRMLMLDPAERI---TVYEALNH 266
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
111-358 2.46e-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: 130.33  E-value: 2.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRK-ASLKVrdrVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14085     5 FEIESELGRGATSVVYRCRQK---GTQKPYAVKKLKKtVDKKI---VRT--EIGVLLRLSHPNIIKLKEIFETPTEISLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGLSKeSVDQEK 266
Cdd:cd14085    77 LELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSK-IVDQQV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM-NMILKAKLGM--PQF--LSAEAQSL 341
Cdd:cd14085   156 TMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILLCGFEPFYDERGDQYMfKRILNCDYDFvsPWWddVSLNAKDL 235
                         250
                  ....*....|....*..
gi 1958807372 342 LRMLFKRNPANRLGSEG 358
Cdd:cd14085   236 VKKLIVLDPKKRLTTQQ 252
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
111-353 2.57e-33

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: 129.04  E-value: 2.57e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLK----VRDRVRTK--MERDILVEVN---HPFIVKLHYAFQ 181
Cdd:cd14004     2 YTILKEMGEGAYGQVNLAIYK---SKGKEVVIKFIFKERILvdtwVRDRKLGTvpLEIHILDTLNkrsHPNIVKLLDFFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 TEGKLYLILD-FLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSke 260
Cdd:cd14004    79 DDEFYYLVMEkHGSGMDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA-- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAYSFCGTVEYMAPEVVnrRGHS---QSADWWSYGVLMFEMLTGTLPFQGKDRnetmnmILKAKLGMPQFLSAE 337
Cdd:cd14004   157 AYIKSGPFDTFVGTIDYAAPEVL--RGNPyggKEQDIWALGVLLYTLVFKENPFYNIEE------ILEADLRIPYAVSED 228
                         250
                  ....*....|....*.
gi 1958807372 338 AQSLLRMLFKRNPANR 353
Cdd:cd14004   229 LIDLISRMLNRDVGDR 244
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
111-356 2.58e-33

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: 128.85  E-value: 2.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLrkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14107     4 YEVKEEIGRGTFG---FVKRVTHKGNGECCAAKFI---PLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILIL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL--DEIGHIKLTDFGLSKEsVDQEKKA 268
Cdd:cd14107    78 ELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQE-ITPSEHQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL--GMPQF--LSAEAQSLLRM 344
Cdd:cd14107   157 FSKYGSPEFVAPEIVHQEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVVswDTPEIthLSEDAKDFIKR 236
                         250
                  ....*....|..
gi 1958807372 345 LFKRNPANRLGS 356
Cdd:cd14107   237 VLQPDPEKRPSA 248
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
117-311 3.60e-33

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 129.49  E-value: 3.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLR-KASLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKL-YLI 189
Cdd:cd13989     1 LGSGGFGYVTLWKHQ---DTGEYVAIKKCRqELSPSDKNRERWCLEVQIMKKLNHPNVVSArdvppELEKLSPNDLpLLA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGD---VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGLSKEsVD 263
Cdd:cd13989    78 MEYCSGGDlrkVLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGrviYKLIDLGYAKE-LD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd13989   157 QGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPF 204
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
464-721 3.82e-33

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: 128.54  E-value: 3.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK---RDPSEEIEILMRYGQHP-----NIISLKEVFDDGKYVYLVT 535
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKdylDQSLDEIRLLELLNKKDkadkyHIVRLKDVFYFKNHLCIVF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGG--ELLdRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDSIKICDFGFAkqlrge 613
Cdd:cd14133    81 ELLSQNlyEFL-KQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYS--RCQIKIIDFGSS------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 ngllltpCYTANFV----------APEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGN--GRFS 681
Cdd:cd14133   152 -------CFLTQRLysyiqsryyrAPEVILGLPYDEKIDMWSLGCILAELYTGEPLF---PGASEVDQLARIIGtiGIPP 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 682 ---LSGGIWDNisRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14133   222 ahmLDQGKADD--ELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
111-369 4.40e-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: 128.10  E-value: 4.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFL-VRKKTGpdagQLYAMKVLRkasLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd06614     2 YKNLEKIGEGASGEVYKaTDRATG----KEVAIKKMR---LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGG---DVFTRlsKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd06614    75 MEYMDGGsltDIITQ--NPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQLTKEKS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQF-----LSAEAQSL 341
Cdd:cd06614   153 KRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYL--EEPPLRALFLITTKGIPPLknpekWSPEFKDF 230
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 342 LRMLFKRNPANRLGSegvEEVKRHAFFS 369
Cdd:cd06614   231 LNKCLVKDPEKRPSA---EELLQHPFLK 255
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
449-736 4.58e-33

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: 130.96  E-value: 4.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 449 PIVQINGNAAQfSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPS----EEIEIlMRYGQHPNIISL 521
Cdd:cd05596    14 PVNEITKLRMN-AEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSKFemiKRSDSaffwEERDI-MAHANSEWIVQL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 522 KEVFDDGKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKI 601
Cdd:cd05596    92 HYAFQDDKYLYMVMDYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNML-LDASGH---LKL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 602 CDFGFAKQLrGENGLLL--TPCYTANFVAPEVLTQQG----YDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILlr 674
Cdd:cd05596   167 ADFGTCMKM-DKDGLVRsdTAVGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLYEMLVGDTPFyADSLVGTYGKIM-- 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 675 igNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQ--RYTAEQVLKHP--------WITQREQLPRHQP--TSDD 736
Cdd:cd05596   244 --NHKNSLQFPDDVEISKDAKSLICAFLTDREVRlgRNGIEEIKAHPffkndqwtWDNIRETVPPVVPelSSDI 315
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
464-721 5.59e-33

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: 128.57  E-value: 5.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID---KNKRDPSEEIEILMRYGQHPNIISLKEVF------DDGKYVYLV 534
Cdd:cd06608     8 FELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDiieDEEEEIKLEINILRKFSNHPNIATFYGAFikkdppGGDDQLWLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGG---ELLDRILKK-KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdsIKICDFGFAKQL 610
Cdd:cd06608    88 MEYCGGGsvtDLVKGLRKKgKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAE----VKLVDFGVSAQL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTPCYTANFVAPEVLT-----QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIGNGRFS--LS 683
Cdd:cd06608   164 DSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMH---PMRALFKIPRNPPPtlKS 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 684 GGIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06608   241 PEKW---SKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
464-661 5.65e-33

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: 128.24  E-value: 5.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK----------NKRDP-SEEIEILMRYGQHPNIISLKEVFDDGKYVY 532
Cdd:cd13993     2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKsgpnskdgndFQKLPqLREIDLHRRVSRHPNIITLHDVFETEVAIY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKKKCF--SEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdeSGHPDSIKICDFGFA--K 608
Cdd:cd13993    82 IVLEYCPNGDLFEAITENRIYvgKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILL---SQDEGTVKLCDFGLAttE 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 609 QLRGENGllltpCYTANFVAPEVLTQ-----QGYD-AACDIWSLGVLLYTMLAGYTPFS 661
Cdd:cd13993   159 KISMDFG-----VGSEFYMAPECFDEvgrslKGYPcAAGDIWSLGIILLNLTFGRNPWK 212
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
470-720 5.79e-33

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: 128.28  E-value: 5.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYS----VCKRCIHSASNMeFAVKIIDK----NKRDPSE----EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd05583     2 LGTGAYGkvflVRKVGGHDAGKL-YAMKVLKKativQKAKTAEhtmtERQVLEAVRQSPFLVTLHYAFQTDAKLHLILDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQ-LRGENGL 616
Cdd:cd05583    81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSEGH---VVLTDFGLSKEfLPGENDR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLT--QQGYDAACDIWSLGVLLYTMLAGYTPFS-NGPNDTPEEILLRIgngrFSLSGGIWDNISRG 693
Cdd:cd05583   157 AYSFCGTIEYMAPEVVRggSDGHDKAVDWWSLGVLTYELLTGASPFTvDGERNSQSEISKRI----LKSHPPIPKTFSAE 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 694 AKDLLSHMLHMDPHQR-----YTAEQVLKHPW 720
Cdd:cd05583   233 AKDFILKLLEKDPKKRlgagpRGAHEIKEHPF 264
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
490-721 5.91e-33

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: 127.90  E-value: 5.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKII-----DKNKRDPSEEI--EILMRYG-QHPNIISL--KEVFDDGKYVYLvtDLMKGGELLDRILKKKCFSEQEAS 559
Cdd:cd06632    28 FAVKEVslvddDKKSRESVKQLeqEIALLSKlRHPNIVQYygTEREEDNLYIFL--EYVPGGSIHKLLQRYGAFEEPVIR 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 NVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRgENGLLLTPCYTANFVAPEVLTQQ--GY 637
Cdd:cd06632   106 LYTRQILSGLAYLHSRNTVHRDIKGANIL-VDTNG---VVKLADFGMAKHVE-AFSFAKSFKGSPYWMAPEVIMQKnsGY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 638 DAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNgrfslSG---GIWDNISRGAKDLLSHMLHMDPHQRYTAEQ 714
Cdd:cd06632   181 GLAVDIWSLGCTVLEMATGKPPWSQY---EGVAAIFKIGN-----SGelpPIPDHLSPDAKDFIRLCLQRDPEDRPTASQ 252

                  ....*..
gi 1958807372 715 VLKHPWI 721
Cdd:cd06632   253 LLEHPFV 259
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
470-721 6.39e-33

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: 128.04  E-value: 6.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKII---------DKNKRDPSE----EIEILmRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06628     8 IGSGSFGSVYLGMNASSGELMAVKQVelpsvsaenKDRKKSMLDalqrEIALL-RELQHENIVQYLGSSSDANHLNIFLE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLrgENGL 616
Cdd:cd06628    87 YVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANIL-VDNKG---GIKISDFGISKKL--EANS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTAN--------FVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNgrfSLSGGIWD 688
Cdd:cd06628   161 LSTKNNGARpslqgsvfWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPF---PDCTQMQAIFKIGE---NASPTIPS 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06628   235 NISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
470-721 8.82e-33

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: 127.80  E-value: 8.82e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYgQHPNIISLK--EVFDDgkYVYLVTDLMKGG 541
Cdd:cd06626     8 IGEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKtikeiaDEMKVLEGL-DHPNLVRYYgvEVHRE--EVYIFMEYCQEG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDriLKKKCFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQL--------R 611
Cdd:cd06626    85 TLEE--LLRHGRILDEAVIRVYTlqLLEGLAYLHENGIVHRDIKPANIFL----DSNGLIKLGDFGSAVKLknntttmaP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GE-NGLLLTPCYTanfvAPEVLTQQ---GYDAACDIWSLGVLLYTMLAGYTPFSNgpNDTPEEILLRIGNGR---FSLSg 684
Cdd:cd06626   159 GEvNSLVGTPAYM----APEVITGNkgeGHGRAADIWSLGCVVLEMATGKRPWSE--LDNEWAIMYHVGMGHkppIPDS- 231
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 685 giwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06626   232 ---LQLSPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
115-357 1.50e-32

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 127.35  E-value: 1.50e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKaslkvRDRVRtKMERDILVEV-------NHPFIVKLHYAFQTEGKLY 187
Cdd:cd14198    14 KELGRGKFA---VVRQCISKSTGQEYAAKFLKK-----RRRGQ-DCRAEILHEIavlelakSNPRVVNLHEVYETTSEII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI---GHIKLTDFGLSKEsV 262
Cdd:cd14198    85 LILEYAAGGEIFNLCVPDLaeMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIyplGDIKIVDFGMSRK-I 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEA 338
Cdd:cd14198   164 GHACELREIMGTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEetfsSVSQLA 243
                         250
                  ....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRLGSE 357
Cdd:cd14198   244 TDFIQKLLVKNPEKRPTAE 262
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
464-720 1.63e-32

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: 127.81  E-value: 1.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYS----VCKRCIHSASNMeFAVKIIDK----NKRDPSE----EIEILMRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd05613     2 FELLKVLGTGAYGkvflVRKVSGHDAGKL-YAMKVLKKativQKAKTAEhtrtERQVLEHIRQSPFLVTLHYAFQTDTKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQ-L 610
Cdd:cd05613    81 HLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENIL-LDSSGH---VVLTDFGLSKEfL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTPCYTANFVAPEVLT--QQGYDAACDIWSLGVLLYTMLAGYTPFS-NGPNDTPEEILLRIGNGRFSLSggiw 687
Cdd:cd05613   157 LDENERAYSFCGTIEYMAPEIVRggDSGHDKAVDWWSLGVLMYELLTGASPFTvDGEKNSQAEISRRILKSEPPYP---- 232
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 688 DNISRGAKDLLSHMLHMDPHQRY-----TAEQVLKHPW 720
Cdd:cd05613   233 QEMSALAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPF 270
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
470-713 1.88e-32

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: 128.98  E-value: 1.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPSEEI----EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05602    15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKailKKKEEKHImserNVLLKNVKHPFLVGLHFSFQTTDKLYFVLDYINGGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd05602    95 LFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENIL-LDSQGH---IVLTDFGLCKENIEPNGTTSTFCG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISRGAKDLLSHML 702
Cdd:cd05602   171 TPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLYGLPPFY---SRNTAEMYDNILNKPLQLK----PNITNSARHLLEGLL 243
                         250
                  ....*....|.
gi 1958807372 703 HMDPHQRYTAE 713
Cdd:cd05602   244 QKDRTKRLGAK 254
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
453-737 1.93e-32

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: 128.46  E-value: 1.93e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 453 INGNAAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEiLMRYGQHPNIISLKEVF- 525
Cdd:cd07856     1 IFGTVFEITTRYSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVlakrtyRELK-LLKHLRHENIISLSDIFi 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 526 DDGKYVYLVTDLMkgGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFG 605
Cdd:cd07856    80 SPLEDIYFVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENC----DLKICDFG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAK-QLRGENGLLLTPCYTanfvAPEV-LTQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPN-------------DTPEE 670
Cdd:cd07856   154 LARiQDPQMTGYVSTRYYR----APEImLTWQKYDVEVDIWSAGCIFAEMLEG-KPLFPGKDhvnqfsiitellgTPPDD 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 671 ILLRIGNG---RFSLS---------GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITqreqlPRHQPTsDDP 737
Cdd:cd07856   229 VINTICSEntlRFVQSlpkrervpfSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYLA-----PYHDPT-DEP 301
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
114-353 1.99e-32

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 126.39  E-value: 1.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd08221     5 VRVLGRGAFGEAVLYRKT---EDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYC 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSF 271
Cdd:cd08221    82 NGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSESSMAESI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM--PQFlSAEAQSLLRMLFKRN 349
Cdd:cd08221   162 VGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEDidEQY-SEEIIQLVHDCLHQD 240

                  ....
gi 1958807372 350 PANR 353
Cdd:cd08221   241 PEDR 244
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
115-311 2.38e-32

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: 126.37  E-value: 2.38e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVF-LVRKKTGPDAgqlyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14082     9 EVLGSGQFGIVYgGKHRKTGRDV----AIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEV-LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG---HIKLTDFGLSKeSVDQEKKAY 269
Cdd:cd14082    85 HGDMLEMILSSEKgRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFAR-IIGEKSFRR 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14082   164 SVVGTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSGTFPF 205
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
117-368 4.00e-32

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: 125.45  E-value: 4.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVflvrkKTGPDAGQL--YAMKVLRKASLKV----RDRVRTKMErdILVEVNHPFIVKLHYAFQTE--GKLYL 188
Cdd:cd14119     1 LGEGSYGKV-----KEVLDTETLcrRAVKILKKRKLRRipngEANVKREIQ--ILRRLNHRNVIKLVDVLYNEekQKLYM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGdvftrlSKEVLFTEEDVKF-------YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd14119    74 VMEYCVGG------LQEMLDSAPDKRLpiwqahgYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 --VDQEKKAYSFCGTVEYMAPEVVN--RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAE 337
Cdd:cd14119   148 dlFAEDDTCTTSQGSPAFQPPEIANgqDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPD 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 338 AQSLLRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14119   228 LQDLLRGMLEKDPEKRF---TIEQIRQHPWF 255
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
111-354 4.33e-32

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: 125.89  E-value: 4.33e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDR--VRTKMER--DILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14195     7 YEMGEELGSGQFA---IVRKCREKGTGKEYAAKFIKKRRLSSSRRgvSREEIERevNILREIQHPNIITLHDIFENKTDV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG----HIKLTDFGLSKEsV 262
Cdd:cd14195    84 VLILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGIAHK-I 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ----FLSAEA 338
Cdd:cd14195   163 EAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEeyfsNTSELA 242
                         250
                  ....*....|....*.
gi 1958807372 339 QSLLRMLFKRNPANRL 354
Cdd:cd14195   243 KDFIRRLLVKDPKKRM 258
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
464-729 5.88e-32

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: 125.67  E-value: 5.88e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKII-----DKNKRDPSEEIEIL--MRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06917     3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLnldtdDDDVSDIQKEVALLsqLKLGQPKNIIKYYGSYLKGPSLWIIMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELlDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENGL 616
Cdd:cd06917    83 YCEGGSI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTN----TGNVKLCDFGVAASLNQNSSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQ-QGYDAACDIWSLGVLLYTMLAGYTPFSNgpNDTPEEILLRIGNGRFSLSGGIWdniSRGAK 695
Cdd:cd06917   158 RSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSD--VDALRAVMLIPKSKPPRLEGNGY---SPLLK 232
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWITQREQLPR 729
Cdd:cd06917   233 EFVAACLDEEPKDRLSADELLKSKWIKQHSKTPT 266
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
109-353 6.00e-32

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 125.56  E-value: 6.00e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKvlrkaslKVRDRVRTKMERDILVEV------NHPFIVKLHYAFQT 182
Cdd:cd14046     6 TDFEELQVLGKGAFGQVVKVRNKLD---GRYYAIK-------KIKLRSESKNNSRILREVmllsrlNHQHVVRYYQAWIE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDF-----LRggDVFTRlskEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd14046    76 RANLYIQMEYcekstLR--DLIDS---GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SK------ESVDQE-KKAYSFC-----------GTVEYMAPEVVNRRG--HSQSADWWSYGVLMFEMltgTLPFQ-GKDR 316
Cdd:cd14046   151 ATsnklnvELATQDiNKSTSAAlgssgdltgnvGTALYVAPEVQSGTKstYNEKVDMYSLGIIFFEM---CYPFStGMER 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 317 NETMNMILKAKLGMPQ-FLS---AEAQSLLRMLFKRNPANR 353
Cdd:cd14046   228 VQILTALRSVSIEFPPdFDDnkhSKQAKLIRWLLNHDPAKR 268
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
470-719 6.05e-32

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: 126.75  E-value: 6.05e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYS----VCKRCIHSASNMeFAVKIIDKNK---RD---PSEEIEILMRYGqHPNIISLKEVFD-DGKyVYLVTDLM 538
Cdd:cd05582     3 LGQGSFGkvflVRKITGPDAGTL-YAMKVLKKATlkvRDrvrTKMERDILADVN-HPFIVKLHYAFQtEGK-LYLILDFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLL 618
Cdd:cd05582    80 RGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENIL-LDEDGH---IKLTDFGLSKESIDHEKKAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEIL-LRIGNGRFslsggiwdnISRGAKD 696
Cdd:cd05582   156 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFqGKDRKETMTMILkAKLGMPQF---------LSPEAQS 226
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 697 LLSHMLHMDPHQRYTA-----EQVLKHP 719
Cdd:cd05582   227 LLRALFKRNPANRLGAgpdgvEEIKRHP 254
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
115-361 1.40e-31

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: 124.34  E-value: 1.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDRVrTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14183    12 RTIGDGNFA---VVKECVERSTGREYALKIINKSKCRGKEHM-IQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFGLSKeSVDqeKKAYS 270
Cdd:cd14183    88 GGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLAT-VVD--GPLYT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQG--KDRNETMNMILKAKLGMP----QFLSAEAQSLLRM 344
Cdd:cd14183   165 VCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRGsgDDQEVLFDQILMGQVDFPspywDNVSDSAKELITM 244
                         250
                  ....*....|....*..
gi 1958807372 345 LFKRNPANRLGSEGVEE 361
Cdd:cd14183   245 MLQVDVDQRYSALQVLE 261
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
110-368 1.62e-31

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: 124.92  E-value: 1.62e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRkktGPDAGQLYAMKvlrkaslKVRDRVRTK-MERDILVEVNHPFIVKLHYAFQTEGK--- 185
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAK---LLETGEVVAIK-------KVLQDKRYKnRELQIMRRLKHPNIVKLKYFFYSSGEkkd 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 ---LYLILDFL--------RggdVFTRLSKEvlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLT 253
Cdd:cd14137    75 evyLNLVMEYMpetlyrviR---HYSKNKQT--IPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 254 DFGLSKESVDQEK-KAYsFCgTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd14137   150 DFGSAKRLVPGEPnVSY-IC-SRYYRAPElIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKV-LGTP 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 332 ---QFLS---------------------------AEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14137   227 treQIKAmnpnytefkfpqikphpwekvfpkrtpPDAIDLLSKILVYNPSKRLTA---LEALAHPFF 290
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
462-732 1.63e-31

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: 125.22  E-value: 1.63e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI--EIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd06656    19 KKYTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENGLLL 618
Cdd:cd06656    99 AGGSLTD-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFSLSGGiwDNISRGAKDL 697
Cdd:cd06656   174 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQNP--ERLSAVFRDF 248
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQP 732
Cdd:cd06656   249 LNRCLEMDVDRRGSAKELLQHPFLKLAKPLSSLTP 283
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
115-359 1.64e-31

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


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 124.75  E-value: 1.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVflvRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMErdILVEVN-HPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14173     8 EVLGEGAYARV---QTCINLITNKEYAVKIIEKRPGHSRSRVFREVE--MLYQCQgHRNVLELIEFFEEEDKFYLVFEKM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGL-------SKESVD 263
Cdd:cd14173    83 RGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLgsgiklnSDCSPI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQS-----ADWWSYGVLMFEMLTGTLPFQGK-------DRNET----MNM----I 323
Cdd:cd14173   163 STPELLTPCGSAEYMAPEVVEAFNEEASiydkrCDLWSLGVILYIMLSGYPPFVGRcgsdcgwDRGEAcpacQNMlfesI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 324 LKAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd14173   243 QEGKYEFPEkdwaHISCAAKDLISKLLVRDAKQRLSAAQV 282
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
110-370 1.93e-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: 124.61  E-value: 1.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKV------RDRVRtkmERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDK---ETGRIVAIKKIKLGERKEakdginFTALR---EIKLLQELKHPNIIGLLDVFGHK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLrggdvFTRLS-----KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07841    75 SNINLVFEFM-----ETDLEkvikdKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP------ 331
Cdd:cd07841   150 RSFGSPNRKMTHQVVTRWYRAPELLfGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEA-LGTPteenwp 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 332 ---------QF--------------LSAEAQSLLRMLFKRNPANRLgseGVEEVKRHAFFSS 370
Cdd:cd07841   229 gvtslpdyvEFkpfpptplkqifpaASDDALDLLQRLLTLNPNKRI---TARQALEHPYFSN 287
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
115-367 2.51e-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: 123.65  E-value: 2.51e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMK---VLRKASLKVRDRVRT-----KMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd06629     7 ELIGKGTYGRVYLAMNAT---TGEMLAVKqveLPKTSSDRADSRQKTvvdalKSEIDTLKDLDHPNIVQYLGFEETEDYF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD--Q 264
Cdd:cd06629    84 SIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDiyG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEA 338
Cdd:cd06629   164 NNGATSMQGSVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPvpedVNLSPEA 243
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd06629   244 LDFLNACFAIDPRDR---PTAAELLSHPF 269
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
111-367 3.38e-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: 123.05  E-value: 3.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLV--RKKTGPdagqlYAMKVL--RKASlkvRDRVRTKMERD--ILVEVNHPFIVKLHYAFQ-TE 183
Cdd:cd14164     2 YTLGTTIGEGSFSKVKLAtsQKYCCK-----VAIKIVdrRRAS---PDFVQKFLPRElsILRRVNHPNIVQMFECIEvAN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG-HIKLTDFGLSKESV 262
Cdd:cd14164    74 GRLYIVME-AAATDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFQGkdrnETMNMILKAKLGM--PQFLSAE-- 337
Cdd:cd14164   153 DYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVTGTMPFDE----TNVRRLRLQQRGVlyPSGVALEep 228
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 338 AQSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd14164   229 CRALIRTLLQFNPSTR---PSIQQVAGNSW 255
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
464-717 4.04e-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: 122.76  E-value: 4.04e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemmdaKARQDCLKEIDLLQQL-NHPNIIKYLASFIENNELNIVLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELlDRILK-----KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFAKQLR 611
Cdd:cd08224    81 LADAGDL-SRLIKhfkkqKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANV-FITANG---VVKLGDLGLGRFFS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GE----NGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTPEEILLRIGNGRFS-LSGgi 686
Cdd:cd08224   156 SKttaaHSLVGTPYY----MSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFY-GEKMNLYSLCKKIEKCEYPpLPA-- 228
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 687 wDNISRGAKDLLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd08224   229 -DLYSQELRDLVAACIQPDPEKRPDISYVLD 258
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
116-358 4.21e-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: 123.20  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKTGPDAGqlYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd14201    13 LVGHGAFAVVFKGRHRKKTDWE--VAIKSINKKNLS-KSQILLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEYCNG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG---------HIKLTDFGLSKeSVDQEK 266
Cdd:cd14201    90 GDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGFAR-YLQSNM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLR 343
Cdd:cd14201   169 MAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIpreTSPYLADLLL 248
                         250
                  ....*....|....*
gi 1958807372 344 MLFKRNPANRLGSEG 358
Cdd:cd14201   249 GLLQRNQKDRMDFEA 263
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
140-372 4.34e-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: 123.60  E-value: 4.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 140 YAMKVLRKASlkvRDRVRtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLA 218
Cdd:cd14175    29 YAVKVIDKSK---RDPSE---EIEILLRYgQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASSVLH 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 219 ELALALDHLHRLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADW 294
Cdd:cd14175   103 TICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDI 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 295 WSYGVLMFEMLTGTLPFqGKDRNETMNMILkAKLGMPQF---------LSAEAQSLLRMLFKRNPANRLGSegvEEVKRH 365
Cdd:cd14175   183 WSLGILLYTMLAGYTPF-ANGPSDTPEEIL-TRIGSGKFtlsggnwntVSDAAKDLVSKMLHVDPHQRLTA---KQVLQH 257

                  ....*..
gi 1958807372 366 AFFSSID 372
Cdd:cd14175   258 PWITQKD 264
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
110-368 4.50e-31

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: 122.85  E-value: 4.50e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrkktgpdagQLYAMKVLRKASLKVRD--RVRTKMErDILVEV------NHPFIVKLHYAFQ 181
Cdd:cd06610     2 DYELIEVIGSGATAVVY-----------AAYCLPKKEKVAIKRIDleKCQTSMD-ELRKEIqamsqcNHPNVVSYYTSFV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 TEGKLYLILDFLRGG---DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd06610    70 VGDELWLVMPLLSGGsllDIMKSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 K---ESVDQEKKA-YSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaklGMPQF 333
Cdd:cd06610   150 AslaTGGDRTRKVrKTFVGTPCWMAPEVMEQvRGYDFKADIWSFGITAIELATGAAPYSKYPPMKVLMLTLQ---NDPPS 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 334 LSAEAQS---------LLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd06610   227 LETGADYkkysksfrkMISLCLQKDPSKRPTA---EELLKHKFF 267
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
115-359 4.82e-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: 123.60  E-value: 4.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKV-FLVRKKTGPDagqlYAMKVLRKASLKVRDRVRTKMERDILVEVNHPfIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd14174     8 ELLGEGAYAKVqGCVSLQNGKE----YAVKIIEKNAGHSRSRVFREVETLYQCQGNKN-ILELIEFFEDDTRFYLVFEKL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGL-------SKESVD 263
Cdd:cd14174    83 RGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLgsgvklnSACTPI 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVV-----NRRGHSQSADWWSYGVLMFEMLTGTLPFQGK-------DRNETMNM--------I 323
Cdd:cd14174   163 TTPELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGHcgtdcgwDRGEVCRVcqnklfesI 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 324 LKAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd14174   243 QEGKYEFPDkdwsHISSEAKDLISKLLVRDAKERLSAAQV 282
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
462-732 6.16e-31

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: 123.30  E-value: 6.16e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI--EIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd06655    19 KKYTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELIinEILvMKELKNPNIVNFLDSFLVGDELFVVMEYL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENGLLL 618
Cdd:cd06655    99 AGGSLTD-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL----GMDGSVKLTDFGFCAQITPEQSKRS 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFSLSGGiwDNISRGAKDL 697
Cdd:cd06655   174 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL---NENPLRALYLIAtNGTPELQNP--EKLSPIFRDF 248
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQP 732
Cdd:cd06655   249 LNRCLEMDVEKRGSAKELLQHPFLKLAKPLSSLTP 283
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
111-368 7.86e-31

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 122.67  E-value: 7.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlrkaslkvrdRVRTKMERD-----------ILVEVNHPFIVKLH-- 177
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKK---TGELVALK-----------KIRMENEKEgfpitaireikLLQKLDHPNVVRLKei 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 ----YAFQTEGKLYLILDFLRGgDvFTRL--SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIK 251
Cdd:cd07840    67 vtskGSAKYKGSIYMVFEYMDH-D-LTGLldNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 252 LTDFGLSKESVDQEKKAY-SFCGTVEYMAPEVVnrRGHSQSA---DWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAk 327
Cdd:cd07840   145 LADFGLARPYTKENNADYtNRVITLWYRPPELL--LGATRYGpevDMWSVGCILAELFTGKPIFQGKTELEQLEKIFEL- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 328 LGMP--------------------------------QFLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07840   222 CGSPteenwpgvsdlpwfenlkpkkpykrrlrevfkNVIDPSALDLLDKLLTLDPKKRISA---DQALQHEYF 291
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
516-723 8.02e-31

Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 123.45  E-value: 8.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 516 PNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGH 595
Cdd:cd05585    54 PFIVPLKFSFQSPEKLYLVLAFINGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENIL-LDYTGH 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 596 pdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpNDTPE---EIL 672
Cdd:cd05585   133 ---IALCDFGLCKLNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLTGLPPFYD--ENTNEmyrKIL 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 673 LRigNGRFSlsggiwDNISRGAKDLLSHMLHMDPHQRY---TAEQVLKHPWITQ 723
Cdd:cd05585   208 QE--PLRFP------DGFDRDAKDLLIGLLNRDPTKRLgynGAQEIKNHPFFDQ 253
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
114-331 8.86e-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: 122.21  E-value: 8.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLK-------VRdrvrtkmERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd07829     4 LEKLGEGTYGVVYKAKDKKT---GEIVALKKIRLDNEEegipstaLR-------EISLLKELKHPNIVKLLDVIHTENKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGgDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-SVdq 264
Cdd:cd07829    74 YLVFEYCDQ-DLKKYLDKrPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAfGI-- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 265 EKKAYsfcgTVE-----YMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMP 331
Cdd:cd07829   151 PLRTY----THEvvtlwYRAPEIlLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQ-ILGTP 218
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
505-721 9.37e-31

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: 122.72  E-value: 9.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILMRyGQHPNIISLKEVF--DDGKYVYLVTDLM----KGgeLLDRilKKKCFSEQEASNVLYVITKTVEYLHSQGVV 578
Cdd:cd07843    54 EINILLK-LQHPNIVTVKEVVvgSNLDKIYMVMEYVehdlKS--LMET--MKQPFLQSEVKCLMLQLLSGVAHLHDNWIL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 579 HRDLKPSNILYmdesGHPDSIKICDFGFAKQLrGENgllLTPcYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYT 652
Cdd:cd07843   129 HRDLKTSNLLL----NNRGILKICDFGLAREY-GSP---LKP-YTQLVVtlwyrAPELLLgAKEYSTAIDMWSVGCIFAE 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 653 MLAGyTPFSNGPNDTPEeiLLRIgngrFSLSGG----IWDNISR--GAK--------------------------DLLSH 700
Cdd:cd07843   200 LLTK-KPLFPGKSEIDQ--LNKI----FKLLGTptekIWPGFSElpGAKkktftkypynqlrkkfpalslsdngfDLLNR 272
                         250       260
                  ....*....|....*....|.
gi 1958807372 701 MLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd07843   273 LLTYDPAKRISAEDALKHPYF 293
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
490-737 1.04e-30

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 123.53  E-value: 1.04e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDK----NKRDPSE---EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVL 562
Cdd:cd05604    24 YAVKVLQKkvilNRKEQKHimaERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGELFFHLQRERSFPEPRARFYA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACD 642
Cdd:cd05604   104 AEIASALGYLHSINIVYRDLKPENIL-LDSQGH---IVLTDFGLCKEGISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 643 IWSLGVLLYTMLAGYTPFSNgpNDTPE---EILLRIGNGRFSLSGGIWdnisrgakDLLSHMLHMDPHQRYTA----EQV 715
Cdd:cd05604   180 WWCLGSVLYEMLYGLPPFYC--RDTAEmyeNILHKPLVLRPGISLTAW--------SILEELLEKDRQLRLGAkedfLEI 249
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 716 LKHP------W--ITQREQLPRHQPTSDDP 737
Cdd:cd05604   250 KNHPffesinWtdLVQKKIPPPFNPNVNGP 279
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
464-721 1.10e-30

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: 123.67  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYS-VCK-RCIHSASNMEFAVK----IIDKN---KRdPSEEIEILMRYGQHPNIISL--KEVFDDGKY-- 530
Cdd:cd07857     2 YELIKELGQGAYGiVCSaRNAETSEEETVAIKkitnVFSKKilaKR-ALRELKLLRHFRGHKNITCLydMDIVFPGNFne 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGelLDRILKkkcfSEQEASNV-----LYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFG 605
Cdd:cd07857    81 LYLYEELMEAD--LHQIIR----SGQPLTDAhfqsfIYQILCGLKYIHSANVLHRDLKPGNLLVNADC----ELKICDFG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAKQL---RGENGLLLTPcYTAN--FVAPEV-LTQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPN------------DT 667
Cdd:cd07857   151 LARGFsenPGENAGFMTE-YVATrwYRAPEImLSFQSYTKAIDVWSVGCILAELLGR-KPVFKGKDyvdqlnqilqvlGT 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 668 P-EEILLRIGNGR-----FSLS-------GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd07857   229 PdEETLSRIGSPKaqnyiRSLPnipkkpfESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYL 295
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
462-732 1.20e-30

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: 122.53  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI--EIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd06654    20 KKYTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELIinEILvMRENKNPNIVNYLDSYLVGDELWVVMEYL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENGLLL 618
Cdd:cd06654   100 AGGSLTD-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL----GMDGSVKLTDFGFCAQITPEQSKRS 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFSLSGGiwDNISRGAKDL 697
Cdd:cd06654   175 TMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL---NENPLRALYLIAtNGTPELQNP--EKLSAIFRDF 249
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQP 732
Cdd:cd06654   250 LNRCLEMDVEKRGSAKELLQHQFLKIAKPLSSLTP 284
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
111-371 1.48e-30

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: 123.02  E-value: 1.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQ-----TEGK 185
Cdd:cd07834     2 YELLKPIGSGAYGVVCSAYDK---RTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRppspeEFND 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRggdvfTRL-----SKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd07834    79 VYIVTELME-----TDLhkvikSPQPL-TDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGLARG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAY--SFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP------ 331
Cdd:cd07834   153 VDPDEDKGFltEYVVTRWYRAPELLlSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEV-LGTPseedlk 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 332 QFLSAEAQSLLRMLFKR--------------------------NPANRLgseGVEEVKRHAFFSSI 371
Cdd:cd07834   232 FISSEKARNYLKSLPKKpkkplsevfpgaspeaidllekmlvfNPKKRI---TADEALAHPYLAQL 294
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
107-367 1.52e-30

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: 121.64  E-value: 1.52e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPA-QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRkaslkvrdrVRTKMERDILVEVN-------HPFIVKLHY 178
Cdd:cd06608     3 DPAgIFELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMD---------IIEDEEEEIKLEINilrkfsnHPNIATFYG 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 179 AFQT------EGKLYLILDFLRGGDVfTRLSKEVL-----FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI 247
Cdd:cd06608    71 AFIKkdppggDDQLWLVMEYCGGGSV-TDLVKGLRkkgkrLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 322
Cdd:cd06608   150 AEVKLVDFGVSAQLDSTLGRRNTFIGTPYWMAPEVIAcdqqpDASYDARCDVWSLGITAIELADGKPPLCDMHPMRALFK 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 323 ILK---AKLGMPQFLSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd06608   230 IPRnppPTLKSPEKWSKEFNDFISECLIKNYEQR---PFTEELLEHPF 274
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
465-680 1.61e-30

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 120.71  E-value: 1.61e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  465 ELKEDIGIGSY-SVCK---RCIHSASNMEFAVKII-----DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:smart00219   2 TLGKKLGEGAFgEVYKgklKGKGGKKKVEVAVKTLkedasEQQIEEFLREARIMRKL-DHPNVVKLLGVCTEEEPLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  536 DLMKGGELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQL---- 610
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPkLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV----GENLVVKISDFGLSRDLyddd 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372  611 --RGENGLLltPcytanfV---APEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNGRF 680
Cdd:smart00219 157 yyRKRGGKL--P------IrwmAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQPY---PGMSNEEVLEYLKNGYR 221
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
465-680 1.62e-30

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: 121.12  E-value: 1.62e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  465 ELKEDIGIGSY-SVCK---RCIHSASNMEFAVKII-----DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:smart00221   2 TLGKKLGEGAFgEVYKgtlKGKGDGKEVEVAVKTLkedasEQQIEEFLREARIMRKL-DHPNIVKLLGVCTEEEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  536 DLMKGGELLDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGE 613
Cdd:smart00221  81 EYMPGGDLLDYLRKNRPkeLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLV----GENLVVKISDFGLSRDLYDD 156
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372  614 NgllLTPCYTANF----VAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNGRF 680
Cdd:smart00221 157 D---YYKVKGGKLpirwMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEPY---PGMSNAEVLEYLKKGYR 222
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
94-356 1.64e-30

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 126.52  E-value: 1.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  94 PITQHVKEGYEKADPAQFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFI 173
Cdd:PTZ00283   17 PDTFAKDEATAKEQAKKYWISRVLGSGATGTVLCAKRVSD---GEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 174 VKLHYAFQTEGK--------LYLILDFLRGGD----VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPEN 241
Cdd:PTZ00283   94 VKCHEDFAKKDPrnpenvlmIALVLDYANAGDlrqeIKSRAKTNRTFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSAN 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 242 ILLDEIGHIKLTDFGLSK--ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET 319
Cdd:PTZ00283  174 ILLCSNGLVKLGDFGFSKmyAATVSDDVGRTFCGTPYYVAPEIWRRKPYSKKADMFSLGVLLYELLTLKRPFDGENMEEV 253
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 320 MNMILKAKLG-MPQFLSAEAQSLLRMLFKRNPANRLGS 356
Cdd:PTZ00283  254 MHKTLAGRYDpLPPSISPEMQEIVTALLSSDPKRRPSS 291
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
525-720 1.94e-30

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 122.81  E-value: 1.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 525 FDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDF 604
Cdd:cd05598    70 FQDKENLYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNIL-IDRDGH---IKLTDF 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 605 GFAKQLRGEN--------GLLLTPcytaNFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG 676
Cdd:cd05598   146 GLCTGFRWTHdskyylahSLVGTP----NYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQPPFL---AQTPAETQLKVI 218
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 677 NGRFSLSGGIWDNISRGAKDLLSHMLhMDPHQR---YTAEQVLKHPW 720
Cdd:cd05598   219 NWRTTLKIPHEANLSPEAKDLILRLC-CDAEDRlgrNGADEIKAHPF 264
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
115-354 3.16e-30

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 120.48  E-value: 3.16e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLR---KASLKVRDRVRTKmerdilvevNHPFIVKLHYAFQT--EGK--LY 187
Cdd:cd14172    10 QVLGLGVNGKVLECFHR---RTGQKCALKLLYdspKARREVEHHWRAS---------GGPHIVHILDVYENmhHGKrcLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKESV 262
Cdd:cd14172    78 IIMECMEGGELFSRIQErgDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 dQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMILKAKLGMPQF--------- 333
Cdd:cd14172   158 -VQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFY-SNTGQAISPGMKRRIRMGQYgfpnpewae 235
                         250       260
                  ....*....|....*....|.
gi 1958807372 334 LSAEAQSLLRMLFKRNPANRL 354
Cdd:cd14172   236 VSEEAKQLIRHLLKTDPTERM 256
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
464-728 4.71e-30

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: 120.75  E-value: 4.71e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKR-------DPSEEIEI-LMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd07841     2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERkeakdgiNFTALREIkLLQELKHPNIIGLLDVFGHKSNINLVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGelLDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLrGE 613
Cdd:cd07841    82 EFMETD--LEKVIKDKSivLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLL-IASDG---VLKLADFGLARSF-GS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTP-CYTANFVAPEVL---TQqgYDAACDIWSLGVLLYTMLAGyTPFSNGPND------------TPEE------- 670
Cdd:cd07841   155 PNRKMTHqVVTRWYRAPELLfgaRH--YGVGVDMWSVGCIFAELLLR-VPFLPGDSDidqlgkifealgTPTEenwpgvt 231
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 671 -ILLRI---------GNGRFSlsggiwdNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQR------EQLP 728
Cdd:cd07841   232 sLPDYVefkpfpptpLKQIFP-------AASDDALDLLQRLLTLNPNKRITARQALEHPYFSNDpaptppSQLP 298
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
118-353 5.41e-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: 119.54  E-value: 5.41e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 118 GQGSFGKVFLVRKKTgpdAGQLYAMKVLrkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGD 197
Cdd:cd14111    12 ARGRFGVIRRCRENA---TGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 198 VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVD----QEKKAYSfcG 273
Cdd:cd14111    86 LLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFG-SAQSFNplslRQLGRRT--G 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFKRNP 350
Cdd:cd14111   163 TLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFDAFKLypnVSQSASLFLKKVLSSYP 242

                  ...
gi 1958807372 351 ANR 353
Cdd:cd14111   243 WSR 245
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
448-729 6.95e-30

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 120.48  E-value: 6.95e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 448 LPIVQINGNAAQFSEAYelkedIGIGSYSVCKRCI--HSASNMEFAVKIIDKNKRDPSE----EIeILMRYGQHPNIISL 521
Cdd:cd06659    10 LRMVVDQGDPRQLLENY-----VKIGEGSTGVVCIarEKHSGRQVAVKMMDLRKQQRREllfnEV-VIMRDYQHPNVVEM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 522 KEVFDDGKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKI 601
Cdd:cd06659    84 YKSYLVGEELWVLMEYLQGGALTD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDG----RVKL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 602 CDFGFAKQLRGE----NGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIgn 677
Cdd:cd06659   159 SDFGFCAQISKDvpkrKSLVGTPYW----MAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYF---SDSPVQAMKRL-- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 678 gRFSLSGGIWD--NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQrEQLPR 729
Cdd:cd06659   230 -RDSPPPKLKNshKASPVLRDFLERMLVRDPQERATAQELLDHPFLLQ-TGLPE 281
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
110-368 8.18e-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: 118.88  E-value: 8.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLK----VRDRVRTKMERDILVEVN---HPFIVKLHYAFQT 182
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRD---GLPVAVKFVPKSRVTewamINGPVPVPLEIALLLKASkpgVPGVIRLLDWYER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGG-DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLTDFG---L 257
Cdd:cd14005    78 PDGFLLIMERPEPCqDLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGcgaL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVdqekkaYS-FCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFqgkdRNETmnMILKAKLGMPQFLS 335
Cdd:cd14005   158 LKDSV------YTdFDGTRVYSPPEwIRHGRYHGRPATVWSLGILLYDMLCGDIPF----ENDE--QILRGNVLFRPRLS 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 336 AEAQSLLRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14005   226 KECCDLISRCLQFDPSKRP---SLEQILSHPWF 255
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
140-382 1.07e-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: 119.73  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 140 YAMKVLRKASlkvRDrvrTKMERDILVEV-NHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLA 218
Cdd:cd14178    31 YAVKIIDKSK---RD---PSEEIEILLRYgQHPNIITLKDVYDDGKFVYLVMELMRGGELLDRILRQKCFSEREASAVLC 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 219 ELALALDHLHRLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADW 294
Cdd:cd14178   105 TITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDAACDI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 295 WSYGVLMFEMLTGTLPF-QGKDrnETMNMILkAKLGMPQF---------LSAEAQSLLRMLFKRNPANRLGSegvEEVKR 364
Cdd:cd14178   185 WSLGILLYTMLAGFTPFaNGPD--DTPEEIL-ARIGSGKYalsggnwdsISDAAKDIVSKMLHVDPHQRLTA---PQVLR 258
                         250       260
                  ....*....|....*....|.
gi 1958807372 365 HAFFSSIDW---NKLYKREVQ 382
Cdd:cd14178   259 HPWIVNREYlsqNQLSRQDVH 279
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
161-368 1.27e-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: 118.38  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 161 ERDILVEVNHPFIVKLHYAFQTEGK-LYLILDFLRGGDVFTR--LSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDL 237
Cdd:cd14109    46 EVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLASTIELVRDnlLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 238 KPENILLdEIGHIKLTDFGLSKESVDqEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd14109   126 RPEDILL-QDDKLKLADFGQSRRLLR-GKLTTLIYGSPEFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGISPFLGDNDR 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 318 ETMNMILKAKLGMP----QFLSAEAQSLLRMLFKRNPANRLgseGVEEVKRHAFF 368
Cdd:cd14109   204 ETLTNVRSGKWSFDssplGNISDDARDFIKKLLVYIPESRL---TVDEALNHPWF 255
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
470-718 1.27e-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: 118.49  E-value: 1.27e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNK-RDPSE------EIEiLMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd14189     9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRvAKPHQrekivnEIE-LHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNiLYMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd14189    88 LAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGN-FFINENME---LKVGDFGLAARLEPPEQRKKTICG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNGRFSLSGgiwdNISRGAKDLLSHML 702
Cdd:cd14189   164 TPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNPPFETL---DLKETYRCIKQVKYTLPA----SLSLPARHLLAGIL 236
                         250
                  ....*....|....*.
gi 1958807372 703 HMDPHQRYTAEQVLKH 718
Cdd:cd14189   237 KRNPGDRLTLDQILEH 252
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
111-303 1.42e-29

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: 118.68  E-value: 1.42e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQTEGKLY 187
Cdd:cd14052     2 FANVELIGSGEFSQVYKVSERVPT--GKVYAVKKLKPNYAGAKDRLRRLEEVSILRELtldGHDNIVQLIDSWEYHGHLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSKEVLFTEED---VKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS-----K 259
Cdd:cd14052    80 IQTELCENGSLDVFLSELGLLGRLDefrVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAtvwplI 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 260 ESVDQEkkaysfcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFE 303
Cdd:cd14052   160 RGIERE-------GDREYIAPEILSEHMYDKPADIFSLGLILLE 196
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
111-322 1.47e-29

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 118.14  E-value: 1.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMK---VLRKASLKVRDR-VRtkmERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd08224     2 YEIEKKIGKGQFSVVYRARCL---LDGRLVALKkvqIFEMMDAKARQDcLK---EIDLLQQLNHPNIIKYLASFIENNEL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVfTRLSKE-----VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd08224    76 NIVLELADAGDL-SRLIKHfkkqkRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFF 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 262 VDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrnETMNM 322
Cdd:cd08224   155 SSKTTAAHSLVGTPYYMSPERIREQGYDFKSDIWSLGCLLYEMAALQSPFYG----EKMNL 211
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
464-720 1.59e-29

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 120.02  E-value: 1.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYS----VCKRCIHSASNMeFAVKIIDK----NKRDPSE----EIEILMRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd05614     2 FELLKVLGTGAYGkvflVRKVSGHDANKL-YAMKVLRKaalvQKAKTVEhtrtERNVLEHVRQSPFLVTLHYAFQTDAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQ-L 610
Cdd:cd05614    81 HLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENIL-LDSEGH---VVLTDFGLSKEfL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTPCYTANFVAPEVL-TQQGYDAACDIWSLGVLLYTMLAGYTPFS-NGPNDTPEEILLRIgngrFSLSGGIWD 688
Cdd:cd05614   157 TEEKERTYSFCGTIEYMAPEIIrGKSGHGKAVDWWSLGILMFELLTGASPFTlEGEKNTQSEVSRRI----LKCDPPFPS 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQR-----YTAEQVLKHPW 720
Cdd:cd05614   233 FIGPVARDLLQKLLCKDPKKRlgagpQGAQEIKEHPF 269
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
464-720 1.63e-29

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


Pssm-ID: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 118.82  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVK-IIDKNKRDPS-----EEIEILMRYgQHPNIISLKEV------FDDGKYV 531
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKkIRMENEKEGFpitaiREIKLLQKL-DHPNVVRLKEIvtskgsAKYKGSI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLM----KGgeLLDRILKKkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFA 607
Cdd:cd07840    80 YMVFEYMdhdlTG--LLDNPEVK--FTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNIL-INNDGV---LKLADFGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQLRGENGLLLTP-CYTANFVAPEVL---TQqgYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIgngrFSLS 683
Cdd:cd07840   152 RPYTKENNADYTNrVITLWYRPPELLlgaTR--YGPEVDMWSVGCILAELFTGKPIF---QGKTELEQLEKI----FELC 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 684 GG----IWDN---------------------------ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07840   223 GSpteeNWPGvsdlpwfenlkpkkpykrrlrevfknvIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
109-357 2.10e-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: 118.35  E-value: 2.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFlvRKKTGPdAGQLYAMKVLrkaSLKVRDRVRTKMERDI-----LVEVNHPFIVKLHYAFQTE 183
Cdd:cd06917     1 SLYRRLELVGRGSYGAVY--RGYHVK-TGRVVALKVL---NLDTDDDDVSDIQKEVallsqLKLGQPKNIIKYYGSYLKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTrLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06917    75 PSLWIIMDYCEGGSIRT-LMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNR-RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKlgmPQFL-----SAE 337
Cdd:cd06917   154 NSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEMATGNPPYSDVDALRAVMLIPKSK---PPRLegngySPL 230
                         250       260
                  ....*....|....*....|
gi 1958807372 338 AQSLLRMLFKRNPANRLGSE 357
Cdd:cd06917   231 LKEFVAACLDEEPKDRLSAD 250
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
462-719 2.64e-29

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: 117.32  E-value: 2.64e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYS-VCK-RCIHSASNME-----FAVKIIDKNKRdPS---EEIEILMRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd14019     1 NKYRIIEKIGEGTFSsVYKaEDKLHDLYDRnkgrlVALKHIYPTSS-PSrilNELECLERLGGSNNVSGLITAFRNEDQV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKkkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdsIKICDFGFA---- 607
Cdd:cd14019    80 VAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGK---GVLVDFGLAqree 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 --KQLRGengllltPCY-TANFVAPEVLTQ---QGydAACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRIGngrfS 681
Cdd:cd14019   154 drPEQRA-------PRAgTRGFRAPEVLFKcphQT--TAIDIWSAGVILLSILSGRFPFFFSSDD--IDALAEIA----T 218
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 682 LSGgiWDNisrgAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14019   219 IFG--SDE----AYDLLDKLLELDPSKRITAEEALKHP 250
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
110-369 3.06e-29

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: 118.13  E-value: 3.06e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVR--------------------------DRVRTKMErd 163
Cdd:cd14200     1 QYKLQSEIGKGSYG---VVKLAYNESDDKYYAMKVLSKKKLLKQygfprrppprgskaaqgeqakplaplERVYQEIA-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 164 ILVEVNHPFIVKLHYAFQ--TEGKLYLILDFLRGGDVFtRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPEN 241
Cdd:cd14200    76 ILKKLDHVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVM-EVPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSN 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 242 ILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSA---DWWSYGVLMFEMLTGTLPFQGKDRNE 318
Cdd:cd14200   155 LLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGkalDVWAMGVTLYCFVYGKCPFIDEFILA 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 319 TMNMILKAKLGMPQ--FLSAEAQSLLRMLFKRNPANRLgseGVEEVKRHAFFS 369
Cdd:cd14200   235 LHNKIKNKPVEFPEepEISEELKDLILKMLDKNPETRI---TVPEIKVHPWVT 284
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
490-740 3.66e-29

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: 118.94  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKNKRDPSEEIEILM---------RYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRIlKKKCFSEQEAsn 560
Cdd:cd05589    27 FAIKALKKGDIIARDEVESLMcekrifetvNSARHPFLVNLFACFQTPEHVCFVMEYAAGGDLMMHI-HEDVFSEPRA-- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 561 VLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYD 638
Cdd:cd05589   104 VFYAacVVLGLQFLHEHKIVYRDLKLDNLL-LDTEGY---VKIADFGLCKEGMGFGDRTSTFCGTPEFLAPEVLTDTSYT 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 639 AACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNG-----RFslsggiwdnISRGAKDLLSHMLHMDPHQRY--- 710
Cdd:cd05589   180 RAVDWWGLGVLIYEMLVGESPF---PGDDEEEVFDSIVNDevrypRF---------LSTEAISIMRRLLRKNPERRLgas 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 711 --TAEQVLKHP--------WITQREQLPRHQPTSDDPPQV 740
Cdd:cd05589   248 erDAEDVKKQPffrnidweALLARKIKPPFVPTIKSPEDV 287
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
111-372 4.71e-29

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: 118.97  E-value: 4.71e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKV-FLVRKKTGPDagqlYAMKVLRKASlkvRDRVRtkmERDILVEV-NHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14176    21 YEVKEDIGVGSYSVCkRCIHKATNME----FAVKIIDKSK---RDPTE---EIEILLRYgQHPNIITLKDVYDDGKYVYV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQ 264
Cdd:cd14176    91 VTELMKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF-QGKDrnETMNMILkAKLGMPQF---------L 334
Cdd:cd14176   171 NGLLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYTPFaNGPD--DTPEEIL-ARIGSGKFslsggywnsV 247
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 335 SAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFFSSID 372
Cdd:cd14176   248 SDTAKDLVSKMLHVDPHQRLTA---ALVLRHPWIVHWD 282
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
464-719 5.49e-29

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 116.93  E-value: 5.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMeFAVKIIDKNKRDPSE------EIEILMRYGQHPNIISLK--EVFDDGKYVYLVt 535
Cdd:cd14131     3 YEILKQLGKGGSSKVYKVLNPKKKI-YALKRVDLEGADEQTlqsyknEIELLKKLKGSDRIIQLYdyEVTDEDDYLYMV- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 dlMKGGEL-LDRILKKKC---FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghpDSIKICDFGFAKQLR 611
Cdd:cd14131    81 --MECGEIdLATILKKKRpkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-----GRLKLIDFGIAKAIQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GE--NGLLLTPCYTANFVAPEVLTQQGYDA----------ACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLRIGNGR 679
Cdd:cd14131   154 NDttSIVRDSQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQHITN--PIAKLQAIIDPN 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 680 FSLSGGIWDNISrgAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14131   232 HEIEFPDIPNPD--LIDVMKRCLQRDPKKRPSIPELLNHP 269
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
464-720 5.59e-29

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: 117.37  E-value: 5.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYGQHPNIISLKEVFDDGKY--VYLVTD 536
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEQvnnlrEIQALRRLSPHPNILRLIEVLFDRKTgrLALVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGG--ELL-DRilkKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghpDSIKICDFGFAKqlrge 613
Cdd:cd07831    81 LMDMNlyELIkGR---KRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-----DILKLADFGSCR----- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 nGLLLTPCYTAN-----FVAPEVLTQQG-YDAACDIWSLGVLLYTMLAGYtPFSNGPND------------TPEEILL-- 673
Cdd:cd07831   148 -GIYSKPPYTEYistrwYRAPECLLTDGyYGPKMDIWAVGCVFFEILSLF-PLFPGTNEldqiakihdvlgTPDAEVLkk 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 674 ----RIGNGRFSLSGGIW-----DNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07831   226 frksRHMNYNFPSKKGTGlrkllPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
122-378 7.24e-29

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: 117.42  E-value: 7.24e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 122 FGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEV-------NHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14177     2 FTDVYELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPSEEIeilmrygQHPNIITLKDVYDDGRYVYLVTELMK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIGH---IKLTDFGLSKESVDQEKKAYS 270
Cdd:cd14177    82 GGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGLLLT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFqGKDRNETMNMILkAKLGMPQF---------LSAEAQSL 341
Cdd:cd14177   162 PCYTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLAGYTPF-ANGPNDTPEEIL-LRIGSGKFslsggnwdtVSDAAKDL 239
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 342 LRMLFKRNPANRLGSegvEEVKRHAFFSSIDWNKLYK 378
Cdd:cd14177   240 LSHMLHVDPHQRYTA---EQVLKHSWIACRDQLPHYQ 273
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
110-304 7.32e-29

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: 116.25  E-value: 7.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLrkaSLKVRDRVRT-KMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIA---TGELAAVKVI---KLEPGDDFEIiQQEISMLKECRHPNIVAYFGSYLRRDKLWI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGG---DVFTRLSKevlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd06613    75 VMEYCGGGslqDIYQVTGP---LSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSAQLTATI 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 266 KKAYSFCGTVEYMAPEV--VNRR-GHSQSADWWSYGVLMFEM 304
Cdd:cd06613   152 AKRKSFIGTPYWMAPEVaaVERKgGYDGKCDIWALGITAIEL 193
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
470-738 9.56e-29

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: 117.86  E-value: 9.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDK---NKRDPSEEI-EI-LMRYGQHPNIISLKEV--------FDDgkyVYLVTD 536
Cdd:cd07858    13 IGRGAYGIVCSAKNSETNEKVAIKKIANafdNRIDAKRTLrEIkLLRHLDHENVIAIKDImppphreaFND---VYIVYE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGelLDRILKkkcfSEQEASN-----VLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLR 611
Cdd:cd07858    90 LMDTD--LHQIIR----SSQTLSDdhcqyFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANC----DLKICDFGLARTTS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPCYTANFVAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFS---------------NGPNDTPEEILLRI 675
Cdd:cd07858   160 EKGDFMTEYVVTRWYRAPELlLNCSEYTTAIDVWSVGCIFAELLGRKPLFPgkdyvhqlklitellGSPSEEDLGFIRNE 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 676 GNGRFSLS---------GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITqreqlPRHQPtSDDPP 738
Cdd:cd07858   240 KARRYIRSlpytprqsfARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLA-----SLHDP-SDEPV 305
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
470-718 1.04e-28

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: 115.49  E-value: 1.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNK-RDPSE------EIEiLMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd14188     9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRvSKPHQrekidkEIE-LHRILHHKHVVQFYHYFEDKENIYILLEYCSRRS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNiLYMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd14188    88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGN-FFINENME---LKVGDFGLAARLEPLEHRRRTICG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggiwDNISRGAKDLLSHML 702
Cdd:cd14188   164 TPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFE---TTNLKETYRCIREARYSLP----SSLLAPAKHLIASML 236
                         250
                  ....*....|....*.
gi 1958807372 703 HMDPHQRYTAEQVLKH 718
Cdd:cd14188   237 SKNPEDRPSLDEIIRH 252
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
105-368 1.08e-28

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: 115.62  E-value: 1.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 105 KADP-AQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlrKASLKVRDRvRTKM--ERDILVEVNHPFIVKLHYAFQ 181
Cdd:cd06648     2 PGDPrSDLDNFVKIGEGSTGIVCIATDKS---TGRQVAVK---KMDLRKQQR-RELLfnEVVIMRDYQHPNIVEMYSSYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 TEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd06648    75 VGDELWVVMEFLEGG-ALTDIVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI---LKAKLGMPQFLSAEA 338
Cdd:cd06648   154 SKEVPRRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIrdnEPPKLKNLHKVSPRL 233
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 339 QSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd06648   234 RSFLDRMLVRDPAQRATA---AELLNHPFL 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
464-721 1.12e-28

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: 115.60  E-value: 1.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKII-----DKNKRDPSE-EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd08220     2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmTKEERQAALnEVKVLSML-HHPNIIEYYESFLEDKALMIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesgHPDSIKICDFGFAKQLRGE-- 613
Cdd:cd08220    81 APGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNK---KRTVVKIGDFGISKILSSKsk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 -NGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLY--TMLAGYTPFSNGPndtpeEILLRIGNGRFSlsgGIWDNI 690
Cdd:cd08220   158 aYTVVGTPCY----ISPELCEGKPYNQKSDIWALGCVLYelASLKRAFEAANLP-----ALVLKIMRGTFA---PISDRY 225
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 691 SRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08220   226 SEELRHLILSMLHLDPNKRPTLSEIMAQPII 256
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
470-720 1.32e-28

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: 117.29  E-value: 1.32e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI-------EILMR--YGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVahtigerNILVRtaLDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTP 620
Cdd:cd05586    81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENIL-LDANGH---IALCDFGLSKADLTDNKTTNTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTPEEILLRIGNGRFSLsggiwDNISRGAKDLLS 699
Cdd:cd05586   157 CGTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMCCGWSPFY-AEDTQQMYRNIAFGKVRFPK-----DVLSDEGRSFVK 230
                         250       260
                  ....*....|....*....|....*
gi 1958807372 700 HMLHMDPHQRYTA----EQVLKHPW 720
Cdd:cd05586   231 GLLNRNPKHRLGAhddaVELKEHPF 255
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
465-679 1.45e-28

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 115.29  E-value: 1.45e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSY-SVCK---RCIHSASNMEFAVKIIDKNKRDPS-----EEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:pfam07714   2 TLGEKLGEGAFgEVYKgtlKGEGENTKIKVAVKTLKEGADEEEredflEEASIMKKL-DHPNIVKLLGVCTQGEPLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKK-CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGE- 613
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLV----SENLVVKISDFGLSRDIYDDd 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 614 -----NGLLLTPCYTanfvAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNGR 679
Cdd:pfam07714 157 yyrkrGGGKLPIKWM----APESLKDGKFTSKSDVWSFGVLLWEIFTlGEQPY---PGMSNEEVLEFLEDGY 221
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
117-311 1.50e-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: 116.22  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL------YLIL 190
Cdd:cd14038     2 LGTGGFGNVLRWINQ---ETGEQVAIKQCRQ-ELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLapndlpLLAM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDV---FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDE----IGHiKLTDFGLSKEsVD 263
Cdd:cd14038    78 EYCQGGDLrkyLNQFENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQgeqrLIH-KIIDLGYAKE-LD 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14038   156 QGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
464-721 1.52e-28

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: 115.29  E-value: 1.52e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd08218     2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEreesrkEVAVLSKM-KHPNIVQYQESFEENGNLYIVMDY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFAKQLRGENG 615
Cdd:cd08218    81 CDGGDLYKRINAQRgvLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNI-FLTKDG---IIKLGDFGIARVLNSTVE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNGRFSlsgGIWDNISRGAK 695
Cdd:cd08218   157 LARTCIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFEAG---NMKNLVLKIIRGSYP---PVPSRYSYDLR 230
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08218   231 SLVSQLFKRNPRDRPSINSILEKPFI 256
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
111-365 1.83e-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: 1.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVflvrkktgpdaGQLYAMKVLRKASLKVRDR-------VRTKMERD--ILVEVNHPFIVKLHYAFQ 181
Cdd:cd14163     2 YQLGKTIGEGTYSKV-----------KEAFSKKHQRKVAIKIIDKsggpeefIQRFLPRElqIVERLDHKNIIHVYEMLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 -TEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIgHIKLTDFGLSKE 260
Cdd:cd14163    71 sADGKIYLVMELAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 -SVDQEKKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFqgkDRNETMNMILKAKLG--MPQFL-- 334
Cdd:cd14163   150 lPKGGRELSQTFCGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVMLCAQLPF---DDTDIPKMLCQQQKGvsLPGHLgv 226
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 335 SAEAQSLLRMLFKRNPANRlgsEGVEEVKRH 365
Cdd:cd14163   227 SRTCQDLLKRLLEPDMVLR---PSIEEVSWH 254
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
452-738 2.46e-28

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 117.06  E-value: 2.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 452 QINGNAAQFSEAYELKEDIGIGSY-SVCkrcihSASNMEFAVKIIDKNKRDPSEEI--------EI-LMRYGQHPNIISL 521
Cdd:cd07877     7 ELNKTIWEVPERYQNLSPVGSGAYgSVC-----AAFDTKTGLRVAVKKLSRPFQSIihakrtyrELrLLKHMKHENVIGL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 522 KEVFDDGKY------VYLVTDLMkgGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESgh 595
Cdd:cd07877    82 LDVFTPARSleefndVYLVTHLM--GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDC-- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 596 pdSIKICDFGFAKQLRGE-NGLLLTPCYTanfvAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN-DTPEEIL 672
Cdd:cd07877   158 --ELKILDFGLARHTDDEmTGYVATRWYR----APEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHiDQLKLIL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 673 LRIGNGRFSLSGGIWDNISRG-----------------------AKDLLSHMLHMDPHQRYTAEQVLKHPWITQreqlpR 729
Cdd:cd07877   232 RLVGTPGAELLKKISSESARNyiqsltqmpkmnfanvfiganplAVDLLEKMLVLDSDKRITAAQALAHAYFAQ-----Y 306

                  ....*....
gi 1958807372 730 HQPtsDDPP 738
Cdd:cd07877   307 HDP--DDEP 313
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
103-353 2.71e-28

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: 114.44  E-value: 2.71e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKadpaqfdlLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQT 182
Cdd:cd08220     2 YEK--------IRVVGRGAYGTVYLCRRK---DDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLS--KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHI-KLTDFGLSK 259
Cdd:cd08220    71 DKALMIVMEYAPGGTLFEYIQqrKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 EsVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLG-MPQFLSAEA 338
Cdd:cd08220   151 I-LSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEEL 229
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd08220   230 RHLILSMLHLDPNKR 244
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
490-738 2.72e-28

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: 116.16  E-value: 2.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKN---KRDPSE----EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVL 562
Cdd:cd05590    23 YAVKVLKKDvilQDDDVEctmtEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACD 642
Cdd:cd05590   103 AEITSALMFLHDKGIIYRDLKLDNVL-LDHEGH---CKLADFGMCKEGIFNGKTTSTFCGTPDYIAPEILQEMLYGPSVD 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 643 IWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGgiWdnISRGAKDLLSHMLHMDPHQRYTA------EQVL 716
Cdd:cd05590   179 WWAMGVLLYEMLCGHAPFE---AENEDDLFEAILNDEVVYPT--W--LSQDAVDILKAFMTKNPTMRLGSltlggeEAIL 251
                         250       260
                  ....*....|....*....|....
gi 1958807372 717 KHPWITQR--EQLPRHQPTsddPP 738
Cdd:cd05590   252 RHPFFKELdwEKLNRRQIE---PP 272
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
470-722 3.18e-28

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: 114.45  E-value: 3.18e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVC--KRCIHSASNMefAVKIIDKNKRDPSE----------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd06630     8 LGTGAFSSCyqARDVKTGTLM--AVKQVSFCRNSSSEqeevveaireEIRMMARL-NHPNIVRMLGATQHKSHFNIFVEW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdSIKICDFGFAKQLR------ 611
Cdd:cd06630    85 MAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLL-VDSTGQ--RLRIADFGAAARLAskgtga 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GE-NGLLLTpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSggIWDNI 690
Cdd:cd06630   162 GEfQGQLLG---TIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPP--IPEHL 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 691 SRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd06630   237 SPGLRDVTLRCLELQPEDRPPARELLKHPVFT 268
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
117-365 3.39e-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: 115.25  E-value: 3.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVL---RKASLKVRDRVRTKmerdilvevNHPFIVKLHYAFQTE---------- 183
Cdd:cd14171    14 LGTGISGPVRVCVKK---STGERFALKILldrPKARTEVRLHMMCS---------GHPNIVQIYDVYANSvqfpgesspr 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLSKE 260
Cdd:cd14171    82 ARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdnSEDAPIKLCDFGFAKV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SvDQEKKAYSFcgTVEYMAPEVV--------NRRG---------HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM--N 321
Cdd:cd14171   162 D-QGDLMTPQF--TPYYVAPQVLeaqrrhrkERSGiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTItkD 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 322 M---ILKAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLgseGVEEVKRH 365
Cdd:cd14171   239 MkrkIMTGSYEFPEeewsQISEMAKDIVRKLLCVDPEERM---TIEEVLHH 286
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
483-722 6.26e-28

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: 114.04  E-value: 6.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 483 HSASNMEFAVKIIDKNK---RDPSEEIEI---LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE---LLDRI------ 547
Cdd:cd05609    21 HRETRQRFAMKKINKQNlilRNQIQQVFVerdILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDcatLLKNIgplpvd 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 548 LKKKCFSEqeasNVLyvitkTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQlrgenGLL-LTP------ 620
Cdd:cd05609   101 MARMYFAE----TVL-----ALEYLHSYGIVHRDLKPDNLL-ITSMGH---IKLTDFGLSKI-----GLMsLTTnlyegh 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 -------------CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIw 687
Cdd:cd05609   163 iekdtrefldkqvCGTPEYIAPEVILRQGYGKPVDWWAMGIILYEFLVGCVPFF---GDTPEELFGQVISDEIEWPEGD- 238
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 688 DNISRGAKDLLSHMLHMDPHQRY---TAEQVLKHPWIT 722
Cdd:cd05609   239 DALPDDAQDLITRLLQQNPLERLgtgGAEEVKQHPFFQ 276
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
491-726 7.42e-28

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: 116.28  E-value: 7.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKN---KRDP----SEEIEILMRyGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLY 563
Cdd:cd05600    40 ALKIMKKKvlfKLNEvnhvLTERDILTT-TNSPWLVKLLYAFQDPENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 564 VITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK----------------QLRGENGLLLTPCYTAN-- 625
Cdd:cd05600   119 EMFAAISSLHQLGYIHRDLKPENFL-IDSSGH---IKLTDFGLASgtlspkkiesmkirleEVKNTAFLELTAKERRNiy 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 626 -------------------FVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGI 686
Cdd:cd05600   195 ramrkedqnyansvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLVGFPPFS---GSTPNETWANLYHWKKTLQRPV 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 687 WD------NISRGAKDLLSHMLhMDPHQRYTA-EQVLKHP------WITQREQ 726
Cdd:cd05600   272 YTdpdlefNLSDEAWDLITKLI-TDPQDRLQSpEQIKNHPffknidWDRLREG 323
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
464-721 7.76e-28

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: 113.17  E-value: 7.76e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSY-SVCK-RCIHSASNMefAVKIIdknKRDPSEEIEIL------MRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd06613     2 YELIQRIGSGTYgDVYKaRNIATGELA--AVKVI---KLEPGDDFEIIqqeismLKECRHPNIVAYFGSYLRRDKLWIVM 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENG 615
Cdd:cd06613    77 EYCGGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANIL-LTEDGD---VKLADFGVSAQLTATIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQ---GYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRF---SLSG-GIWd 688
Cdd:cd06613   153 KRKSFIGTPYWMAPEVAAVErkgGYDGKCDIWALGITAIELAELQPPMF---DLHPMRALFLIPKSNFdppKLKDkEKW- 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 689 niSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06613   229 --SPDFHDFIKKCLTKNPKKRPTATKLLQHPFV 259
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
470-720 8.59e-28

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: 113.19  E-value: 8.59e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNK---RDPSEEIEILMRYGQHPNIISLKEVF--DDGKYVYlVTDLMKGGELL 544
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPStklKDFLREYNISLELSVHPHIIKTYDVAfeTEDYYVF-AQEYAPYGDLF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsgHPDSIKICDFGFAkqlRGENGLLLTPCYTA 624
Cdd:cd13987    80 SIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDK--DCRRVKLCDFGLT---RRVGSTVKRVSGTI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 625 NFVAPEVLT---QQGY--DAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLL 698
Cdd:cd13987   155 PYTAPEVCEakkNEGFvvDPSIDVWAFGVLLFCCLTGNFPWeKADSDDQFYEEFVRWQKRKNTAVPSQWRRFTPKALRMF 234
                         250       260
                  ....*....|....*....|....*
gi 1958807372 699 SHMLHMDPHQRYTAEQV---LKHPW 720
Cdd:cd13987   235 KKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
470-721 9.29e-28

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: 112.83  E-value: 9.29e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKI--IDKNKRDPSEEI-----EI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd06625     8 LGQGAFGQVYLCYDADTGRELAVKQveIDPINTEASKEVkalecEIqLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQL---RGENGlLL 618
Cdd:cd06625    88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANIL-RDSNG---NVKLGDFGASKRLqtiCSSTG-MK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIG--NGRFSLSggiwDNISRGAKD 696
Cdd:cd06625   163 SVTGTPYWMSPEVINGEGYGRKADIWSVGCTVVEMLTTKPPWAEF---EPMAAIFKIAtqPTNPQLP----PHVSEDARD 235
                         250       260
                  ....*....|....*....|....*
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06625   236 FLSLIFVRNKKQRPSAEELLSHSFV 260
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
470-722 9.33e-28

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: 115.18  E-value: 9.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI------EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd05593    23 LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahtlteSRVLKNTRHPFLTSLKYSFQTKDRLCFVMEYVNGGEL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYT 623
Cdd:cd05593   103 FFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLM-LDKDGH---IKITDFGLCKEGITDAATMKTFCGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 624 ANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLrIGNGRFSLSggiwdnISRGAKDLLSHMLH 703
Cdd:cd05593   179 PEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEDIKFPRT------LSADAKSLLSGLLI 251
                         250       260
                  ....*....|....*....|....
gi 1958807372 704 MDPHQRY-----TAEQVLKHPWIT 722
Cdd:cd05593   252 KDPNKRLgggpdDAKEIMRHSFFT 275
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
443-732 9.54e-28

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 115.31  E-value: 9.54e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 443 TSSNVLPIVQINGNAAQFSEaYELKEDIGIGSYSVCKRCIHSASNMEFAVKII-----DKNKRDPSEEIEILmRYGQHPN 517
Cdd:PLN00034   56 SSSSSSASGSAPSAAKSLSE-LERVNRIGSGAGGTVYKVIHRPTGRLYALKVIygnheDTVRRQICREIEIL-RDVNHPN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 518 IISLKEVFDDGKYVYLVTDLMKGGELLDRilkkKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdESGHpd 597
Cdd:PLN00034  134 VVKCHDMFDHNGEIQVLLEFMDGGSLEGT----HIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLI--NSAK-- 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 598 SIKICDFGFAKQLrgenGLLLTPCY----TANFVAPEV----LTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNGPNDTP 668
Cdd:PLN00034  206 NVKIADFGVSRIL----AQTMDPCNssvgTIAYMSPERintdLNHGAYDGyAGDIWSLGVSILEFYLGRFPFGVGRQGDW 281
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 669 EEILLRIGngrFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLPRHQP 732
Cdd:PLN00034  282 ASLMCAIC---MSQPPEAPATASREFRHFISCCLQREPAKRWSAMQLLQHPFILRAQPGQGQGG 342
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
464-709 1.09e-27

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 112.98  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSY-SVCKRCIHSASNMEFAVKII--------------DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDG 528
Cdd:cd08528     2 YAVLELLGSGAFgCVYKVRKKSNGQTLLALKEInmtnpafgrteqerDKSVGDIISEVNIIKEQLRHPNIVRYYKTFLEN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 KYVYLVTDLMKGGELLDRI--LKKKC--FSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILYmdesGHPDSIKICD 603
Cdd:cd08528    82 DRLYIVMELIEGAPLGEHFssLKEKNehFTEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIML----GEDDKVTITD 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 604 FGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFS-L 682
Cdd:cd08528   158 FGLAKQKGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQPPFY---STNMLTLATKIVEAEYEpL 234
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 683 SGGIWdniSRGAKDLLSHMLHMDPHQR 709
Cdd:cd08528   235 PEGMY---SDDITFVIRSCLTPDPEAR 258
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
462-720 1.24e-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: 113.24  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPVikkialREIRMLKQL-KHPNLVNLIEVFRRKRKLHLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGEL--LDRILKKkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLRGE 613
Cdd:cd07847    80 EYCDHTVLneLEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQ----GQIKLCDFGFARILTGP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCYTANFVAPEVL---TQqgYDAACDIWSLGVLLYTMLAGyTPFSNGPNDTPEEILLRIGNGR--------FSL 682
Cdd:cd07847   154 GDDYTDYVATRWYRAPELLvgdTQ--YGPPVDVWAIGCVFAELLTG-QPLWPGKSDVDQLYLIRKTLGDliprhqqiFST 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 683 SG---GI--------------WDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07847   231 NQffkGLsipepetrepleskFPNISSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
461-720 1.28e-27

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 116.26  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPS----EEIEIlMRYGQHPNIISLKEVFDDGKYVYL 533
Cdd:cd05622    72 AEDYEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFemiKRSDSaffwEERDI-MAFANSPWVVQLFYAFQDDRYLYM 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGE 613
Cdd:cd05622   151 VMEYMPGGDLVN-LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNML-LDKSGH---LKLADFGTCMKMNKE 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NgllLTPCYTA----NFVAPEVLTQQG----YDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGG 685
Cdd:cd05622   226 G---MVRCDTAvgtpDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEMLVGDTPFY---ADSLVGTYSKIMNHKNSLTFP 299
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 686 IWDNISRGAKDLLSHMLHMDPHQ--RYTAEQVLKHPW 720
Cdd:cd05622   300 DDNDISKEAKNLICAFLTDREVRlgRNGVEEIKRHLF 336
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
109-317 1.29e-27

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 112.81  E-value: 1.29e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVF-----LVRKKTGPDAGQLYAMkvlrkasLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd08228     2 ANFQIEKKIGRGQFSEVYratclLDRKPVALKKVQIFEM-------MDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIED 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRL----SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd08228    75 NELNIVLELADAGDLSQMIkyfkKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd08228   155 FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMN 212
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
470-721 1.33e-27

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: 113.59  E-value: 1.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI---EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDR 546
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQRRELLfneVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 547 ILKKKCFSEQEASNVLYVItKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLLLTPCYTANF 626
Cdd:cd06658   110 VTHTRMNEEQIATVCLSVL-RALSYLHNQGVIHRDIKSDSILLTSDG----RIKLSDFGFCAQVSKEVPKRKSLVGTPYW 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 627 VAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIgngRFSLSGGIWD--NISRGAKDLLSHMLHM 704
Cdd:cd06658   185 MAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEP---PLQAMRRI---RDNLPPRVKDshKVSSVLRGFLDLMLVR 258
                         250
                  ....*....|....*..
gi 1958807372 705 DPHQRYTAEQVLKHPWI 721
Cdd:cd06658   259 EPSQRATAQELLQHPFL 275
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
485-709 1.34e-27

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: 114.02  E-value: 1.34e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 485 ASNMEFAVKIIDKN---KRDPSE----EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQE 557
Cdd:cd05592    18 GTNQYFAIKALKKDvvlEDDDVEctmiERRVLALASQHPFLTHLFCTFQTESHLFFVMEYLNGGDLMFHIQQSGRFDEDR 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 558 ASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK-QLRGENgLLLTPCYTANFVAPEVLTQQG 636
Cdd:cd05592    98 ARFYGAEIICGLQFLHSRGIIYRDLKLDNVL-LDREGH---IKIADFGMCKeNIYGEN-KASTFCGTPDYIAPEILKGQK 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 637 YDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSggIWdnISRGAKDLLSHMLHMDPHQR 709
Cdd:cd05592   173 YNQSVDWWSFGVLLYEMLIGQSPFH---GEDEDELFWSICNDTPHYP--RW--LTKEAASCLSLLLERNPEKR 238
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
470-709 1.36e-27

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: 113.31  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVK-------IIDKNKRDPSEEIEILMRYgQHPNIISLKEVfDDGKYVYLVTDL----M 538
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKkcrqelsPSDKNRERWCLEVQIMKKL-NHPNVVSARDV-PPELEKLSPNDLpllaM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 K---GGEL---LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpDSI-KICDFGFAKQLr 611
Cdd:cd13989    79 EycsGGDLrkvLNQPENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGG--RVIyKLIDLGYAKEL- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 gENGLLLTPCY-TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngPNDTPEEILLRI--------------- 675
Cdd:cd13989   156 -DQGSLCTSFVgTLQYLAPELFESKKYTCTVDYWSFGTLAFECITGYRPFL--PNWQPVQWHGKVkqkkpehicayedlt 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 676 GNGRFS--------LSGGIWDNISRgakdLLSHMLHMDPHQR 709
Cdd:cd13989   233 GEVKFSselpspnhLSSILKEYLES----WLQLMLRWDPRQR 270
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
109-354 1.79e-27

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 114.54  E-value: 1.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASlkvRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 186
Cdd:PLN00034   74 SELERVNRIGSGAGGTVYKVIHRP---TGRLYALKVIYGNH---EDTVRRQICREIeiLRDVNHPNVVKCHDMFDHNGEI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDV-FTRLSKEVlfteedvkfYLAELAL----ALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:PLN00034  148 QVLLEFMDGGSLeGTHIADEQ---------FLADVARqilsGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKAYSFCGTVEYMAPEVVNR-----RGHSQSADWWSYGVLMFEMLTGTLPF----QGkDRNETMNMI-LKAKLGMP 331
Cdd:PLN00034  219 AQTMDPCNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQG-DWASLMCAIcMSQPPEAP 297
                         250       260
                  ....*....|....*....|...
gi 1958807372 332 QFLSAEAQSLLRMLFKRNPANRL 354
Cdd:PLN00034  298 ATASREFRHFISCCLQREPAKRW 320
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
116-315 1.89e-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: 112.10  E-value: 1.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLR----KASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd14061     1 VIGVGGFGKVYRGIWR-----GEEVAVKAARqdpdEDISVTLENVRQ--EARLFWMLRHPNIIALRGVCLQPPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSK-----EVLFTeedvkfYLAELALALDHLHRLG---IVYRDLKPENILLDE-IGH-------IKLTDF 255
Cdd:cd14061    74 YARGGALNRVLAGrkippHVLVD------WAIQIARGMNYLHNEApvpIIHRDLKSSNILILEaIENedlenktLKITDF 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 256 GLSKESVDQEKkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD 315
Cdd:cd14061   148 GLAREWHKTTR--MSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKGID 205
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
110-311 1.99e-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: 112.43  E-value: 1.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMK-VLRKASLKVRDRvrTKMERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14088     2 RYDLGQVIKTEEFCEIFRAKDKT---TGKLYTCKkFLKRDGRKVRKA--AKNEINILKMVKHPNILQLVDVFETRKEYFI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIGHIK--LTDFGLSKESVDQE 265
Cdd:cd14088    77 FLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVyYNRLKNSKivISDFHLAKLENGLI 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 266 KKAysfCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14088   157 KEP---CGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSGNPPF 199
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
452-739 2.05e-27

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: 114.38  E-value: 2.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 452 QINGNAAQFSEAYELKEDIGIGSY-SVCKrCIHSASNMEFAVKIIDK------NKRDPSEEIEiLMRYGQHPNIISLKEV 524
Cdd:cd07878     5 ELNKTVWEVPERYQNLTPVGSGAYgSVCS-AYDTRLRQKVAVKKLSRpfqsliHARRTYRELR-LLKHMKHENVIGLLDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 525 F------DDGKYVYLVTDLMkgGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdS 598
Cdd:cd07878    83 FtpatsiENFNEVYLVTNLM--GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDC----E 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 599 IKICDFGFAKQLRGE-NGLLLTPCYTanfvAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpND---------- 666
Cdd:cd07878   157 LRILDFGLARQADDEmTGYVATRWYR----APEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPG--NDyidqlkrime 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 667 ---TPE-EILLRIGNGRFS--------LSGGIWDNISRGAK----DLLSHMLHMDPHQRYTAEQVLKHPWITQreqlpRH 730
Cdd:cd07878   231 vvgTPSpEVLKKISSEHARkyiqslphMPQQDLKKIFRGANplaiDLLEKMLVLDSDKRISASEALAHPYFSQ-----YH 305

                  ....*....
gi 1958807372 731 QPtsDDPPQ 739
Cdd:cd07878   306 DP--EDEPE 312
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
117-353 2.20e-27

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: 111.43  E-value: 2.20e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLvrkktGPDAGQLYAMKvlrkaslKVRDRVRTKMERdiLVEVNHPFIVKLHyAFQTEGKLYLIL-DFLRG 195
Cdd:cd14059     1 LGSGAQGAVFL-----GKFRGEEVAVK-------KVRDEKETDIKH--LRKLNHPNIIKFK-GVCTQAPCYCILmEYCPY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAySFCGTV 275
Cdd:cd14059    66 GQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKM-SFAGTV 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 276 EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETM-----NMIlkaKLGMPQFLSAEAQSLLRMLFKRNP 350
Cdd:cd14059   145 AWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIwgvgsNSL---QLPVPSTCPDGFKLLMKQCWNSKP 221

                  ...
gi 1958807372 351 ANR 353
Cdd:cd14059   222 RNR 224
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
114-311 2.41e-27

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 112.52  E-value: 2.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASlkvrdrvRTKMERDILVEVN------HPFIVKLHYAF--QTEGK 185
Cdd:cd06621     6 LSSLGEGAGGSVTKCRLRNT---KTIFALKTITTDP-------NPDVQKQILRELEinkscaSPYIVKYYGAFldEQDSS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVfTRLSKEVLF----TEEDVKFYLAELAL-ALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd06621    76 IGIAMEYCEGGSL-DSIYKKVKKkggrIGEKVLGKIAESVLkGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGE 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 261 SVdqEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd06621   155 LV--NSLAGTFTGTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPF 203
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
480-721 2.60e-27

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 112.52  E-value: 2.60e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 480 RCIHSASNMEFAVKIIdknKRDPSEEI--EIL-----MRYGQHPNIISLKEVFDDGK--YVYLVTDLMKGGELlDRILKK 550
Cdd:cd06621    19 KCRLRNTKTIFALKTI---TTDPNPDVqkQILreleiNKSCASPYIVKYYGAFLDEQdsSIGIAMEYCEGGSL-DSIYKK 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 551 ------KCfSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLrgENGLLLTPCYTA 624
Cdd:cd06621    95 vkkkggRI-GEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNIL-LTRKG---QVKLCDFGVSGEL--VNSLAGTFTGTS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 625 NFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF--SNGPNDTPEEILLRIGNGR-FSLSGGIWDNI--SRGAKDLLS 699
Cdd:cd06621   168 YYMAPERIQGGPYSITSDVWSLGLTLLEVAQNRFPFppEGEPPLGPIELLSYIVNMPnPELKDEPENGIkwSESFKDFIE 247
                         250       260
                  ....*....|....*....|..
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06621   248 KCLEKDGTRRPGPWQMLAHPWI 269
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
464-721 2.71e-27

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: 111.73  E-value: 2.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKED-----IGIGSYSVckrcIHSASNMEFAVKIIDKN--KRDPS------EEIEiLMRYGQHPNIISLKEVFDDGKY 530
Cdd:cd06624     5 YEYDESgervvLGKGTFGV----VYAARDLSTQVRIAIKEipERDSRevqplhEEIA-LHSRLSHKNIVQYLGSVSEDGF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGELLDrILKKKC--FSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdSIKICDFGF 606
Cdd:cd06624    80 FKIFMEQVPGGSLSA-LLRSKWgpLKDNENTIGYYTkqILEGLKYLHDNKIVHRDIKGDNVLVNTYSG---VVKISDFGT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLRGENGLLLTPCYTANFVAPEVLT--QQGYDAACDIWSLGVLLYTMLAGYTPFSN-GPndtPEEILLRIgnGRFSLS 683
Cdd:cd06624   156 SKRLAGINPCTETFTGTLQYMAPEVIDkgQRGYGPPADIWSLGCTIIEMATGKPPFIElGE---PQAAMFKV--GMFKIH 230
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 684 GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06624   231 PEIPESLSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
117-327 3.43e-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: 112.97  E-value: 3.43e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKAS----LKVRDRvrtkmERDILVEVNHPFIVKLhYAFQTE----GKLy 187
Cdd:cd13988     1 LGQGATANVFRGRhKKTG----DLYAVKVFNNLSfmrpLDVQMR-----EFEVLKKLNHKNIVKL-FAIEEElttrHKV- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRL---SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL--LDEIGH--IKLTDFGLSKE 260
Cdd:cd13988    70 LVMELCPCGSLYTVLeepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAARE 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 261 SVDQEKKAySFCGTVEYMAPEVVNR---RGHSQ-----SADWWSYGVLMFEMLTGTLPFQ---GKDRN-ETMNMILKAK 327
Cdd:cd13988   150 LEDDEQFV-SLYGTEEYLHPDMYERavlRKDHQkkygaTVDLWSIGVTFYHAATGSLPFRpfeGPRRNkEVMYKIITGK 227
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
464-720 3.49e-27

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 111.17  E-value: 3.49e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-----------RDPSEeIEILMR--YGQHPNIISLKEVFD--DG 528
Cdd:cd14005     2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewamingpvPVPLE-IALLLKasKPGVPGVIRLLDWYErpDG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 -----KYVYLVTDLmkggelLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdSIKICD 603
Cdd:cd14005    81 fllimERPEPCQDL------FDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTG---EVKLID 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 604 FGFAKQLRgeNGLLLTPCYTANFVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNgpndtPEEILLRIGNgrfsl 682
Cdd:cd14005   152 FGCGALLK--DSVYTDFDGTRVYSPPEWIRHGRYHGrPATVWSLGILLYDMLCGDIPFEN-----DEQILRGNVL----- 219
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 683 sggIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14005   220 ---FRPRLSKECCDLISRCLQFDPSKRPSLEQILSHPW 254
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
110-367 3.61e-27

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: 111.98  E-value: 3.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLkVRD--------------------RVRTKMER-----DI 164
Cdd:cd14199     3 QYKLKDEIGKGSYGVVKLAYNE---DDNTYYAMKVLSKKKL-MRQagfprrppprgaraapegctQPRGPIERvyqeiAI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 165 LVEVNHPFIVKLHYAFQ--TEGKLYLILDFLRGGDVFtRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENI 242
Cdd:cd14199    79 LKKLDHPNVVKLVEVLDdpSEDHLYMVFELVKQGPVM-EVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 243 LLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVN--RRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNET 319
Cdd:cd14199   158 LVGEDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMAPETLSetRKIFSgKALDVWAMGVTLYCFVFGQCPFMDERILSL 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 320 MNMILKAKLGMPQF--LSAEAQSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14199   238 HSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI---SVPEIKLHPW 284
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
464-720 3.76e-27

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: 111.98  E-value: 3.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdknkRDPSEEI--------EI-LMR---YGQHPNIISLKEVFDdGKYV 531
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV----RVPLSEEgiplstirEIaLLKqleSFEHPNVVRLLDVCH-GPRT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILK---KKC----FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDF 604
Cdd:cd07838    76 DRELKLTLVFEHVDQDLAtylDKCpkpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNIL-VTSDGQ---VKLADF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 605 GFAKQLrgENGLLLTPCY-TANFVAPEVLTQQGYDAACDIWSLGVLLYTMlAGYTPFSNGPNDT---------------- 667
Cdd:cd07838   152 GLARIY--SFEMALTSVVvTLWYRAPEVLLQSSYATPVDMWSVGCIFAEL-FNRRPLFRGSSEAdqlgkifdviglpsee 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 668 --PEEILLRIGNGRFSLSGGIWD---NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07838   229 ewPRNSALPRSSFPSYTPRPFKSfvpEIDEEGLDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
464-719 4.17e-27

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: 110.96  E-value: 4.17e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDisrmsrKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKGKLNIVMEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTV--EYLHSQGVVHRDLKPSNIlYMDESghpDSIKICDFGFAKQLRGENG 615
Cdd:cd08529    81 AENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLglSHLHSKKILHRDIKSMNI-FLDKG---DNVKIGDLGVAKILSDTTN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWdniSRGAK 695
Cdd:cd08529   157 FAQTIVGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHPFE---AQNQGALILKIVRGKYPPISASY---SQDLS 230
                         250       260
                  ....*....|....*....|....
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd08529   231 QLIDSCLTKDYRQRPDTTELLRNP 254
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
480-721 5.27e-27

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


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 110.21  E-value: 5.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 480 RCIHSASNMEFAVKIIdkNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDlMKGGELLDRILKKKCFSEQEAS 559
Cdd:cd13976    11 RCVDIHTGEELVCKVV--PVPECHAVLRAYFRLPSHPNISGVHEVIAGETKAYVFFE-RDHGDLHSYVRSRKRLREPEAA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 NVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDSIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVL-TQQGYD 638
Cdd:cd13976    88 RLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEE--RTKLRLESLEDAVILEGEDDSLSDKHGCPAYVSPEILnSGATYS 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 639 A-ACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNGRFSLSGGiwdnISRGAKDLLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd13976   166 GkAADVWSLGVILYTMLVGRYPFHDS---EPASLFAKIRRGQFAIPET----LSPRARCLIRSLLRREPSERLTAEDILL 238

                  ....
gi 1958807372 718 HPWI 721
Cdd:cd13976   239 HPWL 242
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
490-672 6.73e-27

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: 112.20  E-value: 6.73e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVL 562
Cdd:cd05591    23 YAIKVLKKDVILQDDDVDctmtekrILALAAKHPFLTALHSCFQTKDRLFFVMEYVNGGDLMFQIQRARKFDEPRARFYA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACD 642
Cdd:cd05591   103 AEVTLALMFLHRHGVIYRDLKLDNIL-LDAEGH---CKLADFGMCKEGILNGKTTTTFCGTPDYIAPEILQELEYGPSVD 178
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958807372 643 IWSLGVLLYTMLAGYTPF-SNGPNDTPEEIL 672
Cdd:cd05591   179 WWALGVLMYEMMAGQPPFeADNEDDLFESIL 209
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
117-353 6.79e-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: 110.45  E-value: 6.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKvRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14113    15 LGRGRFS---VVKKCDQRGTKRAVATKFVNKKLMK-RDQV--THELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGlskESVDQEKKAY--SF 271
Cdd:cd14113    89 RLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFG---DAVQLNTTYYihQL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 272 CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLLRMLFK 347
Cdd:cd14113   166 LGSPEFAAPEIILGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPddyfKGVSQKAKDFVCFLLQ 245

                  ....*.
gi 1958807372 348 RNPANR 353
Cdd:cd14113   246 MDPAKR 251
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
464-721 7.33e-27

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: 110.43  E-value: 7.33e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSY---------SVCKRCIHSASNMEfavKIIDKNKRDPSEEIeILMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd08225     2 YEIIKKIGEGSFgkiylakakSDSEHCVIKEIDLT---KMPVKEKEASKKEV-ILLAKMKHPNIVTFFASFQENGRLFIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGHpdSIKICDFGFAKQLRG 612
Cdd:cd08225    78 MEYCDGGDLMKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI-FLSKNGM--VAKLGDFGIARQLND 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSlsgGIWDNISR 692
Cdd:cd08225   155 SMELAYTCVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLKHPFE---GNNLHQLVLKICQGYFA---PISPNFSR 228
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08225   229 DLRSLISQLFKVSPRDRPSITSILKRPFL 257
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
111-353 7.50e-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: 110.09  E-value: 7.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKvlrkaslKVRDRVRTKMER-DILVEVN-------HPFIVKLHYAFQT 182
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSR---EDGKLYAVK-------RSRSRFRGEKDRkRKLEEVErheklgeHPNCVRFIKAWEE 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsV 262
Cdd:cd14050    73 KGILYIQTE-LCDTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVE-L 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNrrGH-SQSADWWSYGVLMFEMLTGT-LPFQGKDRNETMNMILKAKLGMPqfLSAEAQS 340
Cdd:cd14050   151 DKEDIHDAQEGDPRYMAPELLQ--GSfTKAADIFSLGITILELACNLeLPSGGDGWHQLRQGYLPEEFTAG--LSPELRS 226
                         250
                  ....*....|...
gi 1958807372 341 LLRMLFKRNPANR 353
Cdd:cd14050   227 IIKLMMDPDPERR 239
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
464-721 7.96e-27

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 110.21  E-value: 7.96e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCI--HSASNMEFAV-KIIDKNKRDPSEEIEILMRYG-----QHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd08222     2 YRVVRKLGSGNFGTVYLVSdlKATADEELKVlKEISVGELQPDETVDANREAKllsklDHPAIVKFHDSFVEKESFCIVT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRI--LKK--KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghpDSIKICDFGFAKQLR 611
Cdd:cd08222    82 EYCEGGDLDDKIseYKKsgTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-----NVIKVGDFGISRILM 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTM------LAGYTPFSngpndtpeeILLRIGNGRF-SLSg 684
Cdd:cd08222   157 GTSDLATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMcclkhaFDGQNLLS---------VMYKIVEGETpSLP- 226
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 685 giwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08222   227 ---DKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
117-311 8.91e-27

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: 111.16  E-value: 8.91e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRkASLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKLYLILD 191
Cdd:cd14039     1 LGTGGFGNVCLYQNQ---ETGEKIAIKSCR-LELSVKNKDRWCHEIQIMKKLNHPNVVKAcdvpeEMNFLVNDVPLLAME 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKE---VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG----HiKLTDFGLSKEsVDQ 264
Cdd:cd14039    77 YCSGGDLRKLLNKPencCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINgkivH-KIIDLGYAKD-LDQ 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14039   155 GSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
469-716 1.08e-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: 110.12  E-value: 1.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS----EEIEILMRYGQHPNIISL--KEVFDDG--KYVYLVTDLMkG 540
Cdd:cd13985     7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLrvaiKEIEIMKRLCGHPNIVQYydSAILSSEgrKEVLLLMEYC-P 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILK--KKCFSEQEASNVLYVITKTVEYLHSQG--VVHRDLKPSNILYMDesghPDSIKICDFGFA-----KQLR 611
Cdd:cd13985    86 GSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSN----TGRFKLCDFGSAttehyPLER 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GEN--------GLLLTPCYTAnfvaPEVLTQQGYDAAC---DIWSLGVLLYTMLAGYTPFSngpndtpEEILLRIGNGRF 680
Cdd:cd13985   162 AEEvniieeeiQKNTTPMYRA----PEMIDLYSKKPIGekaDIWALGCLLYKLCFFKLPFD-------ESSKLAIVAGKY 230
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958807372 681 SLSGGiwDNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd13985   231 SIPEQ--PRYSPELHDLIRHMLTPDPAERPDIFQVI 264
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
464-743 1.23e-26

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: 112.04  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI------EILMRYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd05594    27 FEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahtlteNRVLQNSRHPFLTALKYSFQTHDRLCFVMEY 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGL 616
Cdd:cd05594   107 ANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSEkNVVYRDLKLENLM-LDKDGH---IKITDFGLCKEGIKDGAT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLrIGNGRFSLSggiwdnISRGAKD 696
Cdd:cd05594   183 MKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELIL-MEEIRFPRT------LSPEAKS 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 697 LLSHMLHMDPHQRY-----TAEQVLKHPWITQREQLPRHQPTSDDP--PQVVME 743
Cdd:cd05594   256 LLSGLLKKDPKQRLgggpdDAKEIMQHKFFAGIVWQDVYEKKLVPPfkPQVTSE 309
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
460-716 1.26e-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: 110.07  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-KNKRDPSEEIE---ILMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd13996     4 YLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRlTEKSSASEKVLrevKALAKLNHPNIVRYYTAWVEEPPLYIQM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGEL---LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdeSGHPDSIKICDFGFAK---Q 609
Cdd:cd13996    84 ELCEGGTLrdwIDRRNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFL---DNDDLQVKIGDFGLATsigN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRGENGLLLTPCYTAN-----------FVAPEVLTQQGYDAACDIWSLGVLLYTMLagyTPFSngpndTPEE---ILLRI 675
Cdd:cd13996   161 QKRELNNLNNNNNGNTsnnsvgigtplYASPEQLDGENYNEKADIYSLGIILFEML---HPFK-----TAMErstILTDL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 676 GNGRFSLSGGIWDNISrgaKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd13996   233 RNGILPESFKAKHPKE---ADLIQSLLSKNPEERPSAEQLL 270
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
470-719 1.36e-26

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 109.40  E-value: 1.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE------EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd13997     8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKEraralrEVEAHAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 ---LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFAKQLRG----ENGl 616
Cdd:cd13997    88 qdaLEELSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNI-FISNKG---TCKIGDFGLATRLETsgdvEEG- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 lltpcyTANFVAPEVLTQ-QGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtpeeiLLRIGNGRFSLSGGiwDNISRGAK 695
Cdd:cd13997   163 ------DSRYLAPELLNEnYTHLPKADIFSLGVTVYEAATGEPLPRNGQQ------WQQLRQGKLPLPPG--LVLSQELT 228
                         250       260
                  ....*....|....*....|....
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd13997   229 RLLKVMLDPDPTRRPTADQLLAHD 252
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
462-722 1.43e-26

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: 110.22  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE----EIEILMRYgQHPNIISLKEVF-DDGKyVYLVTD 536
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEdfmvEIDILSEC-KHPNIVGLYEAYfYENK-LWILIE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdsIKICDFGFAKQLRGENG 615
Cdd:cd06611    83 FCDGGALDSIMLElERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGD----VKLADFGVSAKNKSTLQ 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVL-----TQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNG---RFSLSGGiW 687
Cdd:cd06611   159 KRDTFIGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELAQMEPPHH---ELNPMRVLLKILKSeppTLDQPSK-W 234
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 688 dniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd06611   235 ---SSSFNDFLKSCLVKDPDDRPTAAELLKHPFVS 266
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
496-721 1.69e-26

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: 109.44  E-value: 1.69e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 496 DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRIL--KKKCFSEQEASNVLYVITKTVEYLH 573
Cdd:cd08221    40 EKERRDALNEIDILSLL-NHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAqqKNQLFPEEVVLWYLYQIVSAVSHIH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 574 SQGVVHRDLKPSNIlYMDESghpDSIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTM 653
Cdd:cd08221   119 KAGILHRDIKTLNI-FLTKA---DLVKLGDFGISKVLDSESSMAESIVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYEL 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 654 LAGYTPFsNGPNdtPEEILLRIGNGRFslsGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08221   195 LTLKRTF-DATN--PLRLAVKIVQGEY---EDIDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPLL 256
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
462-737 2.08e-26

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: 110.78  E-value: 2.08e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05619     5 EDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVEctmvekrVLSLAWEHPFLTHLFCTFQTKENLFFV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGEN 614
Cdd:cd05619    85 MEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNIL-LDKDGH---IKIADFGMCKENMLGD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNDtpEEIL--LRIGNGRFSLsggiWdnISR 692
Cdd:cd05619   161 AKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQSPF-HGQDE--EELFqsIRMDNPFYPR----W--LEK 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAE-QVLKHP------W--ITQREQLPRHQPTSDDP 737
Cdd:cd05619   232 EAKDILVKLFVREPERRLGVRgDIRQHPffreinWeaLEEREIEPPFKPKVKSP 285
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
458-721 2.15e-26

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 109.18  E-value: 2.15e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 458 AQFSEAYELKEDIGI--GSY---SVCKrciHSASNMEFAVKIIDKNKRDPSE-EIEILMRygQHPNIISLKEVFDDGKYV 531
Cdd:PHA03390   10 VQFLKNCEIVKKLKLidGKFgkvSVLK---HKPTQKLFVQKIIKAKNFNAIEpMVHQLMK--DNPNFIKLYYSVTTLKGH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdeSGHPDSIKICDFGFAKqLR 611
Cdd:PHA03390   85 VLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY---DRAKDRIYLCDYGLCK-II 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GenglllTP-CY--TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPND--TPEEILLRIGNGRFSLSggi 686
Cdd:PHA03390  161 G------TPsCYdgTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELLTGKHPFKEDEDEelDLESLLKRQQKKLPFIK--- 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958807372 687 wdNISRGAKDLLSHMLHMDPHQR-YTAEQVLKHPWI 721
Cdd:PHA03390  232 --NVSKNANDFVQSMLKYNINYRlTNYNEIIKHPFL 265
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
470-678 2.28e-26

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: 109.17  E-value: 2.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSY-SVCKRCIHSASNMEF--AVKIIdKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd00192     3 LGEGAFgEVYKGKLKGGDGKTVdvAVKTL-KEDASESERKDFLkearvMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVL---------YVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRG 612
Cdd:cd00192    82 DLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARNCLV----GEDLVVKISDFGLSRDIYD 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 613 ENglllTPCYTANFV------APEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNdtpEEILLRIGNG 678
Cdd:cd00192   158 DD----YYRKKTGGKlpirwmAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPGLSN---EEVLEYLRKG 223
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
470-723 2.34e-26

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: 109.73  E-value: 2.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYS-VCKRCIHSASNMeFAVKIIDKNKRDPSEEI---EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD 545
Cdd:cd06657    28 IGEGSTGiVCIATVKSSGKL-VAVKKMDLRKQQRRELLfneVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTD 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 rILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdesgHPDSIKICDFGFAKQLRGENGLLLTPCYTAN 625
Cdd:cd06657   107 -IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLT----HDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 626 FVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIgngRFSLSGGIWD--NISRGAKDLLSHMLH 703
Cdd:cd06657   182 WMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEP---PLKAMKMI---RDNLPPKLKNlhKVSPSLKGFLDRLLV 255
                         250       260
                  ....*....|....*....|
gi 1958807372 704 MDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06657   256 RDPAQRATAAELLKHPFLAK 275
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
464-720 2.49e-26

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: 109.69  E-value: 2.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PSEEI-EI-LMRYGQHPNIISLKEVFDDGKYVYLVTdlm 538
Cdd:cd07835     1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDegvPSTAIrEIsLLKELNHPNIVRLLDVVHSENKLYLVF--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 kggELLDRILKKKCFSEQEASN-------VLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQ-- 609
Cdd:cd07835    78 ---EFLDLDLKKYMDSSPLTGLdppliksYLYQLLQGIAFCHSHRVLHRDLKPQNLL-IDTEG---ALKLADFGLARAfg 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 --LRGengllltpcYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIgngrFS 681
Cdd:cd07835   151 vpVRT---------YTHEVVtlwyrAPEILLgSKHYSTPVDIWSVGCIFAEMVTRRPLF---PGDSEIDQLFRI----FR 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 682 LSG----GIW-------------------------DNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07835   215 TLGtpdeDVWpgvtslpdykptfpkwarqdlskvvPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
112-369 2.52e-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: 109.44  E-value: 2.52e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 112 DLLKV--LGQGSFGkvfLVRKKTGPDAGQLYAMKVLRkASLKVRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYL 188
Cdd:cd06617     2 DLEVIeeLGRGAYG---VVDKMRHVPTGTIMAVKRIR-ATVNSQEQKRLLMDLDISMRSVDcPYTVTFYGALFREGDVWI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGG--DVFTRLSKEVLFTEEDVkfyLAELAL----ALDHLH-RLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd06617    78 CMEVMDTSldKFYKKVYDKGLTIPEDI---LGKIAVsivkALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKAYSfCGTVEYMAPEVVN----RRGHSQSADWWSYGVLMFEMLTGTLPFqgkDRNETMNMILK-------AKLGM 330
Cdd:cd06617   155 VDSVAKTID-AGCKPYMAPERINpelnQKGYDVKSDVWSLGITMIELATGRFPY---DSWKTPFQQLKqvveepsPQLPA 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 331 PQFlSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAFFS 369
Cdd:cd06617   231 EKF-SPEFQDFVNKCLKKNYKER---PNYPELLQHPFFE 265
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
114-353 2.66e-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: 108.96  E-value: 2.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLrkaSLKVRDRVRT-KMERDILVEV-NHPFIVKL--HYAFQTEG-KLYL 188
Cdd:cd13985     5 TKQLGEGGFSYVYLAHDVN---TGRRYALKRM---YFNDEEQLRVaIKEIEIMKRLcGHPNIVQYydSAILSSEGrKEVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEV--LFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLDEIGHIKLTDFGlskeSVDQ 264
Cdd:cd13985    79 LLMEYCPGSLVDILEKSPpsPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFG----SATT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAY---SFCGTVE----------YMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrNETMNmILKAKL 328
Cdd:cd13985   155 EHYPLeraEEVNIIEeeiqknttpmYRAPEMIDlysKKPIGEKADIWALGCLLYKLCFFKLPFDE---SSKLA-IVAGKY 230
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 329 GMPQF--LSAEAQSLLRMLFKRNPANR 353
Cdd:cd13985   231 SIPEQprYSPELHDLIRHMLTPDPAER 257
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
462-720 3.12e-26

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


Pssm-ID: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 109.43  E-value: 3.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII------DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFleseddKMVKKIAMREIKMLKQL-RHENLVNLIEVFRRKKRWYLVF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDriLKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRGE 613
Cdd:cd07846    80 EFVDHTVLDD--LEKYPngLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENIL-VSQSG---VVKLCDFGFARTLAAP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCYTANFVAPEVLTQQ-GYDAACDIWSLGVLLYTMLAGyTPFSNGPNDTPE--EILLRIGN---------GRFS 681
Cdd:cd07846   154 GEVYTDYVATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTG-EPLFPGDSDIDQlyHIIKCLGNliprhqelfQKNP 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 682 LSGGI--------------WDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07846   233 LFAGVrlpevkeveplerrYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
107-310 3.27e-26

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: 109.01  E-value: 3.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKV--LRKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd06641     1 DPEElFTKLEKIGKGSFGEVF---KGIDNRTQKVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYLKD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06641    75 TKLWIIMEYLGGGSALDLLEPGPL-DETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLP 310
Cdd:cd06641   154 TQIKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELARGEPP 200
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
462-709 3.30e-26

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: 111.28  E-value: 3.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05618    20 QDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDwvqtekhVFEQASNHPFLVGLHSCFQTESRLFFV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGEN 614
Cdd:cd05618   100 IEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVL-LDSEGH---IKLTDYGMCKEGLRPG 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-----SNGPNDTPEEILLRIgngRFSLSGGIWDN 689
Cdd:cd05618   176 DTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFdivgsSDNPDQNTEDYLFQV---ILEKQIRIPRS 252
                         250       260
                  ....*....|....*....|
gi 1958807372 690 ISRGAKDLLSHMLHMDPHQR 709
Cdd:cd05618   253 LSVKAASVLKSFLNKDPKER 272
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
503-719 3.33e-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: 108.90  E-value: 3.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 503 SEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG--ELLDRILKKKCF--SEQEASNVLYVITKTVEYLHSQGVV 578
Cdd:cd13982    42 DREVQLLRESDEHPNVIRYFCTEKDRQFLYIALELCAASlqDLVESPRESKLFlrPGLEPVRLLRQIASGLAHLHSLNIV 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 579 HRDLKPSNIL--YMDESGHPdSIKICDFGFAKQL-RGENGLLLT--PCYTANFVAPEVLTQQGYD---AACDIWSLG-VL 649
Cdd:cd13982   122 HRDLKPQNILisTPNAHGNV-RAMISDFGLCKKLdVGRSSFSRRsgVAGTSGWIAPEMLSGSTKRrqtRAVDIFSLGcVF 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 650 LYTMLAGYTPFsnGPNdtpeeiLLRIGN---GRFSLSGGIwDNISRG--AKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd13982   201 YYVLSGGSHPF--GDK------LEREANilkGKYSLDKLL-SLGEHGpeAQDLIERMIDFDPEKRPSAEEVLNHP 266
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
111-353 3.40e-26

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: 109.33  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLrKASLKVRDRVRTKM-ERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd07833     3 YEVLGVVGEGAYGVVLKCRNK---ATGEIVAIKKF-KESEDDEDVKKTALrEVKVLRQLRHENIVNLKEAFRRKGRLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFlrggdvFTRLSKEVL------FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd07833    79 FEY------VERTLLELLeaspggLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAY-SFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQflsaEAQSl 341
Cdd:cd07833   153 RPASPLtDYVATRWYRAPELlVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPP----SHQE- 227
                         250
                  ....*....|..
gi 1958807372 342 lrmLFKRNPANR 353
Cdd:cd07833   228 ---LFSSNPRFA 236
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
508-723 4.22e-26

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: 110.20  E-value: 4.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 508 ILMRYGQHPNIISLKEVF------DDGKYVYLVTDLMKGG--ELLDRILKKKcfseqEASNVLYVITKTVEYLHSQGVVH 579
Cdd:cd07850    51 VLMKLVNHKNIIGLLNVFtpqkslEEFQDVYLVMELMDANlcQVIQMDLDHE-----RMSYLLYQMLCGIKHLHSAGIIH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 580 RDLKPSNILYMDESghpdSIKICDFGFAKQlrGENGLLLTP-CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYT 658
Cdd:cd07850   126 RDLKPSNIVVKSDC----TLKILDFGLART--AGTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTV 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 659 PFsngPND--------------TP-EEILLRIGNGR------------------FSLSGGIWDNISRG------AKDLLS 699
Cdd:cd07850   200 LF---PGTdhidqwnkiieqlgTPsDEFMSRLQPTVrnyvenrpkyagysfeelFPDVLFPPDSEEHNklkasqARDLLS 276
                         250       260
                  ....*....|....*....|....
gi 1958807372 700 HMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd07850   277 KMLVIDPEKRISVDDALQHPYINV 300
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
110-360 4.46e-26

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: 108.79  E-value: 4.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETS---SKKTYMAKFVK---VKGADQVLVKKEISILNIARHRNILRLHESFESHEELVMI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLS-KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENIL-LDEIGH-IKLTDFGLSKESVDQEK 266
Cdd:cd14104    75 FEFISGVDIFERITtARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyCTRRGSyIKIIEFGQSRQLKPGDK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP----QFLSAEAQSLL 342
Cdd:cd14104   155 FRLQYT-SAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDdeafKNISIEALDFV 233
                         250
                  ....*....|....*....
gi 1958807372 343 -RMLFKRNPANRLGSEGVE 360
Cdd:cd14104   234 dRLLVKERKSRMTAQEALN 252
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
111-368 6.85e-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: 107.31  E-value: 6.85e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDA----GQLYAMKVLRKASLKVRdrvrTKMERDILVEVN-HPFIVKLHYAFQTEGK 185
Cdd:cd14019     3 YRIIEKIGEGTFSSVYKAEDKLHDLYdrnkGRLVALKHIYPTSSPSR----ILNELECLERLGgSNNVSGLITAFRNEDQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKevlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLTDFGLSKESVDQ 264
Cdd:cd14019    79 VVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGLAQREEDR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMAPEVVNRRGHSQSA-DWWSYGVLMFEMLTGTLP-FQGKDRNETMNMIlkaklgMPQFLSAEAQSLL 342
Cdd:cd14019   156 PEQRAPRAGTRGFRAPEVLFKCPHQTTAiDIWSAGVILLSILSGRFPfFFSSDDIDALAEI------ATIFGSDEAYDLL 229
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 343 RMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14019   230 DKLLELDPSKRITA---EEALKHPFF 252
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
107-310 7.59e-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: 107.83  E-value: 7.59e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKV--LRKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd06640     1 DPEElFTKLERIGKGSFGEVF---KGIDNRTQQVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYVTKYYGSYLKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRLsKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06640    75 TKLWIIMEYLGGGSALDLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLP 310
Cdd:cd06640   154 TQIKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPP 200
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
116-367 7.78e-26

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 107.52  E-value: 7.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKTGpdagQLYAMKvlrKASLKVRDRVRTKM-------ERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd06631     8 VLGKGAYGTVYCGLTSTG----QLIAVK---QVELDTSDKEKAEKeyeklqeEVDLLKTLKHVNIVGYLGTCLEDNVVSI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE------SV 262
Cdd:cd06631    81 FMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRlcinlsSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQ 339
Cdd:cd06631   161 SQSQLLKSMRGTPYWMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVPRLpdkFSPEAR 240
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 340 SLLRMLFKRNPANRLGSegvEEVKRHAF 367
Cdd:cd06631   241 DFVHACLTRDQDERPSA---EQLLKHPF 265
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
461-660 9.25e-26

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: 110.09  E-value: 9.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPS----EEIEIlMRYGQHPNIISLKEVFDDGKYVYL 533
Cdd:cd05621    51 AEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFemiKRSDSaffwEERDI-MAFANSPWVVQLFCAFQDDKYLYM 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrGE 613
Cdd:cd05621   130 VMEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNML-LDKYGH---LKLADFGTCMKM-DE 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 614 NGLLL--TPCYTANFVAPEVLTQQG----YDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd05621   204 TGMVHcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEMLVGDTPF 256
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
108-367 9.77e-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: 107.42  E-value: 9.77e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVL------RKASLKVRdrvRTKMERDILVEVNHPFIVKLHYAFQ 181
Cdd:cd06653     1 PVNWRLGKLLGRGAFGEVYLCYDA---DTGRELAVKQVpfdpdsQETSKEVN---ALECEIQLLKNLRHDRIVQYYGCLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 --TEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd06653    75 dpEEKKLSIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 --ESVDQEKKAY-SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILK-----AKLGMP 331
Cdd:cd06653   155 riQTICMSGTGIkSVTGTPYWMSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWA---EYEAMAAIFKiatqpTKPQLP 231
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 332 QFLSAEAQSLLRMLF---KRNPAnrlgsegVEEVKRHAF 367
Cdd:cd06653   232 DGVSDACRDFLRQIFveeKRRPT-------AEFLLRHPF 263
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
470-666 9.80e-26

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 108.93  E-value: 9.80e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05616     8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDVEctmvekrVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEAsnVLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTP 620
Cdd:cd05616    88 LMYHIQQVGRFKEPHA--VFYAaeIAIGLFFLQSKGIIYRDLKLDNVM-LDSEGH---IKIADFGMCKENIWDGVTTKTF 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 621 CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPND 666
Cdd:cd05616   162 CGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDED 207
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
111-436 1.04e-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: 108.60  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd06650     7 FEKISELGAGNGGVVFKVSHKP---SGLVMARKLIH---LEIKPAIRNQIIRElqVLHECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEdvkfYLAELALA----LDHL-HRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06650    81 CMEHMDGGSLDQVLKKAGRIPEQ----ILGKVSIAvikgLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNEtmnmilkakLGMPQFLSAEAQSLLR 343
Cdd:cd06650   157 S--MANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKE---------LELMFGCQVEGDAAET 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 344 MLFKRNPANRLGSEGVEEVKRHAFFSSIDwnklYKREVQPPFRPASgkpddtfCFDPEFTAKTPKDSPGLPAS-ANAHQL 422
Cdd:cd06650   226 PPRPRTPGRPLSSYGMDSRPPMAIFELLD----YIVNEPPPKLPSG-------VFSLEFQDFVNKCLIKNPAErADLKQL 294
                         330
                  ....*....|....
gi 1958807372 423 FKgFSFVATSIAEE 436
Cdd:cd06650   295 MV-HAFIKRSDAEE 307
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
115-368 1.24e-25

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: 107.13  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRK-KTGpdagQLYAMKVLR--KASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd06630     6 PLLGTGAFSSCYQARDvKTG----TLMAVKQVSfcRNSSSEQEEVVEAIREEIrmMARLNHPNIVRMLGATQHKSHFNIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG-HIKLTDFGLSKESVDQEKKA 268
Cdd:cd06630    82 VEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLASKGTGA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSF----CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGM-----PQFLSAEAQ 339
Cdd:cd06630   162 GEFqgqlLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATtpppiPEHLSPGLR 241
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 340 SLLRMLFKRNPANRlgsEGVEEVKRHAFF 368
Cdd:cd06630   242 DVTLRCLELQPEDR---PPARELLKHPVF 267
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
464-716 1.27e-25

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: 106.60  E-value: 1.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKR----DPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd08219     2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSssavEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRI--LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFAKQLRGENGLL 617
Cdd:cd08219    82 GGDLMQKIklQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNI-FLTQNG---KVKLGDFGSARLLTSPGAYA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGNGRFSlsgGIWDNISRGAKDL 697
Cdd:cd08219   158 CTYVGTPYYVPPEIWENMPYNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQGSYK---PLPSHYSYELRSL 231
                         250
                  ....*....|....*....
gi 1958807372 698 LSHMLHMDPHQRYTAEQVL 716
Cdd:cd08219   232 IKQMFKRNPRSRPSATTIL 250
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
490-737 1.55e-25

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 108.11  E-value: 1.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVL 562
Cdd:cd05620    23 FAVKALKKDVVLIDDDVEctmvekrVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGGDLMFHIQDKGRFDLYRATFYA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQ-LRGENGLLlTPCYTANFVAPEVLTQQGYDAAC 641
Cdd:cd05620   103 AEIVCGLQFLHSKGIIYRDLKLDNVM-LDRDGH---IKIADFGMCKEnVFGDNRAS-TFCGTPDYIAPEILQGLKYTFSV 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 642 DIWSLGVLLYTMLAGYTPFSngpNDTPEEIL--LRIGNGRFSLsggiWdnISRGAKDLLSHMLHMDPHQRYTAEQVLK-H 718
Cdd:cd05620   178 DWWSFGVLLYEMLIGQSPFH---GDDEDELFesIRVDTPHYPR----W--ITKESKDILEKLFERDPTRRLGVVGNIRgH 248
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 719 P------WIT--QREQLPRHQPTSDDP 737
Cdd:cd05620   249 PffktinWTAleKRELDPPFKPKVKSP 275
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
117-364 1.63e-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: 106.97  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGpdagQLYAMKVLRKASLKVRDRV-RTKMErdILVEVNHPFIVKLhYAFQTEGKLY-LILDFLR 194
Cdd:cd14066     1 IGSGGFGTVYKGVLENG----TVVAVKRLNEMNCAASKKEfLTELE--MLGRLRHPNLVRL-LGYCLESDEKlLVYEYMP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRL----SKEVLFTEEDVKFYLaELALALDHLH---RLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV--DQE 265
Cdd:cd14066    74 NGSLEDRLhchkGSPPLPWPQRLKIAK-GIARGLEYLHeecPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPpsESV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAklgmpqFLSAEAQSLLRML 345
Cdd:cd14066   153 SKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEW------VESKGKEELEDIL 226
                         250
                  ....*....|....*....
gi 1958807372 346 FKRnpANRLGSEGVEEVKR 364
Cdd:cd14066   227 DKR--LVDDDGVEEEEVEA 243
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
470-721 1.67e-25

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The Bck1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 106.70  E-value: 1.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE--------------EIEiLMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd06629     9 IGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRadsrqktvvdalksEID-TLKDLDHPNIVQYLGFEETEDYFSIFL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQ---LRG 612
Cdd:cd06629    88 EYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNIL-VDLEG---ICKISDFGISKKsddIYG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCyTANFVAPEVL--TQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFS--LSGGIwd 688
Cdd:cd06629   164 NNGATSMQG-SVFWMAPEVIhsQGQGYSAKVDIWSLGCVVLEMLAGRRPWS---DDEAIAAMFKLGNKRSAppVPEDV-- 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06629   238 NLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
477-720 2.28e-25

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: 106.67  E-value: 2.28e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 477 VCKrCIHSASNMEFAVKIIDKN--KRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRI-- 547
Cdd:cd05605    16 VCA-CQVRATGKMYACKKLEKKriKKRKGEamalnEKQILEKV-NSRFVVSLAYAYETKDALCLVLTIMNGGDLKFHIyn 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 548 LKKKCFSEQEAsnVLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQL------RGENGlllt 619
Cdd:cd05605    94 MGNPGFEEERA--VFYAaeITCGLEHLHSERIVYRDLKPENIL-LDDHGH---VRISDLGLAVEIpegetiRGRVG---- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 pcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSggiwDNISRGAKDLL 698
Cdd:cd05605   164 ---TVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIEGQAPFrARKEKVKREEVDRRVKEDQEEYS----EKFSEEAKSIC 236
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 699 SHMLHMDPHQR-----YTAEQVLKHPW 720
Cdd:cd05605   237 SQLLQKDPKTRlgcrgEGAEDVKSHPF 263
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
491-721 2.71e-25

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 105.98  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKRDP----------SEEIEiLMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELlDRILKKkcF-SEQEAS 559
Cdd:cd06631    29 AVKQVELDTSDKekaekeyeklQEEVD-LLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPGGSI-ASILAR--FgALEEPV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 NVLYV--ITKTVEYLHSQGVVHRDLKPSNILYMdesghPDS-IKICDFGFAKQL-----RGENGLLLTPCY-TANFVAPE 630
Cdd:cd06631   105 FCRYTkqILEGVAYLHNNNVIHRDIKGNNIMLM-----PNGvIKLIDFGCAKRLcinlsSGSQSQLLKSMRgTPYWMAPE 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 631 VLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIGNGRfSLSGGIWDNISRGAKDLLSHMLHMDPHQRY 710
Cdd:cd06631   180 VINETGHGRKSDIWSIGCTVFEMATGKPPWADMN---PMAAIFAIGSGR-KPVPRLPDKFSPEARDFVHACLTRDQDERP 255
                         250
                  ....*....|.
gi 1958807372 711 TAEQVLKHPWI 721
Cdd:cd06631   256 SAEQLLKHPFI 266
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
480-720 2.77e-25

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: 105.50  E-value: 2.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 480 RCIHSASNMEFAVKIIDKNKRdpSEEIEILMRYGQHPNIISLKEVF--DDGKYVYLVTDLmkgGELLDRILKKKCFSEQE 557
Cdd:cd14022    11 RAVHLHSGEELVCKVFDIGCY--QESLAPCFCLPAHSNINQITEIIlgETKAYVFFERSY---GDMHSFVRTCKKLREEE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 558 ASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghPDSIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQG- 636
Cdd:cd14022    86 AARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEE--RTRVKLESLEDAYILRGHDDSLSDKHGCPAYVSPEILNTSGs 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 637 YDA-ACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSlsggIWDNISRGAKDLLSHMLHMDPHQRYTAEQV 715
Cdd:cd14022   164 YSGkAADVWSLGVMLYTMLVGRYPFH---DIEPSSLFSKIRRGQFN----IPETLSPKAKCLIRSILRREPSERLTSQEI 236

                  ....*
gi 1958807372 716 LKHPW 720
Cdd:cd14022   237 LDHPW 241
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
111-368 3.45e-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: 106.20  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKaslkvrdRVRTKMERDILVEVN-------HPFIVKLHYAF-- 180
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQsRKTG----KYYAIKCMKK-------HFKSLEQVNNLREIQalrrlspHPNILRLIEVLfd 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 QTEGKLYLIL--------DFLRGgdvftrlsKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIgHIKL 252
Cdd:cd07831    70 RKTGRLALVFelmdmnlyELIKG--------RKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 253 TDFGlSKESVDQeKKAYS-FCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTgTLP-FQGKDRNETMNMILKAkLG 329
Cdd:cd07831   141 ADFG-SCRGIYS-KPPYTeYISTRWYRAPECLLTDGyYGPKMDIWAVGCVFFEILS-LFPlFPGTNELDQIAKIHDV-LG 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 330 MP------------------------------QFLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07831   217 TPdaevlkkfrksrhmnynfpskkgtglrkllPNASAEGLDLLKKLLAYDPDERITA---KQALRHPYF 282
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
452-735 3.58e-25

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 107.73  E-value: 3.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 452 QINGNAAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKiidKNKRDPSEEI-------EI-LMRYGQHPNIISLKE 523
Cdd:cd07880     5 EVNKTIWEVPDRYRDLKQVGSGAYGTVCSALDRRTGAKVAIK---KLYRPFQSELfakrayrELrLLKHMKHENVIGLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 524 VF------DDGKYVYLVTDLMkgGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpd 597
Cdd:cd07880    82 VFtpdlslDRFHDFYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDC---- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 598 SIKICDFGFAKQLRGE-NGLLLTPCYTanfvAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN-DTPEEILLR 674
Cdd:cd07880   156 ELKILDFGLARQTDSEmTGYVVTRWYR----APEViLNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHlDQLMEIMKV 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 675 IG----------------NGRFSLS-------GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ---REQLP 728
Cdd:cd07880   232 TGtpskefvqklqsedakNYVKKLPrfrkkdfRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEfhdPEDET 311

                  ....*..
gi 1958807372 729 RHQPTSD 735
Cdd:cd07880   312 EAPPYDD 318
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
493-720 3.67e-25

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 107.37  E-value: 3.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 493 KIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYL 572
Cdd:PTZ00426   68 KIIKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 573 HSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENgllLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYT 652
Cdd:PTZ00426  148 QSLNIVYRDLKPENLL-LDKDGF---IKMTDFGFAKVVDTRT---YTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYE 220
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 653 MLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHmlhmDPHQRY-----TAEQVLKHPW 720
Cdd:PTZ00426  221 ILVGCPPFY---ANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSH----DLTKRYgnlkkGAQNVKEHPW 286
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
107-356 3.91e-25

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 105.54  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKASLKVRDRVRTKMERDILvEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd13979     1 DWEPLRLQEPLGSGGFGSVYKATYK-----GETVAVKIVRRRRKNRASRQSFWAELNAA-RLRHENIVRVLAAETGTDFA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YL---ILDFLRGGDVFTRL--SKEVLFTEEDVKfYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS--- 258
Cdd:cd13979    75 SLgliIMEYCGNGTLQQLIyeGSEPLPLAHRIL-ISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSvkl 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkDRNETMNMILKAKL-----GMPQF 333
Cdd:cd13979   154 GEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRELPYAG-LRQHVLYAVVAKDLrpdlsGLEDS 232
                         250       260
                  ....*....|....*....|....
gi 1958807372 334 LSAEA-QSLLRMLFKRNPANRLGS 356
Cdd:cd13979   233 EFGQRlRSLISRCWSAQPAERPNA 256
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
109-317 4.27e-25

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 106.27  E-value: 4.27e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASL-KVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd08229    24 ANFRIEKKIGRGQFSEVY---RATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRL----SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd08229   101 IVLELADAGDLSRMIkhfkKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSS 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd08229   181 KTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMN 234
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
116-315 5.13e-25

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


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 105.50  E-value: 5.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKA----SLKVRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd14146     1 IIGVGGFGKVYRATWK-----GQEVAVKAARQDpdedIKATAESVR--QEAKLFSMLRHPNIIKLEGVCLEEPNLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDV---------------FTRLSKEVLFTeedvkfYLAELALALDHLHR---LGIVYRDLKPENILL------DEI 247
Cdd:cd14146    74 FARGGTLnralaaanaapgprrARRIPPHILVN------WAVQIARGMLYLHEeavVPILHRDLKSSNILLlekiehDDI 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GH--IKLTDFGLSKESVDQEKkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD 315
Cdd:cd14146   148 CNktLKITDFGLAREWHRTTK--MSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGID 215
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
468-723 5.56e-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: 5.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-----RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd06642    10 ERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaedeiEDIQQEITVLSQC-DSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRG----ENGLLL 618
Cdd:cd06642    89 ALD-LLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVL-LSEQG---DVKLADFGVAGQLTDtqikRNTFVG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRI-GNGRFSLSGgiwdNISRGAKDL 697
Cdd:cd06642   164 TPFW----MAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNS---DLHPMRVLFLIpKNSPPTLEG----QHSKPFKEF 232
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06642   233 VEACLNKDPRFRPTAKELLKHKFITR 258
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
104-368 5.99e-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: 105.84  E-value: 5.99e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 104 EKADPAQF--DLLKVlGQGSFGKVFLVRKKtgpDAGQLYAMKVLrkaslKVRDRVRTKM---ERDILVEVNHPFIVKLHY 178
Cdd:cd06659    15 DQGDPRQLleNYVKI-GEGSTGVVCIAREK---HSGRQVAVKMM-----DLRKQQRRELlfnEVVIMRDYQHPNVVEMYK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 179 AFQTEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd06659    86 SYLVGEELWVLMEYLQGG-ALTDIVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA---KLGMPQFLS 335
Cdd:cd06659   165 AQISKDVPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKAS 244
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd06659   245 PVLRDFLERMLVRDPQERATA---QELLDHPFL 274
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
463-721 6.22e-25

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: 104.83  E-value: 6.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 463 AYELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-----KNKRDPSEEIEILMRYGQHPNIISLKEVFDDGK-YVYLVTD 536
Cdd:cd08223     1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNlknasKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESghpDSIKICDFGFAKQLRGEN 614
Cdd:cd08223    81 FCEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNI-FLTKS---NIIKVGDLGIARVLESSS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTpeeILLRIGNGRFSLsggIWDNISRGA 694
Cdd:cd08223   157 DMATTLIGTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNS---LVYKILEGKLPP---MPKQYSPEL 230
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd08223   231 GELIKAMLHQDPEKRPSVKRILRQPYI 257
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
456-721 6.40e-25

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: 105.46  E-value: 6.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 456 NAAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKnKRDPSEEIE----ILMRYGQHPNIISLKEVFDD---- 527
Cdd:cd06639    16 SLADPSDTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDP-ISDVDEEIEaeynILRSLPNHPNVVKFYGMFYKadqy 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 528 -GKYVYLVTDLMKGG---ELLDRILKK-KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdsIKIC 602
Cdd:cd06639    95 vGGQLWLVLELCNGGsvtELVKGLLKCgQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGG----VKLV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 603 DFGFAKQLRGENGLLLTPCYTANFVAPEVLT--QQ---GYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIGN 677
Cdd:cd06639   171 DFGVSAQLTSARLRRNTSVGTPFWMAPEVIAceQQydySYDARCDVWSLGITAIELADGDPPLFDM---HPVKALFKIPR 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 678 GRFS--LSGGIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06639   248 NPPPtlLNPEKW---CRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
112-317 6.48e-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: 105.60  E-value: 6.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 112 DLLKV--LGQGSFGKVFLV-RKKTGpdagqlyamKVLRKASLKV--RDRVRTKM--ERDILVEVNHPFIVKLHYAFQTE- 183
Cdd:cd06620     6 DLETLkdLGAGNGGSVSKVlHIPTG---------TIMAKKVIHIdaKSSVRKQIlrELQILHECHSPYIVSFYGAFLNEn 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKfylaELALA----LDHLHR-LGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd06620    77 NNIIICMEYMDCGSLDKILKKKGPFPEEVLG----KIAVAvlegLTYLYNvHRIIHRDIKPSNILVNSKGQIKLCDFGVS 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 259 KESVDQekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd06620   153 GELINS--IADTFVGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFAGSNDD 209
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
464-709 7.31e-25

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: 107.03  E-value: 7.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDwvqtekhVFEQASSNPFLVGLHSCFQTTSRLFLVIE 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGL 616
Cdd:cd05617    97 YVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVL-LDADGH---IKLTDYGMCKEGLGPGDT 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF---SNGPNDTPEEILLRIgngRFSLSGGIWDNISRG 693
Cdd:cd05617   173 TSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFdiiTDNPDMNTEDYLFQV---ILEKPIRIPRFLSVK 249
                         250
                  ....*....|....*.
gi 1958807372 694 AKDLLSHMLHMDPHQR 709
Cdd:cd05617   250 ASHVLKGFLNKDPKER 265
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
115-354 8.47e-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: 105.50  E-value: 8.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASlKVRDRVRTKMERDilvevNHPFIVKL----HYAFQTEGKLYLI 189
Cdd:cd14170     8 QVLGLGINGKVLqIFNKRTQ----EKFALKMLQDCP-KARREVELHWRAS-----QCPHIVRIvdvyENLYAGRKCLLIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI---GHIKLTDFGLSKESVDQ 264
Cdd:cd14170    78 MECLDGGELFSRIQDrgDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTSH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMILKAKLGMPQF---------LS 335
Cdd:cd14170   158 NSLT-TPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGYPPFY-SNHGLAISPGMKTRIRMGQYefpnpewseVS 235
                         250
                  ....*....|....*....
gi 1958807372 336 AEAQSLLRMLFKRNPANRL 354
Cdd:cd14170   236 EEVKMLIRNLLKTEPTQRM 254
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
104-331 1.18e-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: 104.35  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 104 EKADPAQFDLLKVLGQGSFGKVFlvRKKTGpdaGQLYAMKVLRKAS----LKVRDRVRtkMERDILVEVNHPFIVKLHYA 179
Cdd:cd14145     1 LEIDFSELVLEEIIGIGGFGKVY--RAIWI---GDEVAVKAARHDPdediSQTIENVR--QEAKLFAMLKHPNIIALRGV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKfYLAELALALDHLHRLGIV---YRDLKPENILL------DEIGH- 249
Cdd:cd14145    74 CLKEPNLCLVMEFARGGPLNRVLSGKRIPPDILVN-WAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvenGDLSNk 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 250 -IKLTDFGLSKESVDQEKkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKL 328
Cdd:cd14145   153 iLKITDFGLAREWHRTTK--MSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKL 230

                  ...
gi 1958807372 329 GMP 331
Cdd:cd14145   231 SLP 233
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
115-353 1.22e-24

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: 103.93  E-value: 1.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFlvrKKTGPDAGQLyAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd05085     2 ELLGKGNFGEVY---KGTLKDKTPV-AVKTC-KEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDV--FTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKKAYSFC 272
Cdd:cd05085    77 GGDFlsFLRKKKDELKTKQLVKFSL-DAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQ---EDDGVYSSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 G----TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLF 346
Cdd:cd05085   153 GlkqiPIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCW 232

                  ....*..
gi 1958807372 347 KRNPANR 353
Cdd:cd05085   233 DYNPENR 239
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
464-720 1.25e-24

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: 105.44  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSY-SVCK-RCIHSASNMEFAVKIIDKNKRD-----PSEEIEI-LMRYGQHPNIISLKEVFDDG--KYVYL 533
Cdd:cd07842     2 YEIEGCIGRGTYgRVYKaKRKNGKDGKEYAIKKFKGDKEQytgisQSACREIaLLRELKHENVVSLVEVFLEHadKSVYL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLM--------------KGGELLDRILKkkcfseqeasNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSI 599
Cdd:cd07842    82 LFDYAehdlwqiikfhrqaKRVSIPPSMVK----------SLLWQILNGIHYLHSNWVLHRDLKPANILVMGEGPERGVV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 600 KICDFGFA-------KQLRGENGLLLTPCYTanfvAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPND----T 667
Cdd:cd07842   152 KIGDLGLArlfnaplKPLADLDPVVVTIWYR----APELLLgARHYTKAIDIWAIGCIFAELLTLEPIFKGREAKikksN 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 668 P--EEILLRIgngrFSLSG--------GI-----WDNISRGAK------------------------DLLSHMLHMDPHQ 708
Cdd:cd07842   228 PfqRDQLERI----FEVLGtptekdwpDIkkmpeYDTLKSDTKastypnsllakwmhkhkkpdsqgfDLLRKLLEYDPTK 303
                         330
                  ....*....|..
gi 1958807372 709 RYTAEQVLKHPW 720
Cdd:cd07842   304 RITAEEALEHPY 315
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
470-670 1.28e-24

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: 105.58  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05588     3 IGRGSYAKVLMVELKKTKRIYAMKVIKKELVNDDEDIDwvqtekhVFETASNHPFLVGLHSCFQTESRLFFVIEFVNGGD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd05588    83 LMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVL-LDSEGH---IKLTDYGMCKEGLRPGDTTSTFCG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFS-NGPNDTPEE 670
Cdd:cd05588   159 TPNYIAPEILRGEDYGFSVDWWALGVLMFEMLAGRSPFDiVGSSDNPDQ 207
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
117-342 1.34e-24

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: 103.85  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVrkkTGPDAGQLYAMKvlrkaSLKVRDRVRTKME-RDILV--EVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd06647    15 IGQGASGTVYTA---IDVATGQEVAIK-----QMNLQQQPKKELIiNEILVmrENKNPNIVNYLDSYLVGDELWVVMEYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 273
Cdd:cd06647    87 AGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVG 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQFLSAEAQSLL 342
Cdd:cd06647   166 TPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPELQNPEKLSAI 232
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
460-720 1.69e-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: 105.34  E-value: 1.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII---DKNKRDPSEEIEILMRYGQH-----PNIISLKEVFDDGKYV 531
Cdd:cd14134    10 LTNRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIrnvEKYREAAKIEIDVLETLAEKdpngkSHCVQLRDWFDYRGHM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMkGGELLDRiLKKKC---FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDS---------- 598
Cdd:cd14134    90 CIVFELL-GPSLYDF-LKKNNygpFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDYVKVYnpkkkrqirv 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 599 -----IKICDFGFAkqlrgengllltpCY----------TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSN- 662
Cdd:cd14134   168 pkstdIKLIDFGSA-------------TFddeyhssivsTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTh 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 663 -------------GPndTPEEILLRIGNG--RFSLSGGI--WDNISRGAK------------------------DLLSHM 701
Cdd:cd14134   235 dnlehlammerilGP--LPKRMIRRAKKGakYFYFYHGRldWPEGSSSGRsikrvckplkrlmllvdpehrllfDLIRKM 312
                         330
                  ....*....|....*....
gi 1958807372 702 LHMDPHQRYTAEQVLKHPW 720
Cdd:cd14134   313 LEYDPSKRITAKEALKHPF 331
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
470-719 1.90e-24

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: 103.76  E-value: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLDKKriKKKKGEtmalnEKIILEKV-SSPFIVSLAYAFETKDKLCLVLTLMNGGD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFA------KQLRGEN 614
Cdd:cd05577    80 LKYHIYNVGTRGFSEARAIFYAaeIICGLEHLHNRFIVYRDLKPENIL-LDDHGH---VRISDLGLAvefkggKKIKGRV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GllltpcyTANFVAPEVLTQQ-GYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSggiwDNISR 692
Cdd:cd05577   156 G-------THGYMAPEVLQKEvAYDFSVDWFALGCMLYEMIAGRSPFrQRKEKVDKEELKRRTLEMAVEYP----DSFSP 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 693 GAKDLLSHMLHMDPHQRY-----TAEQVLKHP 719
Cdd:cd05577   225 EARSLCEGLLQKDPERRLgcrggSADEVKEHP 256
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
490-660 1.90e-24

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The cPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 104.78  E-value: 1.90e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKN---KRDPSE----EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEAsnVL 562
Cdd:cd05587    24 YAIKILKKDviiQDDDVEctmvEKRVLALSGKPPFLTQLHSCFQTMDRLYFVMEYVNGGDLMYHIQQVGKFKEPVA--VF 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQGYDAA 640
Cdd:cd05587   102 YAaeIAVGLFFLHSKGIIYRDLKLDNVM-LDAEGH---IKIADFGMCKEGIFGGKTTRTFCGTPDYIAPEIIAYQPYGKS 177
                         170       180
                  ....*....|....*....|
gi 1958807372 641 CDIWSLGVLLYTMLAGYTPF 660
Cdd:cd05587   178 VDWWAYGVLLYEMLAGQPPF 197
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
110-331 1.99e-24

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: 104.55  E-value: 1.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKaslkvrdrvRTKMERDILVEV--------NHP----FIVKL 176
Cdd:cd14210    14 RYEVLSVLGKGSFGQVVKCLdHKTG----QLVAIKIIRN---------KKRFHQQALVEVkilkhlndNDPddkhNIVRY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAFQTEGKLYLildflrggdVFTRLSK---EVL-------FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDE 246
Cdd:cd14210    81 KDSFIFRGHLCI---------VFELLSInlyELLksnnfqgLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 247 IGH--IKLTDFGLS-KESvdqeKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI 323
Cdd:cd14210   152 PSKssIKVIDFGSScFEG----EKVYTYIQSRFYRAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACI 227

                  ....*...
gi 1958807372 324 LKAkLGMP 331
Cdd:cd14210   228 MEV-LGVP 234
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
104-369 2.05e-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: 104.33  E-value: 2.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 104 EKADPAQF-DLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlrkaSLKVRDRVRTKM---ERDILVEVNHPFIVKLHYA 179
Cdd:cd06657    14 DPGDPRTYlDNFIKIGEGSTGIVCIATVKS---SGKLVAVK-----KMDLRKQQRRELlfnEVVIMRDYQHENVVEMYNS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd06657    86 YLVGDELWVVMEFLEGG-ALTDIVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI---LKAKLGMPQFLSA 336
Cdd:cd06657   165 QVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIrdnLPPKLKNLHKVSP 244
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 337 EAQSLLRMLFKRNPANRLGSegvEEVKRHAFFS 369
Cdd:cd06657   245 SLKGFLDRLLVRDPAQRATA---AELLKHPFLA 274
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
107-311 2.06e-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: 103.98  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKV--LRKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd06642     1 DPEElFTKLERIGKGSFGEVY---KGIDNRTKEVVAIKIidLEEAEDEIED---IQQEITVLSQCDSPYITRYYGSYLKG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06642    75 TKLWIIMEYLGGGSALDLLKPGPL-EETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 264 QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd06642   154 TQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPN 201
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
547-718 2.13e-24

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: 104.02  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 547 ILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdeSGHPDSIKICDFGFAKQLRGENGLLL----TPCY 622
Cdd:cd13974   123 VIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVL---NKRTRKITITNFCLGKHLVSEDDLLKdqrgSPAY 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 tanfVAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSL-SGGiwdNISRGAKDLLSH 700
Cdd:cd13974   200 ----ISPDVLSGKPYLGkPSDMWALGVVLFTMLYGQFPFY---DSIPQELFRKIKAAEYTIpEDG---RVSENTVCLIRK 269
                         170
                  ....*....|....*...
gi 1958807372 701 MLHMDPHQRYTAEQVLKH 718
Cdd:cd13974   270 LLVLNPQKRLTASEVLDS 287
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
516-725 2.16e-24

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: 106.09  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 516 PNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGH 595
Cdd:cd05629    61 PWVVSLYYSFQDAQYLYLIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNIL-IDRGGH 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 596 pdsIKICDF----GFAKQ------------------LRGENGLLLTPCY-------------------------TANFVA 628
Cdd:cd05629   140 ---IKLSDFglstGFHKQhdsayyqkllqgksnknrIDNRNSVAVDSINltmsskdqiatwkknrrlmaystvgTPDYIA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 629 PEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILlrigNGRFSLSGGIWDNISRGAKDLLSHMLHMDPH 707
Cdd:cd05629   217 PEIFLQQGYGQECDWWSLGAIMFECLIGWPPFcSENSHETYRKII----NWRETLYFPDDIHLSVEAEDLIRRLITNAEN 292
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 708 Q--RYTAEQVLKHP------WITQRE 725
Cdd:cd05629   293 RlgRGGAHEIKSHPffrgvdWDTIRQ 318
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
113-354 2.22e-24

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: 103.58  E-value: 2.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVF--LVRKKTGPDAGQLYAMKVLRKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05032    10 LIRELGQGSFGMVYegLAKGVVKGEPETRVAIKTVNENA-SMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRL----SKEVLFTEEDV----KFYL--AELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd05032    89 ELMAKGDLKSYLrsrrPEAENNPGLGPptlqKFIQmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTRD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQE--KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKL-----GMPQ 332
Cdd:cd05032   169 IYETDyyRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATlAEQPYQGLSNEEVLKFVIDGGHldlpeNCPD 248
                         250       260
                  ....*....|....*....|..
gi 1958807372 333 FLsaeaQSLLRMLFKRNPANRL 354
Cdd:cd05032   249 KL----LELMRMCWQYNPKMRP 266
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
462-723 2.42e-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: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-----RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06641     4 ELFTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaedeiEDIQQEITVLSQC-DSPYVTKYYGSYLKDTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRG---- 612
Cdd:cd06641    83 YLGGGSALD-LLEPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVL-LSEHGE---VKLADFGVAGQLTDtqik 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGiwdNISR 692
Cdd:cd06641   158 RN*FVGTPFW----MAPEVIKQSAYDSKADIWSLGITAIELARGEPPHS---ELHPMKVLFLIPKNNPPTLEG---NYSK 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06641   228 PLKEFVEACLNKEPSFRPTAKELLKHKFILR 258
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
116-353 2.64e-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: 2.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFlvrkktgpdAGqlyamkvlRKASLKVRDRVRTKMERDI-----LVE-------VNHPFIVKLHYAFQTE 183
Cdd:cd06624    15 VLGKGTFGVVY---------AA--------RDLSTQVRIAIKEIPERDSrevqpLHEeialhsrLSHKNIVQYLGSVSED 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGGDVFTRL-SK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI-GHIKLTDFGLSK 259
Cdd:cd06624    78 GFFKIFMEQVPGGSLSALLrSKwgPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTYsGVVKISDFGTSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPFQgKDRNETMNMIlkaKLGM------- 330
Cdd:cd06624   158 RLAGINPCTETFTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMATGKPPFI-ELGEPQAAMF---KVGMfkihpei 233
                         250       260
                  ....*....|....*....|...
gi 1958807372 331 PQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd06624   234 PESLSEEAKSFILRCFEPDPDKR 256
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
462-723 2.77e-24

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


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 103.59  E-value: 2.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNK-----RDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06640     4 ELFTKLERIGKGSFGEVFKGIDNRTQQVVAIKIIDLEEaedeiEDIQQEITVLSQC-DSPYVTKYYGSYLKGTKLWIIME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRGENGL 616
Cdd:cd06640    83 YLGGGSALD-LLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVL-LSEQG---DVKLADFGVAGQLTDTQIK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 617 LLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRI-GNGRFSLSGgiwdNISRGAK 695
Cdd:cd06640   158 RNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDM---HPMRVLFLIpKNNPPTLVG----DFSKPFK 230
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 696 DLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06640   231 EFIDACLNKDPSFRPTAKELLKHKFIVK 258
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
117-353 2.81e-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: 102.73  E-value: 2.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKaslKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14115     1 IGRGRFS---IVKKCLHKATRKDVAVKFVSK---KMKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD---EIGHIKLTDFGLSKEsVDQEKKAYSFCG 273
Cdd:cd14115    75 RLLDYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDAVQ-ISGHRHVHHLLG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQ--F--LSAEAQSLLRMLFKRN 349
Cdd:cd14115   154 NPEFAAPEVIQGTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDeyFgdVSQAARDFINVILQED 233

                  ....
gi 1958807372 350 PANR 353
Cdd:cd14115   234 PRRR 237
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
516-720 2.87e-24

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: 103.29  E-value: 2.87e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 516 PNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGH 595
Cdd:cd05606    58 PFIVCMTYAFQTPDKLCFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANIL-LDEHGH 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 596 pdsIKICDFGFA-----KQLRGENGllltpcyTANFVAPEVLTQ-QGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPE 669
Cdd:cd05606   137 ---VRISDLGLAcdfskKKPHASVG-------THGYMAPEVLQKgVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKDKH 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 670 EIllrignGRFSLSGGIW--DNISRGAKDLLSHMLHMDPHQRY-----TAEQVLKHPW 720
Cdd:cd05606   207 EI------DRMTLTMNVElpDSFSPELKSLLEGLLQRDVSKRLgclgrGATEVKEHPF 258
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
111-322 3.43e-24

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: 104.05  E-value: 3.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERD--ILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd06615     3 FEKLGELGAGNGGVVTKVLHRP---SGLIMARKLIH---LEIKPAIRNQIIRElkVLHECNSPYIVGFYGAFYSDGEISI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEdvkfYLAELALA----LDHLH-RLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd06615    77 CMEHMDGGSLDQVLKKAGRIPEN----ILGKISIAvlrgLTYLReKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLID 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 264 QekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 322
Cdd:cd06615   153 S--MANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGRYPIPPPDAKELEAM 209
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
109-402 3.50e-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: 104.18  E-value: 3.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASlKVRDRvrTKMERDILVEVNH------PFIVKLHYAFQT 182
Cdd:cd14134    12 NRYKILRLLGEGTFGKVLECWDRK---RKRYVAVKIIRNVE-KYREA--AKIEIDVLETLAEkdpngkSHCVQLRDWFDY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLrGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----------DEIGH- 249
Cdd:cd14134    86 RGHMCIVFELL-GPSLYDFLKKNnyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvdsdyvkvynPKKKRq 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 250 --------IKLTDFGLSkeSVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN 321
Cdd:cd14134   165 irvpkstdIKLIDFGSA--TFDDEYHS-SIVSTRHYRAPEVILGLGWSYPCDVWSIGCILVELYTGELLFQTHDNLEHLA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 322 MILKAkLG-MPQFLSAEAQSLLRMLFKRNpanrlgsegveevkrhaffSSIDWNKL-----YKREVQPPFRPasgKPDDT 395
Cdd:cd14134   242 MMERI-LGpLPKRMIRRAKKGAKYFYFYH-------------------GRLDWPEGsssgrSIKRVCKPLKR---LMLLV 298

                  ....*..
gi 1958807372 396 FCFDPEF 402
Cdd:cd14134   299 DPEHRLL 305
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
123-353 4.39e-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: 102.30  E-value: 4.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 123 GKVFLVRKKTGPDAGQLYAMKVLrkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGGDVFTRL 202
Cdd:cd14110    14 GRFSVVRQCEEKRSGQMLAAKII---PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELCSGPELLYNL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 203 SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGlSKESVDQEKKAYS--FCGTVEYMAP 280
Cdd:cd14110    91 AERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLG-NAQPFNQGKVLMTdkKGDYVETMAP 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 281 EVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQSLLRMLFKRNPANR 353
Cdd:cd14110   170 ELLEGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVQLSRCyagLSGGAVNFLKSTLCAKPWGR 245
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
470-717 4.63e-24

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 102.13  E-value: 4.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVckrcIHSAS--NMEFAVKIID--KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD 545
Cdd:cd14058     1 VGRGSFGV----VCKARwrNQIVAVKIIEseSEKKAFEVEVRQLSRV-DHPNIIKLYGACSNQKPVCLVMEYAEGGSLYN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKKKCFSEQEASNVL---YVITKTVEYLHS---QGVVHRDLKPSNILYMdeSGHPDsIKICDFGFA----KQLRGENG 615
Cdd:cd14058    76 VLHGKEPKPIYTAAHAMswaLQCAKGVAYLHSmkpKALIHRDLKPPNLLLT--NGGTV-LKICDFGTAcdisTHMTNNKG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 llltpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSN--GPNdtpEEILLRIGNG-RFSLSggiwDNISR 692
Cdd:cd14058   153 -------SAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHigGPA---FRIMWAVHNGeRPPLI----KNCPK 218
                         250       260
                  ....*....|....*....|....*
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd14058   219 PIESLMTRCWSKDPEKRPSMKEIVK 243
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
461-721 4.99e-24

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: 102.22  E-value: 4.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNME--FAVKIIDKNKRDPSEEIEILM-RYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14112     2 TGRFSFGSEIFRGRFSVIVKAVDSTTETDahCAVKIFEVSDEASEAVREFESlRTLQHENVQRLIAAFKPSNFAYLVMEK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGgELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdESGHPDSIKICDFGFAKQLRGENglL 617
Cdd:cd14112    82 LQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMF--QSVRSWQVKLVDFGRAQKVSKLG--K 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPEVL-TQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDTPEEILLRIGNGRFSLSgGIWDNISRGAKD 696
Cdd:cd14112   157 VPVDGDTDWASPEFHnPETPITVQSDIWGLGVLTFCLLSGFHPFT-SEYDDEEETKENVIFVKCRPN-LIFVEATQEALR 234
                         250       260
                  ....*....|....*....|....*
gi 1958807372 697 LLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14112   235 FATWALKKSPTRRMRTDEALEHRWL 259
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
110-331 5.19e-24

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: 102.94  E-value: 5.19e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLR------KASLKVRdrvrtkmERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd07836     1 NFKQLEKLGEGTYATVYKGRNRT---TGEIVALKEIHldaeegTPSTAIR-------EISLMKELKHENIVRLHDVIHTE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLRGG-----DVFTRLSKEVLFTeedVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07836    71 NKLMLVFEYMDKDlkkymDTHGVRGALDPNT---VKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 259 KESVDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07836   148 RAFGIPVNTFSNEVVTLWYRAPDVlLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRI-MGTP 220
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
117-313 5.45e-24

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: 102.83  E-value: 5.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVflvRKKTGPDAGQLYAMKVLRKASLKvRDRVRTKMERDILVEVNH-PFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd06616    14 IGRGAFGTV---NKMLHKPSGTIMAVKRIRSTVDE-KEQKRLLMDLDVVMRSSDcPYIVKFYGALFREGDCWICMELMDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 G-DVFTRLSKEVLFTE--EDVkfyLAELAL----ALDHLHR-LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDqekk 267
Cdd:cd06616    90 SlDKFYKYVYEVLDSVipEEI---LGKIAVatvkALNYLKEeLKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVD---- 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 268 aySFCGTVE-----YMAPEVVN----RRGHSQSADWWSYGVLMFEMLTGTLPFQG 313
Cdd:cd06616   163 --SIAKTRDagcrpYMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYPK 215
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
108-367 6.59e-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: 102.04  E-value: 6.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLR--KASLKVRDRVRT-KMERDILVEVNHPFIVKlHYAF---Q 181
Cdd:cd06652     1 PTNWRLGKLLGQGAFGRVYLCYDA---DTGRELAVKQVQfdPESPETSKEVNAlECEIQLLKNLLHERIVQ-YYGClrdP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 TEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd06652    77 QERTLSIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VD---QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILKAKLG-----MPQF 333
Cdd:cd06652   157 QTiclSGTGMKSVTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA---EFEAMAAIFKIATQptnpqLPAH 233
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 334 LSAEAQSLLRMLF---KRNPAnrlgsegVEEVKRHAF 367
Cdd:cd06652   234 VSDHCRDFLKRIFveaKLRPS-------ADELLRHTF 263
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
106-311 7.62e-24

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 102.38  E-value: 7.62e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 106 ADPA-QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASlKVRDRVRTkmERDILVEV-NHPFIVKLHYAFQTE 183
Cdd:cd06639    18 ADPSdTWDIIETIGKGTYGKVYKVTNKKD---GSLAAVKILDPIS-DVDEEIEA--EYNILRSLpNHPNVVKFYGMFYKA 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 -----GKLYLILDFLRGGDVfTRLSKEVL-----FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLT 253
Cdd:cd06639    92 dqyvgGQLWLVLELCNGGSV-TELVKGLLkcgqrLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLV 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 254 DFGLSKESVDQEKKAYSFCGTVEYMAPEVV---NRRGHSQSA--DWWSYGVLMFEMLTGTLPF 311
Cdd:cd06639   171 DFGVSAQLTSARLRRNTSVGTPFWMAPEVIaceQQYDYSYDArcDVWSLGITAIELADGDPPL 233
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
450-725 8.22e-24

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: 102.45  E-value: 8.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 450 IVQINGNAAQFS-EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNkrDPSEE-------IEILMRYGQHPNIISL 521
Cdd:cd06618     2 YLTIDGKKYKADlNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRS--GNKEEnkrilmdLDVVLKSHDCPYIVKC 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 522 KEVFDDGKYVYLVTDLMkgGELLDRILK--KKCFSEQEASNVLYVITKTVEYL-HSQGVVHRDLKPSNILyMDESGhpdS 598
Cdd:cd06618    80 YGYFITDSDVFICMELM--STCLDKLLKriQGPIPEDILGKMTVSIVKALHYLkEKHGVIHRDVKPSNIL-LDESG---N 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 599 IKICDFGFAKQL-------RGENgllltpCytANFVAPEVLTQQG---YDAACDIWSLGVLLYTMLAGYTPFSNgpNDTP 668
Cdd:cd06618   154 VKLCDFGISGRLvdskaktRSAG------C--AAYMAPERIDPPDnpkYDIRADVWSLGISLVELATGQFPYRN--CKTE 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 669 EEILLRIGNGRF-SLSGGiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQRE 725
Cdd:cd06618   224 FEVLTKILNEEPpSLPPN--EGFSPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRYE 279
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
452-735 9.63e-24

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: 103.44  E-value: 9.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 452 QINGNAAQFSEAYELKEDIGIGSY-SVCkrcihSASNMEFAVKI-IDKNKRDPSEEI-------EI-LMRYGQHPNIISL 521
Cdd:cd07879     5 EVNKTVWELPERYTSLKQVGSGAYgSVC-----SAIDKRTGEKVaIKKLSRPFQSEIfakrayrELtLLKHMQHENVIGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 522 KEVF------DDGKYVYLVTDLMKGGelLDRILKKKcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESgh 595
Cdd:cd07879    80 LDVFtsavsgDEFQDFYLVMPYMQTD--LQKIMGHP-LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDC-- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 596 pdSIKICDFGFAKQLRGE-NGLLLTPCYTanfvAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFSN----------- 662
Cdd:cd07879   155 --ELKILDFGLARHADAEmTGYVVTRWYR----APEViLNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGkdyldqltqil 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 663 ------GP------NDTPE----EILLRIGNGRFSLsggIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ--- 723
Cdd:cd07879   229 kvtgvpGPefvqklEDKAAksyiKSLPKYPRKDFST---LFPKASPQAVDLLEKMLELDVDKRLTATEALEHPYFDSfrd 305
                         330
                  ....*....|..
gi 1958807372 724 REQLPRHQPTSD 735
Cdd:cd07879   306 ADEETEQQPYDD 317
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
462-719 9.93e-24

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: 100.85  E-value: 9.93e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII------DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14050     1 QCFTILSKLGEGSFGEVFKVRSREDGKLYAVKRSrsrfrgEKDRKRKLEEVERHEKLGEHPNCVRFIKAWEEKGILYIQT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMkGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFAKQLRGENG 615
Cdd:cd14050    81 ELC-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANI-FLSKDG---VCKLGDFGLVVELDKEDI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLT---PCYtanfVAPEVLtqQG-YDAACDIWSLGVllyTMLAGYT----PfSNGPN-------DTPEEILlrigngrf 680
Cdd:cd14050   156 HDAQegdPRY----MAPELL--QGsFTKAADIFSLGI---TILELACnlelP-SGGDGwhqlrqgYLPEEFT-------- 217
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 681 slsggiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14050   218 -------AGLSPELRSIIKLMMDPDPERRPTAEDLLALP 249
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
481-720 1.02e-23

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: 100.89  E-value: 1.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 481 CIHSASNMEFAVKIIdknkRDPSEEIEILMRYGQHPNIISLKEVF--DDGKYVYLVTDLmkgGELLDRILKKKCFSEQEA 558
Cdd:cd14023    14 QLHSGAELQCKVFPL----KHYQDKIRPYIQLPSHRNITGIVEVIlgDTKAYVFFEKDF---GDMHSYVRSCKRLREEEA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 559 SNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsgHPDSIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLTQQG-Y 637
Cdd:cd14023    87 ARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDE--ERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTGtY 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 638 DA-ACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSlsggIWDNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd14023   165 SGkSADVWSLGVMLYTLLVGRYPFH---DSDPSALFSKIRRGQFC----IPDHVSPKARCLIRSLLRREPSERLTAPEIL 237

                  ....
gi 1958807372 717 KHPW 720
Cdd:cd14023   238 LHPW 241
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
104-368 1.05e-23

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: 102.04  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 104 EKADPAQF--DLLKVlGQGSFGKVFLVRKKtgpDAGQLYAMKvlrkaSLKVRDRVRTKM---ERDILVEVNHPFIVKLHY 178
Cdd:cd06658    16 SPGDPREYldSFIKI-GEGSTGIVCIATEK---HTGKQVAVK-----KMDLRKQQRRELlfnEVVIMRDYHHENVVDMYN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 179 AFQTEGKLYLILDFLRGGdVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd06658    87 SYLVGDELWVVMEFLEGG-ALTDIVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFC 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI---LKAKLGMPQFLS 335
Cdd:cd06658   166 AQVSKEVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIrdnLPPRVKDSHKVS 245
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd06658   246 SVLRGFLDLMLVREPSQRATA---QELLQHPFL 275
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
111-331 1.29e-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: 1.29e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkaslkvrdrVRTKME-------RDI--LVEVNHPFIVKLHYAFQ 181
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKL---TGEVVALKKIR---------LDTETEgvpstaiREIslLKELNHPNIVKLLDVIH 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 TEGKLYLILDFLRGgDV--FTRLSKEVLFTEEDVKFYLAEL--ALALDHLHRlgIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd07860    70 TENKLYLVFEFLHQ-DLkkFMDASALTGIPLPLIKSYLFQLlqGLAFCHSHR--VLHRDLKPQNLLINTEGAIKLADFGL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 258 SKeSVDQEKKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07860   147 AR-AFGVPVRTYTHeVVTLWYRAPEIlLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRT-LGTP 220
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
462-698 1.41e-23

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: 103.58  E-value: 1.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEI-------EILMRyGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVghiraerDILVE-ADSLWVVKMFYSFQDKLNLYLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQL---- 610
Cdd:cd05628    80 MEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLL-LDSKGH---VKLSDFGLCTGLkkah 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 -------------------------------RGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTP 659
Cdd:cd05628   156 rtefyrnlnhslpsdftfqnmnskrkaetwkRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYPP 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 660 FSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLL 698
Cdd:cd05628   236 FC---SETPQETYKKVMNWKETLIFPPEVPISEKAKDLI 271
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
110-365 1.43e-23

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: 100.69  E-value: 1.43e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASL----KVRDRVRTKMERDILVEV----NHPFIVKLHYAFQ 181
Cdd:cd14101     1 QYTMGNLLGKGGFGTVYAGHRISD---GLQVAIKQISRNRVqqwsKLPGVNPVPNEVALLQSVgggpGHRGVIRLLDWFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 TEGKLYLILDF-LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLTDFGlsK 259
Cdd:cd14101    78 IPEGFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLIDFG--S 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPFQgKDRNetmnmILKAKLGMPQFLSAEA 338
Cdd:cd14101   156 GATLKDSMYTDFDGTRVYSPPEWILYHQyHALPATVWSLGILLYDMVCGDIPFE-RDTD-----ILKAKPSFNKRVSNDC 229
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 339 QSLLRMLFKRNPANRlgsEGVEEVKRH 365
Cdd:cd14101   230 RSLIRSCLAYNPSDR---PSLEQILLH 253
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
117-368 1.48e-23

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: 101.72  E-value: 1.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVrkkTGPDAGQLYAMKVLRKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd06655    27 IGQGASGTVFTA---IDVATGQEVAIKQINLQKQPKKELIINEIL--VMKELKNPNIVNFLDSFLVGDELFVVMEYLAGG 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVfTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCGTVE 276
Cdd:cd06655   102 SL-TDVVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 277 YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQFLSAEAQS-LLRMLFKRNPANRLG 355
Cdd:cd06655   181 WMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYL--NENPLRALYLIATNGTPELQNPEKLSpIFRDFLNRCLEMDVE 258
                         250
                  ....*....|....
gi 1958807372 356 SEG-VEEVKRHAFF 368
Cdd:cd06655   259 KRGsAKELLQHPFL 272
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
490-720 1.49e-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: 102.43  E-value: 1.49e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKIIDKN---KRDPS----EEIEILMRyGQHPNIISLKEVFDDGKYVYLVTDLMKGGELL-------DRIlkkkcfSE 555
Cdd:cd05597    29 YAMKILNKWemlKRAETacfrEERDVLVN-GDRRWITKLHYAFQDENYLYLVMDYYCGGDLLtllskfeDRL------PE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 556 QEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgENGLL--LTPCYTANFVAPEVLT 633
Cdd:cd05597   102 EMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVL-LDRNGH---IRLADFGSCLKLR-EDGTVqsSVAVGTPDYISPEILQ 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 634 -----QQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGN--GRFSLSGGIwDNISRGAKDLLSHMLhMDP 706
Cdd:cd05597   177 amedgKGRYGPECDWWSLGVCMYEMLYGETPFY---AESLVETYGKIMNhkEHFSFPDDE-DDVSEEAKDLIRRLI-CSR 251
                         250
                  ....*....|....*..
gi 1958807372 707 HQRY---TAEQVLKHPW 720
Cdd:cd05597   252 ERRLgqnGIDDFKKHPF 268
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
111-332 1.73e-23

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 101.20  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKvlrkaslKVR-----DRVRTKMERDI-----LVEVNHPFIVKLH--- 177
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQD---GRFVALK-------KVRvplseEGIPLSTIREIallkqLESFEHPNVVRLLdvc 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 --YAFQTEGKLYLILDFLRGgDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLT 253
Cdd:cd07838    71 hgPRTDRELKLTLVFEHVDQ-DLATYLDKcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 254 DFGLSkesvdqekKAYSF-------CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKa 326
Cdd:cd07838   150 DFGLA--------RIYSFemaltsvVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFD- 220

                  ....*.
gi 1958807372 327 KLGMPQ 332
Cdd:cd07838   221 VIGLPS 226
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
106-368 2.05e-23

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: 101.34  E-value: 2.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 106 ADPAQ-FDLLKVLGQGSFGKVFlvrkkTGPD--AGQLYAMKVLRKASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQT 182
Cdd:cd06656    15 GDPKKkYTRFEKIGQGASGTVY-----TAIDiaTGQEVAIKQMNLQQQPKKELIINEIL--VMRENKNPNIVNYLDSYLV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 262
Cdd:cd06656    88 GDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL---KAKLGMPQFLSAEAQ 339
Cdd:cd06656   167 PEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIAtngTPELQNPERLSAVFR 246
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 340 SLLRMLFKRNpANRLGSegVEEVKRHAFF 368
Cdd:cd06656   247 DFLNRCLEMD-VDRRGS--AKELLQHPFL 272
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
117-313 2.38e-23

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: 100.83  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLRkasLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILDFL 193
Cdd:cd07835     7 IGEGTYGVVYKARDKLT---GEIVALKKIR---LETEDEgVPSTAIREIslLKELNHPNIVRLLDVVHSENKLYLVFEFL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 rggDV----FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAY 269
Cdd:cd07835    81 ---DLdlkkYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLAR-AFGVPVRTY 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 270 SF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQG 313
Cdd:cd07835   157 THeVVTLWYRAPEIlLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPG 202
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
111-322 2.38e-23

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 99.98  E-value: 2.38e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLrkaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14108     4 YDIHKEIGRGAFSYLRRVKEKS---SDLSFAAKFI---PVRAKKKTSARRELALLAELDHKSIVRFHDAFEKRRVVIIVT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG--HIKLTDFGLSKESVDQEKKa 268
Cdd:cd14108    78 E-LCHEELLERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPNEPQ- 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK-DRNETMNM 322
Cdd:cd14108   156 YCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPFVGEnDRTTLMNI 210
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
525-720 2.55e-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: 102.44  E-value: 2.55e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 525 FDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDF 604
Cdd:cd05627    71 FQDKRNLYLIMEFLPGGDMMTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLL-LDAKGH---VKLSDF 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 605 GFAKQLR-----------------------------------GENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVL 649
Cdd:cd05627   147 GLCTGLKkahrtefyrnlthnppsdfsfqnmnskrkaetwkkNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVI 226
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 650 LYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLhMDPHQRY---TAEQVLKHPW 720
Cdd:cd05627   227 MYEMLIGYPPFC---SETPQETYRKVMNWKETLVFPPEVPISEKAKDLILRFC-TDAENRIgsnGVEEIKSHPF 296
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
111-436 2.77e-23

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 101.66  E-value: 2.77e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERDILV--EVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd06649     7 FERISELGAGNGGVVTKVQHKP---SGLIMARKLIH---LEIKPAIRNQIIRELQVlhECNSPYIVGFYGAFYSDGEISI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHL-HRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQekK 267
Cdd:cd06649    81 CMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDS--M 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNEtmnmiLKAKLGMPQFLSAEAQSLLRMLFK 347
Cdd:cd06649   159 ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAKE-----LEAIFGRPVVDGEEGEPHSISPRP 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 348 RNPANRLGSEGVEEVKRHAFFSSIDwnklYKREVQPPFRPASgkpddtfCFDPEFTAKTPKDSPGLPASANAHQLFKGFS 427
Cdd:cd06649   234 RPPGRPVSGHGMDSRPAMAIFELLD----YIVNEPPPKLPNG-------VFTPDFQEFVNKCLIKNPAERADLKMLMNHT 302

                  ....*....
gi 1958807372 428 FVATSIAEE 436
Cdd:cd06649   303 FIKRSEVEE 311
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
462-719 2.87e-23

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: 101.08  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII-----DKNKRdpseEIEILMRYGQHPNIISLKEVFDDG--KYVYLV 534
Cdd:cd14132    18 DDYEIIRKIGRGKYSEVFEGINIGNNEKVVIKVLkpvkkKKIKR----EIKILQNLRGGPNIVKLLDVVKDPqsKTPSLI 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKkkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmDESghPDSIKICDFGFAKqlrgen 614
Cdd:cd14132    94 FEYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMI-DHE--KRKLRLIDWGLAE------ 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 gllltpCYTAN-----------FVAPEVLTQ-QGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRI-----GN 677
Cdd:cd14132   162 ------FYHPGqeynvrvasryYKGPELLVDyQYYDYSLDMWSLGCMLASMIFRKEPFFHGHDN--YDQLVKIakvlgTD 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 678 GRF--------SLSGGIWDNISRGAK--------------------DLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14132   234 DLYayldkygiELPPRLNDILGRHSKkpwerfvnsenqhlvtpealDLLDKLLRYDHQERITAKEAMQHP 303
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
108-348 3.15e-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: 101.60  E-value: 3.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKV-FLVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd07851    14 PDRYQNLSPVGSGAYGQVcSAFDTKTG----RKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 ------YLILDFLrGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd07851    90 edfqdvYLVTHLM-GADLNNIVKCQKL-SDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SvdqEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQ--FL--- 334
Cdd:cd07851   168 T---DDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNL-VGTPDeeLLkki 243
                         250
                  ....*....|....*
gi 1958807372 335 -SAEAQSLLRMLFKR 348
Cdd:cd07851   244 sSESARNYIQSLPQM 258
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
109-370 3.97e-23

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: 101.29  E-value: 3.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL- 186
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCsAIDTKSG----QKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYa 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 -----YLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG----L 257
Cdd:cd07855    81 dfkdvYVVLD-LMESDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGmargL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP--QFL 334
Cdd:cd07855   160 CTSPEEHKYFMTEYVATRWYRAPELMlSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTV-LGTPsqAVI 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 335 SA------------------------------EAQSLLRMLFKRNPANRLgseGVEEVKRHAFFSS 370
Cdd:cd07855   239 NAigadrvrryiqnlpnkqpvpwetlypkadqQALDLLSQMLRFDPSERI---TVAEALQHPFLAK 301
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
461-721 5.11e-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: 5.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKnKRDPSEEIE----ILMRYGQHPNIISLKEVF-----DDGKYV 531
Cdd:cd06638    17 SDTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDP-IHDIDEEIEaeynILKALSDHPNVVKFYGMYykkdvKNGDQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRI---LKK-KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdsIKICDFGFA 607
Cdd:cd06638    96 WLVLELCNGGSVTDLVkgfLKRgERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGG----VKLVDFGVS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQLRGENGLLLTPCYTANFVAPEVLT--QQ---GYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIG-NGRFS 681
Cdd:cd06638   172 AQLTSTRLRRNTSVGTPFWMAPEVIAceQQldsTYDARCDVWSLGITAIELGDGDPPLA---DLHPMRALFKIPrNPPPT 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 682 L-SGGIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06638   249 LhQPELW---SNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
464-719 5.12e-23

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: 100.07  E-value: 5.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKII-DKNKRDPSEEIEI----LMRYGQHPNIISLKEVFDDGKYVYLVTDLM 538
Cdd:cd07848     3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFkDSEENEEVKETTLrelkMLRTLKQENIVELKEAFRRRGKLYLVFEYV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGG--ELLDRIlkKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQL-RGENG 615
Cdd:cd07848    83 EKNmlELLEEM--PNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLI----SHNDVLKLCDFGFARNLsEGSNA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPNDT--------------PEEILLRIGNGRF- 680
Cdd:cd07848   157 NYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDG-QPLFPGESEIdqlftiqkvlgplpAEQMKLFYSNPRFh 235
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 681 -----------SLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd07848   236 glrfpavnhpqSLERRYLGILSGVLLDLMKNLLKLNPTDRYLTEQCLNHP 285
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
117-353 5.83e-23

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 99.05  E-value: 5.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKASLKVRDRVrtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14058     1 VGRGSFGVVCKARWR-----NQIVAVKIIESESEKKAFEV----EVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRL-SKEVL--FTEEDVKFYLAELALALDHLHRLG---IVYRDLKPENILLDEIGH-IKLTDFGLSkesVDQEKKAY 269
Cdd:cd14058    72 SLYNVLhGKEPKpiYTAAHAMSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTA---CDISTHMT 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIL---KAKLGMPQFLSAEAQSLLRMLF 346
Cdd:cd14058   149 NNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIGGPAFRIMWAvhnGERPPLIKNCPKPIESLMTRCW 228

                  ....*..
gi 1958807372 347 KRNPANR 353
Cdd:cd14058   229 SKDPEKR 235
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
114-325 8.08e-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: 99.18  E-value: 8.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLR-KASLKVRDRVRTKMErdILVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd06619     6 QEILGHGNGGTVY---KAYHLLTRRILAVKVIPlDITVELQKQIMSELE--ILYKCDSPYIIGFYGAFFVENRISICTEF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGG--DVFTRLSKEVLfteedvkfylAELALA----LDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd06619    81 MDGGslDVYRKIPEHVL----------GRIAVAvvkgLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIA 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 267 KAYsfCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK 325
Cdd:cd06619   151 KTY--VGTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPYPQIQKNQGSLMPLQ 207
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
113-353 8.65e-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: 99.27  E-value: 8.65e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKV---FLVRKKTGPDAGQLyAMKVLRKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd05045     4 LGKTLGEGEFGKVvkaTAFRLKGRAGYTTV-AVKMLKENASSSELRDLLS-EFNLLKQVNHPHVIKLYGACSQDGPLLLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDV--FTRLSKEV----------------------LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD 245
Cdd:cd05045    82 VEYAKYGSLrsFLRESRKVgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLVA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 246 EIGHIKLTDFGLSKESVDQEKKAYSFCG--TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNM 322
Cdd:cd05045   162 EGRKMKISDFGLSRDVYEEDSYVKRSKGriPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGIAPERLFNL 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 323 iLKAKLGM--PQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05045   242 -LKTGYRMerPENCSEEMYNLMLTCWKQEPDKR 273
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
106-342 9.51e-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: 99.41  E-value: 9.51e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 106 ADPAQ-FDLLKVLGQGSFGKVFlvrkkTGPD--AGQLYAmkvLRKASLKVRDRvRTKMERDILV--EVNHPFIVKLHYAF 180
Cdd:cd06654    16 GDPKKkYTRFEKIGQGASGTVY-----TAMDvaTGQEVA---IRQMNLQQQPK-KELIINEILVmrENKNPNIVNYLDSY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 QTEGKLYLILDFLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd06654    87 LVGDELWVVMEYLAGGSL-TDVVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMPQFLSAEAQS 340
Cdd:cd06654   166 ITPEQSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMIEGEPPYL--NENPLRALYLIATNGTPELQNPEKLS 243

                  ..
gi 1958807372 341 LL 342
Cdd:cd06654   244 AI 245
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
107-353 1.04e-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: 98.29  E-value: 1.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd05059     2 DPSELTFLKELGSGQFGVVHLGKWRGKIDV----AIKMIKEGSMSEDDFIE---EAKVMMKLSHPKLVQLYGVCTKQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDV--FTRLSKEVLFTEedvkfYLAELAL----ALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd05059    75 FIVTEYMANGCLlnYLRERRGKFQTE-----QLLEMCKdvceAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARY 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAySFcGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 335
Cdd:cd05059   150 VLDDEYTS-SV-GTkfpVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEHISQGyRLYRPHLAP 227
                         250
                  ....*....|....*...
gi 1958807372 336 AEAQSLLRMLFKRNPANR 353
Cdd:cd05059   228 TEVYTIMYSCWHEKPEER 245
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
480-721 1.14e-22

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: 97.64  E-value: 1.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 480 RCIHSASNMEFAVKIIdkNKRDPSEEIEILMRYGQHPNIISLKEVF--DDGKYVYLVTDLmkgGELLDRILKKKCFSEQE 557
Cdd:cd14024    11 RAEHYQTEKEYTCKVL--SLRSYQECLAPYDRLGPHEGVCSVLEVVigQDRAYAFFSRHY---GDMHSHVRRRRRLSEDE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 558 ASNVLYVITKTVEYLHSQGVVHRDLKpsnilymdesghpdsikICDFGFAKQLRGENGLL-LTPCYTAN----------- 625
Cdd:cd14024    86 ARGLFTQMARAVAHCHQHGVILRDLK-----------------LRRFVFTDELRTKLVLVnLEDSCPLNgdddsltdkhg 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 626 ---FVAPEVL-TQQGYDA-ACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGiwdnISRGAKDLLSH 700
Cdd:cd14024   149 cpaYVGPEILsSRRSYSGkAADVWSLGVCLYTMLLGRYPFQ---DTEPAALFAKIRRGAFSLPAW----LSPGARCLVSC 221
                         250       260
                  ....*....|....*....|.
gi 1958807372 701 MLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14024   222 MLRRSPAERLKASEILLHPWL 242
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
470-666 1.22e-22

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: 100.07  E-value: 1.22e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDVEctmvekrVLALQDKPPFLTQLHSCFQTVDRLYFVMEYVNGGD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCY 622
Cdd:cd05615    98 LMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVM-LDSEGH---IKIADFGMCKEHMVEGVTTRTFCG 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPND 666
Cdd:cd05615   174 TPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDED 217
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
110-331 1.39e-22

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: 97.91  E-value: 1.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLkvrdRVRTKMERDILVEVN-HPFIVKLHYAFQTEGKLYL 188
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKT---GEEVAIKIEKKDSK----HPQLEYEAKVYKLLQgGPGIPRLYWFGQEGDYNVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLrGGDVftrlskEVLFTEEDVKF------YLAELALA-LDHLHRLGIVYRDLKPENILL---DEIGHIKLTDFGLS 258
Cdd:cd14016    74 VMDLL-GPSL------EDLFNKCGRKFslktvlMLADQMISrLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQE-------KKAYSFCGTVEYMApevVNR-RGHSQSA--DWWSYG-VLMFeMLTGTLPFQG---KDRNETMNMIL 324
Cdd:cd14016   147 KKYRDPRtgkhipyREGKSLTGTARYAS---INAhLGIEQSRrdDLESLGyVLIY-FLKGSLPWQGlkaQSKKEKYEKIG 222

                  ....*..
gi 1958807372 325 KAKLGMP 331
Cdd:cd14016   223 EKKMNTS 229
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
117-368 1.44e-22

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 97.73  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKV---FLVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGkLYLILDFL 193
Cdd:cd05116     3 LGSGNFGTVkkgYYQMKKVV----KTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAES-WMLVMEMA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYSFCG 273
Cdd:cd05116    78 ELGPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSK-ALRADENYYKAQT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 T----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRMLFK 347
Cdd:cd05116   157 HgkwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQMIEKGErMECPAGCPPEMYDLMKLCWT 236
                         250       260
                  ....*....|....*....|.
gi 1958807372 348 RNPANRLGSEGVEEVKRHAFF 368
Cdd:cd05116   237 YDVDERPGFAAVELRLRNYYY 257
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
460-660 1.54e-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: 98.19  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEaYELKEDIGIGSYSVCKRCIHSASnmEFAVKiidKNKRDPSEEIE----------ILMRYGQHPNIISLKEVFDDGK 529
Cdd:cd14145     5 FSE-LVLEEIIGIGGFGKVYRAIWIGD--EVAVK---AARHDPDEDISqtienvrqeaKLFAMLKHPNIIALRGVCLKEP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 530 YVYLVTDLMKGGELlDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVV---HRDLKPSNILYMDESGHPD----SIKIC 602
Cdd:cd14145    79 NLCLVMEFARGGPL-NRVLSGKRIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILEKVENGDlsnkILKIT 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 603 DFGFAKQLRGENGLLLTPCYTanFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14145   158 DFGLAREWHRTTKMSAAGTYA--WMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
161-353 1.68e-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: 98.16  E-value: 1.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 161 ERDILVEVNHPFIVKLHYAFQTE-GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHL--HRLGIVYRDL 237
Cdd:cd13990    54 EYEIHKSLDHPRIVKLYDVFEIDtDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDL 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 238 KPENILLDEI---GHIKLTDFGLSKEsVDQEKKAYS-------FCGTVEYMAPEVVNRRGH----SQSADWWSYGVLMFE 303
Cdd:cd13990   134 KPGNILLHSGnvsGEIKITDFGLSKI-MDDESYNSDgmeltsqGAGTYWYLPPECFVVGKTppkiSSKVDVWSVGVIFYQ 212
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 304 MLTGTLPFqGKDRNETM----NMILKAKLGmpQF-----LSAEAQSLLRMLFKRNPANR 353
Cdd:cd13990   213 MLYGRKPF-GHNQSQEAileeNTILKATEV--EFpskpvVSSEAKDFIRRCLTYRKEDR 268
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
470-738 2.14e-22

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 98.14  E-value: 2.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05631     8 LGKGGFGEVCACQVRATGKMYACKKLEKKriKKRKGEamalnEKRILEKV-NSRFVVSLAYAYETKDALCLVLTIMNGGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRI--LKKKCFSEQEAsnVLYV--ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQL------RG 612
Cdd:cd05631    87 LKFHIynMGNPGFDEQRA--IFYAaeLCCGLEDLQRERIVYRDLKPENIL-LDDRGH---IRISDLGLAVQIpegetvRG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGllltpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTP-EEILLRIGNGRFSLSggiwDNIS 691
Cdd:cd05631   161 RVG-------TVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKrEEVDRRVKEDQEEYS----EKFS 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 692 RGAKDLLSHMLHMDPHQRY-----TAEQVLKHPwITQREQLPRHQPTSDDPP 738
Cdd:cd05631   230 EDAKSICRMLLTKNPKERLgcrgnGAAGVKQHP-IFKNINFKRLEANMLEPP 280
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
490-718 2.19e-22

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: 97.75  E-value: 2.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVK-IIDKNKRDPSE---EIEILMRYgQHPNIISL-----KEVFDDGKYVYLVTDLMKGGELLDRI----LKKKCFSEQ 556
Cdd:cd13986    28 YALKkILCHSKEDVKEamrEIENYRLF-NHPNILRLldsqiVKEAGGKKEVYLLLPYYKRGSLQDEIerrlVKGTFFPED 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 557 EASNVLYVITKTVEYLHSQ---GVVHRDLKPSNILyMDESGHPdsiKICDFGFAKQLR----------------GENGll 617
Cdd:cd13986   107 RILHIFLGICRGLKAMHEPelvPYAHRDIKPGNVL-LSEDDEP---ILMDLGSMNPARieiegrrealalqdwaAEHC-- 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 ltpcyTANFVAPE---VLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngpndtpEEIL-------LRIGNGRFSLSGGiw 687
Cdd:cd13986   181 -----TMPYRAPElfdVKSHCTIDEKTDIWSLGCTLYALMYGESPF--------ERIFqkgdslaLAVLSGNYSFPDN-- 245
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1958807372 688 DNISRGAKDLLSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd13986   246 SRYSEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
468-720 2.42e-22

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: 97.96  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PSEEI-EI-LMRYGQHPNIISLKEVFDDGKYVYLVTdlmkggE 542
Cdd:cd07860     6 EKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETegvPSTAIrEIsLLKELNHPNIVKLLDVIHTENKLYLVF------E 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKK--KCFSEQEAS-----NVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrgenG 615
Cdd:cd07860    80 FLHQDLKKfmDASALTGIPlplikSYLFQLLQGLAFCHSHRVLHRDLKPQNLL-INTEGA---IKLADFGLARAF----G 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTpCYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIW-- 687
Cdd:cd07860   152 VPVR-TYTHEVVtlwyrAPEILLgCKYYSTAVDIWSLGCIFAEMVTRRALF---PGDSEIDQLFRIFRTLGTPDEVVWpg 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 688 -----------------------DNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07860   228 vtsmpdykpsfpkwarqdfskvvPPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
468-726 2.49e-22

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: 97.88  E-value: 2.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYGQHPNIISL-KEVFDDGKyVYLVTDLMKGG 541
Cdd:cd06617     7 EELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQkrllmDLDISMRSVDCPYTVTFyGALFREGD-VWICMEVMDTS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 elLDRILKK-----KCFSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrgENG 615
Cdd:cd06617    86 --LDKFYKKvydkgLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVL-INRNGQ---VKLCDFGISGYL--VDS 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTP---CytANFVAPE----VLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGpnDTPEEILL--------RIGNGRF 680
Cdd:cd06617   158 VAKTIdagC--KPYMAPErinpELNQKGYDVKSDVWSLGITMIELATGRFPYDSW--KTPFQQLKqvveepspQLPAEKF 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 681 SLSggiwdnisrgAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQ 726
Cdd:cd06617   234 SPE----------FQDFVNKCLKKNYKERPNYPELLQHPFFELHLS 269
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
471-723 2.71e-22

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: 98.03  E-value: 2.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 471 GIGSYSVCKRcihSASNMEFAVKIIDKN---KRDPSE----EIEILMRYgqHPN-IISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05608    13 GFGEVSACQM---RATGKLYACKKLNKKrlkKRKGYEgamvEKRILAKV--HSRfIVSLAYAFQTKTDLCLVMTIMNGGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRIL----KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgeNGLLL 618
Cdd:cd05608    88 LRYHIYnvdeENPGFQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVL-LDDDGN---VRISDLGLAVELK--DGQTK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 TPCY--TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIGNGRFSLSggiwDNISRGAK 695
Cdd:cd05608   162 TKGYagTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAARGPFrARGEKVENKELKQRILNDSVTYS----EKFSPASK 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 696 DLLSHMLHMDPHQRY-----TAEQVLKHPWITQ 723
Cdd:cd05608   238 SICEALLAKDPEKRLgfrdgNCDGLRTHPFFRD 270
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
110-353 2.77e-22

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: 97.61  E-value: 2.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd06622     2 EIEVLDELGKGNYGSVYKVLHRP---TGVTMAMKEIR-LELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGG--DVFTRLSKEVLFTEEDVkfyLAELALALDHLHR-----LGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 262
Cdd:cd06622    78 MEYMDAGslDKLYAGGVATEGIPEDV---LRRITYAVVKGLKflkeeHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTveYMAPEVVNRRGHSQ------SADWWSYGVLMFEMLTGTLPFQgkdrNETMNMILkAKL-------- 328
Cdd:cd06622   155 ASLAKTNIGCQS--YMAPERIKSGGPNQnptytvQSDVWSLGLSILEMALGRYPYP----PETYANIF-AQLsaivdgdp 227
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 329 -GMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd06622   228 pTLPSGYSDDAQDFVAKCLNKIPNRR 253
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
107-367 3.26e-22

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: 97.39  E-value: 3.26e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFLV-RKKTGpdagqlyamkvlRKASLKVRDRVRtKMERDILVEVN-------HPFIVKLH 177
Cdd:cd06638    15 DPSDtWEIIETIGKGTYGKVFKVlNKKNG------------SKAAVKILDPIH-DIDEEIEAEYNilkalsdHPNVVKFY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 YAF-----QTEGKLYLILDFLRGGDVfTRLSKEVL-----FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI 247
Cdd:cd06638    82 GMYykkdvKNGDQLWLVLELCNGGSV-TDLVKGFLkrgerMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 322
Cdd:cd06638   161 GGVKLVDFGVSAQLTSTRLRRNTSVGTPFWMAPEVIAceqqlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 323 ILK---AKLGMPQFLSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd06638   241 IPRnppPTLHQPELWSNEFNDFIRKCLTKDYEKR---PTVSDLLQHVF 285
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
470-760 3.61e-22

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: 99.32  E-value: 3.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSY-SVCKRC---IHSASNMEFAVK--IIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd05626     9 LGIGAFgEVCLACkvdTHALYAMKTLRKkdVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGDM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLR------------ 611
Cdd:cd05626    89 MSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNIL-IDLDGH---IKLTDFGLCTGFRwthnskyyqkgs 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 ---------------------GENGLLLTP--------CY------TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAG 656
Cdd:cd05626   165 hirqdsmepsdlwddvsncrcGDRLKTLEQratkqhqrCLahslvgTPNYIAPEVLLRKGYTQLCDWWSVGVILFEMLVG 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 657 YTPFSnGPndTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQ--RYTAEQVLKHPWITQ-------REQL 727
Cdd:cd05626   245 QPPFL-AP--TPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSAEERlgRNGADDIKAHPFFSEvdfssdiRTQP 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 728 PRHQPT--------------SDDPPQVVMEAVAAAYSVLARNQNRHP 760
Cdd:cd05626   322 APYVPKishpmdtsnfdpveEESPWNDASGDSTRTWDTLCSPNGKHP 368
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
468-721 4.83e-22

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: 96.14  E-value: 4.83e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFA---VKIIDKNKRDP---SEEIEILMRYgQHPNIISLKEVFDDG--KYVYLVTDLMK 539
Cdd:cd13983     7 EVLGRGSFKTVYRAFDTEEGIEVAwneIKLRKLPKAERqrfKQEIEILKSL-KHPNIIKFYDSWESKskKEVIFITELMT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLD----------RILKKKCfsEQeasnvlyvITKTVEYLHSQG--VVHRDLKPSNILYmdeSGHPDSIKICDFGFA 607
Cdd:cd13983    86 SGTLKQylkrfkrlklKVIKSWC--RQ--------ILEGLNYLHTRDppIIHRDLKCDNIFI---NGNTGEVKIGDLGLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQLRGE--NGLLLTPcytaNFVAPEVLtQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLRIGNGRF--SLs 683
Cdd:cd13983   153 TLLRQSfaKSVIGTP----EFMAPEMY-EEHYDEKVDIYAFGMCLLEMATGEYPYSECTN--AAQIYKKVTSGIKpeSL- 224
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 684 ggiwDNI-SRGAKDLLSHMLhMDPHQRYTAEQVLKHPWI 721
Cdd:cd13983   225 ----SKVkDPELKDFIEKCL-KPPDERPSARELLEHPFF 258
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
110-315 5.41e-22

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: 96.64  E-value: 5.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrkkTGPDAGQLYAMKVLRK---ASLKVRDRvRTKMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd14147     4 ELRLEEVIGIGGFGKVY-----RGSWRGELVAVKAARQdpdEDISVTAE-SVRQEARLFAMLAHPNIIALKAVCLEEPNL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFT-----RLSKEVLFTeedvkfYLAELALALDHLHRLGIV---YRDLKPENILL------DEIGH--I 250
Cdd:cd14147    78 CLVMEYAAGGPLSRalagrRVPPHVLVN------WAVQIARGMHYLHCEALVpviHRDLKSNNILLlqpienDDMEHktL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 251 KLTDFGLSKESvdQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKD 315
Cdd:cd14147   152 KITDFGLAREW--HKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGID 214
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
114-360 5.58e-22

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: 97.00  E-value: 5.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd07871    10 LDKLGEGTYATVFKGRSKL---TENLVALKEIR---LEHEEGAPCTAIREVslLKNLKHANIVTLHDIIHTERCLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGgDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd07871    84 YLDS-DLKQYLDNcGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSVPTKTYSN 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQ----------------- 332
Cdd:cd07871   163 EVVTLWYRPPDVlLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRL-LGTPTeetwpgvtsneefrsyl 241
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 333 FLSAEAQSLLrmlfkrNPANRLGSEGVE 360
Cdd:cd07871   242 FPQYRAQPLI------NHAPRLDTDGID 263
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
470-720 6.28e-22

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 97.05  E-value: 6.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIID-KNKRD-----PSEEIEILMRYgQHPNIISLKEVFDdGKY---VYLVT----- 535
Cdd:cd07845    15 IGEGTYGIVYRARDTTSGEIVALKKVRmDNERDgipisSLREITLLLNL-RHPNIVELKEVVV-GKHldsIFLVMeyceq 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLmkgGELLDRIlkKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsGHpdsIKICDFGFAKQLrGENG 615
Cdd:cd07845    93 DL---ASLLDNM--PTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDK-GC---LKIADFGLARTY-GLPA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPC-YTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGyTPFSNGPND------------TPEEillRI------ 675
Cdd:cd07845   163 KPMTPKvVTLWYRAPELLLgCTTYTTAIDMWAVGCILAELLAH-KPLLPGKSEieqldliiqllgTPNE---SIwpgfsd 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 676 --GNGRFSLSGGIWDN-------ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07845   239 lpLVGKFTLPKQPYNNlkhkfpwLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
464-709 6.75e-22

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: 96.25  E-value: 6.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemmdaKARQDCVKEIDLLKQL-NHPNVIKYLDSFIEDNELNIVLE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRIL----KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFG----FAK 608
Cdd:cd08228    83 LADAGDLSQMIKyfkkQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANV-FITATG---VVKLGDLGlgrfFSS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 QLRGENGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTpeeillrigngrFSLSGGI-- 686
Cdd:cd08228   159 KTTAAHSLVGTPYY----MSPERIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNL------------FSLCQKIeq 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 687 -------WDNISRGAKDLLSHMLHMDPHQR 709
Cdd:cd08228   223 cdypplpTEHYSEKLRELVSMCIYPDPDQR 252
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
462-728 7.11e-22

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 96.81  E-value: 7.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PSEEI-EI-LMRYGQHPNIISLKEVFDDGKYVYLVTd 536
Cdd:PLN00009    2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDegvPSTAIrEIsLLKEMQHGNIVRLQDVVHSEKRLYLVF- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 lmkggELLDRILKKKCFSEQEASN-------VLYVITKTVEYLHSQGVVHRDLKPSNILyMDESghPDSIKICDFGFAKQ 609
Cdd:PLN00009   81 -----EYLDLDLKKHMDSSPDFAKnprliktYLYQILRGIAYCHSHRVLHRDLKPQNLL-IDRR--TNALKLADFGLARA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRGENGLLLTPCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIgngrFSLSG---- 684
Cdd:PLN00009  153 FGIPVRTFTHEVVTLWYRAPEILLgSRHYSTPVDIWSVGCIFAEMVNQKPLF---PGDSEIDELFKI----FRILGtpne 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 685 GIW-------------------------DNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQLP 728
Cdd:PLN00009  226 ETWpgvtslpdyksafpkwppkdlatvvPTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLGDAP 294
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
470-719 7.92e-22

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 96.25  E-value: 7.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDPSE-----EIEILMRYGQHpNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05630     8 LGKGGFGEVCACQVRATGKMYACKKLEKKriKKRKGEamalnEKQILEKVNSR-FVVSLAYAYETKDALCLVLTLMNGGD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRI--LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFA------KQLRGEN 614
Cdd:cd05630    87 LKFHIyhMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENIL-LDDHGH---IRISDLGLAvhvpegQTIKGRV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GllltpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTP-EEI--LLRIGNGRFSlsggiwDNIS 691
Cdd:cd05630   163 G-------TVGYMAPEVVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKrEEVerLVKEVPEEYS------EKFS 229
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 692 RGAKDLLSHMLHMDPHQRY-----TAEQVLKHP 719
Cdd:cd05630   230 PQARSLCSMLLCKDPAERLgcrggGAREVKEHP 262
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
107-353 8.41e-22

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 95.70  E-value: 8.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd05114     2 NPSELTFMKELGSGLFGVVRLGKWRAQYKV----AIKAIREGAMSEEDFIE---EAKVMMKLTHPKLVQLYGVCTQQKPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGDVFT-------RLSKEVLFTeedvkfYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd05114    75 YIVTEFMENGCLLNylrqrrgKLSRDMLLS------MCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVDQEKKaySFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFL 334
Cdd:cd05114   149 YVLDDQYT--SSSGAkfpVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSNYEVVEMVSRGhRLYRPKLA 226
                         250
                  ....*....|....*....
gi 1958807372 335 SAEAQSLLRMLFKRNPANR 353
Cdd:cd05114   227 SKSVYEVMYSCWHEKPEGR 245
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
463-719 8.58e-22

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 95.95  E-value: 8.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 463 AYELKEDIGIGSYS-VCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMR--YGQHPNIISLKEVFDDGKYVYL 533
Cdd:cd14052     1 RFANVELIGSGEFSqVYKVSERVPTGKVYAVKKLKPNYAGAKdrlrrlEEVSILREltLDGHDNIVQLIDSWEYHGHLYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGEL---LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdsIKICDFGFAKQL 610
Cdd:cd14052    81 QTELCENGSLdvfLSELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGT----LKIGDFGMATVW 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTPcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGP----------NDTPEEILLRIGN-GR 679
Cdd:cd14052   157 PLIRGIEREG--DREYIAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNGDawqklrsgdlSDAPRLSSTDLHSaSS 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 680 FSLSGGIWD-NISRGAKDL---LSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14052   235 PSSNPPPDPpNMPILSGSLdrvVRWMLSPEPDRRPTADDVLATP 278
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
110-331 8.60e-22

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: 97.37  E-value: 8.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR----------KKTGPDAGQLYAMKVLRkaslkvrdrvrtkmERDILVEVNHPFIVKLH-- 177
Cdd:cd07849     6 RYQNLSYIGEGAYGMVCSAVhkptgqkvaiKKISPFEHQTYCLRTLR--------------EIKILLRFKHENIIGILdi 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 ---YAFQTEGKLYLILDFLRGgDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd07849    72 qrpPTFESFKDVYIVQELMET-DLYKLIKTQHL-SNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGLSKeSVDQEKKAYSF----CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLG 329
Cdd:cd07849   150 FGLAR-IADPEHDHTGFlteyVATRWYRAPEImLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGI-LG 227

                  ..
gi 1958807372 330 MP 331
Cdd:cd07849   228 TP 229
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
105-353 8.91e-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: 96.29  E-value: 8.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 105 KADPAQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRvRTKMERDILVEVNH-PFIVKLHYAFQTE 183
Cdd:cd06618    11 KADLNDLENLGEIGSGTCGQVYKMRHKK---TGHVMAVKQMRRSGNKEENK-RILMDLDVVLKSHDcPYIVKCYGYFITD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLrgGDVFTRLSKEVL-FTEEDVkfyLAELAL----ALDHL-HRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd06618    87 SDVFICMELM--STCLDKLLKRIQgPIPEDI---LGKMTVsivkALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFGI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSfCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEMLTGTLPFQGKDRN-ETMNMILK---AKLGM 330
Cdd:cd06618   162 SGRLVDSKAKTRS-AGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEfEVLTKILNeepPSLPP 240
                         250       260
                  ....*....|....*....|...
gi 1958807372 331 PQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd06618   241 NEGFSPDFCSFVDLCLTKDHRYR 263
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
505-737 1.04e-21

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: 97.16  E-value: 1.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILMRYgQHPNIISLKEVFDDG--------------KYVYLVTDLMKGGelLDRILKKKCFSEQEASNVLYVITKTVE 570
Cdd:cd07854    52 EIKIIRRL-DHDNIVKVYEVLGPSgsdltedvgsltelNSVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 571 YLHSQGVVHRDLKPSNILYMDESGhpdSIKICDFGFAKQLRGE---NGLLLTPCYTANFVAPEVLTQ-QGYDAACDIWSL 646
Cdd:cd07854   129 YIHSANVLHRDLKPANVFINTEDL---VLKIGDFGLARIVDPHyshKGYLSEGLVTKWYRSPRLLLSpNNYTKAIDMWAA 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 647 GVLLYTMLAGYTPFsNGPND-------------TPEE---ILLRIGNGRFSLSGGI--------WDNISRGAKDLLSHML 702
Cdd:cd07854   206 GCIFAEMLTGKPLF-AGAHEleqmqlilesvpvVREEdrnELLNVIPSFVRNDGGEprrplrdlLPGVNPEALDFLEQIL 284
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 703 HMDPHQRYTAEQVLKHPWItQREQLPRHQPTSDDP 737
Cdd:cd07854   285 TFNPMDRLTAEEALMHPYM-SCYSCPFDEPVSLHP 318
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
451-740 1.15e-21

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: 97.41  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 451 VQINGNAAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE-----ILMRYGQHPNIISLKEVF 525
Cdd:cd07876    10 VQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRayrelVLLKCVNHKNIISLLNVF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 526 DDGKYVYLVTDLMKGGELLDRILKKKCFSE---QEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKIC 602
Cdd:cd07876    90 TPQKSLEEFQDVYLVMELMDANLCQVIHMEldhERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDC----TLKIL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 603 DFGFAKQlrGENGLLLTP-CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN-DTPEEILLRIGNGRF 680
Cdd:cd07876   166 DFGLART--ACTNFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHiDQWNKVIEQLGTPSA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 681 SLSGGIWDNI----------------------------------SRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQreq 726
Cdd:cd07876   244 EFMNRLQPTVrnyvenrpqypgisfeelfpdwifpseserdklkTSQARDLLSKMLVIDPDKRISVDEALRHPYITV--- 320
                         330
                  ....*....|....*.
gi 1958807372 727 lpRHQPTSDD--PPQV 740
Cdd:cd07876   321 --WYDPAEAEapPPQI 334
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
110-367 1.28e-21

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: 95.36  E-value: 1.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRkktGPDaGQLYAMKV--LRKASLKVRDRVrtKMERDILVEVNH-PFIVKL--HYAFQTEG 184
Cdd:cd14131     2 PYEILKQLGKGGSSKVYKVL---NPK-KKIYALKRvdLEGADEQTLQSY--KNEIELLKKLKGsDRIIQLydYEVTDEDD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFlRGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEiGHIKLTDFGLSKE-- 260
Cdd:cd14131    76 YLYMVMEC-GEIDLATILKKKRPkpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAiq 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 ----SVDQEkkaySFCGTVEYMAPEVVNRRGHSQ----------SADWWSYGVLMFEMLTGTLPFQgkdrnETMNMIlkA 326
Cdd:cd14131   154 ndttSIVRD----SQVGTLNYMSPEAIKDTSASGegkpkskigrPSDVWSLGCILYQMVYGKTPFQ-----HITNPI--A 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 327 KLG----------MPQFLSAEAQSLLRMLFKRNPANRLgseGVEEVKRHAF 367
Cdd:cd14131   223 KLQaiidpnheieFPDIPNPDLIDVMKRCLQRDPKKRP---SIPELLNHPF 270
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
468-717 1.33e-21

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 94.82  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVK-----IIDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05041     1 EKIGRGNFGDVYRGVLKPDNTEVAVKtcretLPPDLKRKFLQEARILKQY-DHPNIVKLIGVCVQKQPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKC---------FSEQEASNVlyvitktvEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLRG- 612
Cdd:cd05041    80 LLTFLRKKGArltvkqllqMCLDAAAGM--------EYLESKNCIHRDLAARNCLVGEN----NVLKISDFGMSREEEDg 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ----ENGLLLTPcytANFVAPEVLTQQGYDAACDIWSLGVLLY-TMLAGYTPFSNGPNDTPEEILLRigNGRFSLSGGIW 687
Cdd:cd05041   148 eytvSDGLKQIP---IKWTAPEALNYGRYTSESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIES--GYRMPAPELCP 222
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 688 DNISRgakdLLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd05041   223 EAVYR----LMLQCWAYDPENRPSFSEIYN 248
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
497-709 1.36e-21

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: 95.75  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 497 KNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYV-----YLVTDLMKGGELlDRILKK--KC--FSEQEASNVLYVITK 567
Cdd:cd14039    33 KNKDRWCHEIQI-MKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCSGGDL-RKLLNKpeNCcgLKESQVLSLLSDIGS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 568 TVEYLHSQGVVHRDLKPSNILYMDESG---HpdsiKICDFGFAKQLrgENGLLLTPCY-TANFVAPEVLTQQGYDAACDI 643
Cdd:cd14039   111 GIQYLHENKIIHRDLKPENIVLQEINGkivH----KIIDLGYAKDL--DQGSLCTSFVgTLQYLAPELFENKSYTVTVDY 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 644 WSLGVLLYTMLAGYTPF----------SNGPNDTPEEILL---RIGNGRFSLSGGIWDNISR----GAKDLLSHMLHMDP 706
Cdd:cd14039   185 WSFGTMVFECIAGFRPFlhnlqpftwhEKIKKKDPKHIFAveeMNGEVRFSTHLPQPNNLCSlivePMEGWLQLMLNWDP 264

                  ...
gi 1958807372 707 HQR 709
Cdd:cd14039   265 VQR 267
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
460-720 1.40e-21

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


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 95.46  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSE---AYELKEDigigSYSVCKrcIH----SASNMEFAVKIidknkRDPSEEIEIlMRYGQHPNIISLKEVFD-DGKYV 531
Cdd:cd13990    13 FSEvykAFDLVEQ----RYVACK--IHqlnkDWSEEKKQNYI-----KHALREYEI-HKSLDHPRIVKLYDVFEiDTDSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELlDRILKK-KCFSEQEASNVLYVITKTVEYL--HSQGVVHRDLKPSNILyMDESGHPDSIKICDFGFAK 608
Cdd:cd13990    81 CTVLEYCDGNDL-DFYLKQhKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNIL-LHSGNVSGEIKITDFGLSK 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 QLRGEN----GLLLTP--CYTANFVAPEVL----TQQGYDAACDIWSLGVLLYTMLAGYTPFsnGPNDTPEEIL-----L 673
Cdd:cd13990   159 IMDDESynsdGMELTSqgAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQMLYGRKPF--GHNQSQEAILeentiL 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 674 RIGNGRFSLSggiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd13990   237 KATEVEFPSK----PVVSSEAKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
108-340 1.42e-21

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: 96.94  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKV-FLVRKKTGPDAgqlyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd07880    14 PDRYRDLKQVGSGAYGTVcSALDRRTGAKV----AIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 ------YLILDFLrgGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE 260
Cdd:cd07880    90 drfhdfYLVMPFM--GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SvDQEKKAYSFcgTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQ 339
Cdd:cd07880   168 T-DSEMTGYVV--TRWYRAPEVIlNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQ 244

                  .
gi 1958807372 340 S 340
Cdd:cd07880   245 S 245
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
116-331 1.60e-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: 94.67  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFlvrkkTGPDAGQLYAMKVLRKASLK----VRDRVRtkMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd14148     1 IIGVGGFGKVY-----KGLWRGEEVAVKAARQDPDEdiavTAENVR--QEARLFWMLQHPNIIALRGVCLNPPHLCLVME 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKfYLAELALALDHLHR---LGIVYRDLKPENILLDEIGH--------IKLTDFGLSKE 260
Cdd:cd14148    74 YARGGALNRALAGKKVPPHVLVN-WAVQIARGMNYLHNeaiVPIIHRDLKSSNILILEPIEnddlsgktLKITDFGLARE 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 261 SvdQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 331
Cdd:cd14148   153 W--HKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLP 221
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
111-350 1.64e-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: 96.47  E-value: 1.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVN-HPFIVKLHYAFQTE-GK-L 186
Cdd:cd07852     9 YEILKKLGKGAYGIVWkAIDKKTG----EVVALKKIFDAFRNATDAQRTFREIMFLQELNdHPNIIKLLNVIRAEnDKdI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGgDVFTRLSKEVLfteEDV--KFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQ 264
Cdd:cd07852    85 YLVFEYMET-DLHAVIRANIL---EDIhkQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLAR-SLSQ 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFCGTVEYMA------PEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGkdrNETMNMILK--AKLGMP---- 331
Cdd:cd07852   160 LEEDDENPVLTDYVAtrwyraPEIlLGSTRYTKGVDMWSVGCILGEMLLGKPLFPG---TSTLNQLEKiiEVIGRPsaed 236
                         250       260
                  ....*....|....*....|.
gi 1958807372 332 --QFLSAEAQSLLRMLFKRNP 350
Cdd:cd07852   237 ieSIQSPFAATMLESLPPSRP 257
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
525-716 1.68e-21

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 98.55  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 525 FDDGKY---VYLVTDLMKGGELLDRI---LKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdesghPD 597
Cdd:PTZ00267  131 FDDFKSddkLLLIMEYGSGGDLNKQIkqrLKEHLpFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM-----PT 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 598 SI-KICDFGFAKQLRGENGLLLTP--CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsNGPNDtpEEILLR 674
Cdd:PTZ00267  206 GIiKLGDFGFSKQYSDSVSLDVASsfCGTPYYLAPELWERKRYSKKADMWSLGVILYELLTLHRPF-KGPSQ--REIMQQ 282
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 675 IGNGRFSLSGGiwdNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:PTZ00267  283 VLYGKYDPFPC---PVSSGMKALLDPLLSKNPALRPTTQQLL 321
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
460-718 1.93e-21

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: 94.87  E-value: 1.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSY-SVCKrCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDG---------- 528
Cdd:cd14047     4 FRQDFKEIELIGSGGFgQVFK-AKHRIDGKTYAIKRVKLNNEKAEREVKALAKL-DHPNIVRYNGCWDGFdydpetsssn 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 ------KYVYLVTDLMKGGELLDRILK--KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIK 600
Cdd:cd14047    82 ssrsktKCLFIQMEFCEKGTLESWIEKrnGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTG----KVK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 601 ICDFGFAKQLRGENGLLLTPCyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLagyTPFSNGpNDTpEEILLRIGNGRF 680
Cdd:cd14047   158 IGDFGLVTSLKNDGKRTKSKG-TLSYMSPEQISSQDYGKEVDIYALGLILFELL---HVCDSA-FEK-SKFWTDLRNGIL 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 681 SLsggIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd14047   232 PD---IFDKRYKIEKTIIKKMLSKKPEDRPNASEILRT 266
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
117-353 2.02e-21

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: 94.34  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVF--LVRKKTGPDAGqlYAMKVLRKASLKVRDR--VRtkmERDILVEVNHPFIVKLHYAFQTEGkLYLILDF 192
Cdd:cd05060     3 LGHGNFGSVRkgVYLMKSGKEVE--VAVKTLKQEHEKAGKKefLR---EASVMAQLDHPCIVRLIGVCKGEP-LMLVMEL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYSFC 272
Cdd:cd05060    77 APLGPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSR-ALGAGSDYYRAT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 273 GT----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRMLF 346
Cdd:cd05060   156 TAgrwpLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSyGAKPYGEMKGPEVIAMLESGErLPRPEECPQEIYSIMLSCW 235

                  ....*..
gi 1958807372 347 KRNPANR 353
Cdd:cd05060   236 KYRPEDR 242
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
110-413 2.04e-21

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: 95.64  E-value: 2.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF--------- 180
Cdd:cd07864     8 KFDIIGIIGEGTYGQVYKAKDK---DTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVtdkqdaldf 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 -QTEGKLYLILDFLrGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07864    85 kKDKGAFYLVFEYM-DHDLMGLLeSGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYS-FCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKdrNETMNMILKAKL-GMPqfls 335
Cdd:cd07864   164 RLYNSEESRPYTnKVITLWYRPPElLLGEERYGPAIDVWSCGCILGELFTKKPIFQAN--QELAQLELISRLcGSP---- 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 336 aeaqsllrmlfkrNPANRlgsegvEEVKRHAFFSSIDWNKLYKREVQPPF----RPASGKPDDTFCFDPE--FTAKTPKD 409
Cdd:cd07864   238 -------------CPAVW------PDVIKLPYFNTMKPKKQYRRRLREEFsfipTPALDLLDHMLTLDPSkrCTAEQALN 298

                  ....
gi 1958807372 410 SPGL 413
Cdd:cd07864   299 SPWL 302
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
117-311 2.13e-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: 94.52  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrkkTGPDAGQLYAMKVLRKASLKVRDRVrtKM---ERDILVEVNHPFIVKLHYA-FQTEGKLYLILDF 192
Cdd:cd14064     1 IGSGSFGKVY-----KGRCRNKIVAIKRYRANTYCSKSDV--DMfcrEVSILCRLNHPCVIQFVGAcLDDPSQFAIVTQY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHRLG--IVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKK 267
Cdd:cd14064    74 VSGGSLFSLLHEQKRVIDLQSKLIIAvDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESRflQSLDEDNM 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 268 AYSfCGTVEYMAPEVVNRRG-HSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14064   154 TKQ-PGNLRWMAPEVFTQCTrYSIKADVFSYALCLWELLTGEIPF 197
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
464-720 2.28e-21

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: 94.85  E-value: 2.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKII--DKNKRDPSEEI-EI-LMRYGQHPNIISLKEVfddgkyVYLVTDLMK 539
Cdd:cd07836     2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIhlDAEEGTPSTAIrEIsLMKELKHENIVRLHDV------IHTENKLML 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQE--------ASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLR 611
Cdd:cd07836    76 VFEYMDKDLKKYMDTHGVrgaldpntVKSFTYQLLKGIAFCHENRVLHRDLKPQNLL-INKRGE---LKLADFGLARAFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIWDNI 690
Cdd:cd07836   152 IPVNTFSNEVVTLWYRAPDVLLgSRTYSTSIDIWSVGCIMAEMITGRPLF---PGTNNEDQLLKIFRIMGTPTESTWPGI 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 691 S-------------------------RGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07836   229 SqlpeykptfpryppqdlqqlfphadPLGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
115-367 2.40e-21

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 94.76  E-value: 2.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLR---KASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK--LYLI 189
Cdd:cd06651    13 KLLGQGAFGRVYLCYDV---DTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAEktLTIF 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK--ESVDQEKK 267
Cdd:cd06651    90 MEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTICMSGT 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AY-SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQgkdRNETMNMILK-----AKLGMPQFLSAEAQSL 341
Cdd:cd06651   170 GIrSVTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWA---EYEAMAAIFKiatqpTNPQLPSHISEHARDF 246
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 342 LRMLF---KRNPAnrlgsegVEEVKRHAF 367
Cdd:cd06651   247 LGCIFveaRHRPS-------AEELLRHPF 268
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
464-736 2.77e-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: 96.00  E-value: 2.77e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEIL-----MRYGQHPNIISLKEVF-----DDGKYVYL 533
Cdd:cd07859     2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILreiklLRLLRHPDIVEIKHIMlppsrREFKDIYV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMkGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAK-QLRG 612
Cdd:cd07859    82 VFELM-ESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADC----KLKICDFGLARvAFND 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTAN--FVAPEVLTQ--QGYDAACDIWSLGVLLYTMLAGyTPFSNGPN-------------DTPEEILLRI 675
Cdd:cd07859   157 TPTAIFWTDYVATrwYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTG-KPLFPGKNvvhqldlitdllgTPSPETISRV 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 676 GN--GRFSLS----------GGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW---ITQREQLPRHQPTSDD 736
Cdd:cd07859   236 RNekARRYLSsmrkkqpvpfSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYfkgLAKVEREPSAQPITKL 311
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
505-739 2.79e-21

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 95.98  E-value: 2.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGelLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLK 583
Cdd:PTZ00024   70 ELKI-MNEIKHENIMGLVDVYVEGDFINLVMDIMASD--LKKVVDRKIrLTESQVKCILLQILNGLNVLHKWYFMHRDLS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 584 PSNIlYMDESGhpdSIKICDFGFAKQ-----LRGENGLLLTPC----YTANFV-----APEVLT-QQGYDAACDIWSLGV 648
Cdd:PTZ00024  147 PANI-FINSKG---ICKIADFGLARRygyppYSDTLSKDETMQrreeMTSKVVtlwyrAPELLMgAEKYHFAVDMWSVGC 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 649 LLYTMLAGyTPFSNGPNDTPEeiLLRIgngrFSLSG----------------------------GIWDNISRGAKDLLSH 700
Cdd:PTZ00024  223 IFAELLTG-KPLFPGENEIDQ--LGRI----FELLGtpnednwpqakklplyteftprkpkdlkTIFPNASDDAIDLLQS 295
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 701 MLHMDPHQRYTAEQVLKHPWITQreqlprhQPTSDDPPQ 739
Cdd:PTZ00024  296 LLKLNPLERISAKEALKHEYFKS-------DPLPCDPSQ 327
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
117-353 2.99e-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: 2.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpDAGQLYAMKVLRkASLKVRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEgKLYLILDFLRG 195
Cdd:cd05041     3 IGRGNFGDVYRGVLK---PDNTEVAVKTCR-ETLPPDLKRKFLQEARILKQYDHPNIVKLiGVCVQKQ-PIMIVMELVPG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDV--FTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 273
Cdd:cd05041    78 GSLltFLRKKGARLTVKQLLQMCL-DAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEYTVSDGLK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 T--VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRN 349
Cdd:cd05041   157 QipIKWTAPEALNYGRYTSESDVWSFGILLWEIFSlGATPYPGMSNQQTREQIESGyRMPAPELCPEAVYRLMLQCWAYD 236

                  ....
gi 1958807372 350 PANR 353
Cdd:cd05041   237 PENR 240
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
110-367 3.03e-21

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: 93.88  E-value: 3.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKaslkvrDRV----------RTKMERDILVEVNHPF--IVKLH 177
Cdd:cd14100     1 QYQVGPLLGSGGFGSVY---SGIRVADGAPVAIKHVEK------DRVsewgelpngtRVPMEIVLLKKVGSGFrgVIRLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 YAFQTEGKLYLILDFLRG-GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLTDF 255
Cdd:cd14100    72 DWFERPDSFVLVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDF 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 256 G---LSKESVDQEkkaysFCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRnetmnmILKAKLGMP 331
Cdd:cd14100   152 GsgaLLKDTVYTD-----FDGTRVYSPPEWIRfHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE------IIRGQVFFR 220
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958807372 332 QFLSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd14100   221 QRVSSECQHLIKWCLALRPSDR---PSFEDIQNHPW 253
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
117-369 3.22e-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: 94.24  E-value: 3.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFG----KVFLVRKKtgpdagQL-YAMKVLRKASLK-VRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGkLYLIL 190
Cdd:cd05115    12 LGSGNFGcvkkGVYKMRKK------QIdVAIKVLKQGNEKaVRDEMMR--EAQIMHQLDNPYIVRMIGVCEAEA-LMLVM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLS-KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE--SVDQEKK 267
Cdd:cd05115    83 EMASGGPLNKFLSgKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAlgADDSYYK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFLSAEAQSLLRM 344
Cdd:cd05115   163 ARSAGKwPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPYKKMKGPEVMSFIEQGKrMDCPAECPPEMYALMSD 242
                         250       260
                  ....*....|....*....|....*
gi 1958807372 345 LFKRNPANRLGSEGVEEVKRHAFFS 369
Cdd:cd05115   243 CWIYKWEDRPNFLTVEQRMRTYYYS 267
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
470-668 3.35e-21

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 94.64  E-value: 3.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVK-----IIDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYV------YLVTDLM 538
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKqcrqeLSPKNRERWCLEIQIMKRL-NHPNVVAARDVPEGLQKLapndlpLLAMEYC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRI-LKKKCFSEQEAS--NVLYVITKTVEYLHSQGVVHRDLKPSNILYmdESGHPDSI-KICDFGFAKQLrgEN 614
Cdd:cd14038    81 QGGDLRKYLnQFENCCGLREGAilTLLSDISSALRYLHENRIIHRDLKPENIVL--QQGEQRLIhKIIDLGYAKEL--DQ 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 615 GLLLTPCY-TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngPNDTP 668
Cdd:cd14038   157 GSLCTSFVgTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITGFRPFL--PNWQP 209
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
470-660 3.48e-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: 93.90  E-value: 3.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASnmEFAVKIIdknKRDPSEEIEI----------LMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14148     2 IGVGGFGKVYKGLWRGE--EVAVKAA---RQDPDEDIAVtaenvrqearLFWMLQHPNIIALRGVCLNPPHLCLVMEYAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELlDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVV---HRDLKPSNILYMDESGHPD----SIKICDFGFAKQLRG 612
Cdd:cd14148    77 GGAL-NRALAGKKVPPHVLVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEPIENDDlsgkTLKITDFGLAREWHK 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 613 ENGLLLTPCYTanFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14148   156 TTKMSAAGTYA--WMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
464-720 3.54e-21

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: 94.41  E-value: 3.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PSEEI-EI-LMRYGQHPNIISLKEVFDDGKYVYLV---- 534
Cdd:cd07861     2 YTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEegvPSTAIrEIsLLKELQHPNIVCLEDVLMQENRLYLVfefl 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 -TDLMKggeLLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLrge 613
Cdd:cd07861    82 sMDLKK---YLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLL-IDNKG---VIKLADFGLARAF--- 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 nGLLLTpCYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYTMlAGYTPFSNGpnDTPEEILLRI-----------G 676
Cdd:cd07861   152 -GIPVR-VYTHEVVtlwyrAPEVLLgSPRYSTPVDIWSIGTIFAEM-ATKKPLFHG--DSEIDQLFRIfrilgtptediW 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 677 NGRFSL----------SGGIWD----NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07861   227 PGVTSLpdykntfpkwKKGSLRtavkNLDEDGLDLLEKMLIYDPAKRISAKKALVHPY 284
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
108-352 3.69e-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: 95.88  E-value: 3.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKV---FLVRkktgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG 184
Cdd:cd07877    16 PERYQNLSPVGSGAYGSVcaaFDTK------TGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPAR 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KL------YLILDfLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07877    90 SLeefndvYLVTH-LMGADL-NNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESvDQEKKAYsfCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP-----Q 332
Cdd:cd07877   168 RHT-DDEMTGY--VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRL-VGTPgaellK 243
                         250       260
                  ....*....|....*....|....*
gi 1958807372 333 FLSAEA-----QSLLRMLfKRNPAN 352
Cdd:cd07877   244 KISSESarnyiQSLTQMP-KMNFAN 267
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
107-311 3.98e-21

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 94.30  E-value: 3.98e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFLVRK-KTGpdagQLYAMKVLrkaSLKVRDRVRTKMERDILVEVNHPFIVKLHY-AF--- 180
Cdd:cd06636    13 DPAGiFELVEVVGNGTYGQVYKGRHvKTG----QLAAIKVM---DVTEDEEEEIKLEINMLKKYSHHRNIATYYgAFikk 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 ---QTEGKLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDF 255
Cdd:cd06636    86 sppGHDDQLWLVMEFCGAGSVtdLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDF 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 256 GLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQS-----ADWWSYGVLMFEMLTGTLPF 311
Cdd:cd06636   166 GVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDAtydyrSDIWSLGITAIEMAEGAPPL 226
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
117-353 4.02e-21

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: 93.46  E-value: 4.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd05084     4 IGRGNFGEVFSGRLRAD---NTPVAVKSCRE-TLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRL--------SKEVLFTEEDVkfylaelALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKKA 268
Cdd:cd05084    80 DFLTFLrtegprlkVKELIRMVENA-------AAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSRE---EEDGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCG-----TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSL 341
Cdd:cd05084   150 YAATGgmkqiPVKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANLSNQQTREAVEQGvRLPCPENCPDEVYRL 229
                         250
                  ....*....|..
gi 1958807372 342 LRMLFKRNPANR 353
Cdd:cd05084   230 MEQCWEYDPRKR 241
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
108-331 4.15e-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: 95.35  E-value: 4.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd07879    14 PERYTSLKQVGSGAYGSVCsAIDKRTG----EKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 ------YLILDFLrggdvFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07879    90 defqdfYLVMPYM-----QTDLQKimGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLA 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 259 KeSVDQEKKAYSFcgTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKlGMP 331
Cdd:cd07879   165 R-HADAEMTGYVV--TRWYRAPEVIlNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVT-GVP 234
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
462-702 4.37e-21

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: 96.62  E-value: 4.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK---NKRDPS----EEIEILMRyGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05624    72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKwemLKRAETacfrEERNVLVN-GDCQWITTLHYAFQDENYLYLV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgE 613
Cdd:cd05624   151 MDYYVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVL-LDMNGH---IRLADFGSCLKMN-D 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCY--TANFVAPEVLT--QQG---YDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNG--RFSLSG 684
Cdd:cd05624   226 DGTVQSSVAvgTPDYISPEILQamEDGmgkYGPECDWWSLGVCMYEMLYGETPFY---AESLVETYGKIMNHeeRFQFPS 302
                         250
                  ....*....|....*...
gi 1958807372 685 GIWDnISRGAKDLLSHML 702
Cdd:cd05624   303 HVTD-VSEEAKDLIQRLI 319
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
462-722 4.43e-21

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 96.62  E-value: 4.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDK---NKRDPS----EEIEILMRyGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05623    72 EDFEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKwemLKRAETacfrEERDVLVN-GDSQWITTLHYAFQDDNNLYLV 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgE 613
Cdd:cd05623   151 MDYYVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNIL-MDMNGH---IRLADFGSCLKLM-E 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLTPCY--TANFVAPEVLT-----QQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNG--RFSLSG 684
Cdd:cd05623   226 DGTVQSSVAvgTPDYISPEILQamedgKGKYGPECDWWSLGVCMYEMLYGETPFY---AESLVETYGKIMNHkeRFQFPT 302
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 685 GIWDnISRGAKDLLSHMLHMDPHQ--RYTAEQVLKHPWIT 722
Cdd:cd05623   303 QVTD-VSENAKDLIRRLICSREHRlgQNGIEDFKNHPFFV 341
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
461-723 6.11e-21

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: 93.94  E-value: 6.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE----EIEILMRYgQHPNIISLKEVF-DDGKyVYLVT 535
Cdd:cd06644    11 NEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEdymvEIEILATC-NHPYIVKLLGAFyWDGK-LWIMI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGEL------LDRILKkkcfsEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFA-- 607
Cdd:cd06644    89 EFCPGGAVdaimleLDRGLT-----EPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDG----DIKLADFGVSak 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 --KQLRGENGLLLTPCYTA-NFVAPEVLTQQGYDAACDIWSLGVLLYTMlAGYTPFSNGPNdtPEEILLRIGNGRFS--L 682
Cdd:cd06644   160 nvKTLQRRDSFIGTPYWMApEVVMCETMKDTPYDYKADIWSLGITLIEM-AQIEPPHHELN--PMRVLLKIAKSEPPtlS 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 683 SGGIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06644   237 QPSKW---SMEFRDFLKTALDKHPETRPSAAQLLEHPFVSS 274
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
109-368 6.25e-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: 6.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlrkaslkvrdRVRTKMERD-----------ILVEVNHPFIVKLH 177
Cdd:cd07845     7 TEFEKLNRIGEGTYGIVYRARDTT---SGEIVALK-----------KVRMDNERDgipisslreitLLLNLRHPNIVELK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 YAFQteGK----LYLILDFLRGgDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKL 252
Cdd:cd07845    73 EVVV--GKhldsIFLVMEYCEQ-DLASLLdNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 253 TDFGLSKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI-------- 323
Cdd:cd07845   150 ADFGLARTYGLPAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIiqllgtpn 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 324 -----------LKAKLGMPQ-----------FLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07845   230 esiwpgfsdlpLVGKFTLPKqpynnlkhkfpWLSEAGLRLLNFLLMYDPKKRATA---EEALESSYF 293
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
113-312 6.34e-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: 93.60  E-value: 6.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK--LYLI 189
Cdd:cd05038     8 FIKQLGEGHFGSVELCRyDPLGDNTGEQVAVKSL-QPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRrsLRLI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGG--DVFTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKesVDQEKK 267
Cdd:cd05038    87 MEYLPSGslRDYLQRHRDQIDLKRLLLFAS-QICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAK--VLPEDK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGT-----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ 312
Cdd:cd05038   164 EYYYVKEpgespIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQ 213
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
486-718 8.22e-21

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: 92.17  E-value: 8.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 486 SNMEFAVKIIDKNKrdpseEIEIL-MRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDrILKkkcfSEQEASNVLYV 564
Cdd:cd14059    15 RGEEVAVKKVRDEK-----ETDIKhLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYE-VLR----AGREITPSLLV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 -----ITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLrGENGLLLTPCYTANFVAPEVLTQQGYDA 639
Cdd:cd14059    85 dwskqIASGMNYLHLHKIIHRDLKSPNVLV----TYNDVLKISDFGTSKEL-SEKSTKMSFAGTVAWMAPEVIRNEPCSE 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 640 ACDIWSLGVLLYTMLAGYTPFSNGPNDTpeeILLRIGNGrfSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd14059   160 KVDIWSFGVVLWELLTGEIPYKDVDSSA---IIWGVGSN--SLQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILMH 233
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
113-353 8.30e-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: 8.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd05072    11 LVKKLGAGQFGEVWMGYYNNSTKV----AVKTLKPGTMSVQAFLE---EANLMKTLQHDKLVRLYAVVTKEEPIYIITEY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFtrlskEVLFTEEDVKFYL-------AELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd05072    84 MAKGSLL-----DFLKSDEGGKVLLpklidfsAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLL 342
Cdd:cd05072   159 YTAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGyRMPRMENCPDELYDIM 238
                         250
                  ....*....|.
gi 1958807372 343 RMLFKRNPANR 353
Cdd:cd05072   239 KTCWKEKAEER 249
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
462-722 9.18e-21

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 93.17  E-value: 9.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEdymvEIDILASC-DHPNIVKLLDAFYYENNLWILIEF 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFA----KQLRG 612
Cdd:cd06643    84 CAGGAVDAVMLElERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDG----DIKLADFGVSakntRTLQR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYtanfVAPEVL-----TQQGYDAACDIWSLGVLLYTMlAGYTPFSNGPNdtPEEILLRIGNGRFS--LSGG 685
Cdd:cd06643   160 RDSFIGTPYW----MAPEVVmcetsKDRPYDYKADVWSLGVTLIEM-AQIEPPHHELN--PMRVLLKIAKSEPPtlAQPS 232
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 686 IWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd06643   233 RW---SPEFKDFLRKCLEKNVDARWTTSQLLQHPFVS 266
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
216-313 9.51e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 96.79  E-value: 9.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 216 YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG----LSKESVDQEKkaySFCGTVEYMAPE-----VVNRR 286
Cdd:NF033483  112 IMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGiaraLSSTTMTQTN---SVLGTVHYLSPEqarggTVDAR 188
                          90       100
                  ....*....|....*....|....*..
gi 1958807372 287 ghsqsADWWSYGVLMFEMLTGTLPFQG 313
Cdd:NF033483  189 -----SDIYSLGIVLYEMLTGRPPFDG 210
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
470-717 1.32e-20

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: 92.07  E-value: 1.32e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSasNMEFAVKIIdknKRDPSEEIEI----------LMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14061     2 IGVGGFGKVYRGIWR--GEEVAVKAA---RQDPDEDISVtlenvrqearLFWMLRHPNIIALRGVCLQPPNLCLVMEYAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELlDRILKKKCFSEQEASNVLYVITKTVEYLHSQG---VVHRDLKPSNILYMDESGHPD----SIKICDFGFAKQLrg 612
Cdd:cd14061    77 GGAL-NRVLAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIENEDlenkTLKITDFGLAREW-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndtPEEILLRIGNGRFSLSGGIWDNISR 692
Cdd:cd14061   154 HKTTRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPYKG-----IDGLAVAYGVAVNKLTLPIPSTCPE 228
                         250       260
                  ....*....|....*....|....*
gi 1958807372 693 GAKDLLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd14061   229 PFAQLMKDCWQPDPHDRPSFADILK 253
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
490-737 1.43e-20

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 94.18  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 490 FAVKI------IDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLY 563
Cdd:cd05610    32 YAVKVvkkadmINKNMVHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYIS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 564 VITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK-QLRGE---NGLLLTPCY----------------- 622
Cdd:cd05610   112 EVALALDYLHRHGIIHRDLKPDNML-ISNEGH---IKLTDFGLSKvTLNRElnmMDILTTPSMakpkndysrtpgqvlsl 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 --------------------------------TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEE 670
Cdd:cd05610   188 isslgfntptpyrtpksvrrgaarvegerilgTPDYLAPELLLGKPHGPAVDWWALGVCLFEFLTGIPPFN---DETPQQ 264
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 671 ILLRIGNGRFSLSGGiWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP------WITQREQLPRHQPTSDDP 737
Cdd:cd05610   265 VFQNILNRDIPWPEG-EEELSVNAQNAIEILLTMDPTKRAGLKELKQHPlfhgvdWENLQNQTMPFIPQPDDE 336
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
457-718 1.64e-20

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: 92.63  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 457 AAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFD----- 526
Cdd:cd14048     1 TSRFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELARekvlrEVRALAKL-DHPGIVRYFNAWLerppe 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 527 ------DGKYVYLVTDLMKGGELLDRILKKKCFSEQEAS---NVLYVITKTVEYLHSQGVVHRDLKPSNILY-MDesghp 596
Cdd:cd14048    80 gwqekmDEVYLYIQMQLCRKENLKDWMNRRCTMESRELFvclNIFKQIASAVEYLHSKGLIHRDLKPSNVFFsLD----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 597 DSIKICDFGFAKQL-RGE---NGLLLTPCY--------TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLagyTPFSngp 664
Cdd:cd14048   155 DVVKVGDFGLVTAMdQGEpeqTVLTPMPAYakhtgqvgTRLYMSPEQIHGNQYSEKVDIFALGLILFELI---YSFS--- 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 665 ndTPEE---ILLRIGNGRFSLsggIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd14048   229 --TQMErirTLTDVRKLKFPA---LFTNKYPEERDMVQQMLSPSPSERPEAHEVIEH 280
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
470-740 1.73e-20

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: 93.11  E-value: 1.73e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDPSE-----EIEILMRYGQHpNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05632    10 LGKGGFGEVCACQVRATGKMYACKRLEKKriKKRKGEsmalnEKQILEKVNSQ-FVVNLAYAYETKDALCLVLTIMNGGD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRI--LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgENGLLLTP 620
Cdd:cd05632    89 LKFHIynMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENIL-LDDYGH---IRISDLGLAVKIP-EGESIRGR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTP-EEILLRIGNGRFSLSGgiwdNISRGAKDLLS 699
Cdd:cd05632   164 VGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKrEEVDRRVLETEEVYSA----KFSEEAKSICK 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 700 HMLHMDPHQR-----YTAEQVLKHPWItQREQLPRHQPTSDDPPQV 740
Cdd:cd05632   240 MLLTKDPKQRlgcqeEGAGEVKRHPFF-RNMNFKRLEAGMLDPPFV 284
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
469-723 1.76e-20

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: 92.50  E-value: 1.76e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFAVKII---DKNK--RDPSEEIEIlMRYGQHPNIISLKEVF-DDGKYVYLVTDLMKGGE 542
Cdd:cd06620    12 DLGAGNGGSVSKVLHIPTGTIMAKKVIhidAKSSvrKQILRELQI-LHECHSPYIVSFYGAFlNENNNIIICMEYMDCGS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LlDRILKKKC-FSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgeNGLLLTP 620
Cdd:cd06620    91 L-DKILKKKGpFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNIL-VNSKGQ---IKLCDFGVSGELI--NSIADTF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF--SNGPND---TPEEI---LLRIGNG---RFSLSggiwDN 689
Cdd:cd06620   164 VGTSTYMSPERIQGGKYSVKSDVWSLGLSIIELALGEFPFagSNDDDDgynGPMGIldlLQRIVNEpppRLPKD----RI 239
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 690 ISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06620   240 FPKDLRDFVDRCLLKDPRERPSPQLLLDHDPFIQ 273
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
491-718 1.78e-20

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 91.61  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKRDPSEeIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVE 570
Cdd:cd13995    33 ACKLIPVEQFKPSD-VEIQACF-RHENIAELYGALLWEETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLD 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 571 YLHSQGVVHRDLKPSNILYMDESGhpdsiKICDFG----------FAKQLRGengllltpcyTANFVAPEVLTQQGYDAA 640
Cdd:cd13995   111 FLHSKNIIHHDIKPSNIVFMSTKA-----VLVDFGlsvqmtedvyVPKDLRG----------TEIYMSPEVILCRGHNTK 175
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 641 CDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd13995   176 ADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLEDIAQDCSPAMRELLEAALERNPNHRSSAAELLKH 253
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
464-709 2.55e-20

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 91.89  E-value: 2.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEdIGIGSY-SVCKRCIHSASNMeFAVKIIDKN--KRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd05607     5 YEFRV-LGKGGFgEVCAVQVKNTGQM-YACKKLDKKrlKKKSGEkmallEKEILEKV-NSPFIVSLAYAFETKTHLCLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKkkcFSEQ--EASNVLYV---ITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQL 610
Cdd:cd05607    82 SLMNGGDLKYHIYN---VGERgiEMERVIFYsaqITCGILHLHSLKIVYRDMKPENVL-LDDNGN---CRLSDLGLAVEV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGenGLLLTP-CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLrigngRFSLSGGI--- 686
Cdd:cd05607   155 KE--GKPITQrAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELK-----RRTLEDEVkfe 227
                         250       260
                  ....*....|....*....|...
gi 1958807372 687 WDNISRGAKDLLSHMLHMDPHQR 709
Cdd:cd05607   228 HQNFTEEAKDICRLFLAKKPENR 250
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
114-371 2.68e-20

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: 92.37  E-value: 2.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd07873     7 LDKLGEGTYATVYKGRSKL---TDNLVALKEIR---LEHEEGAPCTAIREVslLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd07873    81 YL-DKDLKQYLDDcGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQ------FLSAE------ 337
Cdd:cd07873   160 EVVTLWYRPPDIlLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRI-LGTPTeetwpgILSNEefksyn 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 338 -----AQSLLrmlfkrNPANRLGSEGV-----------------EEVKRHAFFSSI 371
Cdd:cd07873   239 ypkyrADALH------NHAPRLDSDGAdllskllqfegrkrisaEEAMKHPYFHSL 288
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
110-323 2.78e-20

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: 92.43  E-value: 2.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTE----- 183
Cdd:cd07865    13 KYEKLAKIGQGTFGEVFKARhRKTG----QIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTKatpyn 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 ---GKLYLILDFLRGgDVFTRLS-KEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd07865    89 rykGSIYLVFEFCEH-DLAGLLSnKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLAR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 260 E-SVDQEKKAYSFCG---TVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMI 323
Cdd:cd07865   168 AfSLAKNSQPNRYTNrvvTLWYRPPELlLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLI 236
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
108-331 2.79e-20

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 93.19  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKV---FLVRKKtgpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF---- 180
Cdd:cd07878    14 PERYQNLTPVGSGAYGSVcsaYDTRLR------QKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFtpat 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 --QTEGKLYLILDfLRGGDVfTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07878    88 siENFNEVYLVTN-LMGADL-NNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLA 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 259 KESvDQEKKAYsfCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07878   166 RQA-DDEMTGY--VATRWYRAPEImLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEV-VGTP 235
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
111-369 3.02e-20

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: 91.65  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd06645    13 FELIQRIGSGTYGDVYKARNVN---TGELAAIKVIKLEPGEDFAVV--QQEIIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd06645    88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAKRKS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEV--VNRR-GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF-----LSAEAQSLL 342
Cdd:cd06645   168 FIGTPYWMAPEVaaVERKgGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQPPKLkdkmkWSNSFHHFV 247
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 343 RMLFKRNPANRlgsEGVEEVKRHAFFS 369
Cdd:cd06645   248 KMALTKNPKKR---PTAEKLLQHPFVT 271
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
107-367 3.02e-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: 92.09  E-value: 3.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQ-FDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLrkaSLKVRDRVRTKMERDILVEVNHPFIVKLHY-AF---- 180
Cdd:cd06637     3 DPAGiFELVELVGNGTYGQVY---KGRHVKTGQLAAIKVM---DVTGDEEEEIKQEINMLKKYSHHRNIATYYgAFikkn 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 --QTEGKLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG 256
Cdd:cd06637    77 ppGMDDQLWLVMEFCGAGSVtdLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 257 LSKESVDQEKKAYSFCGTVEYMAPEVVN-----RRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRNETMNMILKAKLGMP 331
Cdd:cd06637   157 VSAQLDRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLC--DMHPMRALFLIPRNPAP 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 332 QF----LSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd06637   235 RLkskkWSKKFQSFIESCLVKNHSQR---PSTEQLMKHPF 271
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
469-729 3.37e-20

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: 92.41  E-value: 3.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTD--LMK 539
Cdd:cd06633    28 EIGHGSFGAVYFATNSHTNEVVAIKKMSYSGKQTNEkwqdiikEVKFLQQL-KHPNTIEYKGCYLKDHTAWLVMEycLGS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDriLKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENGLLLT 619
Cdd:cd06633   107 ASDLLE--VHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTE----PGQVKLADFGSASIASPANSFVGT 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 PCYtanfVAPEV---LTQQGYDAACDIWSLGVL----------LYTMLAGYTPFSNGPNDTPeeillrigngrfSLSGGI 686
Cdd:cd06633   181 PYW----MAPEVilaMDEGQYDGKVDIWSLGITcielaerkppLFNMNAMSALYHIAQNDSP------------TLQSNE 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 687 WDNISRGAKDllsHMLHMDPHQRYTAEQVLKHPWItQREQLPR 729
Cdd:cd06633   245 WTDSFRGFVD---YCLQKIPQERPSSAELLRHDFV-RRERPPR 283
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
505-721 3.45e-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: 93.27  E-value: 3.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILMrYGQHPNIISLKEVF-----DDGKYVYLVTDLMKGgELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVH 579
Cdd:cd07853    49 ELKMLC-FFKHDNVLSALDILqpphiDPFEEIYVVTELMQS-DLHKIIVSPQPLSSDHVKVFLYQILRGLKYLHSAGILH 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 580 RDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLLLT-PCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGY 657
Cdd:cd07853   127 RDIKPGNLLVNSNC----VLKICDFGLARVEEPDESKHMTqEVVTQYYRAPEILMgSRHYTSAVDIWSVGCIFAELLGRR 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 658 TPF-SNGPNDTPEEI----------------------LLRIGNGRFSLSG--GIWDNISRGAKDLLSHMLHMDPHQRYTA 712
Cdd:cd07853   203 ILFqAQSPIQQLDLItdllgtpsleamrsacegarahILRGPHKPPSLPVlyTLSSQATHEAVHLLCRMLVFDPDKRISA 282

                  ....*....
gi 1958807372 713 EQVLKHPWI 721
Cdd:cd07853   283 ADALAHPYL 291
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
115-368 3.55e-20

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 91.18  E-value: 3.55e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVflVRKktGPDAGQLYAMKVLRKASLKVRDRvrtkmERDILVEV-NHPFIVKLHYAFQTEGKLYLIL--- 190
Cdd:cd13982     7 KVLGYGSEGTI--VFR--GTFDGRPVAVKRLLPEFFDFADR-----EVQLLRESdEHPNVIRYFCTEKDRQFLYIALelc 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 -----DFLRGGDVFtrlsKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD---EIGHIK--LTDFGLSKE 260
Cdd:cd13982    78 aaslqDLVESPRES----KLFLRPGLEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnAHGNVRamISDFGLCKK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 -SVDQekkaYSF------CGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTL-PFQGKDRNEtMNmILKAKLG 329
Cdd:cd13982   154 lDVGR----SSFsrrsgvAGTSGWIAPEMLSgstKRRQTRAVDIFSLGCVFYYVLSGGShPFGDKLERE-AN-ILKGKYS 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 330 MPQFLSA-----EAQSLLRMLFKRNPANRlgsEGVEEVKRHAFF 368
Cdd:cd13982   228 LDKLLSLgehgpEAQDLIERMIDFDPEKR---PSAEEVLNHPFF 268
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
464-721 4.09e-20

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 91.84  E-value: 4.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdKNKRDPSE----EIEILMRYGQH-----PNIISLKEVFDDGKYVYLV 534
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKII-RNKKRFHQqalvEVKILKHLNDNdpddkHNIVRYKDSFIFRGHLCIV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TdlmkggELLD----RILKKKCFSEQEASNVLYV---ITKTVEYLHSQGVVHRDLKPSNILYMDEsgHPDSIKICDFG-- 605
Cdd:cd14210    94 F------ELLSinlyELLKSNNFQGLSLSLIRKFakqILQALQFLHKLNIIHCDLKPENILLKQP--SKSSIKVIDFGss 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 -FakqlrgENGLLltpcYT---ANFV-APEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSnGPNDT------------- 667
Cdd:cd14210   166 cF------EGEKV----YTyiqSRFYrAPEVILGLPYDTAIDMWSLGCILAELYTGYPLFP-GENEEeqlacimevlgvp 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 668 PEEILLRIGNGR--FSLSGGIWDNISRGAK---------------------DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14210   235 PKSLIDKASRRKkfFDSNGKPRPTTNSKGKkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
464-677 4.61e-20

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: 90.59  E-value: 4.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS--EEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMkgG 541
Cdd:cd14016     2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQleYEAKVYKLLQGGPGIPRLYWFGQEGDYNVMVMDLL--G 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKK--KCFSeqeasnvlyviTKTV-----------EYLHSQGVVHRDLKPSNILyMDESGHPDSIKICDFGFAK 608
Cdd:cd14016    80 PSLEDLFNKcgRKFS-----------LKTVlmladqmisrlEYLHSKGYIHRDIKPENFL-MGLGKNSNKVYLIDFGLAK 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 QLRGEN-----------GLLLTPCYTAnfvapeVLTQQGY-----DaacDIWSLG-VLLYtMLAGYTPFSNGPNDTPEEI 671
Cdd:cd14016   148 KYRDPRtgkhipyregkSLTGTARYAS------INAHLGIeqsrrD---DLESLGyVLIY-FLKGSLPWQGLKAQSKKEK 217

                  ....*.
gi 1958807372 672 LLRIGN 677
Cdd:cd14016   218 YEKIGE 223
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
110-353 5.86e-20

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: 90.19  E-value: 5.86e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLRKASLKVRDRVRTkmERDILVEVNHPFIVKLHyAFQTEGK-LYL 188
Cdd:cd05148     7 EFTLERKLGSGYFGEVWEGLWKNRVRV----AIKILKSDDLLKQQDFQK--EVQALKRLRHKHLISLF-AVCSVGEpVYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS---KESVd 263
Cdd:cd05148    80 ITELMEKGSLlaFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLArliKEDV- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 qekkaYSFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEA 338
Cdd:cd05148   159 -----YLSSDKkipYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTyGQVPYPGMNNHEVYDQITAGyRMPCPAKCPQEI 233
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd05148   234 YKIMLECWAAEPEDR 248
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
491-716 6.68e-20

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: 90.14  E-value: 6.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNK----RDPSEEIEILMRYGQHPNII---SLKEVFDDGKYVYLVTDLMKGGELLDRIlkkkcfseQEASNVLY 563
Cdd:cd13979    30 AVKIVRRRRknraSRQSFWAELNAARLRHENIVrvlAAETGTDFASLGLIIMEYCGNGTLQQLI--------YEGSEPLP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 564 V---------ITKTVEYLHSQGVVHRDLKPSNILyMDESGHPdsiKICDFGFAKQLRGENGLLLTPCY---TANFVAPEV 631
Cdd:cd13979   102 LahrilisldIARALRFCHSHGIVHLDVKPANIL-ISEQGVC---KLCDFGCSVKLGEGNEVGTPRSHiggTYTYRAPEL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 632 LTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNG-RFSLSGGIWDNISRGAKDLLSHMLHMDPHQRY 710
Cdd:cd13979   178 LKGERVTPKADIYSFGITLWQMLTRELPYA---GLRQHVLYAVVAKDlRPDLSGLEDSEFGQRLRSLISRCWSAQPAERP 254

                  ....*.
gi 1958807372 711 TAEQVL 716
Cdd:cd13979   255 NADESL 260
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
464-721 7.05e-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: 90.45  E-value: 7.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE---EIEILMRYGQHPNIISLKEVF--------DDgkYVY 532
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEiklEINMLKKYSHHRNIATYYGAFikksppghDD--QLW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQL 610
Cdd:cd06636    96 LVMEFCGAGSVTDLVKNTKgnALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTPCYTANFVAPEVLT-----QQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIG-NGRFSLSG 684
Cdd:cd06636   172 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDYRSDIWSLGITAIEMAEGAPPLCDM---HPMRALFLIPrNPPPKLKS 248
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 685 GIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06636   249 KKW---SKKFIDFIEGCLVKNYLSRPSTEQLLKHPFI 282
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
505-718 7.13e-20

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


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 90.42  E-value: 7.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILMRYGQHPNIISL-----KEVFDDGKYVYLVTDLMKGGELLD----RILKKkcFSEQEASNVLYVITKTVEYLHS- 574
Cdd:cd14037    50 EIEIMKRLSGHKNIVGYidssaNRSGNGVYEVLLLMEYCKGGGVIDlmnqRLQTG--LTESEILKIFCDVCEAVAAMHYl 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 575 -QGVVHRDLKPSNILYmDESGHpdsIKICDFGFA--KQLRGENGLLL-----------TPCYTAnfvaPEVL---TQQGY 637
Cdd:cd14037   128 kPPLIHRDLKVENVLI-SDSGN---YKLCDFGSAttKILPPQTKQGVtyveedikkytTLQYRA----PEMIdlyRGKPI 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 638 DAACDIWSLGVLLYTMLAGYTPFSNGPNdtpeeilLRIGNGRFSlsggIWDN--ISRGAKDLLSHMLHMDPHQRYTAEQV 715
Cdd:cd14037   200 TEKSDIWALGCLLYKLCFYTTPFEESGQ-------LAILNGNFT----FPDNsrYSKRLHKLIRYMLEEDPEKRPNIYQV 268

                  ...
gi 1958807372 716 LKH 718
Cdd:cd14037   269 SYE 271
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
483-723 7.70e-20

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: 91.20  E-value: 7.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 483 HSASNMEFAVKIIDKNKrDPSEEI-----EI-LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDrILKKKC---F 553
Cdd:cd08216    21 HKPTNTLVAVKKINLES-DSKEDLkflqqEIlTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRD-LLKTHFpegL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 554 SEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTP-CYTANFV----- 627
Cdd:cd08216    99 PELAIAFILRDVLNALEYIHSKGYIHRSVKASHIL-ISGDGK---VVLSGLRYAYSMVKHGKRQRVVhDFPKSSEknlpw 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 628 -APEVLTQ--QGYDAACDIWSLGVLLYTMLAGYTPFSNGP---------NDTPEEIL------LRIGNGRFSLSGGIWDN 689
Cdd:cd08216   175 lSPEVLQQnlLGYNEKSDIYSVGITACELANGVVPFSDMPatqmllekvRGTTPQLLdcstypLEEDSMSQSEDSSTEHP 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 690 ISRGAKDLLSHM-------------LHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd08216   255 NNRDTRDIPYQRtfseafhqfvelcLQRDPELRPSASQLLAHSFFKQ 301
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
110-347 7.74e-20

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 95.19  E-value: 7.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF--QTEGKLY 187
Cdd:PTZ00266    14 EYEVIKKIGNGRFGEVFLVKHKR---TQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFlnKANQKLY 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  188 LILDFLRGGDVFTRLSK-EVLF---TEEDVKFYLAELALALDHLHRLG-------IVYRDLKPENILLD----EIGHI-- 250
Cdd:PTZ00266    91 ILMEFCDAGDLSRNIQKcYKMFgkiEEHAIVDITRQLLHALAYCHNLKdgpngerVLHRDLKPQNIFLStgirHIGKIta 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  251 -----------KLTDFGLSKeSVDQEKKAYSFCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFQgkDRN 317
Cdd:PTZ00266   171 qannlngrpiaKIGDFGLSK-NIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSDMWALGCIIYELCSGKTPFH--KAN 247
                          250       260       270
                   ....*....|....*....|....*....|
gi 1958807372  318 ETMNMILKAKLGmPQFLSAEAQSLLRMLFK 347
Cdd:PTZ00266   248 NFSQLISELKRG-PDLPIKGKSKELNILIK 276
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
111-305 7.88e-20

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 91.86  E-value: 7.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDagqlyamkvlrKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPD-----------PVVLKIGQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGgDVFTRLSKEVLFTEEDVKFYLAELAL-ALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDqEKKAY 269
Cdd:PHA03209  137 PHYSS-DLYTYLTKRSRPLPIDQALIIEKQILeGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVV-APAFL 214
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958807372 270 SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:PHA03209  215 GLAGTVETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
110-331 8.13e-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: 90.44  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHK---ETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGG--DVFTRLSKEVLftEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 267
Cdd:cd07848    79 FEYVEKNmlELLEEMPNGVP--PEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNA 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 268 AYS-FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 331
Cdd:cd07848   157 NYTeYVATRWYRSPELLLGAPYGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLGPLP 221
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
467-661 8.62e-20

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: 90.50  E-value: 8.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 467 KEDIGIGSYSVCKRCIHSASNMEFAVKII-----DKNKRDPSEEIEILMRYGQHPNIISL-KEVFDDGKyVYLVTDLMKG 540
Cdd:cd06616    11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRIrstvdEKEQKRLLMDLDVVMRSSDCPYIVKFyGALFREGD-CWICMELMDI 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GelLDRILK------KKCFSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrgE 613
Cdd:cd06616    90 S--LDKFYKyvyevlDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNIL-LDRNGN---IKLCDFGISGQL--V 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 614 NGLLLT------PcytanFVAPEVLT----QQGYDAACDIWSLGVLLYTMLAGYTPFS 661
Cdd:cd06616   162 DSIAKTrdagcrP-----YMAPERIDpsasRDGYDVRSDVWSLGITLYEVATGKFPYP 214
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
111-331 8.70e-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: 90.36  E-value: 8.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVR-KKTGpdagQLYAMKvlrkaslkvrdrvRTKMER-------------DILVEVNHPFIVKL 176
Cdd:cd07843     7 YEKLNRIEEGTYGVVYRARdKKTG----EIVALK-------------KLKMEKekegfpitslreiNILLKLQHPNIVTV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAF--QTEGKLYLILDF----LRggDVFTRLSKEvlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHI 250
Cdd:cd07843    70 KEVVvgSNLDKIYMVMEYvehdLK--SLMETMKQP--FLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGIL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 251 KLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLG 329
Cdd:cd07843   146 KICDFGLAREYGSPLKPYTQLVVTLWYRAPELLlGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKL-LG 224

                  ..
gi 1958807372 330 MP 331
Cdd:cd07843   225 TP 226
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
470-660 8.82e-20

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: 90.10  E-value: 8.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCihSASNMEFAVKiidKNKRDPSEEIEI----------LMRYGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd14146     2 IGVGGFGKVYRA--TWKGQEVAVK---AARQDPDEDIKAtaesvrqeakLFSMLRHPNIIKLEGVCLEEPNLCLVMEFAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELlDRILKKKCFSEQEAS----------NVLYVITKTVEYLHSQGVV---HRDLKPSNILYMDESGHPD----SIKIC 602
Cdd:cd14146    77 GGTL-NRALAAANAAPGPRRarripphilvNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEKIEHDDicnkTLKIT 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 603 DFGFAKQLRGENGLLLTPCYTanFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14146   156 DFGLAREWHRTTKMSAAGTYA--WMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPY 211
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-368 1.04e-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: 90.13  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVL-------------RKASLkvrdrvrtkmerdiLVEVNHPFIVKLHYAF 180
Cdd:cd07844     5 LDKLGEGSYATVYKGRSKL---TGQLVALKEIrleheegapftaiREASL--------------LKDLKHANIVTLHDII 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 QTEGKLYLILDFLRggdvfTRLSKEV-----LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDF 255
Cdd:cd07844    68 HTKKTLTLVFEYLD-----TDLKQYMddcggGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 256 GLSK-ESVdqEKKAYSF-CGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAkLGMP 331
Cdd:cd07844   143 GLARaKSV--PSKTYSNeVVTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMATGRPLFPGsTDVEDQLHKIFRV-LGTP 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 332 Q---------------------------------FLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07844   220 TeetwpgvssnpefkpysfpfypprplinhaprlDRIPHGEELALKFLQYEPKKRISA---AEAMKHPYF 286
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
112-313 1.05e-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: 90.17  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 112 DLLKV--LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd07861     1 DYTKIekIGEGTYGVVYKGRNKK---TGQIVAMKKIR---LESEEEgVPSTAIREIslLKELQHPNIVCLEDVLMQENRL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGgDV---FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVD 263
Cdd:cd07861    75 YLVFEFLSM-DLkkyLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLAR-AFG 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 264 QEKKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQG 313
Cdd:cd07861   153 IPVRVYTHeVVTLWYRAPEVlLGSPRYSTPVDIWSIGTIFAEMATKKPLFHG 204
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
114-332 1.22e-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: 89.83  E-value: 1.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKtGPDAGQLYAMkVLRKASLKVRDRVRT---KMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAK-GIEEEGGETL-VLVKALQKTKDENLQsefRRELDMFRKLSHKNVVRLLGLCREAEPHYMIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDV--FTRLSKEVLFTEE----DVKFYLA---ELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd05046    88 EYTDLGDLkqFLRATKSKDEKLKppplSTKQKVAlctQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDV 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 262 VDQEkkAYSFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLGMPQ 332
Cdd:cd05046   168 YNSE--YYKLRNAlipLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGELPFYGLSDEEVLNRLQAGKLELPV 240
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
161-357 1.27e-19

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 89.13  E-value: 1.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 161 ERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPE 240
Cdd:cd14112    50 EFESLRTLQHENVQRLIAAFKPSNFAYLVMEKLQE-DVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPD 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 241 NILLDEIG--HIKLTDFGlSKESVDQEKKAYSfCGTVEYMAPEVVNRRGHS--QSaDWWSYGVLMFEMLTGTLPFQG--K 314
Cdd:cd14112   129 NIMFQSVRswQVKLVDFG-RAQKVSKLGKVPV-DGDTDWASPEFHNPETPItvQS-DIWGLGVLTFCLLSGFHPFTSeyD 205
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 315 DRNETMNMILKAKLG---MPQFLSAEAQSLLRMLFKRNPANRLGSE 357
Cdd:cd14112   206 DEEETKENVIFVKCRpnlIFVEATQEALRFATWALKKSPTRRMRTD 251
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
115-353 1.49e-19

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 88.88  E-value: 1.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFL-VRKKTGPdagqlYAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGK-LYLI--- 189
Cdd:cd05034     1 KKLGAGQFGEVWMgVWNGTTK-----VAVKTLKPGTMSPEAFLQ---EAQIMKKLRHDKLVQL-YAVCSDEEpIYIVtel 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 ------LDFLRGGD-VFTRLSKEVLFTeedvkfylAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 262
Cdd:cd05034    72 mskgslLDYLRTGEgRALRLPQLIDMA--------AQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIE 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSfcGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAE 337
Cdd:cd05034   144 DDEYTARE--GAkfpIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNREVLEQVERGyRMPKPPGCPDE 221
                         250
                  ....*....|....*.
gi 1958807372 338 AQSLLRMLFKRNPANR 353
Cdd:cd05034   222 LYDIMLQCWKKEPEER 237
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
110-353 1.50e-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: 90.47  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvRKKTGPDAGQL---YAMKVLRKA-SLKVRDRVRTkmERDILVEVNHPFIVKL-----HYAF 180
Cdd:cd05108     8 EFKKIKVLGSGAFGTVY--KGLWIPEGEKVkipVAIKELREAtSPKANKEILD--EAYVMASVDNPHVCRLlgiclTSTV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 QTEGKLY---LILDFLRGGDvfTRLSKEVLFTeedvkfYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05108    84 QLITQLMpfgCLLDYVREHK--DNIGSQYLLN------WCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSFCGTV--EYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQF 333
Cdd:cd05108   156 AKLLGAEEKEYHAEGGKVpiKWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEISSILEKGeRLPQPPI 235
                         250       260
                  ....*....|....*....|
gi 1958807372 334 LSAEAQSLLRMLFKRNPANR 353
Cdd:cd05108   236 CTIDVYMIMVKCWMIDADSR 255
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
117-305 1.50e-19

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: 89.09  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14065     1 LGKGFFGEVYKVTHRE---TGKVMVMKELKRFD----EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHRLGIVYRDLKPENILLDEIGHIK---LTDFGLSKESVD------QEK 266
Cdd:cd14065    74 TLEELLKSMDEQLPWSQRVSLAkDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLAREMPDektkkpDRK 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14065   154 KRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
496-719 1.50e-19

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 92.62  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 496 DKNKRDPSEEIEILMrygqhpniislkevfddgkyVYLVTDLMKGGELLDRILKK----KCFSEQEASNVLYVITKTVEY 571
Cdd:PTZ00283   99 DFAKKDPRNPENVLM--------------------IALVLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHH 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 572 LHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQ----LRGENGLllTPCYTANFVAPEVLTQQGYDAACDIWSLG 647
Cdd:PTZ00283  159 VHSKHMIHRDIKSANILLCSNG----LVKLGDFGFSKMyaatVSDDVGR--TFCGTPYYVAPEIWRRKPYSKKADMFSLG 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 648 VLLYTMLAGYTPFsNGPNdtPEEILLRIGNGRFSlsgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:PTZ00283  233 VLLYELLTLKRPF-DGEN--MEEVMHKTLAGRYD---PLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
113-353 1.53e-19

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: 89.18  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVRKKtgpdAGQLYAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGKLYLILDF 192
Cdd:cd05067    11 LVERLGAGQFGEVWMGYYN----GHTKVAIKSLKQGSMSPDAFLA---EANLMKQLQHQRLVRLY-AVVTQEPIYIITEY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFtrlskEVLFTEEDVKFYL-------AELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd05067    83 MENGSLV-----DFLKTPSGIKLTInklldmaAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNE 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETM-NMILKAKLGMPQFLSAEAQSLL 342
Cdd:cd05067   158 YTAREGAKfPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVThGRIPYPGMTNPEVIqNLERGYRMPRPDNCPEELYQLM 237
                         250
                  ....*....|.
gi 1958807372 343 RMLFKRNPANR 353
Cdd:cd05067   238 RLCWKERPEDR 248
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
113-361 1.65e-19

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: 89.45  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFL--VRKKTGPDAGQLYAMKVLRKASLkvrDRVRTKMERD--ILVEVNHPFIVKLhYAFQTEGK-LY 187
Cdd:cd05049     9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASS---PDARKDFEREaeLLTNLQHENIVKF-YGVCTEGDpLL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDV--FTRL------------SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLT 253
Cdd:cd05049    85 MVFEYMEHGDLnkFLRShgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 254 DFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LG 329
Cdd:cd05049   165 DFGMSRDiySTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQPWFQLSNTEVIECITQGRlLQ 244
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 330 MPQFLSAEAQSLLRMLFKRNPANRLGSEGVEE 361
Cdd:cd05049   245 RPRTCPSEVYAVMLGCWKREPQQRLNIKDIHK 276
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
107-353 2.02e-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: 88.47  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFL----VRKKTgpdagqlyAMKVLRKASLKVRDrvrTKMERDILVEVNHPFIVKLHYAFQT 182
Cdd:cd05112     2 DPSELTFVQEIGSGQFGLVHLgywlNKDKV--------AIKTIREGAMSEED---FIEEAEVMMKLSHPKLVQLYGVCLE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd05112    71 QAPICLVFEFMEHGCLSDYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFV 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKaySFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSA 336
Cdd:cd05112   151 LDDQYT--SSTGTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGfRLYKPRLAST 228
                         250
                  ....*....|....*..
gi 1958807372 337 EAQSLLRMLFKRNPANR 353
Cdd:cd05112   229 HVYEIMNHCWKERPEDR 245
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
110-368 2.21e-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: 2.21e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKvlrKASLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNR---ETHEIVALK---RVRLDDDDEgVPSSALREIclLKELKHKNIVRLYDVLHSDKKL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDF----LRggDVFTRLSKEVlfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSV 262
Cdd:cd07839    75 TLVFEYcdqdLK--KYFDSCNGDI--DPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLAR-AF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSF-CGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLP-FQGKDRNETMNMILKAkLGMPQF------ 333
Cdd:cd07839   150 GIPVRCYSAeVVTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAELANAGRPlFPGNDVDDQLKRIFRL-LGTPTEeswpgv 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 334 ------------------------LSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07839   229 sklpdykpypmypattslvnvvpkLNSTGRDLLQNLLVCNPVQRISA---EEALQHPYF 284
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
464-723 2.56e-19

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: 88.28  E-value: 2.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEdIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE-------EIEILmRYGQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06607     4 EDLRE-IGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTEkwqdiikEVKFL-RQLRHPNTIEYKGCYLREHTAWLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 --LMKGGELLDriLKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGEN 614
Cdd:cd06607    82 ycLGSASDIVE--VHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTE----PGTVKLADFGSASLVCPAN 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPcYtanFVAPEVL--TQQG-YDAACDIWSLGVL----------LYTMLAGYTPFSNGPNDTPeeillrigngrfS 681
Cdd:cd06607   156 SFVGTP-Y---WMAPEVIlaMDEGqYDGKVDVWSLGITcielaerkppLFNMNAMSALYHIAQNDSP------------T 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 682 LSGGIWDNISRGAKDLLshmLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06607   220 LSSGEWSDDFRNFVDSC---LQKIPQDRPSAEDLLKHPFVTR 258
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
116-353 2.93e-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: 88.09  E-value: 2.93e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLK---VRDRVRTKMERDILVEVNHPF--IVKLHYAFQTEGKLYLIL 190
Cdd:cd14102     7 VLGSGGFGTVYAGSRIAD---GLPVAVKHVVKERVTewgTLNGVMVPLEIVLLKKVGSGFrgVIKLLDWYERPDGFLIVM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLR-GGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIKLTDFG---LSKESVDQE 265
Cdd:cd14102    84 ERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGsgaLLKDTVYTD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 kkaysFCGTVEYMAPEVVN-RRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRnetmnmILKAKLGMPQFLSAEAQSLLRM 344
Cdd:cd14102   164 -----FDGTRVYSPPEWIRyHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEE------ILRGRLYFRRRVSPECQQLIKW 232

                  ....*....
gi 1958807372 345 LFKRNPANR 353
Cdd:cd14102   233 CLSLRPSDR 241
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
465-721 3.18e-19

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: 88.75  E-value: 3.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSYSVCKRCIHSASNMEFAVKII----DKNK-RDPSEEIEILMRyGQHPNIISLKEVFDDGKYVYLVTDLMK 539
Cdd:cd06622     4 EVLDELGKGNYGSVYKVLHRPTGVTMAMKEIrlelDESKfNQIIMELDILHK-AVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELlDRILKKKCFSEQEASNVL----YVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLrgEN 614
Cdd:cd06622    83 AGSL-DKLYAGGVATEGIPEDVLrritYAVVKGLKFLKEEhNIIHRDVKPTNVL-VNGNG---QVKLCDFGVSGNL--VA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQG------YDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIWD 688
Cdd:cd06622   156 SLAKTNIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRYPY---PPETYANIFAQLSAIVDGDPPTLPS 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd06622   233 GYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWL 265
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
107-325 3.44e-19

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: 89.14  E-value: 3.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKaslkVRDRvRTKMERDILVEVN-HPFIVKLHYAFQTEGK 185
Cdd:cd14132    16 SQDDYEIIRKIGRGKYSEVFEGINI---GNNEKVVIKVLKP----VKKK-KIKREIKILQNLRgGPNIVKLLDVVKDPQS 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LY--LILDFLRGGDVFTRLSKevlFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH-IKLTDFGLSkesv 262
Cdd:cd14132    88 KTpsLIFEYVNNTDFKTLYPT---LTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDHEKRkLRLIDWGLA---- 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 dqE----KKAYSF-CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLP-FQGKDRNEtmnMILK 325
Cdd:cd14132   161 --EfyhpGQEYNVrVASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMIFRKEPfFHGHDNYD---QLVK 225
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
470-709 3.57e-19

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: 89.74  E-value: 3.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDPSEEIEI-------LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd05633    13 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMTYAFHTPDKLCFILDLMNG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPdsiKICDFGFAKQLRGENGllLTP 620
Cdd:cd05633    93 GDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL-LDEHGHV---RISDLGLACDFSKKKP--HAS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEVLTQ-QGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEIllrignGRFSLSGGIW--DNISRGAKDL 697
Cdd:cd05633   167 VGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI------DRMTLTVNVElpDSFSPELKSL 240
                         250
                  ....*....|..
gi 1958807372 698 LSHMLHMDPHQR 709
Cdd:cd05633   241 LEGLLQRDVSKR 252
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
470-718 4.04e-19

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


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 88.10  E-value: 4.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSaSNMEFAVKIIdKNKRDPSE------EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGEL 543
Cdd:cd14066     1 IGSGGFGTVYKGVLE-NGTVVAVKRL-NEMNCAASkkefltELEMLGRL-RHPNLVRLLGYCLESDEKLLVYEYMPNGSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRIlkkkcfSEQEASNVLYVITKT---------VEYLHSQG---VVHRDLKPSNILyMDESGHPdsiKICDFGFAK--Q 609
Cdd:cd14066    78 EDRL------HCHKGSPPLPWPQRLkiakgiargLEYLHEECpppIIHGDIKSSNIL-LDEDFEP---KLTDFGLARliP 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPE----EILLRIGNGRFS--LS 683
Cdd:cd14066   148 PSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRkdlvEWVESKGKEELEdiLD 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 684 GGIWDNISR---GAKDLLS---HMLHMDPHQRYTAEQVLKH 718
Cdd:cd14066   228 KRLVDDDGVeeeEVEALLRlalLCTRSDPSLRPSMKEVVQM 268
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
111-354 5.52e-19

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: 87.32  E-value: 5.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLrKASLKVRD------RVRTKMERDIlvEVNHPFIVKLHYAFQTEG 184
Cdd:cd14133     1 YEVLEVLGKGTFGQVV---KCYDLLTGEEVALKII-KNNKDYLDqsldeiRLLELLNKKD--KADKYHIVRLKDVFYFKN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGG-DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG--HIKLTDFGLSKES 261
Cdd:cd14133    75 HLCIVFELLSQNlYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrcQIKIIDFGSSCFL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDqekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN------------MILKAKLG 329
Cdd:cd14133   155 TQ---RLYSYIQSRYYRAPEVILGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLAriigtigippahMLDQGKAD 231
                         250       260
                  ....*....|....*....|....*
gi 1958807372 330 MPQFLsaeaqSLLRMLFKRNPANRL 354
Cdd:cd14133   232 DELFV-----DFLKKLLEIDPKERP 251
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
513-721 5.78e-19

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 87.21  E-value: 5.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 513 GQHPNIISLKEVFDDGKYVYLVTDL-MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMD 591
Cdd:cd14101    64 PGHRGVIRLLDWFEIPEGFLLVLERpQHCQDLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDL 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 592 ESGhpdSIKICDFGFAKQLRGE-----NGllltpcyTANFVAPE-VLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngpn 665
Cdd:cd14101   144 RTG---DIKLIDFGSGATLKDSmytdfDG-------TRVYSPPEwILYHQYHALPATVWSLGILLYDMVCGDIPF----- 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 666 DTPEEILlrigngrfSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14101   209 ERDTDIL--------KAKPSFNKRVSNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
508-721 6.22e-19

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: 89.38  E-value: 6.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 508 ILMRYGQHPNIISLKEVFDDGKY------VYLVTDLMKGGelLDRILKKKcFSEQEASNVLYVITKTVEYLHSQGVVHRD 581
Cdd:cd07874    68 VLMKCVNHKNIISLLNVFTPQKSleefqdVYLVMELMDAN--LCQVIQME-LDHERMSYLLYQMLCGIKHLHSAGIIHRD 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 582 LKPSNILYMDESghpdSIKICDFGFAKQlrGENGLLLTP-CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd07874   145 LKPSNIVVKSDC----TLKILDFGLART--AGTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILF 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 661 SNGPN-DTPEEILLRIGN------------------GRFSLSGGIWDNI----------------SRGAKDLLSHMLHMD 705
Cdd:cd07874   219 PGRDYiDQWNKVIEQLGTpcpefmkklqptvrnyveNRPKYAGLTFPKLfpdslfpadsehnklkASQARDLLSKMLVID 298
                         250
                  ....*....|....*.
gi 1958807372 706 PHQRYTAEQVLKHPWI 721
Cdd:cd07874   299 PAKRISVDEALQHPYI 314
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
110-314 6.31e-19

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 89.90  E-value: 6.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:PHA03207   93 QYNILSSLTPGSEGEVFVCTKH-----GDEQRKKVIVKAVTGGKTPGR---EIDILKTISHRAIINLIHAYRWKSTVCMV 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS--KESVDQEKK 267
Cdd:PHA03207  165 MPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAckLDAHPDTPQ 243
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGK 314
Cdd:PHA03207  244 CYGWSGTLETNSPELLALDPYCAKTDIWSAGLVLFEMSVKNVTLFGK 290
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
470-709 6.47e-19

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: 88.57  E-value: 6.47e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKN--KRDPSEEIEI-------LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd14223     8 IGRGGFGEVYGCRKADTGKMYAMKCLDKKriKMKQGETLALnerimlsLVSTGDCPFIVCMSYAFHTPDKLSFILDLMNG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGllLTP 620
Cdd:cd14223    88 GDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANIL-LDEFGH---VRISDLGLACDFSKKKP--HAS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTANFVAPEVLtQQG--YDAACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEIllrignGRFSLSGGIW--DNISRGAKD 696
Cdd:cd14223   162 VGTHGYMAPEVL-QKGvaYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDKHEI------DRMTLTMAVElpDSFSPELRS 234
                         250
                  ....*....|...
gi 1958807372 697 LLSHMLHMDPHQR 709
Cdd:cd14223   235 LLEGLLQRDVNRR 247
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
518-737 6.87e-19

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: 89.34  E-value: 6.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 518 IISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpd 597
Cdd:cd05625    63 VVRLYYSFQDKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNIL-IDRDGH-- 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 598 sIKICDFGFAKQLR----------GEN--------------------GLLLTP-----------CY------TANFVAPE 630
Cdd:cd05625   140 -IKLTDFGLCTGFRwthdskyyqsGDHlrqdsmdfsnewgdpencrcGDRLKPlerraarqhqrCLahslvgTPNYIAPE 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 631 VLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHmDPHQRY 710
Cdd:cd05625   219 VLLRTGYTQLCDWWSVGVILFEMLVGQPPFL---AQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLCR-GPEDRL 294
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1958807372 711 ---TAEQVLKHPWITQ-------REQLPRHQPTSDDP 737
Cdd:cd05625   295 gknGADEIKAHPFFKTidfssdlRQQSAPYIPKITHP 331
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
107-335 7.04e-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: 87.24  E-value: 7.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVflvrkKTGPDAGQL-YAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK 185
Cdd:cd05113     2 DPKDLTFLKELGTGQFGVV-----KYGKWRGQYdVAIKMIKEGSMSEDEFIE---EAKVMMNLSHEKLVQLYGVCTKQRP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 264
Cdd:cd05113    74 IFIITEYMANGCLLNYLrEMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 265 EKKaySFCGT---VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 335
Cdd:cd05113   154 EYT--SSVGSkfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTNSETVEHVSQGlRLYRPHLAS 227
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
113-349 8.16e-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: 86.99  E-value: 8.16e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYLILDF 192
Cdd:cd14150     4 MLKRIGTGSFGTVF--RGKWHGDV----AVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQW 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLskEVLFTEEDVkFYLAELA----LALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL----SKESVDQ 264
Cdd:cd14150    77 CEGSSLYRHL--HVTETRFDT-MQLIDVArqtaQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLatvkTRWSGSQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSfcGTVEYMAPEVVNRRG---HSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAKLG--MPQFLSAEA 338
Cdd:cd14150   154 QVEQPS--GSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSNiNNRDQIIFMVGRGYLSpdLSKLSSNCP 231
                         250
                  ....*....|....*.
gi 1958807372 339 QSLLRML-----FKRN 349
Cdd:cd14150   232 KAMKRLLidclkFKRE 247
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
460-720 8.57e-19

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: 88.37  E-value: 8.57e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCI-HSASNMEFAVKII---DKNKRDPSEEIEILMRYGQ-HPN----IISLKEVFDDGKY 530
Cdd:cd14213    10 LRARYEIVDTLGEGAFGKVVECIdHKMGGMHVAVKIVknvDRYREAARSEIQVLEHLNTtDPNstfrCVQMLEWFDHHGH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMkGGELLDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDES--------------- 593
Cdd:cd14213    90 VCIVFELL-GLSTYDFIKENSFlpFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDyvvkynpkmkrdert 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 594 -GHPDsIKICDFGFAKQLRGENGLLLTpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSN---------- 662
Cdd:cd14213   169 lKNPD-IKVVDFGSATYDDEHHSTLVS---TRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQThdskehlamm 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 663 ----GPndTPEEILLRIGNGRFSLSGGI-WDNISRGAK------------------------DLLSHMLHMDPHQRYTAE 713
Cdd:cd14213   245 erilGP--LPKHMIQKTRKRKYFHHDQLdWDEHSSAGRyvrrrckplkefmlsqdvdheqlfDLIQKMLEYDPAKRITLD 322

                  ....*..
gi 1958807372 714 QVLKHPW 720
Cdd:cd14213   323 EALKHPF 329
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
110-305 9.72e-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: 87.24  E-value: 9.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPDAgqlYAMKVLRKASlkvRDRVRTKMERDI--LVEVNHPFIVKLHYAF------- 180
Cdd:cd14048     7 DFEPIQCLGRGGFGVVFEAKNKVDDCN---YAVKRIRLPN---NELAREKVLREVraLAKLDHPGIVRYFNAWlerppeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 ----QTEGKLYLILDFLRGGDVFTRLSKEVLFTEED---VKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLT 253
Cdd:cd14048    81 wqekMDEVYLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVG 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 254 DFGL--------SKESVDQEKKAYSF----CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14048   161 DFGLvtamdqgePEQTVLTPMPAYAKhtgqVGTRLYMSPEQIHGNQYSEKVDIFALGLILFELI 224
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
487-678 9.80e-19

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: 86.72  E-value: 9.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 487 NMEFAVKIIDKN----KRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVL 562
Cdd:cd05148    30 RVRVAIKILKSDdllkQQDFQKEVQALKRL-RHKHLISLFAVCSVGEPVYIITELMEKGSLLA-FLRSPEGQVLPVASLI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVE---YLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKqlrgengLLLTPCYTAN-------FVAPEVL 632
Cdd:cd05148   108 DMACQVAEgmaYLEEQNSIHRDLAARNILVGEDL----VCKVADFGLAR-------LIKEDVYLSSdkkipykWTAPEAA 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 633 TQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNG 678
Cdd:cd05148   177 SHGTFSTKSDVWSFGILLYEMFTyGQVPY---PGMNNHEVYDQITAG 220
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
464-732 1.11e-18

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 87.47  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID---KNKRDPSEEIEILMRYGQHPNIISLKEVF--------DDgkYVY 532
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDvtgDEEEEIKQEINMLKKYSHHRNIATYYGAFikknppgmDD--QLW 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LVTDLMKGGELLDRI--LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQL 610
Cdd:cd06637    86 LVMEFCGAGSVTDLIknTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENA----EVKLVDFGVSAQL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 RGENGLLLTPCYTANFVAPEVLT-----QQGYDAACDIWSLGVLLYTMLAGYTPFSNGpndTPEEILLRIG-NGRFSLSG 684
Cdd:cd06637   162 DRTVGRRNTFIGTPYWMAPEVIAcdenpDATYDFKSDLWSLGITAIEMAEGAPPLCDM---HPMRALFLIPrNPAPRLKS 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 685 GIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWItqreqlpRHQP 732
Cdd:cd06637   239 KKW---SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI-------RDQP 276
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
469-718 1.29e-18

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: 86.60  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFA------VKIIDKNKRDPSEEIEILmRYGQHPNII----SLKEVFDDGKYVYLVTDLM 538
Cdd:cd14033     8 EIGRGSFKTVYRGLDTETTVEVAwcelqtRKLSKGERQRFSEEVEML-KGLQHPNIVrfydSWKSTVRGHKCIILVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGEL---LDRILKKKCFSEQEASNVlyvITKTVEYLHSQG--VVHRDLKPSNILYMDESGhpdSIKICDFGFA--KQLR 611
Cdd:cd14033    87 TSGTLktyLKRFREMKLKLLQRWSRQ---ILKGLHFLHSRCppILHRDLKCDNIFITGPTG---SVKIGDLGLAtlKRAS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPcytaNFVAPEvLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLRIGNGRFSLSggIWDNIS 691
Cdd:cd14033   161 FAKSVIGTP----EFMAPE-MYEEKYDEAVDVYAFGMCILEMATSEYPYSECQN--AAQIYRKVTSGIKPDS--FYKVKV 231
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd14033   232 PELKEIIEGCIRTDKDERFTIQDLLEH 258
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
113-353 1.29e-18

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: 86.71  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFL-VRKKTGPDAGQLyAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGKLYLILD 191
Cdd:cd05056    10 LGRCIGEGQFGDVYQgVYMSPENEKIAV-AVKTC-KNCTSPSVREKFLQEAYIMRQFDHPHIVKL-IGVITENPVWIVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDV--FTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-KKA 268
Cdd:cd05056    87 LAPLGELrsYLQVNKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESyYKA 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLF 346
Cdd:cd05056   166 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCW 245

                  ....*..
gi 1958807372 347 KRNPANR 353
Cdd:cd05056   246 AYDPSKR 252
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
117-354 1.29e-18

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: 86.94  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVR-KKTGPDAGQ-LYAMKVLRKASLKVRDRVrtKMERDILVEVNHPFIVKLhYAFQTEGK-LYLILDFL 193
Cdd:cd05092    13 LGEGAFGKVFLAEcHNLLPEQDKmLVAVKALKEATESARQDF--QREAELLTVLQHQHIVRF-YGVCTEGEpLIMVFEYM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDV--FTRL---SKEVLFTEEDVKF----------YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd05092    90 RHGDLnrFLRShgpDAKILDGGEGQAPgqltlgqmlqIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQFL 334
Cdd:cd05092   170 RDiySTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGReLERPRTC 249
                         250       260
                  ....*....|....*....|
gi 1958807372 335 SAEAQSLLRMLFKRNPANRL 354
Cdd:cd05092   250 PPEVYAIMQGCWQREPQQRH 269
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
107-311 1.36e-18

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: 86.46  E-value: 1.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLHyAFQTEGKL 186
Cdd:cd05066     2 DASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTL-KAGYTEKQRRDFLSEASIMGQFDHPNIIHLE-GVVTRSKP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLIL-DFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 264
Cdd:cd05066    80 VMIVtEYMENGSLDAFLRKhDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDD 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 265 EKKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPF 311
Cdd:cd05066   160 PEAAYTTRGgkiPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 210
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
462-723 2.02e-18

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: 86.25  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdknKRDPSEEIE------ILMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd06645    11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVI---KLEPGEDFAvvqqeiIMMKDCKHSNIVAYFGSYLRRDKLWICM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDeSGHpdsIKICDFGFAKQLRGENG 615
Cdd:cd06645    88 EFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTD-NGH---VKLADFGVSAQITATIA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQ---GYDAACDIWSLGVLLYTMLAGYTPFSngpNDTPEEILLRIGNGRFS---LSGGI-WD 688
Cdd:cd06645   164 KRKSFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPMF---DLHPMRALFLMTKSNFQppkLKDKMkWS 240
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 689 NisrGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06645   241 N---SFHHFVKMALTKNPKKRPTAEKLLQHPFVTQ 272
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
462-720 2.43e-18

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 86.99  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCI-HSASNMEFAVKII---DKNKRDPSEEIEILMRygqhpniisLKEVFDDGKYV-YLVTD 536
Cdd:cd14214    13 ERYEIVGDLGEGTFGKVVECLdHARGKSQVALKIIrnvGKYREAARLEINVLKK---------IKEKDKENKFLcVLMSD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMK-GGELLD--RILKKKCFSEQEASNVL-----------YVITKTVEYLHSQGVVHRDLKPSNILYM------------ 590
Cdd:cd14214    84 WFNfHGHMCIafELLGKNTFEFLKENNFQpyplphirhmaYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynesk 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 591 ---DESGHPDSIKICDFGFAKqlrGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN-- 665
Cdd:cd14214   164 sceEKSVKNTSIRVADFGSAT---FDHEHHTTIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENre 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 666 ----------DTPEEILLRIGNGRFSLSGG-IWDNISRGAK------------------------DLLSHMLHMDPHQRY 710
Cdd:cd14214   241 hlvmmekilgPIPSHMIHRTRKQKYFYKGSlVWDENSSDGRyvsenckplmsymlgdslehtqlfDLLRRMLEFDPALRI 320
                         330
                  ....*....|
gi 1958807372 711 TAEQVLKHPW 720
Cdd:cd14214   321 TLKEALLHPF 330
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
109-332 2.45e-18

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 85.93  E-value: 2.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFL-VRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKmERDILVEVNHPFIVKLhYAFQTEGKLY 187
Cdd:cd05057     7 TELEKGKVLGSGAFGTVYKgVWIPEGEKVKIPVAIKVLREETGPKANEEILD-EAYVMASVDHPHLVRL-LGICLSSQVQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGG--DVFTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQE 265
Cdd:cd05057    85 LITQLMPLGclLDYVRNHRDNIGSQLLLNWCV-QIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAK-LLDVD 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 266 KKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQ 332
Cdd:cd05057   163 EKEYHAEGgkvPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTfGAKPYEGIPAVEIPDLLEKGeRLPQPP 234
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
114-371 2.80e-18

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 86.58  E-value: 2.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTGPDagqLYAMKVLRkasLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd07872    11 LEKLGEGTYATVFKGRSKLTEN---LVALKEIR---LEHEEGAPCTAIREVslLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd07872    85 YL-DKDLKQYMDDcGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSVPTKTYSN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 FCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP-----------------Q 332
Cdd:cd07872   164 EVVTLWYRPPDVlLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRL-LGTPteetwpgissndefknyN 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 333 FLSAEAQSLLrmlfkrNPANRLGSEGVE-----------------EVKRHAFFSSI 371
Cdd:cd07872   243 FPKYKPQPLI------NHAPRLDTEGIElltkflqyeskkrisaeEAMKHAYFRSL 292
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
464-720 2.95e-18

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: 86.21  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVK-IIDKNKRD-----PSEEIEILMRYgQHPNIISLKEVF--------DDGK 529
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDgfpitALREIKILKKL-KHPNVVPLIDMAverpdkskRKRG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 530 YVYLVTDLMK---GGELLDRILKkkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGF 606
Cdd:cd07866    89 SVYMVTPYMDhdlSGLLENPSVK---LTESQIKCYMLQLLEGINYLHENHILHRDIKAANIL-IDNQG---ILKIADFGL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLRGE------NGLLLTPCYTANFV-----APE-VLTQQGYDAACDIWSLGVLLYTMLAGyTPFSNGPND-------- 666
Cdd:cd07866   162 ARPYDGPppnpkgGGGGGTRKYTNLVVtrwyrPPElLLGERRYTTAVDIWGIGCVFAEMFTR-RPILQGKSDidqlhlif 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 667 ----TPEEI-------------LLRIGNGRFSLSGGIWDNISRGAkDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07866   241 klcgTPTEEtwpgwrslpgcegVHSFTNYPRTLEERFGKLGPEGL-DLLSKLLSLDPYKRLTASDALEHPY 310
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
465-729 3.02e-18

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: 85.48  E-value: 3.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSY-SVCKRCIHSasnmEFAVKIIDKNkRDPSEEIE----ILMRYGQ--HPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd14063     3 EIKEVIGKGRFgRVHRGRWHG----DVAIKLLNID-YLNEEQLEafkeEVAAYKNtrHDNLVLFMGACMDPPHLAIVTSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdESGhpdSIKICDFGFAK-----QLR 611
Cdd:cd14063    78 CKGRTLYSLIHERKEkFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL--ENG---RVVITDFGLFSlsgllQPG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPCYTANFVAPEVLT----------QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPndtPEEILLRIGNG-RF 680
Cdd:cd14063   153 RREDTLVIPNGWLCYLAPEIIRalspdldfeeSLPFTKASDVYAFGTVWYELLAGRWPFKEQP---AESIIWQVGCGkKQ 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 681 SLSGgiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKhpwitQREQLPR 729
Cdd:cd14063   230 SLSQ---LDIGREVKDILMQCWAYDPEKRPTFSDLLR-----MLERLPK 270
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
505-721 3.52e-18

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: 86.01  E-value: 3.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILmRYGQHPNIISLKEVFDDGK---------------YVYLVTDLMKggeLLDRILKKkcFSEQEASNVLYVITKTV 569
Cdd:cd07864    56 EIKIL-RQLNHRSVVNLKEIVTDKQdaldfkkdkgafylvFEYMDHDLMG---LLESGLVH--FSEDHIKSFMKQLLEGL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 570 EYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLT-PCYTANFVAPEVLT-QQGYDAACDIWSLG 647
Cdd:cd07864   130 NYCHKKNFLHRDIKCSNIL-LNNKGQ---IKLADFGLARLYNSEESRPYTnKVITLWYRPPELLLgEERYGPAIDVWSCG 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 648 VLLYTMLAgYTPFSNGPNDTPE-EILLRIGNgrfSLSGGIWDN--------------------------ISRGAKDLLSH 700
Cdd:cd07864   206 CILGELFT-KKPIFQANQELAQlELISRLCG---SPCPAVWPDviklpyfntmkpkkqyrrrlreefsfIPTPALDLLDH 281
                         250       260
                  ....*....|....*....|.
gi 1958807372 701 MLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd07864   282 MLTLDPSKRCTAEQALNSPWL 302
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
110-332 4.24e-18

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: 85.47  E-value: 4.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRK-KTGpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVN---HPFIVKLHYAFQT--- 182
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDlKNG---GRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVsrt 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 --EGKLYLILDFLrGGDVFTRLSK--EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd07862    79 drETKLTLVFEHV-DQDLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 kesvdqekKAYSF-------CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07862   158 --------RIYSFqmaltsvVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDV-IGLP 228

                  .
gi 1958807372 332 Q 332
Cdd:cd07862   229 G 229
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
491-679 4.32e-18

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: 85.51  E-value: 4.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII-----DKNKRDPSEEIEIlMRYGQHPNIISLKEVFDD--GKYVYLVTDLMKGGELLD-------RILKKKC--FS 554
Cdd:cd05038    37 AVKSLqpsgeEQHMSDFKREIEI-LRTLDHEYIVKYKGVCESpgRRSLRLIMEYLPSGSLRDylqrhrdQIDLKRLllFA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 555 EQeasnvlyvITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLRGENGLlltpcYTAN--------F 626
Cdd:cd05038   116 SQ--------ICKGMEYLGSQRYIHRDLAARNILVESE----DLVKISDFGLAKVLPEDKEY-----YYVKepgespifW 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 627 VAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndTPEEILLRIGNGR 679
Cdd:cd05038   179 YAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQS----PPALFLRMIGIAQ 227
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
115-367 4.40e-18

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: 85.03  E-value: 4.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRkktGPDAGQLYAMK---VLRKASLKVrdrvrTKMERDILVEV-NHPFIVKL--HYAFQTEGKLY- 187
Cdd:cd14037     9 KYLAEGGFAHVYLVK---TSNGGNRAALKrvyVNDEHDLNV-----CKREIEIMKRLsGHKNIVGYidSSANRSGNGVYe 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 --LILDFLRGGDVF----TRLSKEvlFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLDEIGHIKLTDFG--- 256
Cdd:cd14037    81 vlLLMEYCKGGGVIdlmnQRLQTG--LTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGsat 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 257 ---------LSKESVDQEKKAYSfcgTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQgkdrnETMNM-I 323
Cdd:cd14037   159 tkilppqtkQGVTYVEEDIKKYT---TLQYRAPEMIDlyrGKPITEKSDIWALGCLLYKLCFYTTPFE-----ESGQLaI 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 324 LKAKLGMPQF--LSAEAQSLLRMLFKRNPANRlgsEGVEEVKRHAF 367
Cdd:cd14037   231 LNGNFTFPDNsrYSKRLHKLIRYMLEEDPEKR---PNIYQVSYEAF 273
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
114-313 5.28e-18

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: 85.01  E-value: 5.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLrkaSLKVRDRV--RTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd07870     5 LEKLGEGSYATVY---KGISRINGQLVALKVI---SMKTEEGVpfTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRggdvfTRLSKEVL-----FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd07870    79 YMH-----TDLAQYMIqhpggLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSQ 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 267 KAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQG 313
Cdd:cd07870   154 TYSSEVVTLWYRPPDVLlGATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
119-354 5.66e-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: 84.29  E-value: 5.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 119 QGSFGKVFLV--RKKTGPDAGQLYAMKVLRKASLKVRDRVRtkmerdilvevnHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd13995    14 RGAFGKVYLAqdTKTKKRMACKLIPVEQFKPSDVEIQACFR------------HENIAELYGALLWEETVHLFMEAGEGG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIkLTDFGLSKESVDQEKKAYSFCGTVE 276
Cdd:cd13995    82 SVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKDLRGTEI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 277 YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET----MNMILKAK---LGMPQFLSAEAQSLLRMLFKRN 349
Cdd:cd13995   161 YMSPEVILCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAypsyLYIIHKQApplEDIAQDCSPAMRELLEAALERN 240

                  ....*
gi 1958807372 350 PANRL 354
Cdd:cd13995   241 PNHRS 245
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
116-353 5.66e-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: 84.97  E-value: 5.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKASLKVRDRVRTKM-------------------ERDILVEVNHPFIVKL 176
Cdd:cd14000     1 LLGDGGFGSVYRASYK-----GEPVAVKIFNKHTSSNFANVPADTmlrhlratdamknfrllrqELTVLSHLHHPSIVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAfqTEGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELAL----ALDHLHRLGIVYRDLKPENILL-----DEI 247
Cdd:cd14000    76 LGI--GIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALqvadGLRYLHSAMIIYRDLKSHNVLVwtlypNSA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GHIKLTDFGLSKESVDQEKKaySFCGTVEYMAPEVVNRR-GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKa 326
Cdd:cd14000   154 IIIKIADYGISRQCCRMGAK--GSEGTPGFRAPEIARGNvIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFPNEFDIHG- 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 327 klGMPQFLS-------AEAQSLLRMLFKRNPANR 353
Cdd:cd14000   231 --GLRPPLKqyecapwPEVEVLMKKCWKENPQQR 262
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
464-721 5.91e-18

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: 85.91  E-value: 5.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSE---EIEILM------RYGQHpNIISLKEVFDDGKYVYLV 534
Cdd:cd14225    45 YEILEVIGKGSFGQVVKALDHKTNEHVAIKIIRNKKRFHHQalvEVKILDalrrkdRDNSH-NVIHMKEYFYFRNHLCIT 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMkgGELLDRILKK---KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpDSIKICDFGfakqlr 611
Cdd:cd14225   124 FELL--GMNLYELIKKnnfQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENIL-LRQRGQ-SSIKVIDFG------ 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 genglllTPCYTANFV----------APEVLTQQGYDAACDIWSLGVLLYTMLAGYtPFSNGPN------------DTPE 669
Cdd:cd14225   194 -------SSCYEHQRVytyiqsrfyrSPEVILGLPYSMAIDMWSLGCILAELYTGY-PLFPGENeveqlacimevlGLPP 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 670 EILLRIGNGR--FSLSGGIWDNI--SRGAK--------------------DLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14225   266 PELIENAQRRrlFFDSKGNPRCItnSKGKKrrpnskdlasalktsdplflDFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
110-354 6.29e-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: 85.11  E-value: 6.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrkKTGPDAGQLYAMKVLRKASLKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd14040     7 RYLLLHLLGRGGFSEVY----KAFDLYEQRYAAVKIHQLNKSWRDEKKENYhkhacrEYRIHKELDHPRIVKLYDYFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLY-LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLDE---IGHIKLTDFGL 257
Cdd:cd14040    83 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDgtaCGEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SK------ESVDQEKKAYSFCGTVEYMAPE--VVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETM---NMIL 324
Cdd:cd14040   163 SKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqeNTIL 242
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 325 KA---KLGMPQFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd14040   243 KAtevQFPVKPVVSNEAKAFIRRCLAYRKEDRF 275
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
114-353 6.36e-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: 85.93  E-value: 6.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL------Y 187
Cdd:cd07850     5 LKPIGSGAQGIVCAAYDTV---TGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKesvdqeKK 267
Cdd:cd07850    82 LVMELM---DANLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR------TA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVE-----YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMP--QFLSaEAQS 340
Cdd:cd07850   153 GTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIE-QLGTPsdEFMS-RLQP 230
                         250
                  ....*....|...
gi 1958807372 341 LLRMLFKRNPANR 353
Cdd:cd07850   231 TVRNYVENRPKYA 243
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
117-318 6.75e-18

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: 83.98  E-value: 6.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVR-------KK---TGPDAGQLYAMK----VLRKASlkvrdrvrtkmerdilvEVNhpfiVKLHYAFQT 182
Cdd:cd14062     1 IGSGSFGTVYKGRwhgdvavKKlnvTDPTPSQLQAFKnevaVLRKTR-----------------HVN----ILLFMGYMT 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLskEVLfteeDVKFYLAEL-------ALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDF 255
Cdd:cd14062    60 KPQLAIVTQWCEGSSLYKHL--HVL----ETKFEMLQLidiarqtAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDF 133
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 256 GL----SKESVDQEKKAYSfcGTVEYMAPEVVNRRG---HSQSADWWSYGVLMFEMLTGTLPFQGKDRNE 318
Cdd:cd14062   134 GLatvkTRWSGSQQFEQPT--GSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELLTGQLPYSHINNRD 201
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
117-361 6.82e-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: 6.82e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGpdagQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14027     1 LDSGGFGKVSLCFHRTQ----GLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG---------LSKESVDQEKK 267
Cdd:cd14027    77 NLMHVLKKVSVPLSVKGRIIL-EIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwskLTKEEHNEQRE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFC----GTVEYMAPE---VVNRRGhSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAK-----LGMPQFLS 335
Cdd:cd14027   156 VDGTAkknaGTLYYMAPEhlnDVNAKP-TEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGnrpdvDDITEYCP 234
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 336 AEAQSLLRMLFKRNPANRLGSEGVEE 361
Cdd:cd14027   235 REIIDLMKLCWEANPEARPTFPGIEE 260
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
466-660 7.19e-18

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


Pssm-ID: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 84.31  E-value: 7.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSYSVCKRciHSASNMEFAVKiidKNKRDPSEEIEI----------LMRYGQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd14147     7 LEEVIGIGGFGKVYR--GSWRGELVAVK---AARQDPDEDISVtaesvrqearLFAMLAHPNIIALKAVCLEEPNLCLVM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELlDRILKKKCFSEQEASNVLYVITKTVEYLHSQG---VVHRDLKPSNILYM----DESGHPDSIKICDFGFAK 608
Cdd:cd14147    82 EYAAGGPL-SRALAGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLqpieNDDMEHKTLKITDFGLAR 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 609 QLRGENGLLLTPCYTanFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14147   161 EWHKTTQMSAAGTYA--WMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPY 210
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
111-345 7.23e-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: 85.53  E-value: 7.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRvRTKMERDILVEV-NHPFIVKLH-------YAFQt 182
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETSEEETVAIKKITNVFSKKILAK-RALRELKLLRHFrGHKNITCLYdmdivfpGNFN- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 egKLYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE-S 261
Cdd:cd07857    80 --ELYLYEE-LMEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGfS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKA---YSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP------ 331
Cdd:cd07857   157 ENPGENAgfmTEYVATRWYRAPEImLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQV-LGTPdeetls 235
                         250
                  ....*....|....
gi 1958807372 332 QFLSAEAQSLLRML 345
Cdd:cd07857   236 RIGSPKAQNYIRSL 249
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
103-331 8.01e-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: 85.13  E-value: 8.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADpaQFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQT 182
Cdd:cd07869     1 FGKAD--SYEKLEKLGEGSYATVYKGKSKVN---GKLVALKVIRLQEEEGTPFTAIR-EASLLKGLKHANIVLLHDIIHT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGgDVFTRLSKEVL-FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKES 261
Cdd:cd07869    75 KETLTLVFEYVHT-DLCQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAK 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 262 VDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAkLGMP 331
Cdd:cd07869   154 SVPSHTYSNEVVTLWYRPPDVlLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGmKDIQDQLERIFLV-LGTP 224
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
508-721 8.03e-18

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 85.87  E-value: 8.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 508 ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSE---QEASNVLYVITKTVEYLHSQGVVHRDLKP 584
Cdd:cd07875    75 VLMKCVNHKNIIGLLNVFTPQKSLEEFQDVYIVMELMDANLCQVIQMEldhERMSYLLYQMLCGIKHLHSAGIIHRDLKP 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 585 SNILYMDESghpdSIKICDFGFAKQlrGENGLLLTP-CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNG 663
Cdd:cd07875   155 SNIVVKSDC----TLKILDFGLART--AGTSFMMTPyVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGT 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 664 PN-DTPEEILLRIGN------------------GRFSLSGGIWDNI----------------SRGAKDLLSHMLHMDPHQ 708
Cdd:cd07875   229 DHiDQWNKVIEQLGTpcpefmkklqptvrtyveNRPKYAGYSFEKLfpdvlfpadsehnklkASQARDLLSKMLVIDASK 308
                         250
                  ....*....|...
gi 1958807372 709 RYTAEQVLKHPWI 721
Cdd:cd07875   309 RISVDEALQHPYI 321
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
108-343 8.28e-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: 84.26  E-value: 8.28e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05063     4 PSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTL-KPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKFKPAM 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGG--DVFTRlSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd05063    83 IITEYMENGalDKYLR-DHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI-----LKAKLGMPqflSA 336
Cdd:cd05063   162 EGTYTTSGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSNHEVMKAIndgfrLPAPMDCP---SA 238

                  ....*..
gi 1958807372 337 EAQSLLR 343
Cdd:cd05063   239 VYQLMLQ 245
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
110-332 9.59e-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: 85.03  E-value: 9.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPDaGQLYAMKVLrKASLKVRDRVRTKMERDI--LVEVNHPFIVKLHYAF--QTEGK 185
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKNGKD-GKEYAIKKF-KGDKEQYTGISQSACREIalLRELKHENVVSLVEVFleHADKS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDF----LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFGL 257
Cdd:cd07842    79 VYLLFDYaehdLWQIIKFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSFCG---TVEYMAPEVVNRRGHSQSA-DWWSYGVLMFEMLTGTLPFQGK-DRNETMNM--------IL 324
Cdd:cd07842   159 ARLFNAPLKPLADLDPvvvTIWYRAPELLLGARHYTKAiDIWAIGCIFAELLTLEPIFKGReAKIKKSNPfqrdqlerIF 238

                  ....*...
gi 1958807372 325 KAkLGMPQ 332
Cdd:cd07842   239 EV-LGTPT 245
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
113-353 1.02e-17

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: 84.29  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVRKK-TGPDAGQLYAMKVLRKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd05090     9 FMEELGECAFGKIYKGHLYlPGMDHAQLVAIKTLKDYN-NPQQWNEFQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRL------SKEVLFTEED--VKFYL---------AELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd05090    88 FMNQGDLHEFLimrsphSDVGCSSDEDgtVKSSLdhgdflhiaIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGM 330
Cdd:cd05090   168 LGLSREiySSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQlLPC 247
                         250       260
                  ....*....|....*....|...
gi 1958807372 331 PQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05090   248 SEDCPPRMYSLMTECWQEIPSRR 270
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
461-661 1.04e-17

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 86.63  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIeILMRYGQHPNIISLKEVF------DDGKYVYLV 534
Cdd:PTZ00036   65 NKSYKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNREL-LIMKNLNHINIIFLKDYYytecfkKNEKNIFLN 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKCFSEQEASNVL-----YVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdSIKICDFGFAKQ 609
Cdd:PTZ00036  144 VVMEFIPQTVHKYMKHYARNNHALPLFLvklysYQLCRALAYIHSKFICHRDLKPQNLL-IDPNTH--TLKLCDFGSAKN 220
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 610 LRGENGLLLTPCyTANFVAPEV-LTQQGYDAACDIWSLGVLLYTMLAGYTPFS 661
Cdd:PTZ00036  221 LLAGQRSVSYIC-SRFYRAPELmLGATNYTTHIDLWSLGCIIAEMILGYPIFS 272
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
464-720 1.10e-17

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: 84.02  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVckrcIHSASNMEFA-------VKIIDKNKRDPSEEI-EI-LMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd07839     2 YEKLEKIGEGTYGT----VFKAKNRETHeivalkrVRLDDDDEGVPSSALrEIcLLKELKHKNIVRLYDVLHSDKKLTLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TdlmkggELLDRILKK---KCFSEQEASNV---LYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAK 608
Cdd:cd07839    78 F------EYCDQDLKKyfdSCNGDIDPEIVksfMFQLLKGLAFCHSHNVLHRDLKPQNLL-INKNG---ELKLADFGLAR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 QLrgenGLLLTpCYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFSNGpNDTpEEILLRIgngrFSL 682
Cdd:cd07839   148 AF----GIPVR-CYSAEVVtlwyrPPDVLFgAKLYSTSIDMWSAGCIFAELANAGRPLFPG-NDV-DDQLKRI----FRL 216
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 683 SG-------------------------GIWDNI-----SRGaKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07839   217 LGtpteeswpgvsklpdykpypmypatTSLVNVvpklnSTG-RDLLQNLLVCNPVQRISAEEALQHPY 283
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
116-311 1.21e-17

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: 83.43  E-value: 1.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL--DFL 193
Cdd:cd13983     8 VLGRGSFKTVY---RAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELM 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLD-EIGHIKLTDFGLSKESvdQEKKAYS 270
Cdd:cd13983    85 TSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLL--RQSFAKS 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 271 FCGTVEYMAPEVVNrRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd13983   163 VIGTPEFMAPEMYE-EHYDEKVDIYAFGMCLLEMATGEYPY 202
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
114-306 1.30e-17

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 83.79  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLRKASLK-VRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK--LYLI 189
Cdd:cd05081     9 ISQLGKGNFGSVELCRyDPLGDNTGALVAVKQLQHSGPDqQRDFQR---EIQILKALHSDFIVKYRGVSYGPGRrsLRLV 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKA 268
Cdd:cd05081    86 MEYLPSGCLRDFLQRhRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAK-LLPLDKDY 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 269 YSF----CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT 306
Cdd:cd05081   165 YVVrepgQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFT 206
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
107-323 1.63e-17

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: 83.19  E-value: 1.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGK- 185
Cdd:cd05033     2 DASYVTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTL-KSGYSDKQRLDFLTEASIMGQFDHPNVIRL-EGVVTKSRp 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGG--DVFTRLSKEVLFTEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd05033    80 VMIVTEYMENGslDKFLRENDGKFTVTQLVGM-LRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLED 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 264 QEKkAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 323
Cdd:cd05033   159 SEA-TYTTKGgkiPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSNQDVIKAV 221
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
489-718 1.64e-17

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 83.57  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 489 EFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLY 563
Cdd:cd14046    33 YYAIKKIKLRSESKNNsrilrEVMLLSRL-NHQHVVRYYQAWIERANLYIQMEYCEKSTLRDLIDSGLFQDTDRLWRLFR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 564 VITKTVEYLHSQGVVHRDLKPSNIlYMDESGHpdsIKICDFGFAK------------------QLRGENGLLLTPCYTAN 625
Cdd:cd14046   112 QILEGLAYIHSQGIIHRDLKPVNI-FLDSNGN---VKIGDFGLATsnklnvelatqdinkstsAALGSSGDLTGNVGTAL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 626 FVAPEVL--TQQGYDAACDIWSLGVLLYTMlagYTPFSNGpndtPEEIL----LRIGNGRFSLsggIWDNI--SRGAKdL 697
Cdd:cd14046   188 YVAPEVQsgTKSTYNEKVDMYSLGIIFFEM---CYPFSTG----MERVQiltaLRSVSIEFPP---DFDDNkhSKQAK-L 256
                         250       260
                  ....*....|....*....|.
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLKH 718
Cdd:cd14046   257 IRWLLNHDPAKRPSAQELLKS 277
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
464-715 1.81e-17

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: 84.14  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKiidKNKRDPSEEIEILMR--------YGQHPNIISLKE------------ 523
Cdd:cd13977     2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPENVELALRefwalssiQRQHPNVIQLEEcvlqrdglaqrm 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 524 ----------------------VFD--DGKYVYLVTDLMKGGELLDRILKKKCfSEQEASNVLYVITKTVEYLHSQGVVH 579
Cdd:cd13977    79 shgssksdlylllvetslkgerCFDprSACYLWFVMEFCDGGDMNEYLLSRRP-DRQTNTSFMLQLSSALAFLHRNQIVH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 580 RDLKPSNILYMDESGHPdSIKICDFGFAKQLRG-----------ENGLLLTPCYTANFVAPEVLtQQGYDAACDIWSLGV 648
Cdd:cd13977   158 RDLKPDNILISHKRGEP-ILKVADFGLSKVCSGsglnpeepanvNKHFLSSACGSDFYMAPEVW-EGHYTAKADIFALGI 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 649 LLYTMLAGYTpFSNGpnDTPEEIL---LRIGNGRFSLSGGIWDN--------------ISRGAKDLLSHMLHMDPHQRYT 711
Cdd:cd13977   236 IIWAMVERIT-FRDG--ETKKELLgtyIQQGKEIVPLGEALLENpklelqiplkkkksMNDDMKQLLRDMLAANPQERPD 312

                  ....
gi 1958807372 712 AEQV 715
Cdd:cd13977   313 AFQL 316
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
110-350 1.91e-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: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKAslKVRDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd07846     2 KYENLGLVGEGSYGMVMKCRHK---ETGQIVAIKKFLES--EDDKMVKKIAMREIkmLKQLRHENLVNLIEVFRRKKRWY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLrGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEK 266
Cdd:cd07846    77 LVFEFV-DHTVLDDLEKyPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFAR-TLAAPG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYS-FCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMpqfLSAEAQSllrm 344
Cdd:cd07846   155 EVYTdYVATRWYRAPElLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIK-CLGN---LIPRHQE---- 226

                  ....*.
gi 1958807372 345 LFKRNP 350
Cdd:cd07846   227 LFQKNP 232
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
105-357 2.28e-17

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: 82.77  E-value: 2.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 105 KADPAQ-FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDRVRTKMERDILV-EVNHPFIVKLHYAFQT 182
Cdd:cd06646     4 RRNPQHdYELIQRVGSGTYGDVYKARNLH---TGELAAVKIIK---LEPGDDFSLIQQEIFMVkECKHCNIVAYFGSYLS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV 262
Cdd:cd06646    78 REKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVV---NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF-----L 334
Cdd:cd06646   158 ATIAKRKSFIGTPYWMAPEVAaveKNGGYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQPPKLkdktkW 237
                         250       260
                  ....*....|....*....|...
gi 1958807372 335 SAEAQSLLRMLFKRNPANRLGSE 357
Cdd:cd06646   238 SSTFHNFVKISLTKNPKKRPTAE 260
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
110-353 2.38e-17

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: 83.91  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVR----KKTGPDAGQLYAMKVLR-KASLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEG 184
Cdd:cd05101    25 KLTLGKPLGEGCFGQVVMAEavgiDKDKPKEAVTVAVKMLKdDATEKDLSDLVSEMEMMKMIG-KHKNIINLLGACTQDG 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGGDV-----------------FTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI 247
Cdd:cd05101   104 PLYVIVEYASKGNLreylrarrppgmeysydINRVPEEQM-TFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTEN 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GHIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMIL 324
Cdd:cd05101   183 NVMKIADFGLARDinNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFKLLK 262
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 325 KA-KLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05101   263 EGhRMDKPANCTNELYMMMRDCWHAVPSQR 292
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
110-353 2.59e-17

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: 83.04  E-value: 2.59e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKL---HYAFQTEGKL 186
Cdd:cd05074    10 QFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLigvSLRSRAKGRL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 ---YLILDFLRGGDVFT-----RLSKE--VLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG 256
Cdd:cd05074    90 pipMVILPFMKHGDLHTfllmsRIGEEpfTLPLQTLVRFMI-DIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 257 LSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQ 332
Cdd:cd05074   169 LSKKiySGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYAGVENSEIYNYLIKGnRLKQPP 248
                         250       260
                  ....*....|....*....|.
gi 1958807372 333 FLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05074   249 DCLEDVYELMCQCWSPEPKCR 269
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
115-354 2.72e-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: 82.46  E-value: 2.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAG---QLYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILD 191
Cdd:cd05044     1 KFLGSGAFGEVFEGTAKDILGDGsgeTKVAVKTLRKGATD-QEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAEL-ALALD------HLHRLGIVYRDLKPENILLDEIGH----IKLTDFGLSKE 260
Cdd:cd05044    80 LMEGGDLLSYLRAARPTAFTPPLLTLKDLlSICVDvakgcvYLEDMHFVHRDLAARNCLVSSKDYrervVKIGDFGLARD 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 --SVDQEKKAYSFCGTVEYMAPE-VVNRRGHSQSaDWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK-AKLGMPQFLS 335
Cdd:cd05044   160 iyKNDYYRKEGEGLLPVRWMAPEsLVDGVFTTQS-DVWAFGVLMWEILTlGQQPYPARNNLEVLHFVRAgGRLDQPDNCP 238
                         250
                  ....*....|....*....
gi 1958807372 336 AEAQSLLRMLFKRNPANRL 354
Cdd:cd05044   239 DDLYELMLRCWSTDPEERP 257
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
101-307 3.04e-17

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL1/4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 82.80  E-value: 3.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 101 EGYEKadpaqfdlLKVLGQGSFGKVFLVRKKtgpDAGQLYAMK---------VLRKASLKvrdrvrtkmERDILVEVNHP 171
Cdd:cd07847     1 EKYEK--------LSKIGEGSYGVVFKCRNR---ETGQIVAIKkfveseddpVIKKIALR---------EIRMLKQLKHP 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 172 FIVKLHYAFQTEGKLYLILDFLRGgDVFTRLSKEVLFTEED-VKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHI 250
Cdd:cd07847    61 NLVNLIEVFRRKRKLHLVFEYCDH-TVLNELEKNPRGVPEHlIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQI 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 251 KLTDFGLSKESVDQEKKAYSFCGTVEYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTG 307
Cdd:cd07847   140 KLCDFGFARILTGPGDDYTDYVATRWYRAPElLVGDTQYGPPVDVWAIGCVFAELLTG 197
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
475-720 3.38e-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: 82.76  E-value: 3.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 475 YSVCKRcihsASNMEFAVKIIDK------NKRDPSEEIEILMRyGQ-------HPNIISLKEVFDDGKY-VYLVTDLMKG 540
Cdd:cd14011    13 YNGSKK----STKQEVSVFVFEKkqleeySKRDREQILELLKR-GVkqltrlrHPRILTVQHPLEESREsLAFATEPVFA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 ------GELLDRILKKKCFSEQEASNV-----LYVITKTVEYLH-SQGVVHRDLKPSNIlYMDESGHpdsIKICDFGFA- 607
Cdd:cd14011    88 slanvlGERDNMPSPPPELQDYKLYDVeikygLLQISEALSFLHnDVKLVHGNICPESV-VINSNGE---WKLAGFDFCi 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 ----------KQLRGENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTML-AGYTPFSNGPNDTPEEILLRIG 676
Cdd:cd14011   164 sseqatdqfpYFREYDPNLPPLAQPNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSYKKNSNQL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 677 NgrfSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd14011   244 R---QLSLSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPF 284
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
488-726 3.72e-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: 83.18  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 488 MEFAVKIIDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD--LMKGGELLDriLKKKCFSEQEASNVLYVI 565
Cdd:cd06635    58 MSYSGKQSNEKWQDIIKEVKFLQRI-KHPNSIEYKGCYLREHTAWLVMEycLGSASDLLE--VHKKPLQEIEIAAITHGA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 566 TKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENGLLLTPCYtanfVAPEV---LTQQGYDAACD 642
Cdd:cd06635   135 LQGLAYLHSHNMIHRDIKAGNILLTE----PGQVKLADFGSASIASPANSFVGTPYW----MAPEVilaMDEGQYDGKVD 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 643 IWSLGVL----------LYTMLAGYTPFSNGPNDTPeeillrigngrfSLSGGIWDNISRgakDLLSHMLHMDPHQRYTA 712
Cdd:cd06635   207 VWSLGITcielaerkppLFNMNAMSALYHIAQNESP------------TLQSNEWSDYFR---NFVDSCLQKIPQDRPTS 271
                         250
                  ....*....|....
gi 1958807372 713 EQVLKHPWItQREQ 726
Cdd:cd06635   272 EELLKHMFV-LRER 284
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
470-721 3.72e-17

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: 82.38  E-value: 3.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKII--DKNKRDPSEEI-----EI-LMRYGQHPNIISLKEVFDD--GKYVYLVTDLMK 539
Cdd:cd06653    10 LGRGAFGEVYLCYDADTGRELAVKQVpfDPDSQETSKEVnalecEIqLLKNLRHDRIVQYYGCLRDpeEKKLSIFVEYMP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLR-------G 612
Cdd:cd06653    90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL-RDSAG---NVKLGDFGASKRIQticmsgtG 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndtpEEILLRIgngrFSLSGG-----IW 687
Cdd:cd06653   166 IKSVTGTPYW----MSPEVISGEGYGRKADVWSVACTVVEMLTEKPPWAE------YEAMAAI----FKIATQptkpqLP 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 688 DNISRGAKDLLSHMLhMDPHQRYTAEQVLKHPWI 721
Cdd:cd06653   232 DGVSDACRDFLRQIF-VEEKRRPTAEFLLRHPFV 264
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
156-355 4.12e-17

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: 81.64  E-value: 4.12e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 156 VRTKMERdiLVEVNHPFIVKLhYAFQTE-------GKLYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLH 228
Cdd:cd14012    45 LEKELES--LKKLRHPNLVSY-LAFSIErrgrsdgWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 229 RLGIVYRDLKPENILLDEIGH---IKLTDFGLSKESVD---QEKKAYSFcgTVEYMAPEVVNRRGHSQSA-DWWSYGVLM 301
Cdd:cd14012   122 RNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDmcsRGSLDEFK--QTYWLPPELAQGSKSPTRKtDVWDLGLLF 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 302 FEMLTGTLPFQgkdRNETMNMILkaklgMPQFLSAEAQSLLRMLFKRNPANRLG 355
Cdd:cd14012   200 LQMLFGLDVLE---KYTSPNPVL-----VSLDLSASLQDFLSKCLSLDPKKRPT 245
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
118-353 4.99e-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: 81.16  E-value: 4.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 118 GQGSFGKVFlvRKKTGPDaGQLYAMKVLRKaslkvrdrvrTKMERDILVEVNHPFIVKLH--------YAFQTE----GK 185
Cdd:cd14060     2 GGGSFGSVY--RAIWVSQ-DKEVAVKKLLK----------IEKEAEILSVLSHRNIIQFYgaileapnYGIVTEyasyGS 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYlilDFLRGGDvftrlSKEVLFTEedVKFYLAELALALDHLHR---LGIVYRDLKPENILLDEIGHIKLTDFGLSKesV 262
Cdd:cd14060    69 LF---DYLNSNE-----SEEMDMDQ--IMTWATDIAKGMHYLHMeapVKVIHRDLKSRNVVIAADGVLKICDFGASR--F 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK--AKLGMPQFLSAEAQS 340
Cdd:cd14060   137 HSHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEknERPTIPSSCPRSFAE 216
                         250
                  ....*....|...
gi 1958807372 341 LLRMLFKRNPANR 353
Cdd:cd14060   217 LMRRCWEADVKER 229
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
113-323 5.21e-17

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: 82.04  E-value: 5.21e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVF---LVRKKtGPDAGQLYAMKVLRK-ASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05048     9 FLEELGEGAFGKVYkgeLLGPS-SEESAISVAIKTLKEnASPKTQQDFRR--EAELMSDLQHPNIVCLLGVCTKEQPQCM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGI----------------VYRDLKPENILLDEIGHIKL 252
Cdd:cd05048    86 LFEYMAHGDLHEFLVRHSPHSDVGVSSDDDGTASSLDQSDFLHIaiqiaagmeylsshhyVHRDLAARNCLVGDGLTVKI 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 253 TDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 323
Cdd:cd05048   166 SDFGLSRDiySSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyGLQPYYGYSNQEVIEMI 239
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
467-723 5.34e-17

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 81.85  E-value: 5.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 467 KEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN-----KRDPSEEIEILMRYGQhPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd06619     6 QEILGHGNGGTVYKAYHLLTRRILAVKVIPLDitvelQKQIMSELEILYKCDS-PYIIGFYGAFFVENRISICTEFMDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELldRILKKkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLrgENGLLLTPC 621
Cdd:cd06619    85 SL--DVYRK--IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNML-VNTRGQ---VKLCDFGVSTQL--VNSIAKTYV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTP----FSNGPNDTPEEILL--------RIGNGRFSLSggiwdn 689
Cdd:cd06619   155 GTNAYMAPERISGEQYGIHSDVWSLGISFMELALGRFPypqiQKNQGSLMPLQLLQcivdedppVLPVGQFSEK------ 228
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 690 isrgAKDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd06619   229 ----FVHFITQCMRKQPKERPAPENLMDHPFIVQ 258
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
150-348 5.68e-17

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 83.89  E-value: 5.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 150 LKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHR 229
Cdd:PHA03212  122 IKAGQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHE 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 230 LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD-QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGT 308
Cdd:PHA03212  201 NRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDiNANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVLFEMATCH 280
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 309 LPFQGK-------DRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKR 348
Cdd:PHA03212  281 DSLFEKdgldgdcDSDRQIKLIIRRSGTHPNEFPIDAQANLDEIYIG 327
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
468-672 5.91e-17

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: 81.34  E-value: 5.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASnMEFAVKIIDK---NKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELL 544
Cdd:cd05059    10 KELGSGQFGVVHLGKWRGK-IDVAIKMIKEgsmSEDDFIEEAKVMMKL-SHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKqlrgengLLLTPCYT 623
Cdd:cd05059    88 NYLrERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQN----VVKVSDFGLAR-------YVLDDEYT 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 624 ANF--------VAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPN-DTPEEIL 672
Cdd:cd05059   157 SSVgtkfpvkwSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNsEVVEHIS 215
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
515-673 6.28e-17

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 84.85  E-value: 6.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 515 HPNIISlkeVFD---DGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMD 591
Cdd:NF033483   66 HPNIVS---VYDvgeDGGIPYIVMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNIL-IT 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 592 ESGHpdsIKICDFGFAKQLRGE-----NGLLltpcYTANFVAPEvltqQ---GY-DAACDIWSLGVLLYTMLAGYTPFsN 662
Cdd:NF033483  142 KDGR---VKVTDFGIARALSSTtmtqtNSVL----GTVHYLSPE----QargGTvDARSDIYSLGIVLYEMLTGRPPF-D 209
                         170
                  ....*....|.
gi 1958807372 663 GpnDTPEEILL 673
Cdd:NF033483  210 G--DSPVSVAY 218
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
113-353 7.33e-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: 82.32  E-value: 7.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVflVR------KKTGPDAGQLYAMKVLR-KASLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEGK 185
Cdd:cd05099    16 LGKPLGEGCFGQV--VRaeaygiDKSRPDQTVTVAVKMLKdNATDKDLADLISEMELMKLIG-KHKNIINLLGVCTQEGP 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDV-----------------FTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG 248
Cdd:cd05099    93 LYVIVEYAAKGNLreflrarrppgpdytfdITKVPEEQL-SFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDN 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 249 HIKLTDFGLSK--ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK 325
Cdd:cd05099   172 VMKIADFGLARgvHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPYPGIPVEELFKLLRE 251
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 326 A-KLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05099   252 GhRMDKPSNCTHELYMLMRECWHAVPTQR 280
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
113-353 7.35e-17

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 81.30  E-value: 7.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFL-VRKKTGPdagqlYAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQT-EGKLYLIL 190
Cdd:cd05068    12 LLRKLGSGQFGEVWEgLWNNTTP-----VAVKTLKPGTMDPEDFLR---EAQIMKKLRHPKLIQL-YAVCTlEEPIYIIT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKE--VLFTEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK----ESVDQ 264
Cdd:cd05068    83 ELMKHGSLLEYLQGKgrSLQLPQLIDM-AAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARvikvEDEYE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMiLKAKLGMPQFLSAEAQSLLR 343
Cdd:cd05068   162 AREGAKF--PIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQ-VERGYRMPCPPNCPPQLYDI 238
                         250
                  ....*....|..
gi 1958807372 344 ML--FKRNPANR 353
Cdd:cd05068   239 MLecWKADPMER 250
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
462-720 8.06e-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: 81.81  E-value: 8.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD---PS---EEIEILMRYGQHPNIISL---KEVFDDGK-YV 531
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEegvPStalREVSLLQMLSQSIYIVRLldvEHVEENGKpLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTdlmkggELLDRILKKKCFSEQEAS----------NVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdSIKI 601
Cdd:cd07837    81 YLVF------EYLDTDLKKFIDSYGRGPhnplpaktiqSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKG---LLKI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 602 CDFGFAKQLRgenglLLTPCYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRI 675
Cdd:cd07837   152 ADLGLGRAFT-----IPIKSYTHEIVtlwyrAPEVLLgSTHYSTPVDMWSVGCIFAEMSRKQPLF---PGDSELQQLLHI 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 676 gngrFSLSGG----IW-----------------DNISRG-------AKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07837   224 ----FRLLGTpneeVWpgvsklrdwheypqwkpQDLSRAvpdlepeGVDLLTKMLAYDPAKRISAKAALQHPY 292
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
196-368 8.25e-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: 80.85  E-value: 8.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDV--FTRLSKEVlfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDeighikltDFGLSKESVDQEKKAYSFCG 273
Cdd:cd14022    69 GDMhsFVRTCKKL--REEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFK--------DEERTRVKLESLEDAYILRG 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVE----------YMAPEVVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSL 341
Cdd:cd14022   139 HDDslsdkhgcpaYVSPEILNTSGSysGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCL 218
                         170       180
                  ....*....|....*....|....*..
gi 1958807372 342 LRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14022   219 IRSILRREPSERLTS---QEILDHPWF 242
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
464-721 1.01e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 81.55  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVckrcIHSASNMEFAVKIIDKNKRDPS----------EEIEILMRYGQ--HPNIISLKEV-----FD 526
Cdd:cd07863     2 YEPVAEIGVGAYGT----VYKARDPHSGHFVALKSVRVQTnedglplstvREVALLKRLEAfdHPNIVRLMDVcatsrTD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 527 DGKYVYLVTdlmkggELLDRILKKKC-------FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdeSGhpDSI 599
Cdd:cd07863    78 RETKVTLVF------EHVDQDLRTYLdkvpppgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVT--SG--GQV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 600 KICDFGFAKQLRGEngLLLTP-CYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF-SNGPNDTPEEILLRIG- 676
Cdd:cd07863   148 KLADFGLARIYSCQ--MALTPvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFcGNSEADQLGKIFDLIGl 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 677 -------------NGRFSLSG-----GIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd07863   226 ppeddwprdvtlpRGAFSPRGprpvqSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
101-368 1.07e-16

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 81.42  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 101 EGYEKadpaqfdlLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKvlrKASLKVRDR-VRTKMERDI--LVEVNH-PFIVKL 176
Cdd:cd07837     1 DAYEK--------LEKIGEGTYGKVYKARDKN---TGKLVALK---KTRLEMEEEgVPSTALREVslLQMLSQsIYIVRL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAFQTE--GK--LYLILDFLRGG-----DVFTRLSKEVLFTEEdVKFYLAELALALDHLHRLGIVYRDLKPENILLD-E 246
Cdd:cd07837    67 LDVEHVEenGKplLYLVFEYLDTDlkkfiDSYGRGPHNPLPAKT-IQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDkQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 247 IGHIKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK 325
Cdd:cd07837   146 KGLLKIADLGLGRAFTIPIKSYTHEIVTLWYRAPEVLLGSTHySTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFR 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 326 AkLG------------------MPQF-----------LSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd07837   226 L-LGtpneevwpgvsklrdwheYPQWkpqdlsravpdLEPEGVDLLTKMLAYDPAKRISA---KAALQHPYF 293
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
491-717 1.07e-16

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: 80.92  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKRDpSEEIE-----ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNVL--- 562
Cdd:cd05044    30 AVKTLRKGATD-QEKAEflkeaHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDLLSYLRAARPTAFTPPLLTLkdl 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 ----YVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQL--------RGEnGLLltpcyTANFVAPE 630
Cdd:cd05044   109 lsicVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRERVVKIGDFGLARDIykndyyrkEGE-GLL-----PVRWMAPE 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 631 VLTQQGYDAACDIWSLGVLLY-TMLAGYTPFsngPNDTPEEILlrigngRFSLSGGIWDNISRGAKDLLSHMLH---MDP 706
Cdd:cd05044   183 SLVDGVFTTQSDVWAFGVLMWeILTLGQQPY---PARNNLEVL------HFVRAGGRLDQPDNCPDDLYELMLRcwsTDP 253
                         250
                  ....*....|.
gi 1958807372 707 HQRYTAEQVLK 717
Cdd:cd05044   254 EERPSFARILE 264
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
114-366 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 1958807372 114 LKVLGQGSFGKVFlvRKKTGPDAGQL---YAMKVLR-----KASLKVRDrvrtkmERDILVEVNHPFIVKLhYAFQTEGK 185
Cdd:cd05109    12 VKVLGSGAFGTVY--KGIWIPDGENVkipVAIKVLRentspKANKEILD------EAYVMAGVGSPYVCRL-LGICLTST 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDV--FTRLSKEVLFTEeDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVD 263
Cdd:cd05109    83 VQLVTQLMPYGCLldYVRENKDRIGSQ-DLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLAR-LLD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QEKKAYSFCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEA 338
Cdd:cd05109   161 IDETEYHADGgkvPIKWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPAREIPDLLEKGeRLPQPPICTIDV 240
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 339 QSLLRMLFKRNPANRLG-SEGVEEVKRHA 366
Cdd:cd05109   241 YMIMVKCWMIDSECRPRfRELVDEFSRMA 269
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
110-331 1.13e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 81.16  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEV---NHPFIVKLHYAFQT---- 182
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARD---PHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLeafDHPNIVRLMDVCATsrtd 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 -EGKLYLILDFLrGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSk 259
Cdd:cd07863    78 rETKVTLVFEHV-DQDLRTYLDKVPPpgLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA- 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 260 esvdqekKAYSF-------CGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILkAKLGMP 331
Cdd:cd07863   156 -------RIYSCqmaltpvVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIF-DLIGLP 226
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
110-359 1.21e-16

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: 82.38  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKV-----------FLVRKKTGPDAGQLYAMKVLRKASLkvrdrvrtkmerdiLVEVNHPFIVKLHY 178
Cdd:cd07876    22 RYQQLKPIGSGAQGIVcaafdtvlginVAVKKLSRPFQNQTHAKRAYRELVL--------------LKCVNHKNIISLLN 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 179 AFQTEGKL------YLILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKL 252
Cdd:cd07876    88 VFTPQKSLeefqdvYLVMELM---DANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKI 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 253 TDFGLSKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKLGMPq 332
Cdd:cd07876   165 LDFGLARTACTNFMMT-PYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIE-QLGTP- 241
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 333 flSAEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd07876   242 --SAEFMNRLQPTVRNYVENRPQYPGI 266
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
110-305 1.21e-16

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 80.61  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTkmerdiLVEVNHPFIVKLHYAFQTEGK---- 185
Cdd:cd14047     7 DFKEIELIGSGGFGQVFKAKHRI---DGKTYAIKRVKLNNEKAEREVKA------LAKLDHPNIVRYNGCWDGFDYdpet 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 ------------LYLILDFLRGGDVFTRLSK----EVLFTEEDVKFYlaELALALDHLHRLGIVYRDLKPENILLDEIGH 249
Cdd:cd14047    78 sssnssrsktkcLFIQMEFCEKGTLESWIEKrngeKLDKVLALEIFE--QITKGVEYIHSKKLIHRDLKPSNIFLVDTGK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 250 IKLTDFGLSKESVDQEKKAYSFcGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14047   156 VKIGDFGLVTSLKNDGKRTKSK-GTLSYMSPEQISSQDYGKEVDIYALGLILFELL 210
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
113-353 1.23e-16

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: 80.82  E-value: 1.23e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFlvrkktgpdAGQL----YAMKVLRKaSLKVRDRVRTKMErDILVEV------NHPFIVKL-HYAFQ 181
Cdd:cd05075     4 LGKTLGEGEFGSVM---------EGQLnqddSVLKVAVK-TMKIAICTRSEME-DFLSEAvcmkefDHPNVMRLiGVCLQ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 182 -TEGKLY----LILDFLRGGDV-----FTRLSKEVLF--TEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGH 249
Cdd:cd05075    73 nTESEGYpspvVILPFMKHGDLhsfllYSRLGDCPVYlpTQMLVKF-MTDIASGMEYLSSKNFIHRDLAARNCMLNENMN 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 250 IKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA 326
Cdd:cd05075   152 VCVADFGLSKKiyNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYPGVENSEIYDYLRQG 231
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 327 -KLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05075   232 nRLKQPPDCLDGLYELMSSCWLLNPKDR 259
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
482-667 1.27e-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: 81.38  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 482 IHSASNMEFAVKIIdKNKRDPSE------EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK---- 551
Cdd:cd05055    60 SKSDAVMKVAVKML-KPTAHSSErealmsELKIMSHLGNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRKResfl 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 552 ------CFSEQEAsnvlyvitKTVEYLHSQGVVHRDLKPSNILYMdeSGHpdSIKICDFGFAKQLRGEN-----GLLLTP 620
Cdd:cd05055   139 tledllSFSYQVA--------KGMAFLASKNCIHRDLAARNVLLT--HGK--IVKICDFGLARDIMNDSnyvvkGNARLP 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 621 cytANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNDT 667
Cdd:cd05055   207 ---VKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDS 251
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
110-354 1.27e-16

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: 81.64  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrkKTGPDAGQLYAMKVLRKASLKVRDRVRTKM------ERDILVEVNHPFIVKLHYAFQTE 183
Cdd:cd14041     7 RYLLLHLLGRGGFSEVY----KAFDLTEQRYVAVKIHQLNKNWRDEKKENYhkhacrEYRIHKELDHPRIVKLYDYFSLD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLY-LILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILL---DEIGHIKLTDFGL 257
Cdd:cd14041    83 TDSFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLvngTACGEIKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SK-------ESVDQEKKAYSFCGTVEYMAPE--VVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETM---NMI 323
Cdd:cd14041   163 SKimdddsyNSVDGMELTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIlqeNTI 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 324 LKA-KLGMP--QFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd14041   243 LKAtEVQFPpkPVVTPEAKAFIRRCLAYRKEDRI 276
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
113-353 1.27e-16

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: 81.21  E-value: 1.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVR----KKTGPDAGQLYAMKVLRK-ASLKVRDRVRTKMERDILVEvNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05098    17 LGKPLGEGCFGQVVLAEaiglDKDKPNRVTKVAVKMLKSdATEKDLSDLISEMEMMKMIG-KHKNIINLLGACTQDGPLY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDV--FTRLSK--------------EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIK 251
Cdd:cd05098    96 VIVEYASKGNLreYLQARRppgmeycynpshnpEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMK 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 252 LTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-K 327
Cdd:cd05098   176 IADFGLARDihHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFKLLKEGhR 255
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 328 LGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05098   256 MDKPSNCTNELYMMMRDCWHAVPSQR 281
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
111-311 1.37e-16

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: 80.80  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTKMERDILVevNHPFIVKL-HYAFQTEGK---- 185
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLS---TGRLYALKKILCHSKEDVKEAMREIENYRLF--NHPNILRLlDSQIVKEAGgkke 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGG---DVFTRLSKE-VLFTEEDVKFYLAELALALDHLHRLGIV---YRDLKPENILLDEIGHIKLTDFGL- 257
Cdd:cd13986    77 VYLLLPYYKRGslqDEIERRLVKgTFFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSm 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 258 ---------SKESVDQEKKAYSFCgTVEYMAPEVVNRRGHS---QSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd13986   157 nparieiegRREALALQDWAAEHC-TMPYRAPELFDVKSHCtidEKTDIWSLGCTLYALMYGESPF 221
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
491-678 1.49e-16

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 80.53  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKRDPSE---EIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK--CFSEQEAsNVLYVI 565
Cdd:cd05068    36 AVKTLKPGTMDPEDflrEAQI-MKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLQGKGrsLQLPQLI-DMAAQV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 566 TKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENgllltpCYTA--------NFVAPEVLTQQGY 637
Cdd:cd05068   114 ASGMAYLESQNYIHRDLAARNVLV----GENNICKVADFGLARVIKVED------EYEAregakfpiKWTAPEAANYNRF 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 638 DAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNG 678
Cdd:cd05068   184 SIKSDVWSFGILLTEIVTyGRIPY---PGMTNAEVLQQVERG 222
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
170-359 1.54e-16

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: 79.78  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 170 HPFIVKLHYAFQTEGKLYLIL--DFlrgGDV--FTRLSKEVLFTEEDVKFYlaELALALDHLHRLGIVYRDLKPENILLD 245
Cdd:cd13976    44 HPNISGVHEVIAGETKAYVFFerDH---GDLhsYVRSRKRLREPEAARLFR--QIASAVAHCHRNGIVLRDLKLRKFVFA 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 246 EIGHIKLTDFGLSKESV-DQEKKAYS-FCGTVEYMAPEVVNRRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN 321
Cdd:cd13976   119 DEERTKLRLESLEDAVIlEGEDDSLSdKHGCPAYVSPEILNSGATysGKAADVWSLGVILYTMLVGRYPFHDSEPASLFA 198
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958807372 322 MILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd13976   199 KIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDI 236
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
504-670 1.58e-16

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 80.05  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 504 EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK---------CFSEQEASNVLyvitktveYLHS 574
Cdd:cd05085    42 SEARILKQY-DHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLRKKKdelktkqlvKFSLDAAAGMA--------YLES 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 575 QGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQ----LRGENGLLLTPCytaNFVAPEVLTQQGYDAACDIWSLGVLL 650
Cdd:cd05085   113 KNCIHRDLAARNCLV----GENNALKISDFGMSRQeddgVYSSSGLKQIPI---KWTAPEALNYGRYSSESDVWSFGILL 185
                         170       180
                  ....*....|....*....|.
gi 1958807372 651 Y-TMLAGYTPFSNGPNDTPEE 670
Cdd:cd05085   186 WeTFSLGVCPYPGMTNQQARE 206
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
466-665 1.71e-16

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 80.11  E-value: 1.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-SVCKRCIHSASNMEFAVKI-------IDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd05033     8 IEKVIGGGEFgEVCSGSLKLPGKKEIDVAIktlksgySDKQRLDFLTEASIMGQF-DHPNVIRLEGVVTKSRPVMIVTEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELlDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENg 615
Cdd:cd05033    87 MENGSL-DKFLRENdgKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDL----VCKVSDFGLSRRLEDSE- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 616 llltPCYTAN-------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPN 665
Cdd:cd05033   161 ----ATYTTKggkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSyGERPYWDMSN 214
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
115-370 1.83e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 81.35  E-value: 1.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLK---VRDRVRTKM---------ERDILVEVNHPFIVKLHYAFQT 182
Cdd:PTZ00024   15 AHLGEGTYGKVEKAYDTL---TGKIVAIKKVKIIEISndvTKDRQLVGMcgihfttlrELKIMNEIKHENIMGLVDVYVE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL----- 257
Cdd:PTZ00024   92 GDFINLVMDIMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGLarryg 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 --------SKESVDQEKKAY-SFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAk 327
Cdd:PTZ00024  171 yppysdtlSKDETMQRREEMtSKVVTLWYRAPELLmGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGRIFEL- 249
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 328 LGMP-----------------------------QFLSAEAQSLLRMLFKRNPANRLgseGVEEVKRHAFFSS 370
Cdd:PTZ00024  250 LGTPnednwpqakklplyteftprkpkdlktifPNASDDAIDLLQSLLKLNPLERI---SAKEALKHEYFKS 318
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
115-353 1.96e-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: 80.61  E-value: 1.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKV-----FLVRKKtgpDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 188
Cdd:cd05055    41 KTLGAGAFGKVveataYGLSKS---DAVMKVAVKML-KPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILV 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEiGHI-KLTDFGLSKESVDQE 265
Cdd:cd05055   117 ITEYCCYGDLlnFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTH-GKIvKICDFGLARDIMNDS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 266 KkaYSFCGT----VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLGM--PQFLSAEA 338
Cdd:cd05055   196 N--YVVKGNarlpVKWMAPESIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMaqPEHAPAEI 273
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd05055   274 YDIMKTCWDADPLKR 288
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
113-353 1.98e-16

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 80.44  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVRKKTGPD-AGQLYAMKVLRKASLK-VRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK--LYL 188
Cdd:cd14205     8 FLQQLGKGNFGSVEMCRYDPLQDnTGEVVAVKKLQHSTEEhLRDFER---EIEILKSLQHDNIVKYKGVCYSAGRrnLRL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSK-EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKK 267
Cdd:cd14205    85 IMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTK-VLPQDKE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVE----YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGT----------LPFQGKDRNETMNM-----ILK--A 326
Cdd:cd14205   164 YYKVKEPGEspifWYAPESLTESKFSVASDVWSFGVVLYELFTYIeksksppaefMRMIGNDKQGQMIVfhlieLLKnnG 243
                         250       260
                  ....*....|....*....|....*..
gi 1958807372 327 KLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd14205   244 RLPRPDGCPDEIYMIMTECWNNNVNQR 270
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
110-358 2.12e-16

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 81.29  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLV-RKKTGpdagQLYAMKVLRK---------ASLKVRDRVRTKmERDILVEVNHpfiVKLHYA 179
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKAlDHKTN----EHVAIKIIRNkkrfhhqalVEVKILDALRRK-DRDNSHNVIH---MKEYFY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTegklYLILDF-LRGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH--IKLTD 254
Cdd:cd14225   116 FRN----HLCITFeLLGMNLYELIKKNNFqgFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVID 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGlskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPQFL 334
Cdd:cd14225   192 FG---SSCYEHQRVYTYIQSRFYRSPEVILGLPYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEV-LGLPPPE 267
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 335 SAEAQSLLRMLF--KRNPANRLGSEG 358
Cdd:cd14225   268 LIENAQRRRLFFdsKGNPRCITNSKG 293
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
468-663 2.12e-16

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: 79.69  E-value: 2.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASN---MEFAVKIIDKNK-RDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKyVYLVTDLM 538
Cdd:cd05040     1 EKLGDGSFGVVRRGEWTTPSgkvIQVAVKCLKSDVlSQPNAMDDFLkevnaMHSLDHPNLIRLYGVVLSSP-LMMVTELA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRiLKKKC----------FSEQeasnvlyvITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAK 608
Cdd:cd05040    80 PLGSLLDR-LRKDQghflistlcdYAVQ--------IANGMAYLESKRFIHRDLAARNILLAS----KDKVKIGDFGLMR 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 609 QLrGENglllTPCYTANF--------VAPEVLTQQGYDAACDIWSLGVLLYTMlagytpFSNG 663
Cdd:cd05040   147 AL-PQN----EDHYVMQEhrkvpfawCAPESLKTRKFSHASDVWMFGVTLWEM------FTYG 198
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
500-679 2.28e-16

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 80.44  E-value: 2.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 500 RDPSEEIEILmRYGQHPNIISLKEV-FDDGKY-VYLVTDLMKGGELLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQG 576
Cdd:cd14205    50 RDFEREIEIL-KSLQHDNIVKYKGVcYSAGRRnLRLIMEYLPYGSLRDYLQKhKERIDHIKLLQYTSQICKGMEYLGTKR 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 577 VVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL--RGENGLLLTPCYTANF-VAPEVLTQQGYDAACDIWSLGVLLYTM 653
Cdd:cd14205   129 YIHRDLATRNILVENE----NRVKIGDFGLTKVLpqDKEYYKVKEPGESPIFwYAPESLTESKFSVASDVWSFGVVLYEL 204
                         170       180
                  ....*....|....*....|....*.
gi 1958807372 654 LAgYTPFSNGPndtPEEILLRIGNGR 679
Cdd:cd14205   205 FT-YIEKSKSP---PAEFMRMIGNDK 226
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
114-331 2.57e-16

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: 81.08  E-value: 2.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKA-SLKVRDRvRTKMERDILVEVNHPFIVKLHYAFQTEGK-LYLILD 191
Cdd:cd07856    15 LQPVGMGAFG---LVCSARDQLTGQNVAVKKIMKPfSTPVLAK-RTYRELKLLKHLRHENIISLSDIFISPLEdIYFVTE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLrGGDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKKAYSF 271
Cdd:cd07856    91 LL-GTDLHRLLTSRPL-EKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARI---QDPQMTGY 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 272 CGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07856   166 VSTRYYRAPEImLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITEL-LGTP 225
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
110-353 2.87e-16

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: 80.15  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKtGPDAGQLYAMKVLRKaslKVRDRVRTKMERDILVEVN-------HPFIVKLHYAFQT 182
Cdd:cd05053    13 RLTLGKPLGEGAFGQVVKAEAV-GLDNKPNEVVTVAVK---MLKDDATEKDLSDLVSEMEmmkmigkHKNIINLLGACTQ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLIL---------DFLRG--------GDVFTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD 245
Cdd:cd05053    89 DGPLYVVVeyaskgnlrEFLRArrppgeeaSPDDPRVPEEQL-TQKDLVSFAYQVARGMEYLASKKCIHRDLAARNVLVT 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 246 EIGHIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNEtMNM 322
Cdd:cd05053   168 EDNVMKIADFGLARDihHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEE-LFK 246
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1958807372 323 ILKA--KLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05053   247 LLKEghRMEKPQNCTQELYMLMRDCWHEVPSQR 279
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
470-665 2.94e-16

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 79.42  E-value: 2.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG--- 541
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLkeaekMERARHSYVLPLLGVCVERRSLGLVMEYMENGslk 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRI-------LKKKCFSEqeasnvlyvITKTVEYLH--SQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK---- 608
Cdd:cd13978    81 SLLEREiqdvpwsLRFRIIHE---------IALGMNFLHnmDPPLLHHDLKPENIL-LDNHFH---VKISDFGLSKlgmk 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 609 -----QLRGENGLLLTPCYTanfvAPEVL--TQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN 665
Cdd:cd13978   148 sisanRRRGTENLGGTPIYM----APEAFddFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAIN 207
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
113-359 3.27e-16

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: 80.08  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVR-KKTGPDAGQ-LYAMKVLRKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05093     9 LKRELGEGAFGKVFLAEcYNLCPEQDKiLVAVKTLKDASDNARKDFHR--EAELLTNLQHEHIVKFYGVCVEGDPLIMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDV--FTRL-----------SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05093    87 EYMKHGDLnkFLRAhgpdavlmaegNRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGM 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGMPQF 333
Cdd:cd05093   167 SRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNNEVIECITQGRvLQRPRT 246
                         250       260
                  ....*....|....*....|....*.
gi 1958807372 334 LSAEAQSLLRMLFKRNPANRLGSEGV 359
Cdd:cd05093   247 CPKEVYDLMLGCWQREPHMRLNIKEI 272
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
110-352 3.68e-16

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: 80.44  E-value: 3.68e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVF----LVRKKtgpdagqLYAMKVLRKaslKVRDRVRTKMERDILVEVNHP------FIVKLHYA 179
Cdd:cd14226    14 RYEIDSLIGKGSFGQVVkaydHVEQE-------WVAIKIIKN---KKAFLNQAQIEVRLLELMNKHdtenkyYIVRLKRH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLIL--------DFLRGGDvFTRLSKEVlfteedVKFYLAELALALDHLHR--LGIVYRDLKPENILL--DEI 247
Cdd:cd14226    84 FMFRNHLCLVFellsynlyDLLRNTN-FRGVSLNL------TRKFAQQLCTALLFLSTpeLSIIHCDLKPENILLcnPKR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GHIKLTDFGlskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILkAK 327
Cdd:cd14226   157 SAIKIIDFG---SSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNKIV-EV 232
                         250       260
                  ....*....|....*....|....*
gi 1958807372 328 LGMPQFLSAEAQSLLRMLFKRNPAN 352
Cdd:cd14226   233 LGMPPVHMLDQAPKARKFFEKLPDG 257
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
465-715 3.84e-16

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: 79.39  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSY-SVCKRCIHSASNMEFAVKI-IDKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKyVYLVTDL 537
Cdd:cd05056     9 TLGRCIGEGQFgDVYQGVYMSPENEKIAVAVkTCKNCTSPSVREKFLqeayiMRQFDHPHIVKLIGVITENP-VWIVMEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELlDRILKKKCFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENg 615
Cdd:cd05056    88 APLGEL-RSYLQVNKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLVSS----PDCVKLGDFGLSRYMEDES- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 llltpCYTAN-------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNdtpEEILLRIGNG-RFSLSggi 686
Cdd:cd05056   162 -----YYKASkgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMlGVKPFQGVKN---NDVIGRIENGeRLPMP--- 230
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 687 wDNISRGAKDLLSHMLHMDPHQRYTAEQV 715
Cdd:cd05056   231 -PNCPPTLYSLMTKCWAYDPSKRPRFTEL 258
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
462-726 3.84e-16

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: 80.17  E-value: 3.84e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRdPS------EEIEILmrygqH----PNIISLKEVF-DDGKy 530
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIK-PAirnqiiRELKVL-----HecnsPYIVGFYGAFySDGE- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGELlDRILKK-KCFSEQEASNVLYVITKTVEYL---HSqgVVHRDLKPSNILyMDESGhpdSIKICDFGF 606
Cdd:cd06615    74 ISICMEHMDGGSL-DQVLKKaGRIPENILGKISIAVLRGLTYLrekHK--IMHRDVKPSNIL-VNSRG---EIKLCDFGV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLRgeNGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAG----------------------------YT 658
Cdd:cd06615   147 SGQLI--DSMANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAIGrypipppdakeleamfgrpvsegeakesHR 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 659 PFSNGPNDTPE-----EILLRIGNGRF-SLSGGIWdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQREQ 726
Cdd:cd06615   225 PVSGHPPDSPRpmaifELLDYIVNEPPpKLPSGAF---SDEFQDFVDKCLKKNPKERADLKELTKHPFIKRAEL 295
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
117-331 4.38e-16

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 79.96  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVflVRKKTGPDAGQLYAMKVLR------KASLKvrdrvrtkmERDILVEVN--------HpfIVKLHYAFQT 182
Cdd:cd14135     8 LGKGVFSNV--VRARDLARGNQEVAIKIIRnnelmhKAGLK---------ELEILKKLNdadpddkkH--CIRLLRHFEH 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH-IKLTDFGLSK 259
Cdd:cd14135    75 KNHLCLVFESLSMNlrEVLKKYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGSAS 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 260 ESVDQEKKAY---SFcgtveYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMP 331
Cdd:cd14135   155 DIGENEITPYlvsRF-----YRAPEIILGLPYDYPIDMWSVGCTLYELYTGKILFPGKTNNHMLKLMMDLKGKFP 224
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
107-327 4.38e-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: 79.42  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVF--LVRKKTGPDAgQLYAMKVLRKASLKVRDRVRTkmERDILVEVNHPFIV---------- 174
Cdd:cd05043     4 SRERVTLSDLLQEGTFGRIFhgILRDEKGKEE-EVLVKTVKDHASEIQVTMLLQ--ESSLLYGLSHQNLLpilhvciedg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 175 ---KLHYAFQTEGKLYLildFLRGGDVFTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIK 251
Cdd:cd05043    81 ekpMVLYPYMNWGNLKL---FLQQCRLSEANNPQALSTQQLVHMAL-QIACGMSYLHRRGVIHKDIAARNCVIDDELQVK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 252 LTDFGLSKESV--------DQEKKAysfcgtVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNM 322
Cdd:cd05043   157 ITDNALSRDLFpmdyhclgDNENRP------IKWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTPYVEIDPFEMAAY 230

                  ....*
gi 1958807372 323 ILKAK 327
Cdd:cd05043   231 LKDGY 235
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
111-304 4.41e-16

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: 79.03  E-value: 4.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASL-KVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd06607     3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTeKWQDIIK---EVKFLRQLRHPNTIEYKGCYLREHTAWLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRG--GDVFTRLSKevLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGlskeSVDQEKK 267
Cdd:cd06607    80 MEYCLGsaSDIVEVHKK--PLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG----SASLVCP 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEM 304
Cdd:cd06607   154 ANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIEL 193
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
116-353 5.18e-16

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: 78.93  E-value: 5.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVR-KKTGPDAGQlyAMKVLRKASLKvRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL----- 188
Cdd:cd05047     2 VIGEGNFGQVLKARiKKDGLRMDA--AIKRMKEYASK-DDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLaieya 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ----ILDFLRGGDVF-------TRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05047    79 phgnLLDFLRKSRVLetdpafaIANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLS 335
Cdd:cd05047   159 SRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPLNCD 237
                         250
                  ....*....|....*...
gi 1958807372 336 AEAQSLLRMLFKRNPANR 353
Cdd:cd05047   238 DEVYDLMRQCWREKPYER 255
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
110-305 5.32e-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: 5.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYL- 188
Cdd:cd14049     7 EFEEIARLGKGGYGKVYKVRNKLD---GQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLy 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ---------ILDFLRGGDVFTRLS--KEVLFTEEDVKF---YLAELALALDHLHRLGIVYRDLKPENILLDEIG-HIKLT 253
Cdd:cd14049    84 iqmqlcelsLWDWIVERNKRPCEEefKSAPYTPVDVDVttkILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 254 DFGLS-----KESVDQEKKAY-------SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14049   164 DFGLAcpdilQDGNDSTTMSRlnglthtSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF 227
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
117-305 5.39e-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: 78.84  E-value: 5.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLRkaslkvrdRVRTKMERDILVEV------NHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14221     1 LGKGCFGQAI---KVTHRETGEVMVMKELI--------RFDEETQRTFLKEVkvmrclEHPNVLKFIGVLYKDKRLNFIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGG---DVFTRLSKEVLFTEEdVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE-- 265
Cdd:cd14221    70 EYIKGGtlrGIIKSMDSHYPWSQR-VSF-AKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKtq 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 266 ------------KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14221   148 peglrslkkpdrKKRYTVVGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
107-323 5.58e-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: 78.76  E-value: 5.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 107 DPAQFDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKL 186
Cdd:cd05065     2 DVSCVKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTL-KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGG--DVFTRLsKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSK---ES 261
Cdd:cd05065    81 MIITEFMENGalDSFLRQ-NDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleDD 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 262 VDQEKKAYSFCGT--VEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 323
Cdd:cd05065   160 TSDPTYTSSLGGKipIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWDMSNQDVINAI 224
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
505-719 5.60e-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: 5.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILMRYgQHPNIISL------KEVFDDGKYVYLVTDLMKGG---ELLDRILKKKCfsEQEASNVLYVItKTVEYLHSQ 575
Cdd:cd14012    48 ELESLKKL-RHPNLVSYlafsieRRGRSDGWKVYLLTEYAPGGslsELLDSVGSVPL--DTARRWTLQLL-EALEYLHRN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 576 GVVHRDLKPSNILyMDESGHPDSIKICDFGFAKQLRGENGLL-LTPCYTANFVAPEVLTQQG-YDAACDIWSLGVLLYTM 653
Cdd:cd14012   124 GVVHKSLHAGNVL-LDRDAGTGIVKLTDYSLGKTLLDMCSRGsLDEFKQTYWLPPELAQGSKsPTRKTDVWDLGLLFLQM 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 654 LAGYTPF--SNGPNDTPEEILLrigngrfslsggiwdniSRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14012   203 LFGLDVLekYTSPNPVLVSLDL-----------------SASLQDFLSKCLSLDPKKRPTALELLPHE 253
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
468-719 5.96e-16

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 78.98  E-value: 5.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMR------YGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd14051     6 EKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEvyahavLGKHPHVVRYYSAWAEDDHMIIQNEYCNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKK----CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGHPDS------------------- 598
Cdd:cd14051    86 SLADAISENEkageRFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNI-FISRTPNPVSseeeeedfegeednpesne 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 599 --IKICDFGFA---KQLRGENGllltpcyTANFVAPEVLtQQGYD--AACDIWSLGVLLYtMLAGYTPF-SNGPNDTpee 670
Cdd:cd14051   165 vtYKIGDLGHVtsiSNPQVEEG-------DCRFLANEIL-QENYShlPKADIFALALTVY-EAAGGGPLpKNGDEWH--- 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 671 illRIGNGRFSlsggIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14051   233 ---EIRQGNLP----PLPQCSPEFNELLRSMIHPDPEKRPSAAALLQHP 274
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
542-721 6.10e-16

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 78.46  E-value: 6.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHpdsIKICDFGfakqlrgeNGLLLTPC 621
Cdd:cd14102    91 DLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTGE---LKLIDFG--------SGALLKDT 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANF------VAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFsngpnDTPEEILlrigNGRFSLSggiwDNISRGA 694
Cdd:cd14102   160 VYTDFdgtrvySPPEWIRYHRYHGrSATVWSLGVLLYDMVCGDIPF-----EQDEEIL----RGRLYFR----RRVSPEC 226
                         170       180
                  ....*....|....*....|....*..
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14102   227 QQLIKWCLSLRPSDRPTLEQIFDHPWM 253
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
470-664 6.49e-16

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: 78.71  E-value: 6.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIdKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILK 549
Cdd:cd13991    14 IGRGSFGEVHRMEDKQTGFQCAVKKV-RLEVFRAEELMACAGL-TSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQLIKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 550 KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPdsiKICDFGFAKQLR--GENGLLLTPCY---TA 624
Cdd:cd13991    92 QGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDA---FLCDFGHAECLDpdGLGKSLFTGDYipgTE 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 625 NFVAPEVLTQQGYDAACDIWSLGVLLYTMLAG---YTPFSNGP 664
Cdd:cd13991   169 THMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGchpWTQYYSGP 211
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
464-660 6.69e-16

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 78.92  E-value: 6.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID-------KNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd08229    26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQifdlmdaKARADCIKEIDLLKQL-NHPNVIKYYASFIEDNELNIVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDRIL----KKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFG----FAK 608
Cdd:cd08229   105 LADAGDLSRMIKhfkkQKRLIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANV-FITATG---VVKLGDLGlgrfFSS 180
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 609 QLRGENGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd08229   181 KTTAAHSLVGTPYY----MSPERIHENGYNFKSDIWSLGCLLYEMAALQSPF 228
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
470-605 6.69e-16

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: 75.17  E-value: 6.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIID----KNKRDPSEEIEILMRYGQH-PNIISLKEVFDDGKYVYLVTDLMKGGELL 544
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVKIGDdvnnEEGEDLESEMDILRRLKGLeLNIPKVLVTEDVDGPNILLMELVKGGTLI 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 545 DRILKKkCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFG 605
Cdd:cd13968    81 AYTQEE-ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDG----NVKLIDFG 136
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
103-363 6.74e-16

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: 78.92  E-value: 6.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADPAQFDLLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQT 182
Cdd:cd14149     6 YWEIEASEVMLSTRIGSGSFGTVY--KGKWHGDV----AVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLskEVLfteeDVKFYLAEL-------ALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDF 255
Cdd:cd14149    79 KDNLAIVTQWCEGSSLYKHL--HVQ----ETKFQMFQLidiarqtAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 256 GLS--KESVDQEKKAYSFCGTVEYMAPEVVNRRGH---SQSADWWSYGVLMFEMLTGTLPF-QGKDRNETMNMILKAklg 329
Cdd:cd14149   153 GLAtvKSRWSGSQQVEQPTGSILWMAPEVIRMQDNnpfSFQSDVYSYGIVLYELMTGELPYsHINNRDQIIFMVGRG--- 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958807372 330 mpqFLSAEaqslLRMLFKRNPA--NRLGSEGVEEVK 363
Cdd:cd14149   230 ---YASPD----LSKLYKNCPKamKRLVADCIKKVK 258
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
488-746 6.83e-16

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: 79.30  E-value: 6.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 488 MEFAVKIIDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD--LMKGGELLDriLKKKCFSEQEASNVLYVI 565
Cdd:cd06634    48 MSYSGKQSNEKWQDIIKEVKFLQKL-RHPNTIEYRGCYLREHTAWLVMEycLGSASDLLE--VHKKPLQEVEIAAITHGA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 566 TKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENGLLLTPCYtanfVAPEV---LTQQGYDAACD 642
Cdd:cd06634   125 LQGLAYLHSHNMIHRDVKAGNILLTE----PGLVKLGDFGSASIMAPANSFVGTPYW----MAPEVilaMDEGQYDGKVD 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 643 IWSLGVL----------LYTMLAGYTPFSNGPNDTPeeillrigngrfSLSGGIWdniSRGAKDLLSHMLHMDPHQRYTA 712
Cdd:cd06634   197 VWSLGITcielaerkppLFNMNAMSALYHIAQNESP------------ALQSGHW---SEYFRNFVDSCLQKIPQDRPTS 261
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 713 EQVLKHPWItQREQlprhqptsddPPQVVMEAVA 746
Cdd:cd06634   262 DVLLKHRFL-LRER----------PPTVIMDLIQ 284
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
138-368 7.91e-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: 77.78  E-value: 7.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 138 QLYAMKVLRKASLKVRDRVRTKMERDI--LVEVnhpfivklhyaFQTEGKLYLIL--DFlrgGDVFTRLSKEVLFTEEDV 213
Cdd:cd14023    21 LQCKVFPLKHYQDKIRPYIQLPSHRNItgIVEV-----------ILGDTKAYVFFekDF---GDMHSYVRSCKRLREEEA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 214 KFYLAELALALDHLHRLGIVYRDLKPENILL--DEIGHIKLT---DFGLSKESVDQEKKAYsfcGTVEYMAPEVVNRRG- 287
Cdd:cd14023    87 ARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsdEERTQLRLEsleDTHIMKGEDDALSDKH---GCPAYVSPEILNTTGt 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 288 -HSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHA 366
Cdd:cd14023   164 ySGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSERLTA---PEILLHP 240

                  ..
gi 1958807372 367 FF 368
Cdd:cd14023   241 WF 242
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
460-716 8.62e-16

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: 78.32  E-value: 8.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYElKEDIGIGSYSVCKRCIhsASNMEFAVKIIdknkrdpsEEIEILMRYGQHPNIISL-------KEVFDDGKYVY 532
Cdd:cd14036    13 FAFVYE-AQDVGTGKEYALKRLL--SNEEEKNKAII--------QEINFMKKLSGHPNIVQFcsaasigKEESDQGQAEY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 533 LV-TDLMKGG--ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQG--VVHRDLKPSNILYmdesGHPDSIKICDFGFA 607
Cdd:cd14036    82 LLlTELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLI----GNQGQIKLCDFGSA 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 608 KQL---------RGENGLL---LTPCYTANFVAPEVL---TQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtpeeil 672
Cdd:cd14036   158 TTEahypdyswsAQKRSLVedeITRNTTPMYRTPEMIdlySNYPIGEKQDIWALGCILYLLCFRKHPFEDGAK------- 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 673 LRIGNGRFSLSGGiwDNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd14036   231 LRIINAKYTIPPN--DTQYTVFHDLIRSTLKVNPEERLSITEIV 272
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
117-353 9.11e-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: 78.43  E-value: 9.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVR-KKTGPDAGQLYAMKVLRKASlKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEG--KLYLILDFL 193
Cdd:cd05079    12 LGEGHFGKVELCRyDPEGDNTGEQVAVKSLKPES-GGNHIADLKKEIEILRNLYHENIVKYKGICTEDGgnGIKLIMEFL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLSKEV--LFTEEDVKfYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYS- 270
Cdd:cd05079    91 PSGSLKEYLPRNKnkINLKQQLK-YAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK-AIETDKEYYTv 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 ---FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT--------GTL------PFQGKDRNETMNMILK--AKLGMP 331
Cdd:cd05079   169 kddLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTycdsesspMTLflkmigPTHGQMTVTRLVRVLEegKRLPRP 248
                         250       260
                  ....*....|....*....|..
gi 1958807372 332 QFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05079   249 PNCPEEVYQLMRKCWEFQPSKR 270
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
464-661 1.02e-15

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: 77.78  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEI--------LMRYGQHPNIISLKEVFDDG--KYVYL 533
Cdd:cd06652     4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETSKEVnaleceiqLLKNLLHERIVQYYGCLRDPqeRTLSI 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLR-- 611
Cdd:cd06652    84 FMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL-RDSVG---NVKLGDFGASKRLQti 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 612 -----GENGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFS 661
Cdd:cd06652   160 clsgtGMKSVTGTPYW----MSPEVISGEGYGRKADIWSVGCTVVEMLTEKPPWA 210
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
109-317 1.07e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 80.51  E-value: 1.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFL--VRKKT-------GPDAGQLYAMKVLRKASLKVRD--RVRTKMERDILV--EVNHPFIVK 175
Cdd:PHA03210  148 AHFRVIDDLPAGAFGKIFIcaLRASTeeaearrGVNSTNQGKPKCERLIAKRVKAgsRAAIQLENEILAlgRLNHENILK 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 176 LHYAFQTEGKLYLI---LDFlrggDVFTRLSKEVLFTEE-----DVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI 247
Cdd:PHA03210  228 IEEILRSEANTYMItqkYDF----DLYSFMYDEAFDWKDrpllkQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCD 303
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 248 GHIKLTDFG----LSKESVDQEkkaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTL-PFQGKDRN 317
Cdd:PHA03210  304 GKIVLGDFGtampFEKEREAFD---YGWVGTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDFcPIGDGGGK 375
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
464-721 1.45e-15

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: 78.42  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYS-VCKRCIHSASNMEFAVKIIDKNK--RDPSE-EIEILMRYGQHP-----NIISLKEVFDDGKYVYLV 534
Cdd:cd14135     2 YRVYGYLGKGVFSnVVRARDLARGNQEVAIKIIRNNElmHKAGLkELEILKKLNDADpddkkHCIRLLRHFEHKNHLCLV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGelLDRILKK------------KCFSEQeasnvLYVITKtveYLHSQGVVHRDLKPSNILyMDESghPDSIKIC 602
Cdd:cd14135    82 FESLSMN--LREVLKKygknvglnikavRSYAQQ-----LFLALK---HLKKCNILHADIKPDNIL-VNEK--KNTLKLC 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 603 DFGFAKQLrGENGLllTPCYTANFV-APEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGN--GR 679
Cdd:cd14135   149 DFGSASDI-GENEI--TPYLVSRFYrAPEIILGLPYDYPIDMWSVGCTLYELYTGKILF---PGKTNNHMLKLMMDlkGK 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 680 FS---LSGGIW----------------DNISRGA-----------------------------------KDLLSHMLHMD 705
Cdd:cd14135   223 FPkkmLRKGQFkdqhfdenlnfiyrevDKVTKKEvrrvmsdikptkdlktlligkqrlpdedrkkllqlKDLLDKCLMLD 302
                         330
                  ....*....|....*.
gi 1958807372 706 PHQRYTAEQVLKHPWI 721
Cdd:cd14135   303 PEKRITPNEALQHPFI 318
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
117-311 1.69e-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: 77.55  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKvlrkaslKVRDRVRTKMERDILVEVNHPFIVKLHYAFQtEGKLYLILDFLRGG 196
Cdd:cd13991    14 IGRGSFGEVHRMEDKQ---TGFQCAVK-------KVRLEVFRAEELMACAGLTSPRVVPLYGAVR-EGPWVNIFMDLKEG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVK-FYLAELALALDHLHRLGIVYRDLKPENILLDEIG-HIKLTDFGLSkESVD---QEKKAYS- 270
Cdd:cd13991    83 GSLGQLIKEQGCLPEDRAlHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGsDAFLCDFGHA-ECLDpdgLGKSLFTg 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 271 --FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd13991   162 dyIPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGCHPW 204
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
489-653 1.70e-15

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: 76.94  E-value: 1.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 489 EFAVKIIDKNKRDPS---EEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD-------RILKKKC---FSE 555
Cdd:cd05034    21 KVAVKTLKPGTMSPEaflQEAQI-MKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDylrtgegRALRLPQlidMAA 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 556 QEASNvlyvitktVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLrgENGLlltpcYTAN--------FV 627
Cdd:cd05034   100 QIASG--------MAYLESRNYIHRDLAARNILV----GENNVCKVADFGLARLI--EDDE-----YTARegakfpikWT 160
                         170       180
                  ....*....|....*....|....*.
gi 1958807372 628 APEVLTQQGYDAACDIWSLGVLLYTM 653
Cdd:cd05034   161 APEAALYGRFTIKSDVWSFGILLYEI 186
S_TK_X smart00133
Extension to Ser/Thr-type protein kinases;
369-430 1.82e-15

Extension to Ser/Thr-type protein kinases;


Pssm-ID: 214529  Cd Length: 64  Bit Score: 71.24  E-value: 1.82e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372  369 SSIDWNKLYKREVQPPFRPASGKPDDTFCFDPEFTAKTPKDSPGLPASANAHQL--FKGFSFVA 430
Cdd:smart00133   1 RGIDWDKLENKEIEPPFVPKIKSPTDTSNFDPEFTEETPVLTPVDSPLSGGIQQepFRGFSYVF 64
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
464-721 1.88e-15

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: 78.00  E-value: 1.88e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdKNKRDPSE----EIEILMR-------YGQHPNIISLKEVFD----DG 528
Cdd:cd14136    12 YHVVRKLGWGHFSTVWLCWDLQNKRFVALKVV-KSAQHYTEaaldEIKLLKCvreadpkDPGREHVVQLLDDFKhtgpNG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 KYVYLVTDLMkGGELLDRIlkKKCFSEQEASNVLYVITKTV----EYLHSQ-GVVHRDLKPSNILyMDESGHpdSIKICD 603
Cdd:cd14136    91 THVCMVFEVL-GPNLLKLI--KRYNYRGIPLPLVKKIARQVlqglDYLHTKcGIIHTDIKPENVL-LCISKI--EVKIAD 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 604 FGFAkqlrgengllltpCYTAN----------FVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFS--NGPNDTPE-- 669
Cdd:cd14136   165 LGNA-------------CWTDKhftediqtrqYRSPEVILGAGYGTPADIWSTACMAFELATGDYLFDphSGEDYSRDed 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 670 ------EILLRI-----GNGRFSL----SGGIWDNISR----GAKDLLSH------------------MLHMDPHQRYTA 712
Cdd:cd14136   232 hlaliiELLGRIprsiiLSGKYSReffnRKGELRHISKlkpwPLEDVLVEkykwskeeakefasfllpMLEYDPEKRATA 311

                  ....*....
gi 1958807372 713 EQVLKHPWI 721
Cdd:cd14136   312 AQCLQHPWL 320
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
108-311 1.89e-15

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 77.01  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGKVFLvrkktGPDAGQLYAMKVLrKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05039     5 KKDLKLGELIGKGEFGDVML-----GDYRGQKVAVKCL-KDDSTAAQAFLA--EASVMTTLRHPNLVQLLGVVLEGNGLY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESvDQE 265
Cdd:cd05039    77 IVTEYMAKGSLvdYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEA-SSN 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 266 KKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPF 311
Cdd:cd05039   156 QDGGKL--PIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
115-353 2.17e-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: 76.49  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLvrkktGPDAGQL-YAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLI---- 189
Cdd:cd14203     1 VKLGQGCFGEVWM-----GTWNGTTkVAIKTLKPGTMSPEAFLE---EAQIMKKLRHDKLVQL-YAVVSEEPIYIVtefm 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 -----LDFLRGGD-VFTRLSKEVLFTeedvkfylAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD 263
Cdd:cd14203    72 skgslLDFLKDGEgKYLKLPQLVDMA--------AQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 264 QE---KKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEA 338
Cdd:cd14203   144 NEytaRQGAKF--PIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESL 221
                         250
                  ....*....|....*
gi 1958807372 339 QSLLRMLFKRNPANR 353
Cdd:cd14203   222 HELMCQCWRKDPEER 236
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
196-359 2.22e-15

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: 76.46  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESV--DQEKKAYSFCG 273
Cdd:cd14024    69 GDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPlnGDDDSLTDKHG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 TVEYMAPEVVN-RRGHS-QSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPA 351
Cdd:cd14024   149 CPAYVGPEILSsRRSYSgKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPA 228

                  ....*...
gi 1958807372 352 NRLGSEGV 359
Cdd:cd14024   229 ERLKASEI 236
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
461-719 2.28e-15

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 76.99  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELkEDIGIGSYSVCKRCIHSASNMEFAVKIIDK------NKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd14138     5 TEFHEL-EKIGSGEFGSVFKCVKRLDGCIYAIKRSKKplagsvDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQ 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKK----KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIL--------------YMDESGHP 596
Cdd:cd14138    84 NEYCNGGSLADAISENyrimSYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFisrtsipnaaseegDEDEWASN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 597 DSI-KICDFGFAKQLRG---ENGllltpcyTANFVAPEVLtQQGYD--AACDIWSLGVLLYTMlAGYTPF-SNGpnDTPE 669
Cdd:cd14138   164 KVIfKIGDLGHVTRVSSpqvEEG-------DSRFLANEVL-QENYThlPKADIFALALTVVCA-AGAEPLpTNG--DQWH 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 670 EIllrigngRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14138   233 EI-------RQGKLPRIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKHS 275
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
114-312 2.39e-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: 77.25  E-value: 2.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVR-KKTGPDAGQLYAMKVLrKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK--LYLIL 190
Cdd:cd05080     9 IRDLGEGHFGKVSLYCyDPTNDGTGEMVAVKAL-KADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGksLQLIM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDVFTRLSKEVLFTEEdVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYS 270
Cdd:cd05080    88 EYVPLGSLRDYLPKHSIGLAQ-LLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAK-AVPEGHEYYR 165
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 271 FC----GTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQ 312
Cdd:cd05080   166 VRedgdSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDSSQ 211
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
106-372 2.55e-15

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: 78.14  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 106 ADP------AQFDLLKVLGQGSFGKVFLVR----KKTGPDAGQLYAMKVLRK-ASLKVRDRVRTKMERDILVEvNHPFIV 174
Cdd:cd05100     3 ADPkwelsrTRLTLGKPLGEGCFGQVVMAEaigiDKDKPNKPVTVAVKMLKDdATDKDLSDLVSEMEMMKMIG-KHKNII 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 175 KLHYAFQTEGKLYLILDFLRGGDV-----------------FTRLSKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDL 237
Cdd:cd05100    82 NLLGACTQDGPLYVLVEYASKGNLreylrarrppgmdysfdTCKLPEEQL-TFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 238 KPENILLDEIGHIKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGK 314
Cdd:cd05100   161 AARNVLVTEDNVMKIADFGLARDvhNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGI 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 315 DRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRNPANR-LGSEGVEEVKRHAFFSSID 372
Cdd:cd05100   241 PVEELFKLLKEGhRMDKPANCTHELYMIMRECWHAVPSQRpTFKQLVEDLDRVLTVTSTD 300
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
109-328 2.57e-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: 77.02  E-value: 2.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVkLHYAFQTEGKLYL 188
Cdd:cd14151     8 GQITVGQRIGSGSFGTVY--KGKWHGDV----AVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRL-SKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS--KESVDQE 265
Cdd:cd14151    81 VTQWCEGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLAtvKSRWSGS 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 266 KKAYSFCGTVEYMAPEVV---NRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMILKAKL 328
Cdd:cd14151   161 HQFEQLSGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNiNNRDQIIFMVGRGYL 227
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
117-345 2.61e-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: 76.76  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDAgqlYAMKVlrKASLKVRDRVRtkmeRDILVEVNHPFIVKLHYAFQTEG----KLYLILDF 192
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKTW---LAIKC--PPSLHVDDSER----MELLEEAKKMEMAKFRHILPVYGicsePVGLVMEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTeeDVKFYLA-ELALALDHLHRLG--IVYRDLKPENILLDEIGHIKLTDFGLSK---ESVDQEK 266
Cdd:cd14025    75 METGSLEKLLASEPLPW--ELRFRIIhETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKwngLSHSHDL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCGTVEYMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKdrNETMNMILKAKLGMPQFLSA-------E 337
Cdd:cd14025   153 SRDGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQKKPFAGE--NNILHIMVKVVKGHRPSLSPiprqrpsE 230

                  ....*...
gi 1958807372 338 AQSLLRML 345
Cdd:cd14025   231 CQQMICLM 238
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
110-334 2.81e-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: 2.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKaslkVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL 188
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVD---GEEVAMKVESK----SQPKQVLKMEVAVLKKLqGKPHFCRLIGCGRTERYNYI 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ildflrggdVFTRLSK---EVLFTEEDVKFYLA---ELAL----ALDHLHRLGIVYRDLKPENILldeIG-------HIK 251
Cdd:cd14017    74 ---------VMTLLGPnlaELRRSQPRGKFSVSttlRLGIqilkAIEDIHEVGFLHRDVKPSNFA---IGrgpsderTVY 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 252 LTDFGLSKESVDQEK-------KAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQG-KDRNETMNMi 323
Cdd:cd14017   142 ILDFGLARQYTNKDGeverpprNAAGFRGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEFVTGQLPWRKlKDKEEVGKM- 220
                         250
                  ....*....|.
gi 1958807372 324 lKAKLGMPQFL 334
Cdd:cd14017   221 -KEKIDHEELL 230
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
117-305 2.82e-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: 76.78  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASlkvrdrvrTKMERDILVEV------NHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd14154     1 LGKGFFGQAIKVTHRE---TGEVMVMKELIRFD--------EEAQRNFLKEVkvmrslDHPNVLKFIGVLYKDKKLNLIT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDV--FTRLSKEVLFTEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD----- 263
Cdd:cd14154    70 EYIPGGTLkdVLKDMARPLPWAQRVRF-AKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEerlps 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 264 ---------------QEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14154   149 gnmspsetlrhlkspDRKKRYTVVGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
470-655 3.01e-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: 76.38  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKII--DKNKRDPSEEIEiLMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGG---ELL 544
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELkrFDEQRSFLKEVK-LMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGtleELL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRILKKKCFSEQeasnvLYV---ITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIkICDFGFAKQL------RGENG 615
Cdd:cd14065    80 KSMDEQLPWSQR-----VSLakdIASGMAYLHSKNIIHRDLNSKNCLVREANRGRNAV-VADFGLAREMpdektkKPDRK 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA 655
Cdd:cd14065   154 KRLTVVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEIIG 193
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
110-429 3.14e-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: 77.90  E-value: 3.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK---- 185
Cdd:cd07859     1 RYKIQEVIGKGSYG---VVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 -LYLILDfLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQ 264
Cdd:cd07859    78 dIYVVFE-LMESDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAFND 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 265 EKKAY---SFCGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMPqflSAEAQ 339
Cdd:cd07859   157 TPTAIfwtDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDL-LGTP---SPETI 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 340 SllrmlfkrnpanrlgseGVEEVKRHAFFSSIdwnklykREVQP-PFRPASGKPDD-TFCFDPEFTAKTPKDSPGlPASA 417
Cdd:cd07859   233 S-----------------RVRNEKARRYLSSM-------RKKQPvPFSQKFPNADPlALRLLERLLAFDPKDRPT-AEEA 287
                         330
                  ....*....|..
gi 1958807372 418 NAHQLFKGFSFV 429
Cdd:cd07859   288 LADPYFKGLAKV 299
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
113-311 3.26e-15

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 76.17  E-value: 3.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLvrkktGPDAGQLYAMKVLRK----ASLKVRDRVRTKMERDILVEVnhpfivkLHYAFQTEGKLYL 188
Cdd:cd05082    10 LLQTIGKGEFGDVML-----GDYRGNKVAVKCIKNdataQAFLAEASVMTQLRHSNLVQL-------LGVIVEEKGGLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGG---DVFTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE 265
Cdd:cd05082    78 VTEYMAKGslvDYLRSRGRSVLGGDCLLKFSL-DVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQ 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 266 KKAYSfcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPF 311
Cdd:cd05082   157 DTGKL---PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVPY 200
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
117-305 3.35e-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: 76.52  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASLKVRDRVRTkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14222     1 LGKGFFGQAIKVTHKA---TGKVMVMKELIRCDEETQKTFLT--EVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQE----------- 265
Cdd:cd14222    76 TLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKkkpppdkpttk 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 266 ---------KKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14222   156 krtlrkndrKKRYTVVGNPYWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
565-716 3.57e-15

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 75.89  E-value: 3.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFA--KQLRGENGLLLTPCYTANFVAPEVLTQQG---YDA 639
Cdd:cd14062    98 TAQGMDYLHAKNIIHRDLKSNNIFLHEDL----TVKIGDFGLAtvKTRWSGSQQFEQPTGSILWMAPEVIRMQDenpYSF 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 640 ACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRIGNG--RFSLSgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd14062   174 QSDVYAFGIVLYELLTGQLPYSHINNR--DQILFMVGRGylRPDLS-KVRSDTPKALRRLMEDCIKFQRDERPLFPQIL 249
pknD PRK13184
serine/threonine-protein kinase PknD;
111-363 3.64e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.81  E-value: 3.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKktgPDAGQLYAMKVLRKaSLKVRDRVRTKMERD--ILVEVNHPFIVKLhYAFQTEGKL-Y 187
Cdd:PRK13184    4 YDIIRLIGKGGMGEVYLAYD---PVCSRRVALKKIRE-DLSENPLLKKRFLREakIAADLIHPGIVPV-YSICSDGDPvY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRL----SKEVLFTE----EDVKFYLA---ELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG 256
Cdd:PRK13184   79 YTMPYIEGYTLKSLLksvwQKESLSKElaekTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 257 --LSKE---------SVDQEKKAYS-------FCGTVEYMAPEVVnrRGH--SQSADWWSYGVLMFEMLTGTLPFQGKDR 316
Cdd:PRK13184  159 aaIFKKleeedlldiDVDERNICYSsmtipgkIVGTPDYMAPERL--LGVpaSESTDIYALGVILYQMLTLSFPYRRKKG 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 317 NEtmnMILKAKLGMPQ----------FLSaeaQSLLRMLfKRNPANRLGSegVEEVK 363
Cdd:PRK13184  237 RK---ISYRDVILSPIevapyreippFLS---QIAMKAL-AVDPAERYSS--VQELK 284
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
115-313 4.26e-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: 76.54  E-value: 4.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKtgpdaGQLYAMKVLrkaslKVRDRVRTKMERDI--LVEVNHP----FIVKLHYAFQTEGKLYL 188
Cdd:cd14056     1 KTIGKGRYGEVWLGKYR-----GEKVAVKIF-----SSRDEDSWFRETEIyqTVMLRHEnilgFIAADIKSTGSWTQLWL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKFYLAeLALALDHLH--------RLGIVYRDLKPENILLDEIGHIKLTDFGLS-K 259
Cdd:cd14056    71 ITEYHEHGSLYDYLQRNTLDTEEALRLAYS-AASGLAHLHteivgtqgKPAIAHRDLKSKNILVKRDGTCCIADLGLAvR 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 260 ESVDQEKKAYSF---CGTVEYMAPEVVNRRGHSQS------ADWWSYGVLMFEML-----TGT-----LPFQG 313
Cdd:cd14056   150 YDSDTNTIDIPPnprVGTKRYMAPEVLDDSINPKSfesfkmADIYSFGLVLWEIArrceiGGIaeeyqLPYFG 222
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
470-665 4.34e-15

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: 76.06  E-value: 4.34e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSY-SVCKRCIHSASNMEFAVKI-------IDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd05066    12 IGAGEFgEVCSGRLKLPGKREIPVAIktlkagyTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTRSKPVMIVTEYMENG 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ElLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesghpDS---IKICDFGFAKQLRGENgl 616
Cdd:cd05066    91 S-LDAFLRKHdgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILV-------NSnlvCKVSDFGLSRVLEDDP-- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 617 llTPCYTAN-------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPN 665
Cdd:cd05066   161 --EAAYTTRggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPYWEMSN 215
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
504-671 4.78e-15

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: 75.74  E-value: 4.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 504 EEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRI------LKKKCF---SEQEASNVlyvitktvEYLHS 574
Cdd:cd05084    43 QEARILKQY-SHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLrtegprLKVKELirmVENAAAGM--------EYLES 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 575 QGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQ-----LRGENGLLLTPcytANFVAPEVLTQQGYDAACDIWSLGVL 649
Cdd:cd05084   114 KHCIHRDLAARNCLVTEKN----VLKISDFGMSREeedgvYAATGGMKQIP---VKWTAPEALNYGRYSSESDVWSFGIL 186
                         170       180
                  ....*....|....*....|....
gi 1958807372 650 LY-TMLAGYTPFSNGPN-DTPEEI 671
Cdd:cd05084   187 LWeTFSLGAVPYANLSNqQTREAV 210
pknD PRK13184
serine/threonine-protein kinase PknD;
515-717 5.09e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.43  E-value: 5.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 515 HPNIISLKEVFDDGKYVYLVTDLMKGgELLDRILK--------KKCFSEQEAS----NVLYVITKTVEYLHSQGVVHRDL 582
Cdd:PRK13184   61 HPGIVPVYSICSDGDPVYYTMPYIEG-YTLKSLLKsvwqkeslSKELAEKTSVgaflSIFHKICATIEYVHSKGVLHRDL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 583 KPSNILYmdesGHPDSIKICDFGFAKQLRGENGLLLT-------PCY-----------TANFVAPEVLTQQGYDAACDIW 644
Cdd:PRK13184  140 KPDNILL----GLFGEVVILDWGAAIFKKLEEEDLLDidvdernICYssmtipgkivgTPDYMAPERLLGVPASESTDIY 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 645 SLGVLLYTMLAGYTPFSNGPN---------DTPEEIllrigngrfslsgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQV 715
Cdd:PRK13184  216 ALGVILYQMLTLSFPYRRKKGrkisyrdviLSPIEV-------------APYREIPPFLSQIAMKALAVDPAERYSSVQE 282

                  ..
gi 1958807372 716 LK 717
Cdd:PRK13184  283 LK 284
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
109-362 5.27e-15

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 75.83  E-value: 5.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTGPDAgqlyAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHyAFQTEGKLYL 188
Cdd:cd05073    11 ESLKLEKKLGAGQFGEVWMATYNKHTKV----AVKTMKPGSMSVEAFLA---EANVMKTLQHDKLVKLH-AVVTKEPIYI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGGDVFTRLSKEVLFTEEDVKF--YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEK 266
Cdd:cd05073    83 ITEFMAKGSLLDFLKSDEGSKQPLPKLidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEY 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 267 KAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMiLKAKLGMPQFLSA--EAQSLL 342
Cdd:cd05073   163 TAREGAKfPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPYPGMSNPEVIRA-LERGYRMPRPENCpeELYNIM 241
                         250       260
                  ....*....|....*....|
gi 1958807372 343 RMLFKRNPANRLGSEGVEEV 362
Cdd:cd05073   242 MRCWKNRPEERPTFEYIQSV 261
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
489-665 5.70e-15

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 75.76  E-value: 5.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 489 EFAVKIIDK---NKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK-CFSEQEASNVLYV 564
Cdd:cd05112    30 KVAIKTIREgamSEEDFIEEAEVMMKL-SHPKLVQLYGVCLEQAPICLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKqlrgengLLLTPCYTAN--------FVAPEVLTQQG 636
Cdd:cd05112   109 VCEGMAYLEEASVIHRDLAARNCLV----GENQVVKVSDFGMTR-------FVLDDQYTSStgtkfpvkWSSPEVFSFSR 177
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958807372 637 YDAACDIWSLGVLLYTMLA-GYTPFSNGPN 665
Cdd:cd05112   178 YSSKSDVWSFGVLMWEVFSeGKIPYENRSN 207
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
491-660 5.71e-15

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


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 76.30  E-value: 5.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII--DKNKRDPSE---EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVL--- 562
Cdd:cd05053    47 AVKMLkdDATEKDLSDlvsEMEMMKMIGKHKNIINLLGACTQDGPLYVVVEYASKGNLRE-FLRARRPPGEEASPDDprv 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 --------------YVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLRG-------ENGLLltpc 621
Cdd:cd05053   126 peeqltqkdlvsfaYQVARGMEYLASKKCIHRDLAARNVLVTED----NVMKIADFGLARDIHHidyyrktTNGRL---- 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958807372 622 yTANFVAPEVLTQQGYDAACDIWSLGVLLY-TMLAGYTPF 660
Cdd:cd05053   198 -PVKWMAPEALFDRVYTHQSDVWSFGVLLWeIFTLGGSPY 236
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
499-717 6.09e-15

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: 75.75  E-value: 6.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 499 KRDPSEEI--------EILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGgELLDRILKKKCFSEQEASNVLYVITKTVE 570
Cdd:cd13980    33 KPDPALPLrsykqrleEIRDRLLELPNVLPFQKVIETDKAAYLIRQYVKY-NLYDRISTRPFLNLIEKKWIAFQLLHALN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 571 YLHSQGVVHRDLKPSNILyMDESghpDSIKICDFGFAKQ--LRGENGLLLT---------PCYTA--NFVAPEVLTQQGY 637
Cdd:cd13980   112 QCHKRGVCHGDIKTENVL-VTSW---NWVYLTDFASFKPtyLPEDNPADFSyffdtsrrrTCYIApeRFVDALTLDAESE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 638 D------AACDIWSLG-VLLYTMLAGYTPFsngpnDTPEeiLLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRY 710
Cdd:cd13980   188 RrdgeltPAMDIFSLGcVIAELFTEGRPLF-----DLSQ--LLAYRKGEFSPEQVLEKIEDPNIRELILHMIQRDPSKRL 260

                  ....*..
gi 1958807372 711 TAEQVLK 717
Cdd:cd13980   261 SAEDYLK 267
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
542-721 6.50e-15

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 75.39  E-value: 6.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGhpdSIKICDFGfakqlrgeNGLLLTPC 621
Cdd:cd14100    92 DLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTG---ELKLIDFG--------SGALLKDT 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 622 YTANF------VAPEVLTQQGYDA-ACDIWSLGVLLYTMLAGYTPFSNGPNDTPEEILLRigngrfslsggiwDNISRGA 694
Cdd:cd14100   161 VYTDFdgtrvySPPEWIRFHRYHGrSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFR-------------QRVSSEC 227
                         170       180
                  ....*....|....*....|....*..
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14100   228 QHLIKWCLALRPSDRPSFEDIQNHPWM 254
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
468-720 6.59e-15

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 76.15  E-value: 6.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD--PSEEIE--ILMRYGQHPNIISLKEVFDDGK-----YVYLVTDLM 538
Cdd:cd07870     6 EKLGEGSYATVYKGISRINGQLVALKVISMKTEEgvPFTAIReaSLLKGLKHANIVLLHDIIHTKEtltfvFEYMHTDLA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 K------GGelldrilkkkcfseQEASNV---LYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQ 609
Cdd:cd07870    86 QymiqhpGG--------------LHPYNVrlfMFQLLRGLAYIHGQHILHRDLKPQNLLI----SYLGELKLADFGLARA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRgenglllTPC--YTANFVA-----PEVLT-QQGYDAACDIWSLGVLLYTMLAGyTPFSNGPNDTPEEiLLRIGN---- 677
Cdd:cd07870   148 KS-------IPSqtYSSEVVTlwyrpPDVLLgATDYSSALDIWGAGCIFIEMLQG-QPAFPGVSDVFEQ-LEKIWTvlgv 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 678 -------GRFSLSG---------------GIWDNISR--GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07870   219 ptedtwpGVSKLPNykpewflpckpqqlrVVWKRLSRppKAEDLASQMLMMFPKDRISAQDALLHPY 285
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
103-304 7.30e-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: 76.23  E-value: 7.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 103 YEKADPAQ-FDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVL----RKASLKVRDRVRtkmERDILVEVNHPFIVKLH 177
Cdd:cd06633    14 FYKDDPEEiFVDLHEIGHGSFGAVYFATNSH---TNEVVAIKKMsysgKQTNEKWQDIIK---EVKFLQQLKHPNTIEYK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 178 YAFQTEGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALAldHLHRLGIVYRDLKPENILLDEIGHIKLTDF 255
Cdd:cd06633    88 GCYLKDHTAWLVMEYCLGSasDLLEVHKKPLQEVEIAAITHGALQGLA--YLHSHNMIHRDIKAGNILLTEPGQVKLADF 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 256 GlskeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEM 304
Cdd:cd06633   166 G----SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDIWSLGITCIEL 213
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
118-368 8.73e-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: 8.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 118 GQGSFGKVFLVRKK-TGPDAGQ-LYAMKVLRKASLKVRDRVRTKMERDI--LVEVNHPFIV---------KLHYAFQTE- 183
Cdd:cd14011     5 GPGLPWKIYNGSKKsTKQEVSVfVFEKKQLEEYSKRDREQILELLKRGVkqLTRLRHPRILtvqhpleesRESLAFATEp 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 --GKLYLIL-DFLRGGDVFTRLSKEVLFTEEdVKFYLAELALALDHLH-RLGIVYRDLKPENILLDEIGHIKLTDFGLSK 259
Cdd:cd14011    85 vfASLANVLgERDNMPSPPPELQDYKLYDVE-IKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCI 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ESVDQEKKAYSFCG-----------TVEYMAPEVVNRRGHSQSADWWSYGVLMFEML-TGTLPFQGKDRNET----MNMI 323
Cdd:cd14011   164 SSEQATDQFPYFREydpnlpplaqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYnKGKPLFDCVNNLLSykknSNQL 243
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 324 LKAKLGMPQFLSAEAQSLLRMLFKRNPANRLGSegvEEVKRHAFF 368
Cdd:cd14011   244 RQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDA---EQLSKIPFF 285
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
168-331 9.06e-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: 76.67  E-value: 9.06e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 168 VNHPFIVKLHYAFQTEGKL------YLILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPEN 241
Cdd:cd07874    73 VNHKNIISLLNVFTPQKSLeefqdvYLVMELM---DANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 242 ILLDEIGHIKLTDFGLSKeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMN 321
Cdd:cd07874   150 IVVKSDCTLKILDFGLAR-TAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWN 228
                         170
                  ....*....|
gi 1958807372 322 MILKaKLGMP 331
Cdd:cd07874   229 KVIE-QLGTP 237
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
110-331 9.89e-15

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: 76.71  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLR-------KASLKVR--DRVRtKMERDilvevNHPFIVKLHYAF 180
Cdd:cd14224    66 RYEVLKVIGKGSFGQVV---KAYDHKTHQHVALKMVRnekrfhrQAAEEIRilEHLK-KQDKD-----NTMNVIHMLESF 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 QTEGKLYLILDFLrGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH--IKLTDFG 256
Cdd:cd14224   137 TFRNHICMTFELL-SMNLYELIKKNKFqgFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 257 lskESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd14224   216 ---SSCYEHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIEL-LGMP 286
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
509-720 1.00e-14

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: 75.81  E-value: 1.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDGKYVYLVTdlmkggELLDRILKK---KCFSEQEASNV---LYVITKTVEYLHSQGVVHRDL 582
Cdd:cd07873    53 LLKDLKHANIVTLHDIIHTEKSLTLVF------EYLDKDLKQyldDCGNSINMHNVklfLFQLLRGLAYCHRRKVLHRDL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 583 KPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFs 661
Cdd:cd07873   127 KPQNLL-INERGE---LKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLgSTDYSTQIDMWGVGCIFYEMSTGRPLF- 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 662 ngPNDTPEEILLRIgngrFSLSG--------GIWDN----------------------ISRGAKDLLSHMLHMDPHQRYT 711
Cdd:cd07873   202 --PGSTVEEQLHFI----FRILGtpteetwpGILSNeefksynypkyradalhnhaprLDSDGADLLSKLLQFEGRKRIS 275

                  ....*....
gi 1958807372 712 AEQVLKHPW 720
Cdd:cd07873   276 AEEAMKHPY 284
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
470-714 1.12e-14

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: 75.61  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDK-NKRDPSE----EIEILMRYgQHPNIISLKEVFDD--GKYVYLVTDLMKGGE 542
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDvqmrEFEVLKKL-NHKNIVKLFAIEEEltTRHKVLVMELCPCGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 L---LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIL-YMDESGHpdSI-KICDFGFAKQLrGENGLL 617
Cdd:cd13988    80 LytvLEEPSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMrVIGEDGQ--SVyKLTDFGAAREL-EDDEQF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 618 LTPCYTANFVAPE-----VL---TQQGYDAACDIWSLGVLLYTMLAGYTPFSngPNDTP---EEILLRIGNGRfsLSGGI 686
Cdd:cd13988   157 VSLYGTEEYLHPDmyeraVLrkdHQKKYGATVDLWSIGVTFYHAATGSLPFR--PFEGPrrnKEVMYKIITGK--PSGAI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 687 ------------WD-------NISRGAKDL----LSHMLHMDPHQRYTAEQ 714
Cdd:cd13988   233 sgvqksengpieWSgelpvscSLSQGLQTLltpvLANILEADQEKCWGFDQ 283
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
465-669 1.25e-14

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: 75.86  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKED-------IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRdPS------EEIEILMRYGQhPNIISLKEVFDDGKYV 531
Cdd:cd06650     1 ELKDDdfekiseLGAGNGGVVFKVSHKPSGLVMARKLIHLEIK-PAirnqiiRELQVLHECNS-PYIVGFYGAFYSDGEI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELlDRILKKKC-FSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQ 609
Cdd:cd06650    79 SICMEHMDGGSL-DQVLKKAGrIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNIL-VNSRGE---IKLCDFGVSGQ 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 610 LRgeNGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngPNDTPE 669
Cdd:cd06650   154 LI--DSMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPIP--PPDAKE 209
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
117-353 1.30e-14

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: 75.11  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLvrkktGPDAGQL-YAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLILDFLRG 195
Cdd:cd05069    20 LGQGCFGEVWM-----GTWNGTTkVAIKTLKPGTMMPEAFLQ---EAQIMKKLRHDKLVPL-YAVVSEEPIYIVTEFMGK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 GDVFTRLSkevlftEEDVKF--------YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKK 267
Cdd:cd05069    91 GSLLDFLK------EGDGKYlklpqlvdMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYT 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRM 344
Cdd:cd05069   165 ARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKL 244

                  ....*....
gi 1958807372 345 LFKRNPANR 353
Cdd:cd05069   245 CWKKDPDER 253
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
109-326 1.41e-14

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: 75.97  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMK--VLRKASlKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGK- 185
Cdd:cd07854     5 SRYMDLRPLGCGSNGLVF---SAVDSDCDKRVAVKkiVLTDPQ-SVKHALR---EIKIIRRLDHDNIVKVYEVLGPSGSd 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 -------------LYLILDFLRGGdvFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD-EIGHIK 251
Cdd:cd07854    78 ltedvgsltelnsVYIVQEYMETD--LANVLEQGPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 252 LTDFGLSKeSVDQE--KKAYSFCGTVE--YMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKA 326
Cdd:cd07854   156 IGDFGLAR-IVDPHysHKGYLSEGLVTkwYRSPRLLlSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILES 234
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
111-331 1.59e-14

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: 75.04  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAF--------QT 182
Cdd:cd07866    10 YEILGKLGEGTFGEVYKARQI---KTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAverpdkskRK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLrGGDVFTRLSKE-VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeS 261
Cdd:cd07866    87 RGSVYMVTPYM-DHDLSGLLENPsVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLAR-P 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKAYSFCGTVE------------YMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKaKL 328
Cdd:cd07866   165 YDGPPPNPKGGGGGGtrkytnlvvtrwYRPPELLlGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFK-LC 243

                  ...
gi 1958807372 329 GMP 331
Cdd:cd07866   244 GTP 246
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
100-353 1.92e-14

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


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 74.33  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 100 KEGYEKADPAQFdLLKVLGQGSFGKVFlvrkKTGPDAGQLYAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLhYA 179
Cdd:cd05070     1 KDVWEIPRESLQ-LIKRLGNGQFGEVW----MGTWNGNTKVAIKTLKPGTMSPESFLE---EAQIMKKLKHDKLVQL-YA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLILDFLRGGD--VFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05070    72 VVSEEPIYIVTEYMSKGSllDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSFCG-TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFL 334
Cdd:cd05070   152 ARLIEDNEYTARQGAKfPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPQDC 231
                         250
                  ....*....|....*....
gi 1958807372 335 SAEAQSLLRMLFKRNPANR 353
Cdd:cd05070   232 PISLHELMIHCWKKDPEER 250
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
113-323 2.55e-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: 2.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVF--LVRKKTGPDAGQLYAMKVLRKASLKvRDRVRTKMERDILVEVNHPFIVKL-HYAFQTEGKlYLI 189
Cdd:cd05036    10 LIRALGQGAFGEVYegTVSGMPGDPSPLQVAVKTLPELCSE-QDEMDFLMEALIMSKFNHPNIVRCiGVCFQRLPR-FIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDV--FTR-----LSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGLSK 259
Cdd:cd05036    88 LELMAGGDLksFLRenrprPEQPSSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGPgrvAKIGDFGMAR 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 260 E--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 323
Cdd:cd05036   168 DiyRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPYPGKSNQEVMEFV 234
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
116-362 2.63e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 73.45  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFlvrkkTGPDAGQLYAMKVLRK-ASLKVrdrvrTKMERDILVEVNHPFIVKLhYAFQTEGKLyLILDFLR 194
Cdd:cd14068     1 LLGDGGFGSVY-----RAVYRGEDVAVKIFNKhTSFRL-----LRQELVVLSHLHHPSLVAL-LAAGTAPRM-LVMELAP 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHRLGIVYRDLKPENILL-----DEIGHIKLTDFGLSKESVDQEKKa 268
Cdd:cd14068    69 KGSLDALLQQDNASLTRTLQHRIAlHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGIK- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 ySFCGTVEYMAPEVVnrRG---HSQSADWWSYGVLMFEMLT-GTLPFQG-KDRNETMNMILKAKLGMP--QFLSA---EA 338
Cdd:cd14068   148 -TSEGTPGFRAPEVA--RGnviYNQQADVYSFGLLLYDILTcGERIVEGlKFPNEFDELAIQGKLPDPvkEYGCApwpGV 224
                         250       260
                  ....*....|....*....|....
gi 1958807372 339 QSLLRMLFKRNPANRLGSEGVEEV 362
Cdd:cd14068   225 EALIKDCLKENPQCRPTSAQVFDI 248
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
117-305 2.74e-14

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: 73.66  E-value: 2.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTgpdAGQLYAMKVLRKASlkvrDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14155     1 IGSGFFSEVYKVRHRT---SGQVMALKMNTLSS----NRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRL-SKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILL--DEIGHIKLT-DFGLSKE--SVDQEKKAYS 270
Cdd:cd14155    74 NLEQLLdSNEPLSWTVRVKLAL-DIARGLSYLHSKGIFHRDLTSKNCLIkrDENGYTAVVgDFGLAEKipDYSDGKEKLA 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1958807372 271 FCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14155   153 VVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
168-331 2.79e-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: 75.08  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 168 VNHPFIVKLHYAFQTEGKL------YLILDFLrggDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPEN 241
Cdd:cd07875    80 VNHKNIIGLLNVFTPQKSLeefqdvYIVMELM---DANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 242 ILLDEIGHIKLTDFGLSKESvdqekkAYSFCGTVE-----YMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDR 316
Cdd:cd07875   157 IVVKSDCTLKILDFGLARTA------GTSFMMTPYvvtryYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVLFPGTDH 230
                         170
                  ....*....|....*
gi 1958807372 317 NETMNMILKaKLGMP 331
Cdd:cd07875   231 IDQWNKVIE-QLGTP 244
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
116-361 2.82e-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: 74.01  E-value: 2.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKtgpdaGQLYAMKVLrkaslKVRDRVRTKMERDILVEVN--HP----FIVKLHYAFQTEGKLYLI 189
Cdd:cd13998     2 VIGKGRFGEVWKASLK-----NEPVAVKIF-----SSRDKQSWFREKEIYRTPMlkHEnilqFIAADERDTALRTELWLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLFTEEDVKFYLAeLALALDHLH---------RLGIVYRDLKPENILLDEIGHIKLTDFGLS-- 258
Cdd:cd13998    72 TAFHPNGSL*DYLSLHTIDWVSLCRLALS-VARGLAHLHseipgctqgKPAIAHRDLKSKNILVKNDGTCCIADFGLAvr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 -KESVDQEKKA-YSFCGTVEYMAPEV----VNRRGHS--QSADWWSYGVLMFEMLTGT-----------LPFQGKDRN-- 317
Cdd:cd13998   151 lSPSTGEEDNAnNGQVGTKRYMAPEVlegaINLRDFEsfKRVDIYAMGLVLWEMASRCtdlfgiveeykPPFYSEVPNhp 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 318 --ETMNMILKAKLGMPQFLSAEAQSL-LRMLFK-------RNPANRLGSEGVEE 361
Cdd:cd13998   231 sfEDMQEVVVRDKQRPNIPNRWLSHPgLQSLAEtieecwdHDAEARLTAQCIEE 284
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
491-727 3.04e-14

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: 73.48  E-value: 3.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIdknKRDPSEEIEI----LMRYGQHPNIISLKEVF-DDGKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVLYV- 564
Cdd:cd05082    33 AVKCI---KNDATAQAFLaeasVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGSLVD-YLRSRGRSVLGGDCLLKFs 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 --ITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLRGENGLLLTPcytANFVAPEVLTQQGYDAACD 642
Cdd:cd05082   109 ldVCEAMEYLEGNNFVHRDLAARNVLVSED----NVAKVSDFGLTKEASSTQDTGKLP---VKWTAPEALREKKFSTKSD 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 643 IWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNGrFSLSGGiwDNISRGAKDLLSHMLHMDPHQRYTAEQVlkhpwi 721
Cdd:cd05082   182 VWSFGILLWEIYSfGRVPY---PRIPLKDVVPRVEKG-YKMDAP--DGCPPAVYDVMKNCWHLDAAMRPSFLQL------ 249

                  ....*.
gi 1958807372 722 tqREQL 727
Cdd:cd05082   250 --REQL 253
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
117-354 3.54e-14

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 73.46  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKV---------------FLVRK-KTGPDAGQLYAMKVLRKASlKVRDRVRTKMERDILVEVNHPFIVKL---- 176
Cdd:cd14067     1 LGQGGSGTViyraryqgqpvavkrFHIKKcKKRTDGSADTMLKHLRAAD-AMKNFSEFRQEASMLHSLQHPCIVYLigis 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 -H---YAFQTE--GKLYLILDFLRGGDVFTRLSKEVLFTeedVKFylaELALALDHLHRLGIVYRDLKPENIL---LDEI 247
Cdd:cd14067    80 iHplcFALELAplGSLNTVLEENHKGSSFMPLGHMLTFK---IAY---QIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 248 GHI--KLTDFGLSKESVDQekKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILK 325
Cdd:cd14067   154 EHIniKLSDYGISRQSFHE--GALGVEGTPGYQAPEIRPRIVYDEKVDMFSYGMVLYELLSGQRPSLGHHQLQIAKKLSK 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1958807372 326 A---KLGMP---QFLSaeAQSLLRMLFKRNPANRL 354
Cdd:cd14067   232 GirpVLGQPeevQFFR--LQALMMECWDTKPEKRP 264
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
470-660 4.04e-14

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 73.15  E-value: 4.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSY-SVCKRCIHSASN-MEFAVKII-----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGE 542
Cdd:cd05047     3 IGEGNFgQVLKARIKKDGLrMDAAIKRMkeyasKDDHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGN 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKC----------------FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGF 606
Cdd:cd05047    83 LLDFLRKSRVletdpafaianstastLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV----GENYVAKIADFGL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 607 AkqlRGENGLLLTPC--YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05047   159 S---RGQEVYVKKTMgrLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPY 212
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
470-720 4.33e-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: 73.19  E-value: 4.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEI--------LMRYGQHPNIISLKEVFDD--GKYVYLVTDLMK 539
Cdd:cd06651    15 LGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETSKEVsaleceiqLLKNLQHERIVQYYGCLRDraEKTLTIFMEYMP 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLR-------G 612
Cdd:cd06651    95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANIL-RDSAG---NVKLGDFGASKRLQticmsgtG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPCYtanfVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNgpndtPEEILLRIGNGRFSLSGGIWDNISR 692
Cdd:cd06651   171 IRSVTGTPYW----MSPEVISGEGYGRKADVWSLGCTVVEMLTEKPPWAE-----YEAMAAIFKIATQPTNPQLPSHISE 241
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 693 GAKDLLSHMLhMDPHQRYTAEQVLKHPW 720
Cdd:cd06651   242 HARDFLGCIF-VEARHRPSAEELLRHPF 268
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
514-716 4.51e-14

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: 73.31  E-value: 4.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 514 QHPNIISLKEVFDDgkYVYLVTDL-MKGGEL-----LDRILKKKCFSEQEASN-----------VLYVITKTVEYLHSQG 576
Cdd:cd14049    63 QHPNIVGYHTAWME--HVQLMLYIqMQLCELslwdwIVERNKRPCEEEFKSAPytpvdvdvttkILQQLLEGVTYIHSMG 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 577 VVHRDLKPSNILYmdeSGHPDSIKICDFGFA-----------KQLRGENGLLLTPCY-TANFVAPEVLTQQGYDAACDIW 644
Cdd:cd14049   141 IVHRDLKPRNIFL---HGSDIHVRIGDFGLAcpdilqdgndsTTMSRLNGLTHTSGVgTCLYAAPEQLEGSHYDFKSDMY 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 645 SLGVLLytmLAGYTPFsnGPNDTPEEILLRIGNGRFSLSggiWDNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd14049   218 SIGVIL---LELFQPF--GTEMERAEVLTQLRNGQIPKS---LCKRWPVQAKYIKLLTSTEPSERPSASQLL 281
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
115-353 4.95e-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: 73.43  E-value: 4.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKL-----HYAFQTEGKLYLI 189
Cdd:cd14204    13 KVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLlgvclEVGSQRIPKPMVI 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVLftEEDVKF--------YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE- 260
Cdd:cd14204    93 LPFMKYGDLHSFLLRSRL--GSGPQHvplqtllkFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLSKKi 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 -SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAE 337
Cdd:cd14204   171 ySGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLLHGhRLKQPEDCLDE 250
                         250
                  ....*....|....*.
gi 1958807372 338 AQSLLRMLFKRNPANR 353
Cdd:cd14204   251 LYDIMYSCWRSDPTDR 266
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
66-331 5.08e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 75.07  E-value: 5.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  66 VNDLKMVDEPMDEGEPVFC--RREDLVKEIPITQHVKEGYEKAdpaqFDLLKVLGQGSFGKVFlvrKKTGPDAGQLYAMK 143
Cdd:PTZ00036   25 SGKFEMNDKKLDEEERSHNnnAGEDEDEEKMIDNDINRSPNKS----YKLGNIIGNGSFGVVY---EAICIDTSEKVAIK 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 144 -VLRKASLKVRDRVrtkmerdILVEVNHPFIVKLHYAFQTEGK--------LYLILDFL-----RGGDVFTRLSKEV-LF 208
Cdd:PTZ00036   98 kVLQDPQYKNRELL-------IMKNLNHINIIFLKDYYYTECFkkneknifLNVVMEFIpqtvhKYMKHYARNNHALpLF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 209 TeedVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH-IKLTDFGLSKESVDQEKKAYSFCGTVeYMAPEV-VNRR 286
Cdd:PTZ00036  171 L---VKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSYICSRF-YRAPELmLGAT 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 287 GHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:PTZ00036  247 NYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQV-LGTP 290
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
99-367 5.22e-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: 73.93  E-value: 5.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  99 VKEGYEKADPAQ-FDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKASL-KVRDRVRtkmERDILVEVNHPFIVKL 176
Cdd:cd06635    14 IAELFFKEDPEKlFSDLREIGHGSFGAVYFARDVRTSEVVAIKKMSYSGKQSNeKWQDIIK---EVKFLQRIKHPNSIEY 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAFQTEGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLgiVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd06635    91 KGCYLREHTAWLVMEYCLGSasDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNM--IHRDIKAGNILLTEPGQVKLAD 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGlskeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEMLTGTLPFQGKDRNETMNMIlkAKLGMP 331
Cdd:cd06635   169 FG----SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSALYHI--AQNESP 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 332 QFLSAEAQSLLRML----FKRNPANRLGSegvEEVKRHAF 367
Cdd:cd06635   243 TLQSNEWSDYFRNFvdscLQKIPQDRPTS---EELLKHMF 279
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
208-353 5.34e-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: 73.88  E-value: 5.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 208 FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKE---SVDQEKKAYSFCgTVEYMAPEVVN 284
Cdd:cd14207   177 LTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDiykNPDYVRKGDARL-PLKWMAPESIF 255
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 285 RRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLGM--PQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd14207   256 DKIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMraPEFATSEIYQIMLDCWQGDPNER 327
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
110-353 5.58e-14

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


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 72.60  E-value: 5.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvrkkTGPDAGQLYAMKVLrKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGkLYLI 189
Cdd:cd05083     7 KLTLGEIIGEGEFGAVL-----QGEYMGQKVAVKNI-KCDVTAQAFLE---ETAVMTKLQHKNLVRLLGVILHNG-LYIV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKEsvdQEKK 267
Cdd:cd05083    77 MELMSKGNLvnFLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV---GSMG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRML 345
Cdd:cd05083   154 VDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPKMSVKEVKEAVEKGyRMEPPEGCPPDVYSIMTSC 233

                  ....*...
gi 1958807372 346 FKRNPANR 353
Cdd:cd05083   234 WEAEPGKR 241
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
505-662 5.94e-14

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: 72.56  E-value: 5.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEILMRYgQHPNIIS-LKEVFDDGKYVYLVTDLMKGGELLDRI-LKKKCFSEQEASNVLYVITKTVEYLH--SQGVVHR 580
Cdd:cd14064    41 EVSILCRL-NHPCVIQfVGACLDDPSQFAIVTQYVSGGSLFSLLhEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 581 DLKPSNILyMDESGHPDsikICDFG---FAKQLRGEN-----GLLLtpcytanFVAPEVLTQQG-YDAACDIWSLGVLLY 651
Cdd:cd14064   120 DLNSHNIL-LYEDGHAV---VADFGesrFLQSLDEDNmtkqpGNLR-------WMAPEVFTQCTrYSIKADVFSYALCLW 188
                         170
                  ....*....|.
gi 1958807372 652 TMLAGYTPFSN 662
Cdd:cd14064   189 ELLTGEIPFAH 199
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
460-720 6.24e-14

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on serine/threonine residues. The CLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 73.90  E-value: 6.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCI-HSASNMEFAVKII---DKNKRDPSEEIEILMRYGQH-PN----IISLKEVFDDGKY 530
Cdd:cd14215    10 LQERYEIVSTLGEGTFGRVVQCIdHRRGGARVALKIIknvEKYKEAARLEINVLEKINEKdPEnknlCVQMFDWFDYHGH 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMkGGELLDRILKKKCF--SEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYM---------------DES 593
Cdd:cd14215    90 MCISFELL-GLSTFDFLKENNYLpyPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVnsdyeltynlekkrdERS 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 594 GHPDSIKICDFGFAKQLRGENGLLLTpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN-------- 665
Cdd:cd14215   169 VKSTAIRVVDFGSATFDHEHHSTIVS---TRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNrehlamme 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 666 ----DTPEEILLRIGNGRFSLSGGI-WDNISRGAK------------------------DLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd14215   246 rilgPIPSRMIRKTRKQKYFYHGRLdWDENTSAGRyvrenckplrryltseaeehhqlfDLIESMLEYEPSKRLTLAAAL 325

                  ....
gi 1958807372 717 KHPW 720
Cdd:cd14215   326 KHPF 329
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
468-719 6.77e-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: 72.65  E-value: 6.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMR------YGQHPNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd14139     6 EKIGVGEFGSVYKCIKRLDGCVYAIKRSMRPFAGSSNEQLALHEvyahavLGHHPHVVRYYSAWAEDDHMIIQNEYCNGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKK----KCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYM-----------------DESgHPDSI- 599
Cdd:cd14139    86 SLQDAISENtksgNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIFIChkmqsssgvgeevsneeDEF-LSANVv 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 600 -KICDFGFAKQLRG---ENGllltpcyTANFVAPEVLTQQ-GYDAACDIWSLGvLLYTMLAGYTPF-SNGpndtpeEILL 673
Cdd:cd14139   165 yKIGDLGHVTSINKpqvEEG-------DSRFLANEILQEDyRHLPKADIFALG-LTVALAAGAEPLpTNG------AAWH 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 674 RIGNGRFSlsgGIWDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHP 719
Cdd:cd14139   231 HIRKGNFP---DVPQELPESFSSLLKNMIQPDPEQRPSATALARHT 273
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
471-660 7.34e-14

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: 71.91  E-value: 7.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 471 GIGSYSVCKRCIHSASNMEFAVKIIDKNKRdpseEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKK 550
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKLLKIEK----EAEILSVL-SHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNSN 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 551 KCfSEQEASNVL---YVITKTVEYLHSQG---VVHRDLKPSNILYMDESghpdSIKICDFGfAKQLRGENgLLLTPCYTA 624
Cdd:cd14060    77 ES-EEMDMDQIMtwaTDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADG----VLKICDFG-ASRFHSHT-THMSLVGTF 149
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958807372 625 NFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14060   150 PWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPF 185
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
110-389 7.66e-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: 7.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVF--LVRKKTGPDAGQLYAMKVLRKaSLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05061     7 KITLLRELGQGSFGMVYegNARDIIKGEAETRVAVKTVNE-SASLRERIEFLNEASVMKGFTCHHVVRLLGVVSKGQPTL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRLSK----------EVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05061    86 VVMELMAHGDLKSYLRSlrpeaennpgRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGM 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILK-AKLGMPQF 333
Cdd:cd05061   166 TRDiyETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSlAEQPYQGLSNEQVLKFVMDgGYLDQPDN 245
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 334 LSAEAQSLLRMLFKRNPAnrlgsegveevKRHAFFSSIDwnkLYKREVQPPFRPAS 389
Cdd:cd05061   246 CPERVTDLMRMCWQFNPK-----------MRPTFLEIVN---LLKDDLHPSFPEVS 287
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
489-720 7.88e-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: 73.18  E-value: 7.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 489 EFAVKIIDKNKRDPSEEIEI-LMRYGQHPNIISLKEVF--DDGKYVYLVTD--------LMKGGELLDRILKKKCFSEQE 557
Cdd:cd07867    31 EYALKQIEGTGISMSACREIaLLRELKHPNVIALQKVFlsHSDRKVWLLFDyaehdlwhIIKFHRASKANKKPMQLPRSM 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 558 ASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLL--LTP-CYTANFVAPEVLT- 633
Cdd:cd07867   111 VKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPELLLg 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 634 QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNDTP------EEILLRIgngrFSLSG----GIWDNISRG------AKD- 696
Cdd:cd07867   191 ARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKtsnpfhHDQLDRI----FSVMGfpadKDWEDIRKMpeyptlQKDf 266
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 697 ---------------------------LLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07867   267 rrttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 317
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
508-726 7.91e-14

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


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 73.37  E-value: 7.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 508 ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELldRILKKKCFSE--QEA--SNVLYVITKTVEYLHSQGVVHRDLK 583
Cdd:cd08226    51 VLSHFFRHPNIMTHWTVFTEGSWLWVISPFMAYGSA--RGLLKTYFPEgmNEAliGNILYGAIKALNYLHQNGCIHRSVK 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 584 PSNILyMDESGHpdsikicdfgfaKQLRGENGL--LLTPCYTANFV--------------APEVLTQ--QGYDAACDIWS 645
Cdd:cd08226   129 ASHIL-ISGDGL------------VSLSGLSHLysMVTNGQRSKVVydfpqfstsvlpwlSPELLRQdlHGYNVKSDIYS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 646 LGVLLYTMLAGYTPFSN------------GP------NDTPEEILLRIGNGRFSLSGGIWDNISRGA------------- 694
Cdd:cd08226   196 VGITACELARGQVPFQDmrrtqmllqklkGPpyspldIFPFPELESRMKNSQSGMDSGIGESVATSSmtrtmtserlqtp 275
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 695 ---------KDLLSHMLHMDPHQRYTAEQVLKHPWITQ-REQ 726
Cdd:cd08226   276 ssktfspafHNLVELCLQQDPEKRPSASSLLSHSFFKQvKEQ 317
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
115-353 8.59e-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: 72.91  E-value: 8.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKV-----FLVRKKtgpDAGQLYAMKVLRKASLKVRDRVRTKmERDILVEV-NHPFIVKLHYAFQT-EGKLY 187
Cdd:cd05054    13 KPLGRGAFGKViqasaFGIDKS---ATCRTVAVKMLKEGATASEHKALMT-ELKILIHIgHHLNVVNLLGACTKpGGPLM 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRL-SKEVLF-------------------------TEEDVKFYLAELALALDHLHRLGIVYRDLKPEN 241
Cdd:cd05054    89 VIVEFCKFGNLSNYLrSKREEFvpyrdkgardveeeedddelykeplTLEDLICYSFQVARGMEFLASRKCIHRDLAARN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 242 ILLDEIGHIKLTDFGLSKE---SVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRN 317
Cdd:cd05054   169 ILLSENNVVKICDFGLARDiykDPDYVRKGDARL-PLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQMD 247
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 318 ETMNMILK--AKLGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05054   248 EEFCRRLKegTRMRAPEYTTPEIYQIMLDCWHGEPKER 285
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
514-651 9.18e-14

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 72.00  E-value: 9.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 514 QHPNIISLKEVFDDGKYVYLVTDLMKGGELLD--RILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMD 591
Cdd:cd05039    58 RHPNLVQLLGVVLEGNGLYIVTEYMAKGSLVDylRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSE 137
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 592 EsghpDSIKICDFGFAK--QLRGENGLLltPcytANFVAPEVLTQQGYDAACDIWSLGVLLY 651
Cdd:cd05039   138 D----NVAKVSDFGLAKeaSSNQDGGKL--P---IKWTAPEALREKKFSTKSDVWSFGILLW 190
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
461-657 9.22e-14

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 73.59  E-value: 9.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPSEEIEILMRYGQHP----NIISLKEVFDDGKYVYL 533
Cdd:cd14227    14 TNTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHpsyARQGQIEVSILARLSTESaddyNFVRAYECFQHKNHTCL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMKggELLDRILKKKCFSE---QEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQL 610
Cdd:cd14227    94 VFEMLE--QNLYDFLKQNKFSPlplKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDFGSASHV 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1958807372 611 rgENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGY 657
Cdd:cd14227   172 --SKAVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGW 216
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
117-325 9.49e-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: 72.14  E-value: 9.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrkKTGPDAGQLYAMKVLRKASLKVRDRVRTKmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd14664     1 IGRGGAGTVY----KGVMPNGTLVAVKRLKGEGTQGGDHGFQA-EIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRL-----SKEVLFTEEDVKFYLaELALALDHLHR---LGIVYRDLKPENILLDEIGHIKLTDFGLSKESVD-QEKK 267
Cdd:cd14664    76 SLGELLhsrpeSQPPLDWETRQRIAL-GSARGLAYLHHdcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDkDSHV 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 268 AYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFqGKDRNETMNMILK 325
Cdd:cd14664   155 MSSVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF-DEAFLDDGVDIVD 211
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
462-716 1.06e-13

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 71.99  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYS-----VCKRCIHSASNMEFAVKIIDKNKRDpSEEIEIL-----MRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd05032     6 EKITLIRELGQGSFGmvyegLAKGVVKGEPETRVAIKTVNENASM-RERIEFLneasvMKEFNCHHVVRLLGVVSTGQPT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRIlkKKCFSEQEASNVLYVIT------------KTVEYLHSQGVVHRDLKPSNILYMDEsghpDSI 599
Cdd:cd05032    85 LVVMELMAKGDLKSYL--RSRRPEAENNPGLGPPTlqkfiqmaaeiaDGMAYLAAKKFVHRDLAARNCMVAED----LTV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 600 KICDFGFAKQL-------RGENGLLltPcytANFVAPEVLTQQGYDAACDIWSLGVLLYTM--LAG--YTPFSNgpndtp 668
Cdd:cd05032   159 KIGDFGMTRDIyetdyyrKGGKGLL--P---VRWMAPESLKDGVFTTKSDVWSFGVVLWEMatLAEqpYQGLSN------ 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 669 EEILlrigngRFSLSGGIWD---NISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd05032   228 EEVL------KFVIDGGHLDlpeNCPDKLLELMRMCWQYNPKMRPTFLEIV 272
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
114-312 1.06e-13

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: 72.26  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKV-RDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDF 192
Cdd:cd14026     2 LRYLSRGAFGTVSRARHA---DWRVTVAIKCLKLDSPVGdSERNCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTeeDVKF-----YLAELALALDHLHRLG--IVYRDLKPENILLDEIGHIKLTDFGLSK---ESV 262
Cdd:cd14026    79 MTNGSLNELLHEKDIYP--DVAWplrlrILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKwrqLSI 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 263 DQEK--KAYSFCGTVEYMAPEVVN---RRGHSQSADWWSYGVLMFEMLTGTLPFQ 312
Cdd:cd14026   157 SQSRssKSAPEGGTIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFE 211
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
484-654 1.08e-13

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: 71.61  E-value: 1.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 484 SASNMEFAVKIIdKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDdGKYVYLVTDLMKGGELLDRILKKKCFSEQEA 558
Cdd:cd05060    20 SGKEVEVAVKTL-KQEHEKAGKKEFLreasvMAQLDHPCIVRLIGVCK-GEPLMLVMELAPLGPLLKYLKKRREIPVSDL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 559 SNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQLRGENGLlltpcYTA--------NFVAPE 630
Cdd:cd05060    98 KELAHQVAMGMAYLESKHFVHRDLAARNVLLVNR----HQAKISDFGMSRALGAGSDY-----YRAttagrwplKWYAPE 168
                         170       180
                  ....*....|....*....|....
gi 1958807372 631 VLTQQGYDAACDIWSLGVLLYTML 654
Cdd:cd05060   169 CINYGKFSSKSDVWSYGVTLWEAF 192
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
217-354 1.12e-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: 72.53  E-value: 1.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 217 LAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFG--LSKES----VDQEKKAYSFCGTVEYMAPEVVNRR 286
Cdd:cd14018   144 ILQLLEGVDHLVRHGIAHRDLKSDNILLeldfDGCPWLVIADFGccLADDSiglqLPFSSWYVDRGGNACLMAPEVSTAV 223
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 287 G------HSQSADWWSYGVLMFEMLTGTLPF--QGKDRNETMNMILKAKLGMPQFLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd14018   224 PgpgvviNYSKADAWAVGAIAYEIFGLSNPFygLGDTMLESRSYQESQLPALPSAVPPDVRQVVKDLLQRDPNKRV 299
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
504-660 1.16e-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: 72.15  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 504 EEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRIlkkKCFSE------QEASNVLYVITKTVEYLHSQGV 577
Cdd:cd14158    63 QEIQV-MAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSLLDRL---ACLNDtpplswHMRCKIAQGTANGINYLHENNH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 578 VHRDLKPSNILyMDESGHPdsiKICDFGFAKQLRGENGLLLTPCY--TANFVAPEVLtQQGYDAACDIWSLGVLLYTMLA 655
Cdd:cd14158   139 IHRDIKSANIL-LDETFVP---KISDFGLARASEKFSQTIMTERIvgTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIIT 213

                  ....*
gi 1958807372 656 GYTPF 660
Cdd:cd14158   214 GLPPV 218
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
465-660 1.20e-13

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: 71.82  E-value: 1.20e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSY-SVCKRCIHSASNMEFAVKI-------IDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05065     7 KIEEVIGAGEFgEVCRGRLKLPGKREIFVAIktlksgyTEKQRRDFLSEASIMGQF-DHPNIIHLEGVVTKSRPVMIITE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGElLDRILKKK--CFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGEN 614
Cdd:cd05065    86 FMENGA-LDSFLRQNdgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNL----VCKVSDFGLSRFLEDDT 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 615 GlllTPCYTAN--------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05065   161 S---DPTYTSSlggkipirWTAPEAIAYRKFTSASDVWSYGIVMWEVMSyGERPY 212
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
502-670 1.24e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.99  E-value: 1.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 502 PSEEIE-ILMRYGQHPNIISLKEVFDDGKYVYLV-----TDLMKGGELLDRILkkkcfSEQEASNVLYVITKTVEYLHSQ 575
Cdd:PHA03209  102 GTTLIEaMLLQNVNHPSVIRMKDTLVSGAITCMVlphysSDLYTYLTKRSRPL-----PIDQALIIEKQILEGLRYLHAQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 576 GVVHRDLKPSNILYMDEsghpDSIKICDFGFAK-QLRGENGLLLTPCYTANfvAPEVLTQQGYDAACDIWSLGVLLYTML 654
Cdd:PHA03209  177 RIIHRDVKTENIFINDV----DQVCIGDLGAAQfPVVAPAFLGLAGTVETN--APEVLARDKYNSKADIWSAGIVLFEML 250
                         170
                  ....*....|....*.
gi 1958807372 655 AGYTPFSNGPNDTPEE 670
Cdd:PHA03209  251 AYPSTIFEDPPSTPEE 266
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
464-648 1.66e-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: 71.60  E-value: 1.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdknKRDPSEEI-----EILM-RYGQHPNIISLKEVFDDGKYVYLVTDL 537
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKII---KLEPGDDFsliqqEIFMvKECKHCNIVAYFGSYLSREKLWICMEY 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 MKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLL 617
Cdd:cd06646    88 CGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNG----DVKLADFGVAAKITATIAKR 163
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1958807372 618 LTPCYTANFVAPEVLTQQ---GYDAACDIWSLGV 648
Cdd:cd06646   164 KSFIGTPYWMAPEVAAVEkngGYNQLCDIWAVGI 197
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
110-369 1.67e-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: 71.68  E-value: 1.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLlkVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQT--EGK-- 185
Cdd:cd14031    13 KFDI--ELGRGAFKTVY---KGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKkc 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSV 262
Cdd:cd14031    88 IVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKLGMPQF---LSAEAQ 339
Cdd:cd14031   166 MRTSFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGIKPASFnkvTDPEVK 244
                         250       260       270
                  ....*....|....*....|....*....|
gi 1958807372 340 SLLRMLFKRNPANRLgseGVEEVKRHAFFS 369
Cdd:cd14031   245 EIIEGCIRQNKSERL---SIKDLLNHAFFA 271
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
489-720 1.78e-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: 72.40  E-value: 1.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 489 EFAVKIIDKNKRDPSEEIEI-LMRYGQHPNIISLKEVF--DDGKYVYLVTDLMKGGelLDRILKKKCFSEQE-------- 557
Cdd:cd07868    46 DYALKQIEGTGISMSACREIaLLRELKHPNVISLQKVFlsHADRKVWLLFDYAEHD--LWHIIKFHRASKANkkpvqlpr 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 558 --ASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENGLL--LTP-CYTANFVAPEVL 632
Cdd:cd07868   124 gmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPELL 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 633 T-QQGYDAACDIWSLGVLLYTMLAGYTPFS------NGPNDTPEEILLRIGNGRFSLSGGIWDNISR------------- 692
Cdd:cd07868   204 LgARHYTKAIDIWAIGCIFAELLTSEPIFHcrqediKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKmpehstlmkdfrr 283
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 693 ---------------------GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07868   284 ntytncslikymekhkvkpdsKAFHLLQKLLTMDPIKRITSEQAMQDPY 332
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
110-331 1.89e-13

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: 72.85  E-value: 1.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVrkkTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEgklylI 189
Cdd:cd07853     1 DVEPDRPIGYGAFGVVWSV---TDPRDGKRVALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPP-----H 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRLSKEVL---------FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS-K 259
Cdd:cd07853    73 IDPFEEIYVVTELMQSDLhkiivspqpLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLArV 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07853   153 EEPDESKHMTQEVVTQYYRAPEIlMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDL-LGTP 224
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
463-720 1.92e-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: 71.64  E-value: 1.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 463 AYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRD--PSEEI-EI-LMRYGQHPNIISLKEVFDDGKYVYLVTdlm 538
Cdd:cd07844     1 TYKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEgaPFTAIrEAsLLKDLKHANIVTLHDIIHTKKTLTLVF--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 kggELLDRILKK---KCFSEQEASNV---LYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAkqlRG 612
Cdd:cd07844    78 ---EYLDTDLKQymdDCGGGLSMHNVrlfLFQLLRGLAYCHQRRVLHRDLKPQNLL-ISERGE---LKLADFGLA---RA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENglLLTPCYTANFVA-----PEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPF--SNGPNDTPEEILLRIG-------- 676
Cdd:cd07844   148 KS--VPSKTYSNEVVTlwyrpPDVLLgSTEYSTSLDMWGVGCIFYEMATGRPLFpgSTDVEDQLHKIFRVLGtpteetwp 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 677 -----------NGRFSLS---GGIWDNISR--GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07844   226 gvssnpefkpySFPFYPPrplINHAPRLDRipHGEELALKFLQYEPKKRISAAEAMKHPY 285
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
114-331 2.01e-13

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: 72.28  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFlvrKKTGPDAGQLYAMKVL--RKASLKvrdrvRTKMERDILVEVNHPF-------IVKLHYAFQTEG 184
Cdd:cd14212     4 LDLLGQGTFGQVV---KCQDLKTNKLVAVKVLknKPAYFR-----QAMLEIAILTLLNTKYdpedkhhIVRLLDHFMHHG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLrGGDVFtRLSKEVLF---TEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEI--GHIKLTDFGlsk 259
Cdd:cd14212    76 HLCIVFELL-GVNLY-ELLKQNQFrglSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIKLIDFG--- 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 260 ESVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGtLP-FQGkdrNETMNMILK--AKLGMP 331
Cdd:cd14212   151 SACFENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLGCIAAELFLG-LPlFPG---NSEYNQLSRiiEMLGMP 221
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
470-724 2.01e-13

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: 71.20  E-value: 2.01e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRcihSASNMEFAVKIIDKNKRDPSE------EIEILmRYGQHPNIISLKEVFDDGKYVyLVTDLMKGGEL 543
Cdd:cd14150     8 IGTGSFGTVFR---GKWHGDVAVKILKVTEPTPEQlqafknEMQVL-RKTRHVNILLFMGFMTRPNFA-IITQWCEGSSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 544 LDRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFA---------KQLRGE 613
Cdd:cd14150    83 YRHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNI-FLHEGL---TVKIGDFGLAtvktrwsgsQQVEQP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 614 NGLLLtpcytanFVAPEVLTQQG---YDAACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRIGNGRFS--LSgGIWD 688
Cdd:cd14150   159 SGSIL-------WMAPEVIRMQDtnpYSFQSDVYAYGVVLYELMSGTLPYSNINNR--DQIIFMVGRGYLSpdLS-KLSS 228
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQR 724
Cdd:cd14150   229 NCPKAMKRLLIDCLKFKREERPLFPQILVSIELLQR 264
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
469-723 2.07e-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: 71.62  E-value: 2.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFAV-----KIIDKNKRDPSEEIEILMRYGQHPNIISLKEVFDDG----KYVYLVTDLMK 539
Cdd:cd14030    32 EIGRGSFKTVYKGLDTETTVEVAWcelqdRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTvkgkKCIVLVTELMT 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 540 GGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQG--VVHRDLKPSNILYMDESGhpdSIKICDFGFAKQLRGE--NG 615
Cdd:cd14030   112 SGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG---SVKIGDLGLATLKRASfaKS 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPcytaNFVAPEvLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLRIGNGrfsLSGGIWDNIS-RGA 694
Cdd:cd14030   189 VIGTP----EFMAPE-MYEEKYDESVDVYAFGMCMLEMATSEYPYSECQN--AAQIYRRVTSG---VKPASFDKVAiPEV 258
                         250       260
                  ....*....|....*....|....*....
gi 1958807372 695 KDLLSHMLHMDPHQRYTAEQVLKHPWITQ 723
Cdd:cd14030   259 KEIIEGCIRQNKDERYAIKDLLNHAFFQE 287
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
465-656 2.11e-13

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 70.98  E-value: 2.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 465 ELKEDIGIGSYSVCKRCIHSASNMEFAVKII----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKY-------VYL 533
Cdd:cd13975     3 KLGRELGRGQYGVVYACDSWGGHFPCALKSVvppdDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYgggssiaVLL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 534 VTDLMK---------GGELLDRIlkkkcfseQEASNVLyvitKTVEYLHSQGVVHRDLKPSNILyMDESghpDSIKICDF 604
Cdd:cd13975    83 IMERLHrdlytgikaGLSLEERL--------QIALDVV----EGIRFLHSQGLVHRDIKLKNVL-LDKK---NRAKITDL 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 605 GFAKQLRGENGLLL-TPCYtanfVAPEVLTQQgYDAACDIWSLGVLLYTMLAG 656
Cdd:cd13975   147 GFCKPEAMMSGSIVgTPIH----MAPELFSGK-YDNSVDVYAFGILFWYLCAG 194
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
509-711 2.24e-13

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 70.99  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEV-FDDGKYVyLVTDLMKGGELLdRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNI 587
Cdd:cd14027    44 MMNRLRHSRVVKLLGViLEEGKYS-LVMEYMEKGNLM-HVLKKVSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENI 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 588 LyMDESGHpdsIKICDFGFA-------------KQLRGENGLLLTPCYTANFVAPEVLTQQGYDAA--CDIWSLGVLLYT 652
Cdd:cd14027   122 L-VDNDFH---IKIADLGLAsfkmwskltkeehNEQREVDGTAKKNAGTLYYMAPEHLNDVNAKPTekSDVYSFAIVLWA 197
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 653 MLAGYTPFSNGPNDtpEEILLRIGNGRFSLSGGIWDNISRGAKDLLSHMLHMDPHQRYT 711
Cdd:cd14027   198 IFANKEPYENAINE--DQIIMCIKSGNRPDVDDITEYCPREIIDLMKLCWEANPEARPT 254
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
462-660 2.36e-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: 71.57  E-value: 2.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSY-SVCKRCIHSASN-MEFAVKII-----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLV 534
Cdd:cd05089     2 EDIKFEDVIGEGNFgQVIKAMIKKDGLkMNAAIKMLkefasENDHRDFAGELEVLCKLGHHPNIINLLGACENRGYLYIA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDLMKGGELLDRILKKKC----------------FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDS 598
Cdd:cd05089    82 IEYAPYGNLLDFLRKSRVletdpafakehgtastLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLV----GENLV 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 599 IKICDFGFAkqlRGENGLLLTPC--YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05089   158 SKIADFGLS---RGEEVYVKKTMgrLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPY 219
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
464-721 2.43e-13

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: 72.47  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKR---DPSEEIEILM------RYGQHpNIISLKEVFDDGKYVYLV 534
Cdd:cd14224    67 YEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVRNEKRfhrQAAEEIRILEhlkkqdKDNTM-NVIHMLESFTFRNHICMT 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 TDL--MKGGELLDRIlKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDE--SGhpdsIKICDFGFAKQl 610
Cdd:cd14224   146 FELlsMNLYELIKKN-KFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQgrSG----IKVIDFGSSCY- 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 611 rgENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYtPFSNGPND------------TPEEILLR---- 674
Cdd:cd14224   220 --EHQRIYTYIQSRFYRAPEVILGARYGMPIDMWSFGCILAELLTGY-PLFPGEDEgdqlacmiellgMPPQKLLEtskr 296
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 675 ------------------IGNGRFSLSGG--------------IWDNISRGAKD-----LLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd14224   297 aknfisskgypryctvttLPDGSVVLNGGrsrrgkmrgppgskDWVTALKGCDDplfldFLKRCLEWDPAARMTPSQALR 376

                  ....
gi 1958807372 718 HPWI 721
Cdd:cd14224   377 HPWL 380
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
491-664 2.71e-13

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 71.98  E-value: 2.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII-----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRI----------------LK 549
Cdd:cd05100    48 AVKMLkddatDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLrarrppgmdysfdtckLP 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 550 KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL-------RGENGLLltpcy 622
Cdd:cd05100   128 EEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTED----NVMKIADFGLARDVhnidyykKTTNGRL----- 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGP 664
Cdd:cd05100   199 PVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIP 241
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
491-717 2.72e-13

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 71.53  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII-----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK-------------- 551
Cdd:cd05099    48 AVKMLkdnatDKDLADLISEMELMKLIGKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdytfditkvp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 552 ----CFseQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL-------RGENGLLltp 620
Cdd:cd05099   128 eeqlSF--KDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTED----NVMKIADFGLARGVhdidyykKTSNGRL--- 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 cyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEI--LLRIGNGRFSLSggiwdNISRGAKDL 697
Cdd:cd05099   199 --PVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPY---PGIPVEELfkLLREGHRMDKPS-----NCTHELYML 268
                         250       260
                  ....*....|....*....|
gi 1958807372 698 LSHMLHMDPHQRYTAEQVLK 717
Cdd:cd05099   269 MRECWHAVPTQRPTFKQLVE 288
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
116-353 3.05e-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: 71.18  E-value: 3.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVflVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEV-NHPFIVKLHYAFQTEGKLYL------ 188
Cdd:cd05089     9 VIGEGNFGQV--IKAMIKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIaieyap 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ---ILDFLRGGDVFTR---LSKE----VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd05089    87 ygnLLDFLRKSRVLETdpaFAKEhgtaSTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLS 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSA 336
Cdd:cd05089   167 RGEEVYVKKTMGRL-PVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRMEKPRNCDD 245
                         250
                  ....*....|....*..
gi 1958807372 337 EAQSLLRMLFKRNPANR 353
Cdd:cd05089   246 EVYELMRQCWRDRPYER 262
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
108-331 3.40e-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: 71.63  E-value: 3.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 108 PAQFDLLKVLGQGSFGkvfLVRKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK-- 185
Cdd:cd07858     4 DTKYVPIKPIGRGAYG---IVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHRea 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 ---LYLILDFLRggdvfTRL-----SKEVLfTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd07858    81 fndVYIVYELMD-----TDLhqiirSSQTL-SDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 258 SKESVDQEKKAYSFCGTVEYMAPEVV-NRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:cd07858   155 ARTTSEKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITEL-LGSP 228
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
115-353 3.52e-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: 3.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGkvfLVRKK--TGPDAGQL-YAMKVLRKASLKVRDRVRtkmerDILVEVN------HPFIVKLhYAFQTEGK 185
Cdd:cd05040     1 EKLGDGSFG---VVRRGewTTPSGKVIqVAVKCLKSDVLSQPNAMD-----DFLKEVNamhsldHPNLIRL-YGVVLSSP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKE----VLFTEEDvkfYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeS 261
Cdd:cd05040    72 LMMVTELAPLGSLLDRLRKDqghfLISTLCD---YAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMR-A 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 262 VDQEKKAY----------SFCgtveymAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA--KL 328
Cdd:cd05040   148 LPQNEDHYvmqehrkvpfAWC------APESLKTRKFSHASDVWMFGVTLWEMFTyGEEPWLGLNGSQILEKIDKEgeRL 221
                         250       260
                  ....*....|....*....|....*
gi 1958807372 329 GMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05040   222 ERPDDCPQDIYNVMLQCWAHKPADR 246
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
116-353 3.62e-13

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: 71.18  E-value: 3.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 116 VLGQGSFGKVFLVRKKTgpDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVN-HPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd05088    14 VIGEGNFGQVLKARIKK--DGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLGhHPNIINLLGACEHRGYLYLAIEYAP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFtEEDVKF-----------------YLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGL 257
Cdd:cd05088    92 HGNLLDFLRKSRVL-ETDPAFaianstastlssqqllhFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 258 SKESVDQEKKAYSFCgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI-LKAKLGMPQFLS 335
Cdd:cd05088   171 SRGQEVYVKKTMGRL-PVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLpQGYRLEKPLNCD 249
                         250
                  ....*....|....*...
gi 1958807372 336 AEAQSLLRMLFKRNPANR 353
Cdd:cd05088   250 DEVYDLMRQCWREKPYER 267
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
117-353 3.73e-13

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 70.49  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrKKTGPDAGQLyAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLhYAFQTEGKLYLILDFLRGG 196
Cdd:cd05071    17 LGQGCFGEVW---MGTWNGTTRV-AIKTLKPGTMSPEAFLQ---EAQVMKKLRHEKLVQL-YAVVSEEPIYIVTEYMSKG 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKE---VLFTEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYSFCG 273
Cdd:cd05071    89 SLLDFLKGEmgkYLRLPQLVDM-AAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 274 -TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLFKRNP 350
Cdd:cd05071   168 fPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNREVLDQVERGyRMPCPPECPESLHDLMCQCWRKEP 247

                  ...
gi 1958807372 351 ANR 353
Cdd:cd05071   248 EER 250
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
113-323 3.79e-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: 70.82  E-value: 3.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFlVRKKTGPDAG---QLYAMKVLR-KASLKVRDRVRTK-MERDILvevNHPFIVKLHYAFQTEGKLY 187
Cdd:cd05091    10 FMEELGEDRFGKVY-KGHLFGTAPGeqtQAVAIKTLKdKAEGPLREEFRHEaMLRSRL---QHPNIVCLLGVVTKEQPMS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLRGGDVFTRL--------------SKEVLFTEEDVKFY--LAELALALDHLHRLGIVYRDLKPENILLDEIGHIK 251
Cdd:cd05091    86 MIFSYCSHGDLHEFLvmrsphsdvgstddDKTVKSTLEPADFLhiVTQIAAGMEYLSSHHVVHKDLATRNVLVFDKLNVK 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 252 LTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMI 323
Cdd:cd05091   166 ISDLGLFREvyAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSNQDVIEMI 240
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
115-308 3.90e-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: 70.85  E-value: 3.90e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKAS-------LKVRDRVRtkmerdilvevNHPF---IVKLHYAFQTEG 184
Cdd:cd13981     6 KELGEGGYASVYLAKDDDEQSDGSLVALKVEKPPSiwefyicDQLHSRLK-----------NSRLresISGAHSAHLFQD 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLILDFLRGG---DVF--TRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL--------------- 244
Cdd:cd13981    75 ESILVMDYSSQGtllDVVnkMKNKTGGGMDEPLAMFFTIELLKVVEALHEVGIIHGDIKPDNFLLrleicadwpgegeng 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 245 -DEIGhIKLTDFGLSKESVDQEKKAySF---CGTVEYMAPEVVNRRGHSQSADWwsYGV--LMFEMLTGT 308
Cdd:cd13981   155 wLSKG-LKLIDFGRSIDMSLFPKNQ-SFkadWHTDSFDCIEMREGRPWTYQIDY--FGIaaTIHVMLFGK 220
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
461-722 4.08e-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: 70.88  E-value: 4.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 461 SEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEI----LMRYGQHPNIISLKEVFDDGKYVYLV-- 534
Cdd:cd07869     4 ADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIreasLLKGLKHANIVLLHDIIHTKETLTLVfe 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 535 ---TDLMK------GGELLDRIlkkKCFseqeasnvLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFG 605
Cdd:cd07869    84 yvhTDLCQymdkhpGGLHPENV---KLF--------LFQLLRGLSYIHQRYILHRDLKPQNLLISDTG----ELKLADFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAKQLRGENGLLLTPCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN--DTPEEILLRIGN----- 677
Cdd:cd07869   149 LARAKSVPSHTYSNEVVTLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDiqDQLERIFLVLGTpnedt 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 678 ------------GRFSLSGG-----IWDNIS--RGAKDLLSHMLHMDPHQRYTAEQVLKHPWIT 722
Cdd:cd07869   229 wpgvhslphfkpERFTLYSPknlrqAWNKLSyvNHAEDLASKLLQCFPKNRLSAQAALSHEYFS 292
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
469-665 4.27e-13

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 70.52  E-value: 4.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFA------VKIIDKNKRDPSEEIEILmRYGQHPNII----SLKEVFDDGKYVYLVTDLM 538
Cdd:cd14031    17 ELGRGAFKTVYKGLDTETWVEVAwcelqdRKLTKAEQQRFKEEAEML-KGLQHPNIVrfydSWESVLKGKKCIVLVTELM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQG--VVHRDLKPSNILYMDESGhpdSIKICDFGFAKQLRgeNGL 616
Cdd:cd14031    96 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTG---SVKIGDLGLATLMR--TSF 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 617 LLTPCYTANFVAPEvLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN 665
Cdd:cd14031   171 AKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQN 218
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
501-661 4.34e-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: 70.34  E-value: 4.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 501 DPSEEIEILmRYGQHPNIISLKEVFDD--GKYVYLVTDLMKGGELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGV 577
Cdd:cd05079    52 DLKKEIEIL-RNLYHENIVKYKGICTEdgGNGIKLIMEFLPSGSLKEYLPRNKNkINLKQQLKYAVQICKGMDYLGSRQY 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 578 VHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGL------LLTPCYtanFVAPEVLTQQGYDAACDIWSLGVLLY 651
Cdd:cd05079   131 VHRDLAARNVLVESEH----QVKIGDFGLTKAIETDKEYytvkddLDSPVF---WYAPECLIQSKFYIASDVWSFGVTLY 203
                         170
                  ....*....|....
gi 1958807372 652 TML----AGYTPFS 661
Cdd:cd05079   204 ELLtycdSESSPMT 217
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
464-657 4.95e-13

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 70.83  E-value: 4.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN---KRDPSEEIEILMRYGQHP----NIISLKEVFDDGKYVYLVTD 536
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHpsyARQGQIEVGILARLSNENadefNFVRAYECFQHRNHTCLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKggELLDRILKKKCFSE---QEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLrgE 613
Cdd:cd14229    82 MLE--QNLYDFLKQNKFSPlplKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHV--S 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 614 NGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGY 657
Cdd:cd14229   158 KTVCSTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGW 201
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
470-715 5.52e-13

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: 69.60  E-value: 5.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASnmEFAVKIIDKNK--RDPSEEIEILMRYgQHPNIISLKEVFDDGKYvyLVTDLMKGGELlDRI 547
Cdd:cd14068     2 LGDGGFGSVYRAVYRGE--DVAVKIFNKHTsfRLLRQELVVLSHL-HHPSLVALLAAGTAPRM--LVMELAPKGSL-DAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 548 LK--KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMdeSGHPDS---IKICDFGFAkQLRGENGlLLTPCY 622
Cdd:cd14068    76 LQqdNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLF--TLYPNCaiiAKIADYGIA-QYCCRMG-IKTSEG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQ-GYDAACDIWSLGVLLYTMLAGYTPFSNG---PNDTPE-EILLRIGNGRFSLSGGIWDnisrGAKDL 697
Cdd:cd14068   152 TPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTCGERIVEGlkfPNEFDElAIQGKLPDPVKEYGCAPWP----GVEAL 227
                         250
                  ....*....|....*...
gi 1958807372 698 LSHMLHMDPHQRYTAEQV 715
Cdd:cd14068   228 IKDCLKENPQCRPTSAQV 245
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
497-715 5.52e-13

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 69.95  E-value: 5.52e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 497 KNKRDPSEEIEILMRYgQHPNIISLkeVFDDGKYVYLVTDLMKGGELlDRILKKKCFSEQEASNVL-----YVITKTVEY 571
Cdd:cd14000    52 KNFRLLRQELTVLSHL-HHPSIVYL--LGIGIHPLMLVLELAPLGSL-DHLLQQDSRSFASLGRTLqqriaLQVADGLRY 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 572 LHSQGVVHRDLKPSNI----LYMDESGHpdsIKICDFGFAKQL--RGENGLLLTPcytaNFVAPEVLT-QQGYDAACDIW 644
Cdd:cd14000   128 LHSAMIIYRDLKSHNVlvwtLYPNSAII---IKIADYGISRQCcrMGAKGSEGTP----GFRAPEIARgNVIYNEKVDVF 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 645 SLGVLLYTMLAGYTPFSNGpNDTPEEillrigngrFSLSGGIWDNIS-------RGAKDLLSHMLHMDPHQRYTAEQV 715
Cdd:cd14000   201 SFGMLLYEILSGGAPMVGH-LKFPNE---------FDIHGGLRPPLKqyecapwPEVEVLMKKCWKENPQQRPTAVTV 268
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
117-311 5.81e-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: 70.22  E-value: 5.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKtgpdaGQLYAMKVLRKASLKVRDRVRTKMERDI--LVEVNHPFIVKLhYAFQTEG-KLYLILDFL 193
Cdd:cd14158    23 LGEGGFGVVFKGYIN-----DKNVAVKKLAAMVDISTEDLTKQFEQEIqvMAKCQHENLVEL-LGYSCDGpQLCLVYTYM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 194 RGGDVFTRLS--KEVLFTEEDVKFYLAE-LALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS 270
Cdd:cd14158    97 PNGSLLDRLAclNDTPPLSWHMRCKIAQgTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEKFSQTIMT 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1958807372 271 --FCGTVEYMAPEVVnrRGH-SQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14158   177 erIVGTTAYMAPEAL--RGEiTPKSDIFSFGVVLLEIITGLPPV 218
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
211-318 6.08e-13

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 70.68  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 211 EDVKFYLAELALALDHLHR-LGIVYRDLKPENILLDE-IGHIKLTDFGlskESVDQEKKAYSFCGTVEYMAPEVVNRRGH 288
Cdd:cd14136   119 PLVKKIARQVLQGLDYLHTkCGIIHTDIKPENVLLCIsKIEVKIADLG---NACWTDKHFTEDIQTRQYRSPEVILGAGY 195
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1958807372 289 SQSADWWSYGVLMFEMLTGTL---PFQGKD--RNE 318
Cdd:cd14136   196 GTPADIWSTACMAFELATGDYlfdPHSGEDysRDE 230
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
491-717 6.10e-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: 70.43  E-value: 6.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII--DKNKRDPSE---EIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK-----------CFS 554
Cdd:cd05098    49 AVKMLksDATEKDLSDlisEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycynpsHNP 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 555 EQEAS-----NVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL-------RGENGLLltpcy 622
Cdd:cd05098   129 EEQLSskdlvSCAYQVARGMEYLASKKCIHRDLAARNVLVTED----NVMKIADFGLARDIhhidyykKTTNGRL----- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPndtPEEILlrigngRFSLSGGIWDNISRGAKDLLSHM 701
Cdd:cd05098   200 PVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVP---VEELF------KLLKEGHRMDKPSNCTNELYMMM 270
                         250
                  ....*....|....*....
gi 1958807372 702 ---LHMDPHQRYTAEQVLK 717
Cdd:cd05098   271 rdcWHAVPSQRPTFKQLVE 289
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
110-331 6.98e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 69.85  E-value: 6.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTgpdAGQLYAMKVLRkasLKVRDR-VRTKMERDI--LVEVNHPFIVKLHYAFQTEGKL 186
Cdd:PLN00009    3 QYEKVEKIGEGTYGVVYKARDRV---TNETIALKKIR---LEQEDEgVPSTAIREIslLKEMQHGNIVRLQDVVHSEKRL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLrGGDVFTRLSKEVLFTEED--VKFYLAEL--ALALDHLHRlgIVYRDLKPENILLD-EIGHIKLTDFGLSKES 261
Cdd:PLN00009   77 YLVFEYL-DLDLKKHMDSSPDFAKNPrlIKTYLYQIlrGIAYCHSHR--VLHRDLKPQNLLIDrRTNALKLADFGLARAF 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 262 VDQEKKAYSFCGTVEYMAPEV-VNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAkLGMP 331
Cdd:PLN00009  154 GIPVRTFTHEVVTLWYRAPEIlLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRI-LGTP 223
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
111-353 7.65e-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: 69.49  E-value: 7.65e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKTgpDAGQLyaMKVLRKaSLKVRDRVRTKMERDI-----LVEVNHPFIVKL-HYAFQTEG 184
Cdd:cd05035     1 LKLGKILGEGEFGSVMEAQLKQ--DDGSQ--LKVAVK-TMKVDIHTYSEIEEFLseaacMKDFDHPNVMRLiGVCFTASD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYL-----ILDFLRGGDVFTRL-------SKEVLFTEEDVKFyLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKL 252
Cdd:cd05035    76 LNKPpspmvILPFMKHGDLHSYLlysrlggLPEKLPLQTLLKF-MVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 253 TDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KL 328
Cdd:cd05035   155 ADFGLSRKiySGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYPGVENHEIYDYLRNGnRL 234
                         250       260
                  ....*....|....*....|....*
gi 1958807372 329 GMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05035   235 KQPEDCLDEVYFLMYFCWTVDPKDR 259
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
464-720 8.71e-13

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


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 70.09  E-value: 8.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPS------EEIEILMRYgQHPNIISLKEV-------FDDGK- 529
Cdd:cd07865    14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGfpitalREIKILQLL-KHENVVNLIEIcrtkatpYNRYKg 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 530 YVYLVTDL----MKGgeLLDRILKKkcFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFG 605
Cdd:cd07865    93 SIYLVFEFcehdLAG--LLSNKNVK--FTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANIL-ITKDG---VLKLADFG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 606 FAKQL-RGENGllLTPCYTANFV-----APEVLT-QQGYDAACDIWSLGVLLYTMLAGYtPFSNGpnDTPEEILLRIGNG 678
Cdd:cd07865   165 LARAFsLAKNS--QPNRYTNRVVtlwyrPPELLLgERDYGPPIDMWGAGCIMAEMWTRS-PIMQG--NTEQHQLTLISQL 239
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 679 RFSLSGGIWDNISR----------------------------GAKDLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07865   240 CGSITPEVWPGVDKlelfkkmelpqgqkrkvkerlkpyvkdpYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
186-356 8.88e-13

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 70.28  E-value: 8.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDvftrLSKEVLFTEEDVKF---YLAELALALDHLHRLGIVYRDLKPENILLDEIGH---IKLTDFGLSK 259
Cdd:cd13977   110 LWFVMEFCDGGD----MNEYLLSRRPDRQTntsFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLSK 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 260 ----------ESVDQEKKAYS-FCGTVEYMAPEVvnRRGH-SQSADWWSYGVLMFEM--------------LTGTLPFQG 313
Cdd:cd13977   186 vcsgsglnpeEPANVNKHFLSsACGSDFYMAPEV--WEGHyTAKADIFALGIIIWAMveritfrdgetkkeLLGTYIQQG 263
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 314 KDRNETMNMIL---KAKLGMPQ----FLSAEAQSLLRMLFKRNPANRLGS 356
Cdd:cd13977   264 KEIVPLGEALLenpKLELQIPLkkkkSMNDDMKQLLRDMLAANPQERPDA 313
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
117-353 8.97e-13

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 69.48  E-value: 8.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKK-TGPDAGQ-LYAMKVLRK-ASLKVR-DRVRtkmERDILVEVNHPFIVKLhYAFQTEGK-LYLILD 191
Cdd:cd05050    13 IGQGAFGRVFQARAPgLLPYEPFtMVAVKMLKEeASADMQaDFQR---EAALMAEFDHPNIVKL-LGVCAVGKpMCLLFE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 192 FLRGGDVFTRLSKEVLFTEEDVKFYLAELA------LALDHLHRLGI----------------VYRDLKPENILLDEIGH 249
Cdd:cd05050    89 YMAYGDLNEFLRHRSPRAQCSLSHSTSSARkcglnpLPLSCTEQLCIakqvaagmaylserkfVHRDLATRNCLVGENMV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 250 IKLTDFGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA 326
Cdd:cd05050   169 VKIADFGLSRNiySADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAHEEVIYYVRDG 248
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 327 K-LGMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd05050   249 NvLSCPDNCPLELYNLMRLCWSKLPSDR 276
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
486-665 9.07e-13

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: 69.12  E-value: 9.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 486 SNMEFAVKIIDK---NKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK-CFSEQEASNV 561
Cdd:cd05114    27 AQYKVAIKAIREgamSEEDFIEEAKVMMKL-THPKLVQLYGVCTQQKPIYIVTEFMENGCLLNYLRQRRgKLSRDMLLSM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 562 LYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKqlrgengLLLTPCYTANFVA--------PEVLT 633
Cdd:cd05114   106 CQDVCEGMEYLERNNFIHRDLAARNCLVNDTG----VVKVSDFGMTR-------YVLDDQYTSSSGAkfpvkwspPEVFN 174
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958807372 634 QQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPN 665
Cdd:cd05114   175 YSKFSSKSDVWSFGVLMWEVFTeGKMPFESKSN 207
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
113-362 9.08e-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: 69.65  E-value: 9.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 113 LLKVLGQGSFGKVFLVR-KKTGPDAGQ-LYAMKVLRKASLKVRDRVrtKMERDILVEVNHPFIVKLHYAFQTEGKLYLIL 190
Cdd:cd05094     9 LKRELGEGAFGKVFLAEcYNLSPTKDKmLVAVKTLKDPTLAARKDF--QREAELLTNLQHDHIVKFYGVCGDGDPLIMVF 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 191 DFLRGGDV--FTRLSKEVLFTEEDVKFYLAELALALDHLHRL------GIVY--------RDLKPENILLDEIGHIKLTD 254
Cdd:cd05094    87 EYMKHGDLnkFLRAHGPDAMILVDGQPRQAKGELGLSQMLHIatqiasGMVYlasqhfvhRDLATRNCLVGANLLVKIGD 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGLSKE--SVDQEKKAYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAK-LGM 330
Cdd:cd05094   167 FGMSRDvySTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPWFQLSNTEVIECITQGRvLER 246
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 331 PQFLSAEAQSLLRMLFKRNPANRLGSEGVEEV 362
Cdd:cd05094   247 PRVCPKEVYDIMLGCWQREPQQRLNIKEIYKI 278
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
470-655 1.02e-12

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


Pssm-ID: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 68.66  E-value: 1.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKI--IDKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRI 547
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMntLSSNRANMLREVQLMNRL-SHPNILRFMGVCVHQGQLHALTEYINGGNLEQLL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 548 LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIkICDFGFAKQL--RGENGLLLTPCYTAN 625
Cdd:cd14155    80 DSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENGYTAV-VGDFGLAEKIpdYSDGKEKLAVVGSPY 158
                         170       180       190
                  ....*....|....*....|....*....|
gi 1958807372 626 FVAPEVLTQQGYDAACDIWSLGVLLYTMLA 655
Cdd:cd14155   159 WMAPEVLRGEPYNEKADVFSYGIILCEIIA 188
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
114-332 1.04e-12

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: 69.71  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFL-VRKKTGPDAGQLYAMKVLRKASlKVRDRVRTKMERDILVEVNHPFIVKLhYAFQTEGKLYLILDF 192
Cdd:cd05110    12 VKVLGSGAFGTVYKgIWVPEGETVKIPVAIKILNETT-GPKANVEFMDEALIMASMDHPHLVRL-LGVCLSPTIQLVTQL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDV--FTRLSKEVLFTEEDVKfYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKeSVDQEKKAYS 270
Cdd:cd05110    90 MPHGCLldYVHEHKDNIGSQLLLN-WCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLAR-LLEGDEKEYN 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 271 FCG---TVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKAKLgMPQ 332
Cdd:cd05110   168 ADGgkmPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLLEKGER-LPQ 232
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
110-311 1.07e-12

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


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 68.95  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLlkVLGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK---- 185
Cdd:cd14032     4 KFDI--ELGRGSFKTVY---KGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKgkrc 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSV 262
Cdd:cd14032    79 IVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1958807372 263 DQEKKAYSFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14032   157 KRASFAKSVIGTPEFMAPEMYEEH-YDESVDVYAFGMCMLEMATSEYPY 204
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
509-720 1.19e-12

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: 69.27  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDGKYVYLVTdlmkggELLDRILKK---KCFSEQEASNV---LYVITKTVEYLHSQGVVHRDL 582
Cdd:cd07871    56 LLKNLKHANIVTLHDIIHTERCLTLVF------EYLDSDLKQyldNCGNLMSMHNVkifMFQLLRGLSYCHKRKILHRDL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 583 KPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTPCYTANFVAPEVLT-QQGYDAACDIWSLGVLLYTMLAGYTPFs 661
Cdd:cd07871   130 KPQNLL-INEKGE---LKLADFGLARAKSVPTKTYSNEVVTLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGRPMF- 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 662 ngPNDTPEEILLRIgngrFSLSGG----IWDNISRGAK--------------------------DLLSHMLHMDPHQRYT 711
Cdd:cd07871   205 --PGSTVKEELHLI----FRLLGTpteeTWPGVTSNEEfrsylfpqyraqplinhaprldtdgiDLLSSLLLYETKSRIS 278

                  ....*....
gi 1958807372 712 AEQVLKHPW 720
Cdd:cd07871   279 AEAALRHSY 287
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
460-721 1.28e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 69.32  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEILMRYG----------QHPNIISLKEVFD-DG 528
Cdd:cd14040     4 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHAcreyrihkelDHPRIVKLYDYFSlDT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 KYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHS--QGVVHRDLKPSNILYMDESGHPDsIKICDFGF 606
Cdd:cd14040    84 DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACGE-IKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLR----GENGLLLTP------------CYTANFVAPEVLTQqgydaaCDIWSLGVLLYTMLAGYTPFsnGPNDTPEE 670
Cdd:cd14040   163 SKIMDddsyGVDGMDLTSqgagtywylppeCFVVGKEPPKISNK------VDVWSVGVIFFQCLYGRKPF--GHNQSQQD 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 671 IL-----LRIGNGRFSLSggiwDNISRGAKDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14040   235 ILqentiLKATEVQFPVK----PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYL 286
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
491-664 1.37e-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: 69.27  E-value: 1.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII-----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEASNV---- 561
Cdd:cd05101    60 AVKMLkddatEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDInrvp 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 562 ------------LYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL-------RGENGLLltpcy 622
Cdd:cd05101   140 eeqmtfkdlvscTYQLARGMEYLASQKCIHRDLAARNVLVTEN----NVMKIADFGLARDInnidyykKTTNGRL----- 210
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGP 664
Cdd:cd05101   211 PVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIP 253
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
509-678 1.43e-12

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: 68.91  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD--------RILKKKC--FSEQeasnvlyvITKTVEYLHSQGVV 578
Cdd:cd05072    55 LMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLLDflksdeggKVLLPKLidFSAQ--------IAEGMAYIERKNYI 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 579 HRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLTQQGYDAACDIWSLGVLL 650
Cdd:cd05072   127 HRDLRAANVLVSESL----MCKIADFGLARVIEDNE-------YTAregakfpiKWTAPEAINFGSFTIKSDVWSFGILL 195
                         170       180
                  ....*....|....*....|....*....
gi 1958807372 651 YTMLA-GYTPFsngPNDTPEEILLRIGNG 678
Cdd:cd05072   196 YEIVTyGKIPY---PGMSNSDVMSALQRG 221
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
99-304 1.53e-12

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: 69.28  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  99 VKEGYEKADPAQ-FDLLKVLGQGSFGKVFLVRKKTGPDAGQLYAMKVLRKAS-LKVRDRVRtkmERDILVEVNHPFIVKL 176
Cdd:cd06634     4 VAELFFKDDPEKlFSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSGKQSnEKWQDIIK---EVKFLQKLRHPNTIEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 177 HYAFQTEGKLYLILDFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALAldHLHRLGIVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd06634    81 RGCYLREHTAWLVMEYCLGSasDLLEVHKKPLQEVEIAAITHGALQGLA--YLHSHNMIHRDVKAGNILLTEPGLVKLGD 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 255 FGlskeSVDQEKKAYSFCGTVEYMAPEVVNRRGHSQ---SADWWSYGVLMFEM 304
Cdd:cd06634   159 FG----SASIMAPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIEL 207
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
466-657 1.70e-12

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 68.22  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSYSVCKRCIHSASNMEFAVKIIdknKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKYVYLVTDLMKG 540
Cdd:cd05052    10 MKHKLGGGQYGEVYEGVWKKYNLTVAVKTL---KEDTMEVEEFLkeaavMKEIKHPNLVQLLGVCTREPPFYIITEFMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 541 GELLDrILKKKCFSEQEASNVLYVITKT---VEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENgll 617
Cdd:cd05052    87 GNLLD-YLRECNREELNAVVLLYMATQIasaMEYLEKKNFIHRDLAARNCLV----GENHLVKVADFGLSRLMTGDT--- 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1958807372 618 ltpcYTAN--------FVAPEVLTQQGYDAACDIWSLGVLLYTmLAGY 657
Cdd:cd05052   159 ----YTAHagakfpikWTAPESLAYNKFSIKSDVWAFGVLLWE-IATY 201
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
491-655 1.88e-12

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 68.58  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII----DKNKRDP-----SEEIEILmRYGQHPNIISLKeVFD---DGKyVYLVtdlMKGGE--LLDRILKKK----- 551
Cdd:cd14001    32 AVKKInskcDKGQRSLyqerlKEEAKIL-KSLNHPNIVGFR-AFTkseDGS-LCLA---MEYGGksLNDLIEERYeaglg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 552 CFSEQEASNVLYVITKTVEYLHSQG-VVHRDLKPSNILYmdeSGHPDSIKICDFGFAKQLRGENGLLLTPcyTANFV--- 627
Cdd:cd14001   106 PFPAATILKVALSIARALEYLHNEKkILHGDIKSGNVLI---KGDFESVKLCDFGVSLPLTENLEVDSDP--KAQYVgte 180
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958807372 628 ---APEVLTQQGY--DAAcDIWSLGVLLYTMLA 655
Cdd:cd14001   181 pwkAKEALEEGGVitDKA-DIFAYGLVLWEMMT 212
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
117-305 1.92e-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: 67.93  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKaslkvrDRVRTKMERDI--LVEVNHPFIVKLHYAFQTEGKLYLILDFLR 194
Cdd:cd14156     1 IGSGFFSKVYKVTHGAT---GKVMVVKIYKN------DVDQHKIVREIslLQKLSHPNIVRYLGICVKDEKLHPILEYVS 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GGDVFTRLSKEVLFTEEDVKFYLA-ELALALDHLHRLGIVYRDLKPENILLDEIGHIK---LTDFGLSKESV-----DQE 265
Cdd:cd14156    72 GGCLEELLAREELPLSWREKVELAcDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVGempanDPE 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1958807372 266 KKaYSFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEML 305
Cdd:cd14156   152 RK-LSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
450-721 2.43e-12

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


Pssm-ID: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 68.88  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 450 IVQINgnaAQFSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdKNKRDPSE----EIEILMRYGQHP-----NIIS 520
Cdd:cd14226     4 IVKNG---EKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKII-KNKKAFLNqaqiEVRLLELMNKHDtenkyYIVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 521 LKEVFDDGKYVYLVT--------DLMK----GGELLDRILKkkcFSEQEASNVLYVITKTVEylhsqgVVHRDLKPSNIL 588
Cdd:cd14226    80 LKRHFMFRNHLCLVFellsynlyDLLRntnfRGVSLNLTRK---FAQQLCTALLFLSTPELS------IIHCDLKPENIL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 589 --YMDESghpdSIKICDFGfakqlrgenglllTPCYTAN----------FVAPEVLTQQGYDAACDIWSLGVLLYTMLAG 656
Cdd:cd14226   151 lcNPKRS----AIKIIDFG-------------SSCQLGQriyqyiqsrfYRSPEVLLGLPYDLAIDMWSLGCILVEMHTG 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 657 yTPFSNGPNDT-------------PEEIL----------LRIGNGRFSL--SGGIWDNISRGA----------------- 694
Cdd:cd14226   214 -EPLFSGANEVdqmnkivevlgmpPVHMLdqapkarkffEKLPDGTYYLkkTKDGKKYKPPGSrklheilgvetggpggr 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 695 ---------------KDLLSHMLHMDPHQRYTAEQVLKHPWI 721
Cdd:cd14226   293 ragepghtvedylkfKDLILRMLDYDPKTRITPAEALQHSFF 334
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
497-676 2.57e-12

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 68.00  E-value: 2.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 497 KNKRDPSEEIEILmRYGQHPNIISLKEV-FDDGKY-VYLVTDLMKGGELLDRILKKKcfSEQEASNVL---YVITKTVEY 571
Cdd:cd05081    47 DQQRDFQREIQIL-KALHSDFIVKYRGVsYGPGRRsLRLVMEYLPSGCLRDFLQRHR--ARLDASRLLlysSQICKGMEY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 572 LHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQL--RGENGLLLTPCYTANF-VAPEVLTQQGYDAACDIWSLGV 648
Cdd:cd05081   124 LGSRRCVHRDLAARNILVESEA----HVKIADFGLAKLLplDKDYYVVREPGQSPIFwYAPESLSDNIFSRQSDVWSFGV 199
                         170       180
                  ....*....|....*....|....*...
gi 1958807372 649 LLYTMLAgytpFSNGPNDTPEEILLRIG 676
Cdd:cd05081   200 VLYELFT----YCDKSCSPSAEFLRMMG 223
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
565-722 2.58e-12

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 68.04  E-value: 2.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILYmdeSGHPDSIKICDFGFAKQlrgENGLLLTPCYTANFVAPEV-----LTQQGYD- 638
Cdd:cd14020   119 VLEALAFLHHEGYVHADLKPRNILW---SAEDECFKLIDFGLSFK---EGNQDVKYIQTDGYRAPEAelqncLAQAGLQs 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 639 -----AACDIWSLGVLLYTMLAG----YTPFSNGPNDTPEEILLRIgngrFSLSGGIWDNI-SRGAKDLLSHMLHMDPHQ 708
Cdd:cd14020   193 etectSAVDLWSLGIVLLEMFSGmklkHTVRSQEWKDNSSAIIDHI----FASNAVVNPAIpAYHLRDLIKSMLHNDPGK 268
                         170
                  ....*....|....
gi 1958807372 709 RYTAEQVLKHPWIT 722
Cdd:cd14020   269 RATAEAALCSPFFS 282
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
164-333 2.82e-12

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 67.50  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 164 ILVEVNHPFIVKL-HYAFQTEGKLYLILDFLRGGDV--FTRLSKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPE 240
Cdd:cd05058    49 IMKDFSHPNVLSLlGICLPSEGSPLVVLPYMKHGDLrnFIRSETHNPTVKDLIGFGL-QVAKGMEYLASKKFVHRDLAAR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 241 NILLDEIGHIKLTDFGLSKESVDQE------KKAYSFcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQG 313
Cdd:cd05058   128 NCMLDESFTVKVADFGLARDIYDKEyysvhnHTGAKL--PVKWMALESLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPD 205
                         170       180
                  ....*....|....*....|.
gi 1958807372 314 KDRNETMNMILKA-KLGMPQF 333
Cdd:cd05058   206 VDSFDITVYLLQGrRLLQPEY 226
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
470-655 2.98e-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: 67.54  E-value: 2.98e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASNMEFAVKIIdKNKRDPS---EEIEILMRYgQHPNIIS-LKEVFDDGKyVYLVTDLMKGGELLD 545
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIY-KNDVDQHkivREISLLQKL-SHPNIVRyLGICVKDEK-LHPILEYVSGGCLEE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIkICDFGFAKQL------RGENGLLL 618
Cdd:cd14156    78 LLAREELpLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGREAV-VTDFGLAREVgempanDPERKLSL 156
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1958807372 619 TPcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA 655
Cdd:cd14156   157 VG--SAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILA 191
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
470-678 3.35e-12

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: 67.69  E-value: 3.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSY-SVCKRCIHSASNMEFAVKI-------IDKNKRDPSEEIEILMRYGQHpNIISLKEVFDDGKYVYLVTDLMKGG 541
Cdd:cd05063    13 IGAGEFgEVFRGILKMPGRKEVAVAIktlkpgyTEKQRQDFLSEASIMGQFSHH-NIIRLEGVVTKFKPAMIITEYMENG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELlDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENglllT 619
Cdd:cd05063    92 AL-DKYLRDHDgeFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNL----ECKVSDFGLSRVLEDDP----E 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 620 PCYTAN-------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNdtpEEILLRIGNG 678
Cdd:cd05063   163 GTYTTSggkipirWTAPEAIAYRKFTSASDVWSFGIVMWEVMSfGERPYWDMSN---HEVMKAINDG 226
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
460-672 4.94e-12

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 67.78  E-value: 4.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYELKEDIGIGSYSVCKRCIHSASNMEFAVKI--IDKNKRDPSEE--------IEILMRYGQHPNIISLKEVFD-DG 528
Cdd:cd14041     4 LNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYFSlDT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 529 KYVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHS--QGVVHRDLKPSNILYMDESGHPDsIKICDFGF 606
Cdd:cd14041    84 DSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTACGE-IKITDFGL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 607 AKQLRGEN-----GLLLTP------------CYTANFVAPEVLTQqgydaaCDIWSLGVLLYTMLAGYTPFsnGPNDTPE 669
Cdd:cd14041   163 SKIMDDDSynsvdGMELTSqgagtywylppeCFVVGKEPPKISNK------VDVWSVGVIFYQCLYGRKPF--GHNQSQQ 234

                  ...
gi 1958807372 670 EIL 672
Cdd:cd14041   235 DIL 237
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
110-313 5.99e-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: 66.99  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFlvRKKTGPDAgqlyAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLI 189
Cdd:cd14063     1 ELEIKEVIGKGRFGRVH--RGRWHGDV----AIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 190 LDFLRGGDVFTRL--SKEVLFTEEDVKFYLaELALALDHLHRLGIVYRDLKPENILLDEiGHIKLTDFGLSKESvdqekk 267
Cdd:cd14063    75 TSLCKGRTLYSLIheRKEKFDFNKTVQIAQ-QICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSLS------ 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 268 AYSFCGTVE-----------YMAPEVVN------RRGH----SQSADWWSYGVLMFEMLTGTLPFQG 313
Cdd:cd14063   147 GLLQPGRREdtlvipngwlcYLAPEIIRalspdlDFEEslpfTKASDVYAFGTVWYELLAGRWPFKE 213
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
227-354 6.71e-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: 67.05  E-value: 6.71e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 227 LHRLGIVYRDLKPENILLDEIGH-IKLTDFGLSKESVDQEKKAYSFCGTVEYMAPEVVNRRGHS-QSADWWSYGVLMFEM 304
Cdd:cd13974   148 LHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSEDDLLKDQRGSPAYISPDVLSGKPYLgKPSDMWALGVVLFTM 227
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 305 LTGTLPFQGKDRNETMNMILKAKLGMPQ--FLSAEAQSLLRMLFKRNPANRL 354
Cdd:cd13974   228 LYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRL 279
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
110-323 7.26e-12

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: 67.35  E-value: 7.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVflVRKKTGPDAGQLYAMKVLRKASlKVRDRVRtkMERDILVEVNHP------FIVKLHYAFQTE 183
Cdd:cd14215    13 RYEIVSTLGEGTFGRV--VQCIDHRRGGARVALKIIKNVE-KYKEAAR--LEINVLEKINEKdpenknLCVQMFDWFDYH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 184 GKLYLILDFLrGGDVFTRLSKE--VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---------------DE 246
Cdd:cd14215    88 GHMCISFELL-GLSTFDFLKENnyLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFvnsdyeltynlekkrDE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 247 ----IGHIKLTDFGlsKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNM 322
Cdd:cd14215   167 rsvkSTAIRVVDFG--SATFDHEHHS-TIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAM 243

                  .
gi 1958807372 323 I 323
Cdd:cd14215   244 M 244
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
117-353 7.66e-12

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 66.29  E-value: 7.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVF-LVRKKTGpdagQLYAMKVLRKASLKVRDRVRtkmERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRG 195
Cdd:cd05052    14 LGGGQYGEVYeGVWKKYN----LTVAVKTLKEDTMEVEEFLK---EAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 196 G---DVFTRLSKEVLftEEDVKFYLA-ELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKAYS- 270
Cdd:cd05052    87 GnllDYLRECNREEL--NAVVLLYMAtQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAg 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 271 --FcgTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLT-GTLPFQGKDRNETMNMILKA-KLGMPQFLSAEAQSLLRMLF 346
Cdd:cd05052   165 akF--PIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYELLEKGyRMERPEGCPPKVYELMRACW 242

                  ....*..
gi 1958807372 347 KRNPANR 353
Cdd:cd05052   243 QWNPSDR 249
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
560-720 1.48e-11

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 65.82  E-value: 1.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 NVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTpCYTANFVAPEVLTQQGYDA 639
Cdd:cd07862   114 DMMFQLLRGLDFLHSHRVVHRDLKPQNIL-VTSSGQ---IKLADFGLARIYSFQMALTSV-VVTLWYRAPEVLLQSSYAT 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 640 ACDIWSLGVLLYTMLAgYTPFSNGPND--------------TPEEILLRIGNGRFSLSG-------GIWDNISRGAKDLL 698
Cdd:cd07862   189 PVDLWSVGCIFAEMFR-RKPLFRGSSDvdqlgkildviglpGEEDWPRDVALPRQAFHSksaqpieKFVTDIDELGKDLL 267
                         170       180
                  ....*....|....*....|..
gi 1958807372 699 SHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07862   268 LKCLTFNPAKRISAYSALSHPY 289
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
504-671 1.51e-11

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 65.69  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 504 EEIEILmRYGQHPNIISLKEVFDD--GKYVYLVTDLMKGGELLDRILKKKC-------FSEQeasnvlyvITKTVEYLHS 574
Cdd:cd05080    55 QEIDIL-KTLYHENIVKYKGCCSEqgGKSLQLIMEYVPLGSLRDYLPKHSIglaqlllFAQQ--------ICEGMAYLHS 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 575 QGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLR--------GENGllLTPCYtanFVAPEVLTQQGYDAACDIWSL 646
Cdd:cd05080   126 QHYIHRDLAARNVLLDNDR----LVKIGDFGLAKAVPegheyyrvREDG--DSPVF---WYAPECLKEYKFYYASDVWSF 196
                         170       180
                  ....*....|....*....|....*
gi 1958807372 647 GVLLYTMLAGYTPFSNGPNDTPEEI 671
Cdd:cd05080   197 GVTLYELLTHCDSSQSPPTKFLEMI 221
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
462-720 1.62e-11

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: 66.17  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKII--DKNKRDPSEEIE--ILMRYGQHPNIISLKEVFDDGKYVYLVTdl 537
Cdd:cd07872     6 ETYIKLEKLGEGTYATVFKGRSKLTENLVALKEIrlEHEEGAPCTAIRevSLLKDLKHANIVTLHDIVHTDKSLTLVF-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 538 mkggELLDRILKK---KCFSEQEASNV---LYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLR 611
Cdd:cd07872    84 ----EYLDKDLKQymdDCGNIMSMHNVkifLYQILRGLAYCHRRKVLHRDLKPQNLL-INERGE---LKLADFGLARAKS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 GENGLLLTPCYTANFVAPEVLTQQG-YDAACDIWSLGVLLYTMLAGYTPFsngPNDTPEEILLRIGNGRFSLSGGIWDNI 690
Cdd:cd07872   156 VPTKTYSNEVVTLWYRPPDVLLGSSeYSTQIDMWGVGCIFFEMASGRPLF---PGSTVEDELHLIFRLLGTPTEETWPGI 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 691 SRGAK--------------------------DLLSHMLHMDPHQRYTAEQVLKHPW 720
Cdd:cd07872   233 SSNDEfknynfpkykpqplinhaprldtegiELLTKFLQYESKKRISAEEAMKHAY 288
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
491-664 1.66e-11

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: 65.51  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIdKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDdGKYVYLVTDLMKGGELLDRILKKK---------CFSEQ 556
Cdd:cd05057    40 AIKVL-REETGPKANEEILdeayvMASVDHPHLVRLLGICL-SSQVQLITQLMPLGCLLDYVRNHRdnigsqlllNWCVQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 557 easnvlyvITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQL-RGENGLLLTPCYTA-NFVAPEVLTQ 634
Cdd:cd05057   118 --------IAKGMSYLEEKRLVHRDLAARNVLVKT----PNHVKITDFGLAKLLdVDEKEYHAEGGKVPiKWMALESIQY 185
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1958807372 635 QGYDAACDIWSLGVLLYTMLA-GYTPFSNGP 664
Cdd:cd05057   186 RIYTHKSDVWSYGVTVWELMTfGAKPYEGIP 216
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
110-325 1.87e-11

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: 66.19  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVF----LVRKKTGpdagqlYAMKVLRKASlKVRDRVRtkMERDILVEV------NHPFIVKLHYA 179
Cdd:cd14214    14 RYEIVGDLGEGTFGKVVecldHARGKSQ------VALKIIRNVG-KYREAAR--LEINVLKKIkekdkeNKFLCVLMSDW 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLILDFLrGGDVFTRLsKEVLFTE---EDVKFYLAELALALDHLHRLGIVYRDLKPENILLD----------- 245
Cdd:cd14214    85 FNFHGHMCIAFELL-GKNTFEFL-KENNFQPyplPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVnsefdtlynes 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 246 ---EIGHIK-----LTDFGlsKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd14214   163 kscEEKSVKntsirVADFG--SATFDHEHHT-TIVATRHYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTHENR 239

                  ....*...
gi 1958807372 318 ETMNMILK 325
Cdd:cd14214   240 EHLVMMEK 247
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
473-660 1.88e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 66.79  E-value: 1.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 473 GSYSVCKRcIHSASNMEFAVKIIDKNKrDPSEEIEILmRYGQHPNIISLKEVFDDGKYVYLVTDLMKGgELLDRILKKKC 552
Cdd:PHA03207  106 GEVFVCTK-HGDEQRKKVIVKAVTGGK-TPGREIDIL-KTISHRAIINLIHAYRWKSTVCMVMPKYKC-DLFTYVDRSGP 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 553 FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIlYMDEsghPDSIKICDFGFAKQLRGENGlllTP-CY----TANFV 627
Cdd:PHA03207  182 LPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENI-FLDE---PENAVLGDFGAACKLDAHPD---TPqCYgwsgTLETN 254
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958807372 628 APEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:PHA03207  255 SPELLALDPYCAKTDIWSAGLVLFEMSVKNVTL 287
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
464-665 2.17e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 67.84  E-value: 2.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIID----KNKRDPSEEIEI-LMRYGQHPNIISLKEVFDD--GKYVYLVTD 536
Cdd:PTZ00266    15 YEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISyrglKEREKSQLVIEVnVMRELKHKNIVRYIDRFLNkaNQKLYILME 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372  537 LMKGGELLDRIlkKKCF------SEQEASNVLYVITKTVEYLHS-------QGVVHRDLKPSNILYMDESGHPDSI---- 599
Cdd:PTZ00266    95 FCDAGDLSRNI--QKCYkmfgkiEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIRHIGKItaqa 172
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372  600 ---------KICDFGFAKQLrGENGLLLTPCYTANFVAPEVLTQQ--GYDAACDIWSLGVLLYTMLAGYTPFSNGPN 665
Cdd:PTZ00266   173 nnlngrpiaKIGDFGLSKNI-GIESMAHSCVGTPYYWSPELLLHEtkSYDDKSDMWALGCIIYELCSGKTPFHKANN 248
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
117-256 2.33e-11

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: 62.07  E-value: 2.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDAgqlYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGKLYLILDFLRGG 196
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIG---VAVKIGDDVNNEEGEDLESEMDILRRLKGLELNIPKVLVTEDVDGPNILLMELVKGG 77
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 197 DVFTRLSKEVLFtEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFG 256
Cdd:cd13968    78 TLIAYTQEEELD-EKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
462-669 2.54e-11

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: 65.84  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKN-----KRDPSEEIEILMRYGQhPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEikpaiRNQIIRELQVLHECNS-PYIVGFYGAFYSDGEISICME 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELlDRILKK-KCFSEQEASNVLYVITKTVEYLHSQ-GVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRgeN 614
Cdd:cd06649    84 HMDGGSL-DQVLKEaKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNIL-VNSRGE---IKLCDFGVSGQLI--D 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 615 GLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPFSngPNDTPE 669
Cdd:cd06649   157 SMANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPIP--PPDAKE 209
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
469-665 2.91e-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: 64.71  E-value: 2.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNMEFA------VKIIDKNKRDPSEEIEILmRYGQHPNIISLKEVFDDG----KYVYLVTDLM 538
Cdd:cd14032     8 ELGRGSFKTVYKGLDTETWVEVAwcelqdRKLTKVERQRFKEEAEML-KGLQHPNIVRFYDFWESCakgkRCIVLVTELM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQG--VVHRDLKPSNILYMDESGhpdSIKICDFGFAKQLRGE--N 614
Cdd:cd14032    87 TSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTG---SVKIGDLGLATLKRASfaK 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 615 GLLLTPcytaNFVAPEvLTQQGYDAACDIWSLGVLLYTMLAGYTPFSNGPN 665
Cdd:cd14032   164 SVIGTP----EFMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECQN 209
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
117-311 3.01e-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: 65.07  E-value: 3.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 192
Cdd:cd14030    33 IGRGSFKTVY---KGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTEL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLG--IVYRDLKPENILLD-EIGHIKLTDFGLSkeSVDQEKKAY 269
Cdd:cd14030   110 MTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRASFAK 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1958807372 270 SFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14030   188 SVIGTPEFMAPEMYEEK-YDESVDVYAFGMCMLEMATSEYPY 228
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
469-660 4.00e-11

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 64.21  E-value: 4.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHSASNME--FAVKIIDKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDdGKYVYLVTDLMKGG 541
Cdd:cd05116     2 ELGSGNFGTVKKGYYQMKKVVktVAVKILKNEANDPALKDELLreanvMQQLDNPYIVRMIGICE-AESWMLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 542 ELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLLLTPC 621
Cdd:cd05116    81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQH----YAKISDFGLSKALRADENYYKAQT 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958807372 622 ---YTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05116   157 hgkWPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSyGQKPY 199
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
468-679 4.26e-11

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


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 64.13  E-value: 4.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCiHSASNMEFAVKIIDK---NKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELL 544
Cdd:cd05113    10 KELGTGQFGVVKYG-KWRGQYDVAIKMIKEgsmSEDEFIEEAKVMMNL-SHEKLVQLYGVCTKQRPIFIITEYMANGCLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQ-LRGENGLLLTPCY 622
Cdd:cd05113    88 NYLREmRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCL-VNDQG---VVKVSDFGLSRYvLDDEYTSSVGSKF 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 623 TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNdtpEEILLRIGNGR 679
Cdd:cd05113   164 PVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKMPYERFTN---SETVEHVSQGL 218
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
466-716 4.64e-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: 64.31  E-value: 4.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-SVCKRCIHSasnmEFAVKIIDKNKRDPSE------EIEILmRYGQHPNIIsLKEVFDDGKYVYLVTDLM 538
Cdd:cd14151    12 VGQRIGSGSFgTVYKGKWHG----DVAVKMLNVTAPTPQQlqafknEVGVL-RKTRHVNIL-LFMGYSTKPQLAIVTQWC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAK--------- 608
Cdd:cd14151    86 EGSSLYHHLhIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHED----LTVKIGDFGLATvksrwsgsh 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 609 QLRGENGLLLtpcytanFVAPEVLTQQG---YDAACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRIGNGRFSLS-G 684
Cdd:cd14151   162 QFEQLSGSIL-------WMAPEVIRMQDknpYSFQSDVYAFGIVLYELMTGQLPYSNINNR--DQIIFMVGRGYLSPDlS 232
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1958807372 685 GIWDNISRGAKDLLSHMLHMDPHQRYTAEQVL 716
Cdd:cd14151   233 KVRSNCPKAMKRLMAECLKKKRDERPLFPQIL 264
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
516-720 5.09e-11

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: 64.10  E-value: 5.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 516 PNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKkcFSEQEASNVL-------------YV-----------ITKTVEY 571
Cdd:cd05576    51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKF--LNDKEIHQLFadlderlaaasrfYIpeeciqrwaaeMVVALDA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 572 LHSQGVVHRDLKPSNILyMDESGHpdsIKICDFG----FAKQLRGEngllltpCYTANFVAPEVLTQQGYDAACDIWSLG 647
Cdd:cd05576   129 LHREGIVCRDLNPNNIL-LNDRGH---IQLTYFSrwseVEDSCDSD-------AIENMYCAPEVGGISEETEACDWWSLG 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958807372 648 VLLYTMLAGYTPFSNGPNDTpeeillrigNGRFSLSggIWDNISRGAKDLLSHMLHMDPHQRYTA-----EQVLKHPW 720
Cdd:cd05576   198 ALLFELLTGKALVECHPAGI---------NTHTTLN--IPEWVSEEARSLLQQLLQFNPTERLGAgvagvEDIKSHPF 264
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
487-671 5.97e-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: 63.75  E-value: 5.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 487 NMEFAVKIIDKNKRDPSEEIEI--LMRYGQHPNIISLKEVFDDgKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVLYV 564
Cdd:cd05067    31 HTKVAIKSLKQGSMSPDAFLAEanLMKQLQHQRLVRLYAVVTQ-EPIYIITEYMENGSLVD-FLKTPSGIKLTINKLLDM 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVE---YLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLT 633
Cdd:cd05067   109 AAQIAEgmaFIEERNYIHRDLRAANILVSDTL----SCKIADFGLARLIEDNE-------YTAregakfpiKWTAPEAIN 177
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1958807372 634 QQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNdtPEEI 671
Cdd:cd05067   178 YGTFTIKSDVWSFGILLTEIVThGRIPYPGMTN--PEVI 214
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
509-718 6.16e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 65.02  E-value: 6.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGgELLDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNIL 588
Cdd:PHA03212  136 ILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAENIF 214
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 589 YmdesGHPDSIKICDFGFA--------KQLRGENGLLLTPcytanfvAPEVLTQQGYDAACDIWSLGVLLYTMLAGY--- 657
Cdd:PHA03212  215 I----NHPGDVCLGDFGAAcfpvdinaNKYYGWAGTIATN-------APELLARDPYGPAVDIWSAGIVLFEMATCHdsl 283
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 658 ---------------------------TPFSNGPNDTPEEILLRIG--NGRFSLSGGIWDNISRGAKD---LLSHMLHMD 705
Cdd:PHA03212  284 fekdgldgdcdsdrqikliirrsgthpNEFPIDAQANLDEIYIGLAkkSSRKPGSRPLWTNLYELPIDleyLICKMLAFD 363
                         250
                  ....*....|...
gi 1958807372 706 PHQRYTAEQVLKH 718
Cdd:PHA03212  364 AHHRPSAEALLDF 376
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
487-713 1.05e-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: 62.63  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 487 NMEFAVKIIDKNKRDPS---EEIEIlMRYGQHPNIISLKEVFDDgKYVYLVTDLMKGGELLD-------RILKKKCFSEQ 556
Cdd:cd14203    19 TTKVAIKTLKPGTMSPEaflEEAQI-MKKLRHDKLVQLYAVVSE-EPIYIVTEFMSKGSLLDflkdgegKYLKLPQLVDM 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 557 EASnvlyvITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENgllLTPCYTANF----VAPEVL 632
Cdd:cd14203    97 AAQ-----IASGMAYIERMNYIHRDLRAANILVGDNL----VCKIADFGLARLIEDNE---YTARQGAKFpikwTAPEAA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 633 TQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNG-RFSLSGGIWDNIsrgaKDLLSHMLHMDPHQRY 710
Cdd:cd14203   165 LYGRFTIKSDVWSFGILLTELVTkGRVPY---PGMNNREVLEQVERGyRMPCPPGCPESL----HELMCQCWRKDPEERP 237

                  ...
gi 1958807372 711 TAE 713
Cdd:cd14203   238 TFE 240
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
114-310 1.09e-10

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


Pssm-ID: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 63.19  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 114 LKVLGQGSFGKVFLVrkKTGPDAGQL---YAMKVLRKASLKVRDRV---RTKMERDILVEVNHPFIVKLHyAFQ--TEGK 185
Cdd:cd14001     4 MKKLGYGTGVNVYLM--KRSPRGGSSrspWAVKKINSKCDKGQRSLyqeRLKEEAKILKSLNHPNIVGFR-AFTksEDGS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFlrGGDVFTRLSKEVLFTEEDvKFYLA-------ELALALDHLHR-LGIVYRDLKPENILLD---EIghIKLTD 254
Cdd:cd14001    81 LCLAMEY--GGKSLNDLIEERYEAGLG-PFPAAtilkvalSIARALEYLHNeKKILHGDIKSGNVLIKgdfES--VKLCD 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 255 FGLS---KE--SVDQEKKAYsFCGTVEYMAPEVVNRRGH-SQSADWWSYGVLMFEMLTGTLP 310
Cdd:cd14001   156 FGVSlplTEnlEVDSDPKAQ-YVGTEPWKAKEALEEGGViTDKADIFAYGLVLWEMMTLSVP 216
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
498-660 1.25e-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: 63.48  E-value: 1.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 498 NKRDPSEEIEILMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKC----------------FSEQEASNV 561
Cdd:cd05088    50 DHRDFAGELEVLCKLGHHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKSRVletdpafaianstastLSSQQLLHF 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 562 LYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAK----QLRGENGLLltpcyTANFVAPEVLTQQGY 637
Cdd:cd05088   130 AADVARGMDYLSQKQFIHRDLAARNILV----GENYVAKIADFGLSRgqevYVKKTMGRL-----PVRWMAIESLNYSVY 200
                         170       180
                  ....*....|....*....|....
gi 1958807372 638 DAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05088   201 TTNSDVWSYGVLLWEIVSlGGTPY 224
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
112-334 1.62e-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: 63.08  E-value: 1.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 112 DLLKVLGQGSFGK--VFLVRKKtgpDAGQLYAMKvlrKASLKVRDRVRTK-MERDILV--EVNHPFIVKLHYAFQTEGKL 186
Cdd:cd08216     1 ELLYEIGKCFKGGgvVHLAKHK---PTNTLVAVK---KINLESDSKEDLKfLQQEILTsrQLQHPNILPYVTSFVVDNDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 187 YLILDFLRGGdvftrlSKEVL--------FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLS 258
Cdd:cd08216    75 YVVTPLMAYG------SCRDLlkthfpegLPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQ-EKKAYSFCGTVE------YMAPEVV--NRRGHSQSADWWSYGVLMFEMLTGTLPFqgKDRNETMNMILKAKLG 329
Cdd:cd08216   149 YSMVKHgKRQRVVHDFPKSseknlpWLSPEVLqqNLLGYNEKSDIYSVGITACELANGVVPF--SDMPATQMLLEKVRGT 226

                  ....*
gi 1958807372 330 MPQFL 334
Cdd:cd08216   227 TPQLL 231
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
117-311 1.66e-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: 62.33  E-value: 1.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFlvrKKTGPDAGQLYAMKVLRKASLKVRDRVRTKMERDILVEVNHPFIVKLHYAFQTEGK----LYLILDF 192
Cdd:cd14033     9 IGRGSFKTVY---RGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRghkcIILVTEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 193 LRGGDVFTRLSKevlFTEEDVKFYLAELALALDHLHRLG-----IVYRDLKPENILLD-EIGHIKLTDFGLSkeSVDQEK 266
Cdd:cd14033    86 MTSGTLKTYLKR---FREMKLKLLQRWSRQILKGLHFLHsrcppILHRDLKCDNIFITgPTGSVKIGDLGLA--TLKRAS 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 267 KAYSFCGTVEYMAPEVVNRRgHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd14033   161 FAKSVIGTPEFMAPEMYEEK-YDEAVDVYAFGMCILEMATSEYPY 204
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
509-650 1.76e-10

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: 62.53  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGeLLDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSN 586
Cdd:cd14154    43 VMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGG-TLKDVLKDMArpLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHN 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 587 ILYMDESghpdSIKICDFGFAKQLRGENGLLLTPC----------------YTA----NFVAPEVLTQQGYDAACDIWSL 646
Cdd:cd14154   122 CLVREDK----TVVVADFGLARLIVEERLPSGNMSpsetlrhlkspdrkkrYTVvgnpYWMAPEMLNGRSYDEKVDIFSF 197

                  ....
gi 1958807372 647 GVLL 650
Cdd:cd14154   198 GIVL 201
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
117-317 1.94e-10

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: 62.78  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDAGQlYAMKVLRKASLKVRdrvrTKMERDILVEVNHPFIVKLHYAF--QTEGKLYLILDFLR 194
Cdd:cd07867    10 VGRGTYGHVYKAKRKDGKDEKE-YALKQIEGTGISMS----ACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GgDV-----FTRLSKE----VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFGLS--- 258
Cdd:cd07867    85 H-DLwhiikFHRASKAnkkpMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlf 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 259 ----KESVDQEKKAYSFCgtveYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd07867   164 nsplKPLADLDPVVVTFW----YRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED 223
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
464-615 1.94e-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: 62.28  E-value: 1.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIE--ILMRYGQHPNIISLKEVFDDGKYVYLVTDLMkGG 541
Cdd:cd14017     2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKMEvaVLKKLQGKPHFCRLIGCGRTERYNYIVMTLL-GP 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 542 EL--LDRILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESGHPDSIKICDFGFAKQLRGENG 615
Cdd:cd14017    81 NLaeLRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIGRGPSDERTVYILDFGLARQYTNKDG 156
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
514-660 2.74e-10

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: 61.43  E-value: 2.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 514 QHPNIISLKEV-FDDGkyVYLVTDLMKGGELLDRILKKKCFSEQEASNVLYV--ITKTVEYLHSQGVVHRDLKPSNILyM 590
Cdd:cd05083    57 QHKNLVRLLGViLHNG--LYIVMELMSKGNLVNFLRSRGRALVPVIQLLQFSldVAEGMEYLESKKLVHRDLAARNIL-V 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 591 DESGhpdSIKICDFGFAK-QLRGENGLLLTPCYTAnfvaPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05083   134 SEDG---VAKISDFGLAKvGSMGVDNSRLPVKWTA----PEALKNKKFSSKSDVWSYGVLLWEVFSyGRAPY 198
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
111-331 3.22e-10

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


Pssm-ID: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 62.35  E-value: 3.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRdrvRTKMERDILVEVN------HPFiVKLHYAFQTEG 184
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKR---GTNEIVAVKILKNHPSYAR---QGQIEVGILARLSnenadeFNF-VRAYECFQHRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 185 KLYLIL--------DFLRGgDVFTRLSKEVlfteedVKFYLAELALALDHLHRLGIVYRDLKPENILL-DEIGH---IKL 252
Cdd:cd14229    75 HTCLVFemleqnlyDFLKQ-NKFSPLPLKV------IRPILQQVATALKKLKSLGLIHADLKPENIMLvDPVRQpyrVKV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 253 TDFGlSKESVDQekkaySFCGTV----EYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKl 328
Cdd:cd14229   148 IDFG-SASHVSK-----TVCSTYlqsrYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQ- 220

                  ...
gi 1958807372 329 GMP 331
Cdd:cd14229   221 GLP 223
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
531-672 4.77e-10

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 61.58  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGELLDRILK-KKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQ 609
Cdd:cd05108    83 VQLITQLMPFGCLLDYVREhKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKT----PQHVKITDFGLAKL 158
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 610 LRGENgllltPCYTAN-------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNDTPEEIL 672
Cdd:cd05108   159 LGAEE-----KEYHAEggkvpikWMALESILHRIYTHQSDVWSYGVTVWELMTfGSKPYDGIPASEISSIL 224
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
563-660 5.21e-10

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 61.94  E-value: 5.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 563 YVITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL--------RGENGLLLtpcytaNFVAPEVLTQ 634
Cdd:cd14207   187 FQVARGMEFLSSRKCIHRDLAARNILLSEN----NVVKICDFGLARDIyknpdyvrKGDARLPL------KWMAPESIFD 256
                          90       100
                  ....*....|....*....|....*..
gi 1958807372 635 QGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd14207   257 KIYSTKSDVWSYGVLLWEIFSlGASPY 283
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
484-660 5.43e-10

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. 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: 61.35  E-value: 5.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 484 SASNMEFAVKIIdKNKRDPSE------EIEILMRYGQHPNIISL-KEVFDDGKYVYLVTDLMKGGELLDRI-LKKKCFS- 554
Cdd:cd05054    34 SATCRTVAVKML-KEGATASEhkalmtELKILIHIGHHLNVVNLlGACTKPGGPLMVIVEFCKFGNLSNYLrSKREEFVp 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 555 ----------EQEASNVLY--------------VITKTVEYLHSQGVVHRDLKPSNILYMDEsghpDSIKICDFGFAKQL 610
Cdd:cd05054   113 yrdkgardveEEEDDDELYkepltledlicysfQVARGMEFLASRKCIHRDLAARNILLSEN----NVVKICDFGLARDI 188
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 611 RGEngllltPCYTAN--------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05054   189 YKD------PDYVRKgdarlplkWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPY 241
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
491-679 5.60e-10

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: 60.95  E-value: 5.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIdkNKRDPSEEIE------ILMRYGQHPNIISLKEV-FDDGKYVYLVTDLMKGGELLDRILkkkcfSEQEASNVLY 563
Cdd:cd05058    27 AVKSL--NRITDIEEVEqflkegIIMKDFSHPNVLSLLGIcLPSEGSPLVVLPYMKHGDLRNFIR-----SETHNPTVKD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 564 VI------TKTVEYLHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQL--------RGENGLLLTpcytANFVAP 629
Cdd:cd05058   100 LIgfglqvAKGMEYLASKKFVHRDLAARNCM-LDESFT---VKVADFGLARDIydkeyysvHNHTGAKLP----VKWMAL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1958807372 630 EVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNGR 679
Cdd:cd05058   172 ESLQTQKFTTKSDVWSFGVLLWELMTrGAPPY---PDVDSFDITVYLLQGR 219
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
505-675 6.08e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 62.40  E-value: 6.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 505 EIEIL-MRYGQHPNIISLKEVFDDGKYVYLVT-----DL---MKGGEL--LDRILKKkcfseqEASNVLYVITKTVEYLH 573
Cdd:PHA03210  211 ENEILaLGRLNHENILKIEEILRSEANTYMITqkydfDLysfMYDEAFdwKDRPLLK------QTRAIMKQLLCAVEYIH 284
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 574 SQGVVHRDLKPSNIlYMDESGhpdSIKICDFGFAKQLRGEN-----GLLLTpcYTANfvAPEVLTQQGYDAACDIWSLGV 648
Cdd:PHA03210  285 DKKLIHRDIKLENI-FLNCDG---KIVLGDFGTAMPFEKEReafdyGWVGT--VATN--SPEILAGDGYCEITDIWSCGL 356
                         170       180
                  ....*....|....*....|....*...
gi 1958807372 649 LLYTMLA-GYTPFsNGPNDTPEEILLRI 675
Cdd:PHA03210  357 ILLDMLShDFCPI-GDGGGKPGKQLLKI 383
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
111-349 6.76e-10

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: 61.64  E-value: 6.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 111 FDLLKVLGQGSFGKVFLVRKKtgpDAGQLYAMKVLRKASLKVRdrvRTKMERDILVEVNHPF-----IVKLHYAFQTEGK 185
Cdd:cd14227    17 YEVLEFLGRGTFGQVVKCWKR---GTNEIVAIKILKNHPSYAR---QGQIEVSILARLSTESaddynFVRAYECFQHKNH 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDV-FTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIG----HIKLTDFGlske 260
Cdd:cd14227    91 TCLVFEMLEQNLYdFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSrqpyRVKVIDFG---- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 261 SVDQEKKAY--SFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNETMNMILKAKlGMPQFLSAEA 338
Cdd:cd14227   167 SASHVSKAVcsTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQ-GLPAEYLLSA 245
                         250
                  ....*....|.
gi 1958807372 339 QSLLRMLFKRN 349
Cdd:cd14227   246 GTKTTRFFNRD 256
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
509-662 8.44e-10

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: 60.41  E-value: 8.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKK------CFSEQEAS--------NVLYV---ITKTVEY 571
Cdd:cd05090    60 LMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLIMRSphsdvgCSSDEDGTvkssldhgDFLHIaiqIAAGMEY 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 572 LHSQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLLTP--CYTANFVAPEVLTQQGYDAACDIWSLGVL 649
Cdd:cd05090   140 LSSHFFVHKDLAARNIL-VGEQLH---VKISDLGLSREIYSSDYYRVQNksLLPIRWMPPEAIMYGKFSSDSDIWSFGVV 215
                         170
                  ....*....|....*..
gi 1958807372 650 LYTM----LAGYTPFSN 662
Cdd:cd05090   216 LWEIfsfgLQPYYGFSN 232
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
462-732 9.33e-10

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: 60.47  E-value: 9.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYSVCKRCIHSAsNMEFAVKIIDKNKRDPS---EEIEIlMRYGQHPNIISLKEVFDDgKYVYLVTDLM 538
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWMGTWNG-NTKVAIKTLKPGTMSPEsflEEAQI-MKKLKHDKLVQLYAVVSE-EPIYIVTEYM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLD-------RILKKKCFSEQEASnvlyvITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLR 611
Cdd:cd05070    86 SKGSLLDflkdgegRALKLPNLVDMAAQ-----VAAGMAYIERMNYIHRDLRSANILV----GNGLICKIADFGLARLIE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 612 -GENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNG-RFSLSggiwD 688
Cdd:cd05070   157 dNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTkGRVPY---PGMNNREVLEQVERGyRMPCP----Q 229
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 689 NISRGAKDLLSHMLHMDPHQRYTAE--QVLKHPWITQREqlPRHQP 732
Cdd:cd05070   230 DCPISLHELMIHCWKKDPEERPTFEylQGFLEDYFTATE--PQYQP 273
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
491-665 1.26e-09

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: 60.03  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKII-DKNKRDPSEEI--EILMRYG-QHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRIL-------------KKKCF 553
Cdd:cd05091    40 AIKTLkDKAEGPLREEFrhEAMLRSRlQHPNIVCLLGVVTKEQPMSMIFSYCSHGDLHEFLVmrsphsdvgstddDKTVK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 554 SEQEASNVLYVITKT---VEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGEN--GLLLTPCYTANFVA 628
Cdd:cd05091   120 STLEPADFLHIVTQIaagMEYLSSHHVVHKDLATRNVLVFDKL----NVKISDLGLFREVYAADyyKLMGNSLLPIRWMS 195
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958807372 629 PEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPN 665
Cdd:cd05091   196 PEAIMYGKFSIDSDIWSYGVVLWEVFSyGLQPYCGYSN 233
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
470-650 1.63e-09

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 59.57  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIHSASN----MEFAVKIIDKNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLD 545
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGkvmvMKELIRCDEETQKTFLTEVKV-MRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILY-MDesghpDSIKICDFGFA----------------- 607
Cdd:cd14222    80 FLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIkLD-----KTVVVADFGLSrliveekkkpppdkptt 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1958807372 608 -KQLRGENGLLLTPCYTAN--FVAPEVLTQQGYDAACDIWSLGVLL 650
Cdd:cd14222   155 kKRTLRKNDRKKRYTVVGNpyWMAPEMLNGKSYDEKVDIFSFGIVL 200
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
117-317 1.67e-09

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: 60.07  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDAGQlYAMKVLRKASLKVRdrvrTKMERDILVEVNHPFIVKLHYAF--QTEGKLYLILDFLR 194
Cdd:cd07868    25 VGRGTYGHVYKAKRKDGKDDKD-YALKQIEGTGISMS----ACREIALLRELKHPNVISLQKVFlsHADRKVWLLFDYAE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 195 GgDV-----FTRLSKE----VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL----DEIGHIKLTDFGLS--- 258
Cdd:cd07868   100 H-DLwhiikFHRASKAnkkpVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlf 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958807372 259 ----KESVDQEKKAYSFCgtveYMAPE-VVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRN 317
Cdd:cd07868   179 nsplKPLADLDPVVVTFW----YRAPElLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED 238
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
509-678 1.79e-09

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 59.27  E-value: 1.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDgKYVYLVTDLMKGGELLDrILKKKCFSEQEASNVLYV---ITKTVEYLHSQGVVHRDLKPS 585
Cdd:cd05073    59 VMKTLQHDKLVKLHAVVTK-EPIYIITEFMAKGSLLD-FLKSDEGSKQPLPKLIDFsaqIAEGMAFIEQRNYIHRDLRAA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 586 NILYMDESghpdSIKICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-G 656
Cdd:cd05073   137 NILVSASL----VCKIADFGLARVIEDNE-------YTAregakfpiKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyG 205
                         170       180
                  ....*....|....*....|..
gi 1958807372 657 YTPFsngPNDTPEEILLRIGNG 678
Cdd:cd05073   206 RIPY---PGMSNPEVIRALERG 224
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
488-650 2.28e-09

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: 59.20  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 488 MEFAVKIIDKNKRDPSEEIEIlMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRI--LKKKCFSEQEASnVLYVI 565
Cdd:cd14221    23 MKELIRFDEETQRTFLKEVKV-MRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIksMDSHYPWSQRVS-FAKDI 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 566 TKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLLLTPC----------YTA----NFVAPEV 631
Cdd:cd14221   101 ASGMAYLHSMNIIHRDLNSHNCLVRENK----SVVVADFGLARLMVDEKTQPEGLRslkkpdrkkrYTVvgnpYWMAPEM 176
                         170
                  ....*....|....*....
gi 1958807372 632 LTQQGYDAACDIWSLGVLL 650
Cdd:cd14221   177 INGRSYDEKVDVFSFGIVL 195
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
115-354 2.78e-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: 2.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRK-KTGPDagqlYAMKVLRKASLKVRdrvrtkmeRDILVEVN-------HPFIVKLHYA------- 179
Cdd:cd14036     6 RVIAEGGFAFVYEAQDvGTGKE----YALKRLLSNEEEKN--------KAIIQEINfmkklsgHPNIVQFCSAasigkee 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 180 FQTEGKLYLIL-DFLRGG--DVFTRLSKEVLFTEEDVKFYLAELALALDHLHR--LGIVYRDLKPENILLDEIGHIKLTD 254
Cdd:cd14036    74 SDQGQAEYLLLtELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKqsPPIIHRDLKIENLLIGNQGQIKLCD 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 255 FGLSKESVDQEKKAYSFC--GTVE----------YMAPEVVNRRGH---SQSADWWSYGVLMFEMLTGTLPFQ--GKDRn 317
Cdd:cd14036   154 FGSATTEAHYPDYSWSAQkrSLVEdeitrnttpmYRTPEMIDLYSNypiGEKQDIWALGCILYLLCFRKHPFEdgAKLR- 232
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1958807372 318 etmnmILKAKLGMPQFLSAEA--QSLLRMLFKRNPANRL 354
Cdd:cd14036   233 -----IINAKYTIPPNDTQYTvfHDLIRSTLKVNPEERL 266
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
561-659 3.45e-09

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


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 58.44  E-value: 3.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 561 VLYVITKTVEYLHSQGVVHRDLKPSNILY--MDESGHPDsIKICDFGFAKQL--RGENGLLLTPCYTAnfvaPEVLTQQG 636
Cdd:cd14067   119 IAYQIAAGLAYLHKKNIIFCDLKSDNILVwsLDVQEHIN-IKLSDYGISRQSfhEGALGVEGTPGYQA----PEIRPRIV 193
                          90       100
                  ....*....|....*....|...
gi 1958807372 637 YDAACDIWSLGVLLYTMLAGYTP 659
Cdd:cd14067   194 YDEKVDMFSYGMVLYELLSGQRP 216
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
109-353 4.74e-09

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: 58.11  E-value: 4.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRK---ASLKVRDRVRTKMERDILVEvnHPFIVKLHYAFQTEGK 185
Cdd:cd14138     5 TEFHELEKIGSGEFGSVFKCVKRLD---GCIYAIKRSKKplaGSVDEQNALREVYAHAVLGQ--HSHVVRYYSAWAEDDH 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 186 LYLILDFLRGGDVFTRLSKEV----LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILL---------------DE 246
Cdd:cd14138    80 MLIQNEYCNGGSLADAISENYrimsYFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFIsrtsipnaaseegdeDE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 247 IGH----IKLTDFG-LSKESVDQEKKaysfcGTVEYMAPEVVNRR-GHSQSADWWSYGVLMFEMLTGT-LPFQGKDRNET 319
Cdd:cd14138   160 WASnkviFKIGDLGhVTRVSSPQVEE-----GDSRFLANEVLQENyTHLPKADIFALALTVVCAAGAEpLPTNGDQWHEI 234
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1958807372 320 MNMILKAklgMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd14138   235 RQGKLPR---IPQVLSQEFLDLLKVMIHPDPERR 265
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
460-679 6.05e-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: 57.78  E-value: 6.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 460 FSEAYElkedigiGSYsvckRCIHSASN-MEFAVKIIDKnkrDPSEEIE-------ILMRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd05036    19 FGEVYE-------GTV----SGMPGDPSpLQVAVKTLPE---LCSEQDEmdflmeaLIMSKFNHPNIVRCIGVCFQRLPR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKKKCFSEQEAS----NVLYV---ITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDSIKICDF 604
Cdd:cd05036    85 FILLELMAGGDLKSFLRENRPRPEQPSSltmlDLLQLaqdVAKGCRYLEENHFIHRDIAARNCL-LTCKGPGRVAKIGDF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 605 GFAKQL-------RGENGLLltpcyTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEIL-LRI 675
Cdd:cd05036   164 GMARDIyradyyrKGGKAML-----PVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlGYMPY---PGKSNQEVMeFVT 235

                  ....
gi 1958807372 676 GNGR 679
Cdd:cd05036   236 SGGR 239
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
462-717 7.88e-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: 57.67  E-value: 7.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 462 EAYELKEDIGIGSYS-----VCKRCIHSASNMEFAVKIIDKNKrDPSEEIEIL-----MRYGQHPNIISLKEVFDDGKYV 531
Cdd:cd05061     6 EKITLLRELGQGSFGmvyegNARDIIKGEAETRVAVKTVNESA-SLRERIEFLneasvMKGFTCHHVVRLLGVVSKGQPT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMKGGELLDRILKKKCFSE----------QEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKI 601
Cdd:cd05061    85 LVVMELMAHGDLKSYLRSLRPEAEnnpgrppptlQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDF----TVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 602 CDFGFAKQL-------RGENGLLltpcyTANFVAPEVLTQQGYDAACDIWSLGVLLY--TMLAG--YTPFSNgpndtpEE 670
Cdd:cd05061   161 GDFGMTRDIyetdyyrKGGKGLL-----PVRWMAPESLKDGVFTTSSDMWSFGVVLWeiTSLAEqpYQGLSN------EQ 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 671 ILlrigngRFSLSGGIWD---NISRGAKDLLSHMLHMDPHQRYTAEQVLK 717
Cdd:cd05061   230 VL------KFVMDGGYLDqpdNCPERVTDLMRMCWQFNPKMRPTFLEIVN 273
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
491-732 8.14e-09

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: 57.39  E-value: 8.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKRDPS---EEIEIlMRYGQHPNIISLKEVFDDgKYVYLVTDLMKGGELLDrILKK---KCFSEQEASNVLYV 564
Cdd:cd05069    40 AIKTLKPGTMMPEaflQEAQI-MKKLRHDKLVPLYAVVSE-EPIYIVTEFMGKGSLLD-FLKEgdgKYLKLPQLVDMAAQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLTQQG 636
Cdd:cd05069   117 IADGMAYIERMNYIHRDLRAANILVGDNL----VCKIADFGLARLIEDNE-------YTArqgakfpiKWTAPEAALYGR 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 637 YDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEILLRIGNG-RFSLSGGIWDNIsrgaKDLLSHMLHMDPHQRYTAE- 713
Cdd:cd05069   186 FTIKSDVWSFGILLTELVTkGRVPY---PGMVNREVLEQVERGyRMPCPQGCPESL----HELMKLCWKKDPDERPTFEy 258
                         250       260
                  ....*....|....*....|
gi 1958807372 714 -QVLKHPWITQREqlPRHQP 732
Cdd:cd05069   259 iQSFLEDYFTATE--PQYQP 276
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
170-344 9.22e-09

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


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 57.96  E-value: 9.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 170 HPFIVKLHYAFQTEGKLYLILDFLRGGDV-------FTRLSKEVLfteedVKFYLAELALALDHLHRLGIVYRDLKPENI 242
Cdd:cd08226    58 HPNIMTHWTVFTEGSWLWVISPFMAYGSArgllktyFPEGMNEAL-----IGNILYGAIKALNYLHQNGCIHRSVKASHI 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 243 LLDEIGHIKLTdfGLSK-----ESVDQEKKAYSF----CGTVEYMAPEVVNR--RGHSQSADWWSYGVLMFEMLTGTLPF 311
Cdd:cd08226   133 LISGDGLVSLS--GLSHlysmvTNGQRSKVVYDFpqfsTSVLPWLSPELLRQdlHGYNVKSDIYSVGITACELARGQVPF 210
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1958807372 312 QGKDRNETMNMILKAKLGMPQFLSAEAQSLLRM 344
Cdd:cd08226   211 QDMRRTQMLLQKLKGPPYSPLDIFPFPELESRM 243
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
468-715 1.06e-08

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: 57.12  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSVCKRCIHSASNMEFAVKIIDKNKRDPSEEIEIL-----MRYGQHPNIISLKEVFDDGkyVYLVTDLMKGGE 542
Cdd:cd14025     2 EKVGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLeeakkMEMAKFRHILPVYGICSEP--VGLVMEYMETGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LlDRILKKKCFSEQEASNVLYVITKTVEYLHSQG--VVHRDLKPSNILyMDESGHpdsIKICDFGFAKQLRGENGLLL-- 618
Cdd:cd14025    80 L-EKLLASEPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANIL-LDAHYH---VKISDFGLAKWNGLSHSHDLsr 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 619 -TPCYTANFVAPEVLTQQG--YDAACDIWSLGVLLYTMLAGYTPFSNGPNDTpeEILLRIGNG-RFSLSggiwdNISRGA 694
Cdd:cd14025   155 dGLRGTIAYLPPERFKEKNrcPDTKHDVYSFAIVIWGILTQKKPFAGENNIL--HIMVKVVKGhRPSLS-----PIPRQR 227
                         250       260
                  ....*....|....*....|....*...
gi 1958807372 695 KDLLSHMLHM-------DPHQRYTAEQV 715
Cdd:cd14025   228 PSECQQMICLmkrcwdqDPRKRPTFQDI 255
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
466-729 1.37e-08

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: 56.96  E-value: 1.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-SVCKRCIHSasnmEFAVKIIDKNKRDPSE------EIEILmRYGQHPNIISLKEVFDDGKyVYLVTDLM 538
Cdd:cd14149    16 LSTRIGSGSFgTVYKGKWHG----DVAVKILKVVDPTPEQfqafrnEVAVL-RKTRHVNILLFMGYMTKDN-LAIVTQWC 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 539 KGGELLDRI-LKKKCFSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFA--KQLRGENG 615
Cdd:cd14149    90 EGSSLYKHLhVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGL----TVKIGDFGLAtvKSRWSGSQ 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 616 LLLTPCYTANFVAPEVLTQQG---YDAACDIWSLGVLLYTMLAGYTPFSNGPNDtpEEILLRIGNGRFSLS-GGIWDNIS 691
Cdd:cd14149   166 QVEQPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMTGELPYSHINNR--DQIIFMVGRGYASPDlSKLYKNCP 243
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQVLKHPWITQrEQLPR 729
Cdd:cd14149   244 KAMKRLVADCIKKVKEERPLFPQILSSIELLQ-HSLPK 280
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
565-660 1.43e-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: 56.69  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQL---------RGENGLLltpcytaNFVAPEVLTQQ 635
Cdd:cd05043   125 IACGMSYLHRRGVIHKDIAARNCVIDDEL----QVKITDNALSRDLfpmdyhclgDNENRPI-------KWMSLESLVNK 193
                          90       100
                  ....*....|....*....|....*.
gi 1958807372 636 GYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05043   194 EYSSASDVWSFGVLLWELMTlGQTPY 219
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
491-676 1.44e-08

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: 56.89  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKrDPSEEIEILMRYG-----QHPNIISLKEVFDDGKYVYLVTDLMKGGEL---LDRILKKKC---------- 552
Cdd:cd05045    34 AVKMLKENA-SSSELRDLLSEFNllkqvNHPHVIKLYGACSQDGPLLLIVEYAKYGSLrsfLRESRKVGPsylgsdgnrn 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 553 -----FSEQEASNVLYVIT------KTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLL---- 617
Cdd:cd05045   113 ssyldNPDERALTMGDLISfawqisRGMQYLAEMKLVHRDLAARNVLVAEGR----KMKISDFGLSRDVYEEDSYVkrsk 188
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 618 -LTPcytANFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFsngPNDTPEEI--LLRIG 676
Cdd:cd05045   189 gRIP---VKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPY---PGIAPERLfnLLKTG 245
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
464-647 1.45e-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: 57.26  E-value: 1.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 464 YELKEDIGIGSYSVCKRCIHSASNMEFAVKIIdKNK----RDPSEEIEILM--------RYGQHpnIISLKEVFDDGKYV 531
Cdd:cd14212     1 YLVLDLLGQGTFGQVVKCQDLKTNKLVAVKVL-KNKpayfRQAMLEIAILTllntkydpEDKHH--IVRLLDHFMHHGHL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 532 YLVTDLMkGGELLDRILKKKC--FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGHPDsIKICDFGFAKQ 609
Cdd:cd14212    78 CIVFELL-GVNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENIL-LVNLDSPE-IKLIDFGSACF 154
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958807372 610 lrgENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLG 647
Cdd:cd14212   155 ---ENYTLYTYIQSRFYRSPEVLLGLPYSTAIDMWSLG 189
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
217-310 1.71e-08

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 56.34  E-value: 1.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 217 LAELALALD------HLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVdqeKKAYSFCGTVEYMAPEVVNrrGH-S 289
Cdd:cd13975   102 EERLQIALDvvegirFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEA---MMSGSIVGTPIHMAPELFS--GKyD 176
                          90       100
                  ....*....|....*....|...
gi 1958807372 290 QSADWWSYGVLMFEMLTG--TLP 310
Cdd:cd13975   177 NSVDVYAFGILFWYLCAGhvKLP 199
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
491-672 1.78e-08

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: 56.61  E-value: 1.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIDKNKrDPSEEIE-----ILMRYGQHPNIISLKEVFDDgKYVYLVTDLMKGGELLDRILK-KKCFSEQEASNVLYV 564
Cdd:cd05110    40 AIKILNETT-GPKANVEfmdeaLIMASMDHPHLVRLLGVCLS-PTIQLVTQLMPHGCLLDYVHEhKDNIGSQLLLNWCVQ 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQLRGENGLlltpcYTAN-------FVAPEVLTQQGY 637
Cdd:cd05110   118 IAKGMMYLEERRLVHRDLAARNVLVKS----PNHVKITDFGLARLLEGDEKE-----YNADggkmpikWMALECIHYRKF 188
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1958807372 638 DAACDIWSLGVLLYTMLA-GYTPFSNGPNDTPEEIL 672
Cdd:cd05110   189 THQSDVWSYGVTIWELMTfGGKPYDGIPTREIPDLL 224
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
473-728 2.14e-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: 56.46  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 473 GSYSVCKRCIHSASNMEFAVK-------IIDKNKRDPSEEIEILMRyGQHPNIISLKEVFDDGKYVYLVTDLMKGGELlD 545
Cdd:cd14026     8 GAFGTVSRARHADWRVTVAIKclkldspVGDSERNCLLKEAEILHK-ARFSYILPILGICNEPEFLGIVTEYMTNGSL-N 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 546 RILKKKCFSEQEA----SNVLYVITKTVEYLH--SQGVVHRDLKPSNILyMDESGHpdsIKICDFGFAK-------QLRG 612
Cdd:cd14026    86 ELLHEKDIYPDVAwplrLRILYEIALGVNYLHnmSPPLLHHDLKTQNIL-LDGEFH---VKIADFGLSKwrqlsisQSRS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 613 ENGLLLTPcyTANFVAPEVLT---QQGYDAACDIWSLGVLLYTMLAGYTPFSNGPNdtPEEILLrigngrfslsggiwdN 689
Cdd:cd14026   162 SKSAPEGG--TIIYMPPEEYEpsqKRRASVKHDIYSYAIIMWEVLSRKIPFEEVTN--PLQIMY---------------S 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 690 ISRGAK-DLLSHMLHMDPHQRYTAEQVLKHPWITQREQLP 728
Cdd:cd14026   223 VSQGHRpDTGEDSLPVDIPHRATLINLIESGWAQNPDERP 262
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
531-669 2.69e-08

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: 55.80  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 531 VYLVTDLMKGGELLDRILKKKC-FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesghPDSIKICDFGFAKQ 609
Cdd:cd05109    83 VQLVTQLMPYGCLLDYVRENKDrIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKS----PNHVKITDFGLARL 158
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 610 LRGENGLlltpcYTAN-------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGP-NDTPE 669
Cdd:cd05109   159 LDIDETE-----YHADggkvpikWMALESILHRRFTHQSDVWSYGVTVWELMTfGAKPYDGIPaREIPD 222
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
109-323 2.74e-08

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: 56.40  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 109 AQFDLLKVLGQGSFGKVFLVRKKTGpdAGQLYAMKVLRKAslkvrDRVRTKMERDILV-------EVNHPF-IVKLHYAF 180
Cdd:cd14213    12 ARYEIVDTLGEGAFGKVVECIDHKM--GGMHVAVKIVKNV-----DRYREAARSEIQVlehlnttDPNSTFrCVQMLEWF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 181 QTEGKLYLILDFLrGGDVFTRLSKEVL--FTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGH--------- 249
Cdd:cd14213    85 DHHGHVCIVFELL-GLSTYDFIKENSFlpFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILFVQSDYvvkynpkmk 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 250 ----------IKLTDFGlsKESVDQEKKAySFCGTVEYMAPEVVNRRGHSQSADWWSYGVLMFEMLTGTLPFQGKDRNET 319
Cdd:cd14213   164 rdertlknpdIKVVDFG--SATYDDEHHS-TLVSTRHYRAPEVILALGWSQPCDVWSIGCILIEYYLGFTVFQTHDSKEH 240

                  ....
gi 1958807372 320 MNMI 323
Cdd:cd14213   241 LAMM 244
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
466-651 4.61e-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: 55.16  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-----SVCKRCIHSASNMEFAVKII-----DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVT 535
Cdd:cd05049     9 LKRELGEGAFgkvflGECYNLEPEQDKMLVAVKTLkdassPDARKDFEREAELLTNL-QHENIVKFYGVCTEGDPLLMVF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 536 DLMKGGELLD---------RILKKKCFSEQE--ASNVLYV---ITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKI 601
Cdd:cd05049    88 EYMEHGDLNKflrshgpdaAFLASEDSAPGEltLSQLLHIavqIASGMVYLASQHFVHRDLATRNCLV----GTNLVVKI 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1958807372 602 CDFGFAKQLRGEN-----GLLLTPcytANFVAPEVLTQQGYDAACDIWSLGVLLY 651
Cdd:cd05049   164 GDFGMSRDIYSTDyyrvgGHTMLP---IRWMPPESILYRKFTTESDVWSFGVVLW 215
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
117-307 5.38e-08

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 54.94  E-value: 5.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 117 LGQGSFGKVFLVRKKTGPDA--GQLYAMKVLRKASLKVRDRVRTKmERDILVEVN-HPFIVKL------HYAFQTEGKLy 187
Cdd:cd14020     8 LGQGSSASVYRVSSGRGADQptSALKEFQLDHQGSQESGDYGFAK-ERAALEQLQgHRNIVTLygvftnHYSANVPSRC- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 188 LILDFLrggDVftRLSKEVLFTEED------VKFYLAELALALDHLHRLGIVYRDLKPENILL---DEIghIKLTDFGLS 258
Cdd:cd14020    86 LLLELL---DV--SVSELLLRSSNQgcsmwmIQHCARDVLEALAFLHHEGYVHADLKPRNILWsaeDEC--FKLIDFGLS 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKaysFCGTVEYMAPE-----------VVNRRGHSQSADWWSYGVLMFEMLTG 307
Cdd:cd14020   159 FKEGNQDVK---YIQTDGYRAPEaelqnclaqagLQSETECTSAVDLWSLGIVLLEMFSG 215
STKc_Bub1_BubR1 cd13981
Catalytic domain of the Serine/Threonine kinases, Spindle assembly checkpoint proteins Bub1 ...
523-656 7.28e-08

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


Pssm-ID: 270883 [Multi-domain]  Cd Length: 298  Bit Score: 54.67  E-value: 7.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 523 EVFDDGKYvyLVTDLMKGGELLDRILKKKCFSEQ--EASNVLYVIT---KTVEYLHSQGVVHRDLKPSNILYMDE----- 592
Cdd:cd13981    70 HLFQDESI--LVMDYSSQGTLLDVVNKMKNKTGGgmDEPLAMFFTIellKVVEALHEVGIIHGDIKPDNFLLRLEicadw 147
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958807372 593 ----SGHPDS--IKICDFGFAKQLR--GENGLLLTPCYTANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAG 656
Cdd:cd13981   148 pgegENGWLSkgLKLIDFGRSIDMSlfPKNQSFKADWHTDSFDCIEMREGRPWTYQIDYFGIAATIHVMLFG 219
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
488-662 8.58e-08

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: 54.30  E-value: 8.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 488 MEFAVKIIDKN-----KRDPSEEIEiLMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELLDRILKKKCFSEQEAS--- 559
Cdd:cd05048    36 ISVAIKTLKENaspktQQDFRREAE-LMSDLQHPNIVCLLGVCTKEQPQCMLFEYMAHGDLHEFLVRHSPHSDVGVSsdd 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 560 -------------NVLYVITKTVEYLHSQGVVHRDLKPSNILYMDesGHpdSIKICDFGFAKQLrgengllltpcYTANF 626
Cdd:cd05048   115 dgtassldqsdflHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGD--GL--TVKISDFGLSRDI-----------YSSDY 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958807372 627 -------------VAPEVLTQQGYDAACDIWSLGVLLYTM----LAGYTPFSN 662
Cdd:cd05048   180 yrvqsksllpvrwMPPEAILYGKFTTESDVWSFGVVLWEIfsygLQPYYGYSN 232
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
469-660 8.59e-08

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: 54.18  E-value: 8.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 469 DIGIGSYSVCKRCIHS--ASNMEFAVKII----DKNKRDPSEEIEILMRYGQHPNIISLKEVFDdGKYVYLVTDLMKGGE 542
Cdd:cd05115    11 ELGSGNFGCVKKGVYKmrKKQIDVAIKVLkqgnEKAVRDEMMREAQIMHQLDNPYIVRMIGVCE-AEALMLVMEMASGGP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 543 LLDRILKKKcfSEQEASNV---LYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRGENGLllt 619
Cdd:cd05115    90 LNKFLSGKK--DEITVSNVvelMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQH----YAKISDFGLSKALGADDSY--- 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 620 pcYTA--------NFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPF 660
Cdd:cd05115   161 --YKArsagkwplKWYAPECINFRKFSSRSDVWSYGVTMWEAFSyGQKPY 208
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
468-653 9.50e-08

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: 54.37  E-value: 9.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 468 EDIGIGSYSvckrCIHSAS--NMEFAVKIID-KNKRDPSEEIEI----LMRygqHPNII----SLKEVFDDGKYVYLVTD 536
Cdd:cd13998     1 EVIGKGRFG----EVWKASlkNEPVAVKIFSsRDKQSWFREKEIyrtpMLK---HENILqfiaADERDTALRTELWLVTA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELLDrILKKKCFSEQEASNVLYVITKTVEYLHSQ---------GVVHRDLKPSNILYmdesgHPD-SIKICDFGF 606
Cdd:cd13998    74 FHPNGSL*D-YLSLHTIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILV-----KNDgTCCIADFGL 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 607 AkqLRGENGLLLTP------CYTANFVAPEVLTQ----QGYDA--ACDIWSLGVLLYTM 653
Cdd:cd13998   148 A--VRLSPSTGEEDnanngqVGTKRYMAPEVLEGainlRDFESfkRVDIYAMGLVLWEM 204
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
466-651 1.42e-07

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: 53.82  E-value: 1.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-----SVCKRCIHSASNMEFAVKII----DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05092     9 LKWELGEGAFgkvflAECHNLLPEQDKMLVAVKALkeatESARQDFQREAELLTVL-QHQHIVRFYGVCTEGEPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELlDRILKK-----KCFSEQEA--------SNVLYVITKTVE---YLHSQGVVHRDLKPSNILYmdesGHPDSIK 600
Cdd:cd05092    88 YMRHGDL-NRFLRShgpdaKILDGGEGqapgqltlGQMLQIASQIASgmvYLASLHFVHRDLATRNCLV----GQGLVVK 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958807372 601 ICDFGFAKQLRGEN-----GLLLTPCytaNFVAPEVLTQQGYDAACDIWSLGVLLY 651
Cdd:cd05092   163 IGDFGMSRDIYSTDyyrvgGRTMLPI---RWMPPESILYRKFTTESDIWSFGVVLW 215
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
491-654 1.74e-07

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: 53.43  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIdkNKRD-PS--EEIEI----LMRygqHPNIisLKEVFDDGK------YVYLVTDLMKGGELLDrILKKKCFSEQE 557
Cdd:cd14056    22 AVKIF--SSRDeDSwfRETEIyqtvMLR---HENI--LGFIAADIKstgswtQLWLITEYHEHGSLYD-YLQRNTLDTEE 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 558 ASNVLYVITKTVEYLHSQ--------GVVHRDLKPSNILYMDesghPDSIKICDFGFAkqLRGENGLLLTP------CYT 623
Cdd:cd14056    94 ALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKR----DGTCCIADLGLA--VRYDSDTNTIDippnprVGT 167
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1958807372 624 ANFVAPEVLTQQ-------GYDAAcDIWSLGVLLYTML 654
Cdd:cd14056   168 KRYMAPEVLDDSinpksfeSFKMA-DIYSFGLVLWEIA 204
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
466-671 4.37e-07

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 52.32  E-value: 4.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-----SVCKRCIHSASNMEFAVKII-DKN---KRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05094     9 LKRELGEGAFgkvflAECYNLSPTKDKMLVAVKTLkDPTlaaRKDFQREAELLTNL-QHDHIVKFYGVCGDGDPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGELlDRILK--------------KKCFSEQEASNVLYVITKTVE---YLHSQGVVHRDLKPSNILYmdesGHPDSI 599
Cdd:cd05094    88 YMKHGDL-NKFLRahgpdamilvdgqpRQAKGELGLSQMLHIATQIASgmvYLASQHFVHRDLATRNCLV----GANLLV 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958807372 600 KICDFGFAKQLRGEN-----GLLLTPCytaNFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTP-FSNGPNDTPEEI 671
Cdd:cd05094   163 KIGDFGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQPwFQLSNTEVIECI 238
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
470-660 1.07e-06

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: 50.96  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 470 IGIGSYSVCKRCIhSASNMEFAVKIIDKNKRDPSE-----EIEILMRYgQHPNIISLKEVFDDGKYVYLVTDLMKGGELl 544
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLKGEGTQGGDhgfqaEIQTLGMI-RHRNIVRLRGYCSNPTTNLLVYEYMPNGSL- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 545 DRILKKKCFSEQ----EASNVLYV-ITKTVEYLH---SQGVVHRDLKPSNILyMDESGHPdsiKICDFGFAKQLRGENGL 616
Cdd:cd14664    78 GELLHSRPESQPpldwETRQRIALgSARGLAYLHhdcSPLIIHRDVKSNNIL-LDEEFEA---HVADFGLAKLMDDKDSH 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1958807372 617 LLTPCY-TANFVAPEVLTQQGYDAACDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14664   154 VMSSVAgSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPF 198
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
509-732 1.62e-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: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 509 LMRYGQHPNIISLKEVFDDgKYVYLVTDLMKGGELLDrilkkkcFSEQEASNVLYV---------ITKTVEYLHSQGVVH 579
Cdd:cd05071    57 VMKKLRHEKLVQLYAVVSE-EPIYIVTEYMSKGSLLD-------FLKGEMGKYLRLpqlvdmaaqIASGMAYVERMNYVH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 580 RDLKPSNILYmdesGHPDSIKICDFGFAKQLRGENgllltpcYTA--------NFVAPEVLTQQGYDAACDIWSLGVLLY 651
Cdd:cd05071   129 RDLRAANILV----GENLVCKVADFGLARLIEDNE-------YTArqgakfpiKWTAPEAALYGRFTIKSDVWSFGILLT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 652 TMLA-GYTPFsngPNDTPEEILlrigngrfslsggiwDNISRGAK------------DLLSHMLHMDPHQRYTAE--QVL 716
Cdd:cd05071   198 ELTTkGRVPY---PGMVNREVL---------------DQVERGYRmpcppecpeslhDLMCQCWRKEPEERPTFEylQAF 259
                         250
                  ....*....|....*.
gi 1958807372 717 KHPWITQREqlPRHQP 732
Cdd:cd05071   260 LEDYFTSTE--PQYQP 273
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
110-353 1.63e-06

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 50.31  E-value: 1.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAFQT 182
Cdd:cd14139     1 EFLELEKIGVGEFGSVYKCIKRLD---GCVYAIKRSMRPFAGSSN------EQLALHEVyahavlgHHPHVVRYYSAWAE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKEV----LFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILldeIGHiKLTDFGLS 258
Cdd:cd14139    72 DDHMIIQNEYCNGGSLQDAISENTksgnHFEEPELKDILLQVSMGLKYIHNSGLVHLDIKPSNIF---ICH-KMQSSSGV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 259 KESVDQEKKAYSFCGTV----------------------EYMAPEVVNRR-GHSQSADWWSYGvLMFEMLTGT--LPFQG 313
Cdd:cd14139   148 GEEVSNEEDEFLSANVVykigdlghvtsinkpqveegdsRFLANEILQEDyRHLPKADIFALG-LTVALAAGAepLPTNG 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1958807372 314 KDRNEtmnmILKAKL-GMPQFLSAEAQSLLRMLFKRNPANR 353
Cdd:cd14139   227 AAWHH----IRKGNFpDVPQELPESFSSLLKNMIQPDPEQR 263
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
115-357 2.03e-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: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 115 KVLGQGSFGKVFLVRKKTGPDAGQLYamkVLRKASLKVRDRV-RTKMERDILVEVNH--PF---IVKLHYAfqtegklYL 188
Cdd:cd13980     6 KSLGSTRFLKVARARHDEGLVVVKVF---VKPDPALPLRSYKqRLEEIRDRLLELPNvlPFqkvIETDKAA-------YL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 189 ILDFLRGgDVFTRLSKEVLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLDEIGHIKLTDFGLSKESVDQEKKA 268
Cdd:cd13980    76 IRQYVKY-NLYDRISTRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFASFKPTYLPEDNP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 269 YSF-----------CgtveYMAPE----------VVNRRG--HSQSADWWSYGVLMFEMLT-GTLPFqgkdrneTMNMIL 324
Cdd:cd13980   155 ADFsyffdtsrrrtC----YIAPErfvdaltldaESERRDgeLTPAMDIFSLGCVIAELFTeGRPLF-------DLSQLL 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1958807372 325 KAKLG---MPQFLSA----EAQSLLRMLFKRNPANRLGSE 357
Cdd:cd13980   224 AYRKGefsPEQVLEKiedpNIRELILHMIQRDPSKRLSAE 263
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
466-679 3.99e-06

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 49.27  E-value: 3.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 466 LKEDIGIGSY-----SVCKRCIHSASNMEFAVKII----DKNKRDPSEEIEILMRYgQHPNIISLKEVFDDGKYVYLVTD 536
Cdd:cd05093     9 LKRELGEGAFgkvflAECYNLCPEQDKILVAVKTLkdasDNARKDFHREAELLTNL-QHEHIVKFYGVCVEGDPLIMVFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 537 LMKGGEL--------LDRIL--KKKCFSEQEASNVLYV---ITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICD 603
Cdd:cd05093    88 YMKHGDLnkflrahgPDAVLmaEGNRPAELTQSQMLHIaqqIAAGMVYLASQHFVHRDLATRNCLV----GENLLVKIGD 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 604 FGFAKQLRGEN-----GLLLTPCytaNFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNDtpeEILLRIGN 677
Cdd:cd05093   164 FGMSRDVYSTDyyrvgGHTMLPI---RWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQPWYQLSNN---EVIECITQ 237

                  ..
gi 1958807372 678 GR 679
Cdd:cd05093   238 GR 239
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
110-245 4.38e-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: 48.94  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 110 QFDLLKVLGQGSFGKVFLVRKKTGpdaGQLYAMKVLRKASLKVRDrvrtkmERDILVEV-------NHPFIVKLHYAFQT 182
Cdd:cd14051     1 EFHEVEKIGSGEFGSVYKCINRLD---GCVYAIKKSKKPVAGSVD------EQNALNEVyahavlgKHPHVVRYYSAWAE 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958807372 183 EGKLYLILDFLRGGDVFTRLSKE----VLFTEEDVKFYLAELALALDHLHRLGIVYRDLKPENILLD 245
Cdd:cd14051    72 DDHMIIQNEYCNGGSLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFIS 138
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
569-660 9.90e-06

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: 48.26  E-value: 9.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 569 VEYLHSQGVVHRDLKPSNILY-MDESGHPdSIKICDFGFAkqLRGENGLLLTPcYTANFV---------APEVLTQQ--- 635
Cdd:cd14018   151 VDHLVRHGIAHRDLKSDNILLeLDFDGCP-WLVIADFGCC--LADDSIGLQLP-FSSWYVdrggnaclmAPEVSTAVpgp 226
                          90       100
                  ....*....|....*....|....*....
gi 1958807372 636 ----GYDAAcDIWSLGVLLYTMLAGYTPF 660
Cdd:cd14018   227 gvviNYSKA-DAWAVGAIAYEIFGLSNPF 254
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
565-677 6.44e-05

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 45.38  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 565 ITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRgeNGLLLTPCYTA----NFVAPEVLTQQGYDAA 640
Cdd:cd05075   122 IASGMEYLSSKNFIHRDLAARNCM-LNENM---NVCVADFGLSKKIY--NGDYYRQGRISkmpvKWIAIESLADRVYTTK 195
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1958807372 641 CDIWSLGVLLYTMLA-GYTPFsngPNDTPEEI--LLRIGN 677
Cdd:cd05075   196 SDVWSFGVTMWEIATrGQTPY---PGVENSEIydYLRQGN 232
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
491-715 1.92e-04

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


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 44.05  E-value: 1.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 491 AVKIIdknKRDPSEEIEI-------LMRYGQHPNIISLKEVFDDGKYVYLVTDLMKGGELlDRILKKKC----------- 552
Cdd:cd05050    39 AVKML---KEEASADMQAdfqreaaLMAEFDHPNIVKLLGVCAVGKPMCLLFEYMAYGDL-NEFLRHRSpraqcslshst 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 553 ------------FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYmdesGHPDSIKICDFGFAKQLrgenglLLTP 620
Cdd:cd05050   115 ssarkcglnplpLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLV----GENMVVKIADFGLSRNI------YSAD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 621 CYTAN--------FVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNdtpEEILLRIGNGRFSlsgGIWDNIS 691
Cdd:cd05050   185 YYKASendaipirWMPPESIFYNRYTTESDVWAYGVVLWEIFSyGMQPYYGMAH---EEVIYYVRDGNVL---SCPDNCP 258
                         250       260
                  ....*....|....*....|....
gi 1958807372 692 RGAKDLLSHMLHMDPHQRYTAEQV 715
Cdd:cd05050   259 LELYNLMRLCWSKLPSDRPSFASI 282
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
486-673 2.38e-04

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: 43.77  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 486 SNMEFAVKIIDKNKRDPSEEIEIL-----MRYGQHPNIISLKEV---FDDGKYV--YLVTDLMKGGELLDRILKKKCFSE 555
Cdd:cd14204    34 TNHKVAVKTMKLDNFSQREIEEFLseaacMKDFNHPNVIRLLGVcleVGSQRIPkpMVILPFMKYGDLHSFLLRSRLGSG 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 556 ------QEASNVLYVITKTVEYLHSQGVVHRDLKPSNILYMDESghpdSIKICDFGFAKQLRG-----ENGLLLTPcytA 624
Cdd:cd14204   114 pqhvplQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDM----TVCVADFGLSKKIYSgdyyrQGRIAKMP---V 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958807372 625 NFVAPEVLTQQGYDAACDIWSLGVLLYTMLA-GYTPFSNGPNDTPEEILL 673
Cdd:cd14204   187 KWIAVESLADRVYTVKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLL 236
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
486-709 1.15e-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: 41.83  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 486 SNMEFAVKIIdKNKRDPSEEIEILMRYG------QHPNIISLKEVFDDGK------YVYLVTDLMKGGELLDRILKKKC- 552
Cdd:cd05074    36 SFQKVAVKML-KADIFSSSDIEEFLREAacmkefDHPNVIKLIGVSLRSRakgrlpIPMVILPFMKHGDLHTFLLMSRIg 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 553 -----FSEQEASNVLYVITKTVEYLHSQGVVHRDLKPSNILyMDESGhpdSIKICDFGFAKQLRGENgLLLTPCYT---A 624
Cdd:cd05074   115 eepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCM-LNENM---TVCVADFGLSKKIYSGD-YYRQGCASklpV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958807372 625 NFVAPEVLTQQGYDAACDIWSLGVLLY-TMLAGYTPFSNGPNDTPEEILlrIGNGRFSLSGGIWDNISrgakDLLSHMLH 703
Cdd:cd05074   190 KWLALESLADNVYTTHSDVWAFGVTMWeIMTRGQTPYAGVENSEIYNYL--IKGNRLKQPPDCLEDVY----ELMCQCWS 263

                  ....*.
gi 1958807372 704 MDPHQR 709
Cdd:cd05074   264 PEPKCR 269
 
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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