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Conserved domains on  [gi|3426027|gb|AAC32232|]
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RIP protein kinase [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 10197126)

protein kinase family protein containing a Death domain (DD), may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
23-290 0e+00

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: 521.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAeMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGT 182
Cdd:cd14027  81 VLKK-VSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIIS 262
Cdd:cd14027 160 AKKNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREIID 239
                       250       260
                ....*....|....*....|....*...
gi 3426027  263 LMKLCWEANPEARPTFPGIEEKFRPFYL 290
Cdd:cd14027 240 LMKLCWEANPEARPTFPGIEEKFRPFYL 267
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
583-668 1.88e-51

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal 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 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 accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260048  Cd Length: 86  Bit Score: 172.62  E-value: 1.88e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  583 TDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLL 662
Cdd:cd08777   1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDLL 80

                ....*.
gi 3426027  663 SSLIYV 668
Cdd:cd08777  81 VSLLQV 86
 
Name Accession Description Interval E-value
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
23-290 0e+00

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: 521.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAeMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGT 182
Cdd:cd14027  81 VLKK-VSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIIS 262
Cdd:cd14027 160 AKKNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREIID 239
                       250       260
                ....*....|....*....|....*...
gi 3426027  263 LMKLCWEANPEARPTFPGIEEKFRPFYL 290
Cdd:cd14027 240 LMKLCWEANPEARPTFPGIEEKFRPFYL 267
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
22-285 2.37e-63

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: 210.87  E-value: 2.37e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      22 ELDSGGFGKVSLCFHRTQGLMI-----MKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:smart00221   6 KLGEGAFGEVYKGTLKGKGDGKevevaVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      97 KGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehn 174
Cdd:smart00221  85 GGDLLDYLRKNRPKELSLSDllSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS-------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     175 elREVDGTA--KKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFAN-KEPYENAICeQQLIMCIKSGNRPdv 249
Cdd:smart00221 151 --RDLYDDDyyKVKGGKLpiRWMAPESLKE--GKFTSKSDVWSFGVLLWEIFTLgEEPYPGMSN-AEVLEYLKKGYRL-- 223
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 3426027     250 dDITEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:smart00221 224 -PKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
22-285 2.47e-56

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: 191.94  E-value: 2.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     22 ELDSGGFGKVSLCFHRTQGLMI-----MKTVYKGPNCIEHnEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKGEGENTkikvaVKTLKEGADEEER-EDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     97 KGNLMHVLKaEMSTPLSVKGRI--ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneehn 174
Cdd:pfam07714  85 GGDLLDFLR-KHKRKLTLKDLLsmALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIY---------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    175 elreVDGTAKKNGGTLY---YMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFAN-KEPYENaICEQQLIMCIKSGNRPdvd 250
Cdd:pfam07714 154 ----DDDYYRKRGGGKLpikWMAPESLKD--GKFTSKSDVWSFGVLLWEIFTLgEQPYPG-MSNEEVLEFLEDGYRL--- 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 3426027    251 DITEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:pfam07714 224 PQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
583-668 1.88e-51

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal 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 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 accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260048  Cd Length: 86  Bit Score: 172.62  E-value: 1.88e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  583 TDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLL 662
Cdd:cd08777   1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDLL 80

                ....*.
gi 3426027  663 SSLIYV 668
Cdd:cd08777  81 VSLLQV 86
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-276 5.73e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 147.47  E-value: 5.73e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFHRTQG----LMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGrpvaLKVLRPELAADP--EARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEmsTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehn 174
Cdd:COG0515  91 GESLADLLRRR--GPLPPAEalRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIA-------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 elREVDGTAKKNG----GTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVD 250
Cdd:COG0515 155 --RALGGATLTQTgtvvGTPGYMAPEQARG--EPVDPRSDVYSLGVTLYELLTGRPPFD-GDSPAELLRAHLREPPPPPS 229
                       250       260
                ....*....|....*....|....*.
gi 3426027  251 DITEYCPREIISLMKLCWEANPEARP 276
Cdd:COG0515 230 ELRPDLPPALDAIVLRALAKDPEERY 255
Death pfam00531
Death domain;
584-667 1.62e-22

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 92.04  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    584 DKHLDPIREN---LGKHWKNCARKLGFTQSQIDEIDHDYERdgLKEKVYQMLQKWVMREGiKGATVGKLAQALHQCSRID 660
Cdd:pfam00531   1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR--LRSQTYELLRLWEQREG-KNATVGTLLEALRKLGRRD 77

                  ....*..
gi 3426027    661 LLSSLIY 667
Cdd:pfam00531  78 AAEKIQS 84
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
580-667 6.72e-21

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 87.47  E-value: 6.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     580 TSLTDKHLDPIREN-LGKHWKNCARKLGFTQSQIDEIDHDYERDgLKEKVYQMLQKWVMREGIKgATVGKLAQALHQCSR 658
Cdd:smart00005   1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRD-LAEQSVQLLRLWEQREGKN-ATLGTLLEALRKMGR 78

                   ....*....
gi 3426027     659 IDLLSSLIY 667
Cdd:smart00005  79 DDAVELLRS 87
PHA02988 PHA02988
hypothetical protein; Provisional
63-289 6.97e-21

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 93.27  E-value: 6.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    63 EAKMMNRLRHSRVVKLLGVIIEEG----KYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHK 137
Cdd:PHA02988  68 EIKNLRRIDSNNILKIYGFIIDIVddlpRLSLILEYCTRGYLREVLDKEKDLSFKTKLDMAIDCCKGLYNLYKYtNKPYK 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   138 DLKPENILVDNDFHIKIADLGLasFKMWSKlnneehnelrevdgTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVV 217
Cdd:PHA02988 148 NLTSVSFLVTENYKLKIICHGL--EKILSS--------------PPFKNVNFMVYFSYKMLNDIFSEYTIKDDIYSLGVV 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027   218 LWAIFANKEPYENAICEQQLIMCIKSGNRPDVDditEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:PHA02988 212 LWEIFTGKIPFENLTTKEIYDLIINKNNSLKLP---LDCPLEIKCIVEACTSHDSIKRPNIKEILYNLSLYK 280
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
63-218 6.24e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 81.38  E-value: 6.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    63 EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEmsTPLSVkgRIILEIIEGMC----YLHGKGVIHKD 138
Cdd:NF033483  57 EAQSAASLSHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREH--GPLSP--EEAVEIMIQILsaleHAHRNGIVHRD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   139 LKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNG----GTLYYMAPEHLNDVNAkpTEKSDVYSF 214
Cdd:NF033483 133 IKPQNILITKDGRVKVTDFGIA----------------RALSSTTMTQTnsvlGTVHYLSPEQARGGTV--DARSDIYSL 194

                 ....
gi 3426027   215 AVVL 218
Cdd:NF033483 195 GIVL 198
 
Name Accession Description Interval E-value
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
23-290 0e+00

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: 521.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14027   1 LDSGGFGKVSLCFHRTQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLMH 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAeMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGT 182
Cdd:cd14027  81 VLKK-VSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDGT 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIIS 262
Cdd:cd14027 160 AKKNAGTLYYMAPEHLNDVNAKPTEKSDVYSFAIVLWAIFANKEPYENAINEDQIIMCIKSGNRPDVDDITEYCPREIID 239
                       250       260
                ....*....|....*....|....*...
gi 3426027  263 LMKLCWEANPEARPTFPGIEEKFRPFYL 290
Cdd:cd14027 240 LMKLCWEANPEARPTFPGIEEKFRPFYL 267
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
23-287 1.87e-127

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: 377.56  E-value: 1.87e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRT-QGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd13978   1 LGSGGFGTVSKARHVSwFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAE-MSTPLSVKGRIILEIIEGMCYLHG--KGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEhnelre 178
Cdd:cd13978  81 SLLEREiQDVPWSLRFRIIHEIALGMNFLHNmdPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRR------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIKS-GNRPDVDDITEYC- 256
Cdd:cd13978 155 --RGTENLGGTPIYMAPEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAI-NPLLIMQIVSkGDRPSLDDIGRLKq 231
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  257 ---PREIISLMKLCWEANPEARPTFpgIEEKFRP 287
Cdd:cd13978 232 ienVQELISLMIRCWDGNPDARPTF--LECLDRL 263
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
25-285 9.01e-67

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: 219.33  E-value: 9.01e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQgLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd13999   3 SGSFGEVYKGKWRGT-DVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLYDLL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 -KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneehnelreVDGTA 183
Cdd:cd13999  82 hKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIK---------------NSTTE 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  184 KKNG--GTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPdvdDITEYCPREII 261
Cdd:cd13999 147 KMTGvvGTPRWMAPEVLRGEPY--TEKADVYSFGIVLWELLTGEVPFKELSPIQIAAAVVQKGLRP---PIPPDCPPELS 221
                       250       260
                ....*....|....*....|....
gi 3426027  262 SLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd13999 222 KLIKRCWNEDPEKRPSFSEIVKRL 245
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
22-285 2.37e-63

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: 210.87  E-value: 2.37e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      22 ELDSGGFGKVSLCFHRTQGLMI-----MKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:smart00221   6 KLGEGAFGEVYKGTLKGKGDGKevevaVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      97 KGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehn 174
Cdd:smart00221  85 GGDLLDYLRKNRPKELSLSDllSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS-------------- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     175 elREVDGTA--KKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFAN-KEPYENAICeQQLIMCIKSGNRPdv 249
Cdd:smart00221 151 --RDLYDDDyyKVKGGKLpiRWMAPESLKE--GKFTSKSDVWSFGVLLWEIFTLgEEPYPGMSN-AEVLEYLKKGYRL-- 223
                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 3426027     250 dDITEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:smart00221 224 -PKPPNCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
22-285 2.18e-61

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 205.46  E-value: 2.18e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      22 ELDSGGFGKVSLCFHRTQGLMI-----MKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:smart00219   6 KLGEGAFGEVYKGKLKGKGGKKkvevaVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      97 KGNLMHVLKA-EMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehne 175
Cdd:smart00219  85 GGDLLSYLRKnRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLS--------------- 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     176 lREVDGTA--KKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFAN-KEPYENAICeQQLIMCIKSGNRPdvd 250
Cdd:smart00219 150 -RDLYDDDyyRKRGGKLpiRWMAPESLKE--GKFTSKSDVWSFGVLLWEIFTLgEQPYPGMSN-EEVLEYLKNGYRL--- 222
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 3426027     251 DITEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:smart00219 223 PQPPNCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
22-286 1.51e-59

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: 200.84  E-value: 1.51e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLC-FHRTQGLMIMKTVYKGPNC--IEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd00192   2 KLGEGAFGEVYKGkLKGGDGKTVDVAVKTLKEDasESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLK-------AEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskln 169
Cdd:cd00192  82 DLLDFLRksrpvfpSPEPSTLSLKDllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLS--------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neehnELREVDGTAKKNGGT---LYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFAN-KEPYENAICeQQLIMCIKSGN 245
Cdd:cd00192 153 -----RDIYDDDYYRKKTGGklpIRWMAPESLKD--GIFTSKSDVWSFGVLLWEIFTLgATPYPGLSN-EEVLEYLRKGY 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 3426027  246 RPdvdDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd00192 225 RL---PKPENCPDELYELMLSCWQLDPEDRPTFSELVERLE 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
25-281 1.68e-59

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 200.45  E-value: 1.68e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027      25 SGGFGKVSLCFHR-TQGLMIMKTVYKgPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:smart00220   9 EGSFGKVYLARDKkTGKLVAIKVIKK-KKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDL 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     104 LKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTA 183
Cdd:smart00220  88 LKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLA----------------RQLDPGE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     184 KKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNrPDVDDITEYCPREII 261
Cdd:smart00220 152 KLTTfvGTPEYMAPEVLL--GKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPK-PPFPPPEWDISPEAK 228
                          250       260
                   ....*....|....*....|
gi 3426027     262 SLMKLCWEANPEARPTFPGI 281
Cdd:smart00220 229 DLIRKLLVKDPEKRLTAEEA 248
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
22-285 2.47e-56

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: 191.94  E-value: 2.47e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     22 ELDSGGFGKVSLCFHRTQGLMI-----MKTVYKGPNCIEHnEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKGEGENTkikvaVKTLKEGADEEER-EDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     97 KGNLMHVLKaEMSTPLSVKGRI--ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneehn 174
Cdd:pfam07714  85 GGDLLDFLR-KHKRKLTLKDLLsmALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIY---------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    175 elreVDGTAKKNGGTLY---YMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFAN-KEPYENaICEQQLIMCIKSGNRPdvd 250
Cdd:pfam07714 154 ----DDDYYRKRGGGKLpikWMAPESLKD--GKFTSKSDVWSFGVLLWEIFTLgEQPYPG-MSNEEVLEFLEDGYRL--- 223
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 3426027    251 DITEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:pfam07714 224 PQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
583-668 1.88e-51

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal 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 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 accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260048  Cd Length: 86  Bit Score: 172.62  E-value: 1.88e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  583 TDKHLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDGLKEKVYQMLQKWVMREGIKGATVGKLAQALHQCSRIDLL 662
Cdd:cd08777   1 TEKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDYERDGLKEKVHQMLEKWKMKEGSKGATVGKLAKALEGCIKSDLL 80

                ....*.
gi 3426027  663 SSLIYV 668
Cdd:cd08777  81 VSLLQV 86
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
23-285 2.68e-49

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: 171.30  E-value: 2.68e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKgPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd00180   1 LGKGSFGKVYKARDKETGkKVAVKVIPK-EKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKaEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEHNELREV 179
Cdd:cd00180  80 DLLK-ENKGPLSEEEalSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLA------KDLDSDDSLLKTT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTakkngGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIfankepyenaiceqqlimciksgnrpdvdditeycpRE 259
Cdd:cd00180 153 GGT-----TPPYYAPPELLGGRYY--GPKVDIWSLGVILYEL------------------------------------EE 189
                       250       260
                ....*....|....*....|....*.
gi 3426027  260 IISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd00180 190 LKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
23-277 4.52e-48

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: 169.62  E-value: 4.52e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCF-HRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd06606   8 LGKGSFGSVYLALnLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSLA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLNNEEHNELRevdg 181
Cdd:cd06606  88 SLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFG-CAKRLAEIATGEGTKSLR---- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 takkngGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIksGNRPDVDDITEYCPREII 261
Cdd:cd06606 163 ------GTPYWMAPEVIRG--EGYGRAADIWSLGCTVIEMATGKPPWSELGNPVAALFKI--GSSGEPPPIPEHLSEEAK 232
                       250
                ....*....|....*.
gi 3426027  262 SLMKLCWEANPEARPT 277
Cdd:cd06606 233 DFLRKCLQRDPKKRPT 248
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
9-284 9.62e-45

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: 160.59  E-value: 9.62e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    9 VIKMKssDFLESAELDSGGFGKVSLCFHRTQGLMI--MKTVYKGPNciehneALLEEAKMMNRLRHSRVVKLLGVIIEEG 86
Cdd:cd05039   2 AINKK--DLKLGELIGKGEFGDVMLGDYRGQKVAVkcLKDDSTAAQ------AFLAEASVMTTLRHPNLVQLLGVVLEGN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   87 KYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRII--LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkm 164
Cdd:cd05039  74 GLYIVTEYMAKGSLVDYLRSRGRAVITRKDQLGfaLDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK--- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  165 wsklnneehnelrevDGTAKKNGGTL--YYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCI 241
Cdd:cd05039 151 ---------------EASSNQDGGKLpiKWTAPEALR--EKKFSTKSDVWSFGILLWEIYSfGRVPYPR-IPLKDVVPHV 212
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 3426027  242 KSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd05039 213 EKGYRMEA---PEGCPPEVYKVMKNCWELDPAKRPTFKQLREK 252
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
25-281 5.56e-44

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: 158.81  E-value: 5.56e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQglmimKT--VYKGPNCI-----EHNEaLLEEAKMMNRLRHSRVVKLLGVIIEegKYSLVMEYMEK 97
Cdd:cd14025   6 SGGFGQVYKVRHKHW-----KTwlAIKCPPSLhvddsERME-LLEEAKKMEMAKFRHILPVYGICSE--PVGLVMEYMET 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEmSTPLSVKGRIILEIIEGMCYLH--GKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEHNE 175
Cdd:cd14025  78 GSLEKLLASE-PLPWELRFRIIHETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGLA------KWNGLSHSH 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 LREVDGTAkkngGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEY 255
Cdd:cd14025 151 DLSRDGLR----GTIAYLPPERFKEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGENNILHIMVKVVKGHRPSLSPIPRQ 226
                       250       260
                ....*....|....*....|....*....
gi 3426027  256 CPRE---IISLMKLCWEANPEARPTFPGI 281
Cdd:cd14025 227 RPSEcqqMICLMKRCWDQDPRKRPTFQDI 255
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
22-277 1.07e-42

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: 155.05  E-value: 1.07e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHN-EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd14014   7 LLGRGGMGEVYRARDTLLGRPVaIKVLRPELAEDEEFrERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEYVEGGS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnneehnELREV 179
Cdd:cd14014  87 LADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARA------------LGDSG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIKSGNRPDVDDITEYCPRE 259
Cdd:cd14014 155 LTQTGSVLGTPAYMAPEQAR--GGPVDPRSDIYSLGVVLYELLTGRPPFDGDS-PAAVLAKHLQEAPPPPSPLNPDVPPA 231
                       250
                ....*....|....*...
gi 3426027  260 IISLMKLCWEANPEARPT 277
Cdd:cd14014 232 LDAIILRALAKDPEERPQ 249
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
57-288 1.81e-41

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 151.77  E-value: 1.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   57 NEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHG-KGV 134
Cdd:cd13992  40 KRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLlNREIKMDWMFKSSFIKDIVKGMNYLHSsSIG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASFKmwsklnNEEHNELREVDGTAKKnggtLYYMAPEHL--NDVNAKPTEKSDVY 212
Cdd:cd13992 120 YHGRLKSSNCLVDSRWVVKLTDFGLRNLL------EEQTNHQLDEDAQHKK----LLWTAPELLrgSLLEVRGTQKGDVY 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  213 SFAVVLWAIFANKEPYENAICEQQLIMCIKSGN---RPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPF 288
Cdd:cd13992 190 SFAIILYEILFRSDPFALEREVAIVEKVISGGNkpfRPELAVLLDEFPPRLVLLVKQCWAENPEKRPSFKQIKKTLTEN 268
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
23-283 3.28e-41

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: 150.36  E-value: 3.28e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14003   8 LGEGSFGKVKLARHKLTGEKVaIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYASGGELF 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEmsTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnNEEHNELREV 179
Cdd:cd14003  88 DYIVNN--GRLSEDeaRRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNE-------FRGGSLLKTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 dgtakknGGTLYYMAPEHLNDvnaKP--TEKSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKSGNRPDVDDITEycp 257
Cdd:cd14003 159 -------CGTPAYAAPEVLLG---RKydGPKADVWSLGVILYAMLTGYLPFDDD-NDSKLFRKILKGKYPIPSHLSP--- 224
                       250       260
                ....*....|....*....|....*.
gi 3426027  258 rEIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14003 225 -DARDLIRRMLVVDPSKRITIEEILN 249
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
23-278 9.16e-41

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: 150.45  E-value: 9.16e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNE--ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14026   5 LSRGAFGTVSRARHADWRVTVAIKCLKLDSPVGDSErnCLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTNGSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTP---LSVKGRIILEIIEGMCYLHGKG--VIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNE 175
Cdd:cd14026  85 NELLHEKDIYPdvaWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSISQSRSSKS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 LREvdgtakknGGTLYYMAPEHLNDVNAKPTE-KSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDitE 254
Cdd:cd14026 165 APE--------GGTIIYMPPEEYEPSQKRRASvKHDIYSYAIIMWEVLSRKIPFEEVTNPLQIMYSVSQGHRPDTGE--D 234
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  255 YCPREI------ISLMKLCWEANPEARPTF 278
Cdd:cd14026 235 SLPVDIphratlINLIESGWAQNPDERPSF 264
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
20-277 1.42e-40

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: 149.07  E-value: 1.42e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   20 SAELDSGGFGKV--SLCFHRTQGLMIMKTVYKGPNCIE--HNEALLEeakmmnRLRHSRVVKLLGVI--IEEGKYSLV-M 92
Cdd:cd13979   8 QEPLGSGGFGSVykATYKGETVAVKIVRRRRKNRASRQsfWAELNAA------RLRHENIVRVLAAEtgTDFASLGLIiM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKaEMSTPLSVKGR--IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMwsklnn 170
Cdd:cd13979  82 EYCGNGTLQQLIY-EGSEPLPLAHRilISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFG-CSVKL------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eehNELREVDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVD 250
Cdd:cd13979 154 ---GEGNEVGTPRSHIGGTYTYRAPELLK--GERVTPKADIYSFGITLWQMLTRELPYA-GLRQHVLYAVVAKDLRPDLS 227
                       250       260
                ....*....|....*....|....*...
gi 3426027  251 DITEYCPREII-SLMKLCWEANPEARPT 277
Cdd:cd13979 228 GLEDSEFGQRLrSLISRCWSAQPAERPN 255
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
22-277 1.30e-39

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: 146.47  E-value: 1.30e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd05117   7 VLGRGSFGVVRLAVHKKTGEEYaVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMELCTGGEL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDN---DFHIKIADLGLASFKmwsklnnEEHNELR 177
Cdd:cd05117  87 FDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIF-------EEGEKLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVdgtakknGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEP-YENaiCEQQLIMCIKSG----NRPDVDDI 252
Cdd:cd05117 160 TV-------CGTPYYVAPEVLK--GKGYGKKCDIWSLGVILYILLCGYPPfYGE--TEQELFEKILKGkysfDSPEWKNV 228
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCpreiISLMKLCWEANPEARPT 277
Cdd:cd05117 229 SEEA----KDLIKRLLVVDPKKRLT 249
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
23-277 1.38e-38

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: 143.85  E-value: 1.38e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLC-------------FHRTQglMIMKTVYKGPNCIEHN--EALLEEAKMMNRLRHSRVVKLLGVI--IEE 85
Cdd:cd14008   1 LGRGSFGKVKLAldtetgqlyaikiFNKSR--LRKRREGKNDRGKIKNalDDVRREIAIMKKLDHPNIVRLYEVIddPES 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEYMEKGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFk 163
Cdd:cd14008  79 DKLYLVLEYCEGGPVMELDSGDRVPPLPEETarKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEM- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 mwsklnneehneLREVDGTAKKNGGTLYYMAPEHLnDVNAKP--TEKSDVYSFAVVLWAIFANKEPYEnaiCEQQLIMCI 241
Cdd:cd14008 158 ------------FEDGNDTLQKTAGTPAFLAPELC-DGDSKTysGKAADIWALGVTLYCLVFGRLPFN---GDNILELYE 221
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 3426027  242 KSGNRPDVDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14008 222 AIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRIT 257
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
21-285 3.52e-38

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: 142.32  E-value: 3.52e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVslcfhrTQG-LMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGN 99
Cdd:cd05083  12 EIIGEGEFGAV------LQGeYMGQKVAVKNIKCDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLY-IVMELMSKGN 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAE--MSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnneehnELR 177
Cdd:cd05083  85 LVNFLRSRgrALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV------------GSM 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKnggtLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNRPDVddiTEYC 256
Cdd:cd05083 153 GVDNSRLP----VKWTAPEALK--NKKFSSKSDVWSYGVLLWEVFSyGRAPYPK-MSVKEVKEAVEKGYRMEP---PEGC 222
                       250       260
                ....*....|....*....|....*....
gi 3426027  257 PREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05083 223 PPDVYSIMTSCWEAEPGKRPSFKKLREKL 251
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
23-285 4.13e-38

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: 142.91  E-value: 4.13e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHR----TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS--LVMEYME 96
Cdd:cd05038  12 LGEGHFGSVELCRYDplgdNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRRSlrLIMEYLP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVL---KAEMSTPLSVkgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEH 173
Cdd:cd05038  92 SGSLRDYLqrhRDQIDLKRLL--LFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLA------KVLPEDK 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 -----NELREVdgtakknggTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYENAI--------CEQ----- 235
Cdd:cd05038 164 eyyyvKEPGES---------PIFWYAPECLRE--SRFSSASDVWSFGVTLYELFTYGDPSQSPPalflrmigIAQgqmiv 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 3426027  236 -QLIMCIKSG---NRPDvdditeYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05038 233 tRLLELLKSGerlPRPP------SCPDEVYDLMKECWEYEPQDRPSFSDLILII 280
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
21-276 5.73e-38

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 147.47  E-value: 5.73e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFHRTQG----LMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:COG0515  13 RLLGRGGMGVVYLARDLRLGrpvaLKVLRPELAADP--EARERFRREARALARLNHPNIVRVYDVGEEDGRPYLVMEYVE 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEmsTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehn 174
Cdd:COG0515  91 GESLADLLRRR--GPLPPAEalRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIA-------------- 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 elREVDGTAKKNG----GTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVD 250
Cdd:COG0515 155 --RALGGATLTQTgtvvGTPGYMAPEQARG--EPVDPRSDVYSLGVTLYELLTGRPPFD-GDSPAELLRAHLREPPPPPS 229
                       250       260
                ....*....|....*....|....*.
gi 3426027  251 DITEYCPREIISLMKLCWEANPEARP 276
Cdd:COG0515 230 ELRPDLPPALDAIVLRALAKDPEERY 255
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
22-289 9.89e-38

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: 141.72  E-value: 9.89e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEhneALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd05072  14 KLGAGQFGEVWMGYYNNSTKVAVKTLKPGTMSVQ---AFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneEHNELREV 179
Cdd:cd05072  91 DFLKSDEGGKVLLPKLIDFsaQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVI--------EDNEYTAR 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGtAKKnggTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNR-PDVdditEYCP 257
Cdd:cd05072 163 EG-AKF---PIKWTAPEAIN--FGSFTIKSDVWSFGILLYEIVTyGKIPYP-GMSNSDVMSALQRGYRmPRM----ENCP 231
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  258 REIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:cd05072 232 DELYDIMKTCWKEKAEERPTFDYLQSVLDDFY 263
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
22-278 1.74e-37

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: 140.28  E-value: 1.74e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd05059  11 ELGSGQFGVVHLGKWRGKIDVAIKMIKEG---SMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEmstPLSVKGRIILE----IIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneehnelr 177
Cdd:cd05059  88 NYLRER---RGKFQTEQLLEmckdVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYV-------------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 eVDGTAKKNGGTLY---YMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNRPDVDDIt 253
Cdd:cd05059 151 -LDDEYTSSVGTKFpvkWSPPEVFM--YSKFSSKSDVWSFGVLMWEVFSeGKMPYER-FSNSEVVEHISQGYRLYRPHL- 225
                       250       260
                ....*....|....*....|....*
gi 3426027  254 eyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05059 226 --APTEVYTIMYSCWHEKPEERPTF 248
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
22-291 2.29e-36

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: 137.33  E-value: 2.29e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEhneALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGNLM 101
Cdd:cd05067  14 RLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSPD---AFLAEANLMKQLQHQRLVRLYAVVTQEPIY-IITEYMENGSLV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneEHNELREV 179
Cdd:cd05067  90 DFLKTPSGIKLTINKLLDMaaQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLI--------EDNEYTAR 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGtAKKnggTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNR-PDVDDiteyCP 257
Cdd:cd05067 162 EG-AKF---PIKWTAPEAIN--YGTFTIKSDVWSFGILLTEIVThGRIPYP-GMTNPEVIQNLERGYRmPRPDN----CP 230
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  258 REIISLMKLCWEANPEARPTFPGIEEKFRPFYLS 291
Cdd:cd05067 231 EELYQLMRLCWKERPEDRPTFEYLRSVLEDFFTA 264
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
58-284 8.57e-36

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: 135.64  E-value: 8.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRII---LEIIEGMCYLHG--- 131
Cdd:cd14058  31 KAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLYNVLHGKEPKPIYTAAHAMswaLQCAKGVAYLHSmkp 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  132 KGVIHKDLKPENILVDNDFH-IKIADLGLASFKMWSKLNNEehnelrevdgtakkngGTLYYMAPEHLNdvNAKPTEKSD 210
Cdd:cd14058 111 KALIHRDLKPPNLLLTNGGTvLKICDFGTACDISTHMTNNK----------------GSAAWMAPEVFE--GSKYSEKCD 172
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  211 VYSFAVVLWAIFANKEPYENAICEQ-QLIMCIKSGNRPdvdDITEYCPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd14058 173 VFSWGIILWEVITRRKPFDHIGGPAfRIMWAVHNGERP---PLIKNCPKPIESLMTRCWSKDPEKRPSMKEIVKI 244
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
22-281 1.06e-35

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: 135.93  E-value: 1.06e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSL-CFHR-----TQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd05032  13 ELGQGSFGMVYEgLAKGvvkgePETRVAIKTVNENASMRERIE-FLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVKGRII----------LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmw 165
Cdd:cd05032  92 AKGDLKSYLRSRRPEAENNPGLGPptlqkfiqmaAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMT----- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  166 sklnneehNELREVDGTAKKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAI--FAnKEPYENAICEQQLIMCI 241
Cdd:cd05032 167 --------RDIYETDYYRKGGKGLLpvRWMAPESLKD--GVFTTKSDVWSFGVVLWEMatLA-EQPYQGLSNEEVLKFVI 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 3426027  242 KSG--NRPdvdditEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05032 236 DGGhlDLP------ENCPDKLLELMRMCWQYNPKMRPTFLEI 271
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
26-286 4.92e-35

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: 133.57  E-value: 4.92e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMImktvykgpNCIEHN---EALLEEAKMMNRLRHSRVVKLLGVIIEE-GKYSLVMEYMEKGNLM 101
Cdd:cd05082  17 GEFGDVMLGDYRGNKVAV--------KCIKNDataQAFLAEASVMTQLRHSNLVQLLGVIVEEkGGLYIVTEYMAKGSLV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREV 179
Cdd:cd05082  89 DYLRSRGRSVLGGDCllKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLT----------------KEA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNGGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNRPDVDDiteYCPR 258
Cdd:cd05082 153 SSTQDTGKLPVKWTAPEALRE--KKFSTKSDVWSFGILLWEIYSfGRVPYPR-IPLKDVVPRVEKGYKMDAPD---GCPP 226
                       250       260
                ....*....|....*....|....*...
gi 3426027  259 EIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05082 227 AVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
23-284 1.90e-34

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: 132.16  E-value: 1.90e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVslcFHRT----------QGLMIMKTVYKGPNcIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd05044   3 LGSGAFGEV---FEGTakdilgdgsgETKVAVKTLRKGAT-DQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLK-AEMSTP----LSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILV-DNDFH---IKIADLGLAs 161
Cdd:cd05044  79 ELMEGGDLLSYLRaARPTAFtpplLTLKDllSICVDVAKGCVYLEDMHFVHRDLAARNCLVsSKDYRervVKIGDFGLA- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  162 fkmwsklnneehNELREVDGTAKKNGGTL--YYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLI 238
Cdd:cd05044 158 ------------RDIYKNDYYRKEGEGLLpvRWMAPESL--VDGVFTTQSDVWAFGVLMWEILTlGQQPYP-ARNNLEVL 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 3426027  239 MCIKSGNRPDVDDiteYCPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd05044 223 HFVRAGGRLDQPD---NCPDDLYELMLRCWSTDPEERPSFARILEQ 265
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
22-277 2.16e-34

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: 131.56  E-value: 2.16e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLM----IMKTVYKgpnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd05122   7 KIGKGGFGVVYKARHKKTGQIvaikKINLESK-----EKKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFCSG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMST-PLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneehnel 176
Cdd:cd05122  82 GSLKDLLKNTNKTlTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQL------------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 reVDGTAKKN-GGTLYYMAPEHLNDvnaKP-TEKSDVYSFAVVLWAIFANKEPYENaICEQQLIMCIKSGNRPDVDDITE 254
Cdd:cd05122 149 --SDGKTRNTfVGTPYWMAPEVIQG---KPyGFKADIWSLGITAIEMAEGKPPYSE-LPPMKALFLIATNGPPGLRNPKK 222
                       250       260
                ....*....|....*....|...
gi 3426027  255 YCPrEIISLMKLCWEANPEARPT 277
Cdd:cd05122 223 WSK-EFKDFLKKCLQKDPEKRPT 244
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
54-288 3.51e-34

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 131.56  E-value: 3.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   54 IEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEmstplSVK------GRIILEIIEGMC 127
Cdd:cd14042  43 IDLTREVLKELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDILENE-----DIKldwmfrYSLIHDIVKGMH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  128 YLHGKGVI-HKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREvdgtakknggtLYYMAPEHL--NDVNAK 204
Cdd:cd14042 118 YLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYAK-----------LLWTAPELLrdPNPPPP 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  205 PTEKSDVYSFAVVLWAIFANKEPYENA--------ICEQQLIMCIKSGNRPDVDDITeyCPREIISLMKLCWEANPEARP 276
Cdd:cd14042 187 GTQKGDVYSFGIILQEIATRQGPFYEEgpdlspkeIIKKKVRNGEKPPFRPSLDELE--CPDEVLSLMQRCWAEDPEERP 264
                       250
                ....*....|..
gi 3426027  277 TFPGIEEKFRPF 288
Cdd:cd14042 265 DFSTLRNKLKKL 276
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
23-278 3.99e-34

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: 131.24  E-value: 3.99e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKtVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVK-RLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPNGSLED 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKA-EMSTPLSVKGR--IILEIIEGMCYLHGKG---VIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEHNEL 176
Cdd:cd14066  80 RLHChKGSPPLPWPQRlkIAKGIARGLEYLHEECpppIIHGDIKSSNILLDEDFEPKLTDFGLA------RLIPPSESVS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 REVDGTakkngGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMC---IKSGNRPDVDDIT 253
Cdd:cd14066 154 KTSAVK-----GTIGYLAPEYIRT--GRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLvewVESKGKEELEDIL 226
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 3426027  254 EYCPR-----------EIISLMKLCWEANPEARPTF 278
Cdd:cd14066 227 DKRLVdddgveeeeveALLRLALLCTRSDPSLRPSM 262
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
25-281 8.47e-34

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: 129.82  E-value: 8.47e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLC-FHRTQGLMIMKTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEgKYSLVMEYMEKGNL--- 100
Cdd:cd14062   3 SGSFGTVYKGrWHGDVAVKKLNVTDPTP---SQLQAFKNEVAVLRKTRHVNILLFMGYMTKP-QLAIVTQWCEGSSLykh 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVL--KAEMSTPLSvkgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFK-MWSKLNNEEhnelr 177
Cdd:cd14062  79 LHVLetKFEMLQLID----IARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATVKtRWSGSQQFE----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdgtakKNGGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGN-RPDVDDITEY 255
Cdd:cd14062 150 -------QPTGSILWMAPEVIRMQDENPySFQSDVYAFGIVLYELLTGQLPYSHINNRDQILFMVGRGYlRPDLSKVRSD 222
                       250       260
                ....*....|....*....|....*.
gi 3426027  256 CPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14062 223 TPKALRRLMEDCIKFQRDERPLFPQI 248
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
16-277 8.94e-34

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: 129.84  E-value: 8.94e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQG-LMIMKTV-YKGPNCIEHNEALlEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd08529   1 DFEILNKLGKGSFGVVYKVVRKVDGrVYALKQIdISRMSRKMREEAI-DEARVLSKLNSPYVIKYYDSFVDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMWSKLNNE 171
Cdd:cd08529  80 YAENGDLHSLIKSQRGRPLPEDQiwKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVA--KILSDTTNF 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 EHNELrevdgtakkngGTLYYMAPEHLNDvnaKP-TEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVD 250
Cdd:cd08529 158 AQTIV-----------GTPYYLSPELCED---KPyNEKSDVWALGCVLYELCTGKHPFE-AQNQGALILKIVRGKYPPIS 222
                       250       260
                ....*....|....*....|....*..
gi 3426027  251 diTEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd08529 223 --ASYSQ-DLSQLIDSCLTKDYRQRPD 246
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
15-278 9.35e-34

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: 129.68  E-value: 9.35e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd05112   4 SELTFVQEIGSGQFGLVHLGYWLNKDKVAIKTIREG---AMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLKAEMSTpLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnnee 172
Cdd:cd05112  81 MEHGCLSDYLRTQRGL-FSAETllGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVL-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelrevDGTAKKNGGTLY---YMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFAN-KEPYENAiCEQQLIMCIKSGNR-- 246
Cdd:cd05112 152 -------DDQYTSSTGTKFpvkWSSPEVFS--FSRYSSKSDVWSFGVLMWEVFSEgKIPYENR-SNSEVVEDINAGFRly 221
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  247 -PDVdditeyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05112 222 kPRL------ASTHVYEIMNHCWKERPEDRPSF 248
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
23-283 1.06e-33

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: 130.61  E-value: 1.06e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSL-----CFHRTQGLMIMKTVYKGPNCIEHNEA-LLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd05053  20 LGEGAFGQVVKaeavgLDNKPNEVVTVAVKMLKDDATEKDLSdLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVVVEYA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVKGRIILEIIE----------------GMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGL 159
Cdd:cd05053 100 SKGNLREFLRARRPPGEEASPDDPRVPEEqltqkdlvsfayqvarGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGL 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  160 AsfkmwsklnneehNELREVDGTAKKNGGTLYY--MAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQ 236
Cdd:cd05053 180 A-------------RDIHHIDYYRKTTNGRLPVkwMAPEALFD--RVYTHQSDVWSFGVLLWEIFTlGGSPYP-GIPVEE 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 3426027  237 LIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd05053 244 LFKLLKEGHRMEK---PQNCTQELYMLMRDCWHEVPSQRPTFKQLVE 287
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
23-278 2.49e-33

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 129.76  E-value: 2.49e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLC-----------------FHRTQGLMIMKTVYKGPNcIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE 85
Cdd:cd05051  13 LGEGQFGEVHLCeanglsdltsddfigndNKDEPVLVAVKMLRPDAS-KNAREDFLKEVKIMSQLKDPNIVRLLGVCTRD 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGR-----------IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIK 153
Cdd:cd05051  92 EPLCMIVEYMENGDLNQFLqKHEAETQGASATNsktlsygtllyMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIK 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  154 IADLGLAsfkmwsklNNEEHNELREVDGTAKKnggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAI--FANKEPYEnA 231
Cdd:cd05051 172 IADFGMS--------RNLYSGDYYRIEGRAVL---PIRWMAWESI--LLGKFTTKSDVWAFGVTLWEIltLCKEQPYE-H 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 3426027  232 ICEQQLIMCI----KSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05051 238 LTDEQVIENAgeffRDDGMEVYLSRPPNCPKEIYELMLECWRRDEEDRPTF 288
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
26-289 3.28e-33

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: 128.02  E-value: 3.28e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGpNCIEHNEAL--LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd05123   4 GSFGKVLLVRKKdTGKLYAMKVLRKK-EIIKRKEVEhtLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGELFS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnelREVDGT 182
Cdd:cd05123  83 HLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAK---------------ELSSDG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY--ENaicEQQLIMCIKSgnrpdvDDIT--EYC 256
Cdd:cd05123 148 DRTYTfcGTPEYLAPEVLL--GKGYGKAVDWWSLGVLLYEMLTGKPPFyaEN---RKEIYEKILK------SPLKfpEYV 216
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  257 PREIISLMKLCWEANPEARPTFPGIEE-KFRPFY 289
Cdd:cd05123 217 SPEAKSLISGLLQKDPTKRLGSGGAEEiKAHPFF 250
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
58-285 7.24e-33

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: 127.01  E-value: 7.24e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVI 135
Cdd:cd05034  35 EAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLLDYLRTGEGRALRLPQLIDMaaQIASGMAYLESRNYI 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASfkmwsKLNNEEHnelrevdgTAKKngGTLY---YMAPEHLNDvnAKPTEKSDVY 212
Cdd:cd05034 115 HRDLAARNILVGENNVCKVADFGLAR-----LIEDDEY--------TARE--GAKFpikWTAPEAALY--GRFTIKSDVW 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  213 SFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNR---PdvdditEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05034 178 SFGILLYEIVTyGRVPYP-GMTNREVLEQVERGYRmpkP------PGCPDELYDIMLQCWKKEPEERPTFEYLQSFL 247
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
25-289 1.01e-32

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: 127.33  E-value: 1.01e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQG-LMIMKTVYK----GPNcieHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd05579   3 RGAYGRVYLAKKKSTGdLYAIKVIKKrdmiRKN---QVDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREV 179
Cdd:cd05579  80 LYSLLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVGLVRRQIKLSIQKKSNG 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNG--GTLYYMAPEHLNDVNAKPTekSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIKSG--NRPDVDDITEY 255
Cdd:cd05579 160 APEKEDRRivGTPDYLAPEILLGQGHGKT--VDWWSLGVILYEFLVGIPPF-HAETPEEIFQNILNGkiEWPEDPEVSDE 236
                       250       260       270
                ....*....|....*....|....*....|....*
gi 3426027  256 CPREIISLMKLcweaNPEARPTFPGIEE-KFRPFY 289
Cdd:cd05579 237 AKDLISKLLTP----DPEKRLGAKGIEEiKNHPFF 267
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
25-295 1.33e-32

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: 126.74  E-value: 1.33e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQGLMImKTVYKGPnCIEHN---EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14061   4 VGGFGKVYRGIWRGEEVAV-KAARQDP-DEDISvtlENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGALN 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLkAEMSTPLSVKGRIILEIIEGMCYLHGKG---VIHKDLKPENILV------DNDFHI--KIADLGLAsfkmwsklnn 170
Cdd:cd14061  82 RVL-AGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILIleaienEDLENKtlKITDFGLA---------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eehnelREVDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENaiceqqlIMCIKSGNRPDV 249
Cdd:cd14061 151 ------REWHKTTRMSaAGTYAWMAPEVIK--SSTFSKASDVWSYGVLLWELLTGEVPYKG-------IDGLAVAYGVAV 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  250 DDIT----EYCPREIISLMKLCWEANPEARPTFPGIeekfrpfyLSQLEE 295
Cdd:cd14061 216 NKLTlpipSTCPEPFAQLMKDCWQPDPHDRPSFADI--------LKQLEN 257
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
22-289 1.66e-32

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: 126.31  E-value: 1.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGL----MIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGkYSLVMEYMEK 97
Cdd:cd05060   2 ELGHGNFGSVRKGVYLMKSGkeveVAVKTLKQEHEKAGKKE-FLREASVMAQLDHPCIVRLIGVCKGEP-LMLVMELAPL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLNNEEHNELR 177
Cdd:cd05060  80 GPLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGM------SRALGAGSDYYR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdgtAKKNGG-TLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDIteyC 256
Cdd:cd05060 154 -----ATTAGRwPLKWYAPECIN--YGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEE---C 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  257 PREIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:cd05060 224 PQEIYSIMLSCWKYRPEDRPTFSELESTFRRDP 256
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
25-277 2.10e-32

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: 126.04  E-value: 2.10e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQG-LMIMKTVY-KGPNCIEHNEALlEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd08215  10 KGSFGSAYLVRRKSDGkLYVLKEIDlSNMSEKEREEAL-NEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYADGGDLAQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILE----IIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMwskLNNEEHnelre 178
Cdd:cd08215  89 KIKKQKKKGQPFPEEQILDwfvqICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGIS--KV---LESTTD----- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdgTAKKNGGTLYYMAPEHLNDvnaKP-TEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVDDIteYcP 257
Cdd:cd08215 159 ---LAKTVVGTPYYLSPELCEN---KPyNYKSDIWALGCVLYELCTLKHPFE-ANNLPALVYKIVKGQYPPIPSQ--Y-S 228
                       250       260
                ....*....|....*....|
gi 3426027  258 REIISLMKLCWEANPEARPT 277
Cdd:cd08215 229 SELRDLVNSMLQKDPEKRPS 248
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
55-284 2.45e-32

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: 125.63  E-value: 2.45e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTpLSVKG--RIILEIIEGMCYLHGK 132
Cdd:cd05041  35 DLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLLTFLRKKGAR-LTVKQllQMCLDAAAGMEYLESK 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnNEEHNELREVDGTAKKNggTLYYMAPEHLNdvNAKPTEKSDVY 212
Cdd:cd05041 114 NCIHRDLAARNCLVGENNVLKISDFGMS---------REEEDGEYTVSDGLKQI--PIKWTAPEALN--YGRYTSESDVW 180
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  213 SFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNR---PdvdditEYCPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd05041 181 SFGILLWEIFSlGATPYPG-MSNQQTREQIESGYRmpaP------ELCPEAVYRLMLQCWAYDPENRPSFSEIYNE 249
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
15-279 2.63e-32

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: 125.92  E-value: 2.63e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGL-MIMKTVYKGPNcIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRPSGQiMAVKVIRLEID-EALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnnee 172
Cdd:cd06605  80 YMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSG----------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelREVDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQ-----QLIMCIKSGNRP 247
Cdd:cd06605 149 ----QLVDSLAKTFVGTRSYMAPERIS--GGKYTVKSDIWSLGLSLVELATGRFPYPPPNAKPsmmifELLSYIVDEPPP 222
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  248 DVDdiTEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd06605 223 LLP--SGKFSPDFQDFVSQCLQKDPTERPSYK 252
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
60-295 3.66e-32

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: 127.00  E-value: 3.66e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEM--------------STPLSVKGRI--ILEI 122
Cdd:cd05099  64 LISEMELMKLIgKHKNIINLLGVCTQEGPLYVIVEYAAKGNLREFLRARRppgpdytfditkvpEEQLSFKDLVscAYQV 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTL--YYMAPEHLND 200
Cdd:cd05099 144 ARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADFGLA-------------RGVHDIDYYKKTSNGRLpvKWMAPEALFD 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  201 vnAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd05099 211 --RVYTHQSDVWSFGILMWEIFTlGGSPYP-GIPVEELFKLLREGHRMDK---PSNCTHELYMLMRECWHAVPTQRPTFK 284
                       250
                ....*....|....*.
gi 3426027  280 GIEEKFRPFYLSQLEE 295
Cdd:cd05099 285 QLVEALDKVLAAVSEE 300
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
15-218 3.67e-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: 125.94  E-value: 3.67e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCiEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd14046   6 TDFEELQVLGKGAFGQVVKVRNKLDGrYYAIKKIKLRSES-KNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKM-----WSKL 168
Cdd:cd14046  85 YCEKSTLRDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKlnvelATQD 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 NNEEHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVL 218
Cdd:cd14046 165 INKSTSAALGSSGDLTGNVGTALYVAPEVQSGTKSTYNEKVDMYSLGIIF 214
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
23-290 4.56e-32

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: 125.31  E-value: 4.56e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14154   1 LGKGFFGQAIKVTHRETGeVMVMKELIRFDE--EAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKaEMSTPLS--VKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEHNELREV 179
Cdd:cd14154  79 DVLK-DMARPLPwaQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLA------RLIVEERLPSGNM 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNG-------------GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAIceqqlimciksgnr 246
Cdd:cd14154 152 SPSETLRHlkspdrkkrytvvGNPYWMAPEMLN--GRSYDEKVDIFSFGIVLCEIIGRVEADPDYL-------------- 215
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  247 PDVDDIT-----------EYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYL 290
Cdd:cd14154 216 PRTKDFGlnvdsfrekfcAGCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYL 270
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
22-288 5.74e-32

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: 125.14  E-value: 5.74e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEhneALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGNLM 101
Cdd:cd05073  18 KLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVE---AFLAEANVMKTLQHDKLVKLHAVVTKEPIY-IITEFMAKGSLL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneEHNELREV 179
Cdd:cd05073  94 DFLKSDEGSKQPLPKLIDFsaQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVI--------EDNEYTAR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKnggtLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPDVddiTEYCPR 258
Cdd:cd05073 166 EGAKFP----IKWTAPEAIN--FGSFTIKSDVWSFGILLMEIVTyGRIPYP-GMSNPEVIRALERGYRMPR---PENCPE 235
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  259 EIISLMKLCWEANPEARPTFPGIEEKFRPF 288
Cdd:cd05073 236 ELYNIMMRCWKNRPEERPTFEYIQSVLDDF 265
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
23-283 6.00e-32

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: 124.53  E-value: 6.00e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKtVYKgpNCIEHNeALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14065   1 LGKGFFGEVYKVTHRETGkVMVMK-ELK--RFDEQR-SFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLK-AEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLAsfkmwsklnnEEHNELR 177
Cdd:cd14065  77 ELLKsMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLA----------REMPDEK 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKN---GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA--NKEPyENAICEQQLIMCIKSGNRPDVDDi 252
Cdd:cd14065 147 TKKPDRKKRltvVGSPYWMAPEMLR--GESYDEKVDVFSFGIVLCEIIGrvPADP-DYLPRTMDFGLDVRAFRTLYVPD- 222
                       250       260       270
                ....*....|....*....|....*....|.
gi 3426027  253 teyCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14065 223 ---CPPSFLPLAIRCCQLDPEKRPSFVELEH 250
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
22-286 7.72e-32

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: 125.47  E-value: 7.72e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKV------SLCFHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd05061  13 ELGQGSFGMVyegnarDIIKGEAETRVAVKTVNESASLRERIE-FLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVKGR----------IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmw 165
Cdd:cd05061  92 AHGDLKSYLRSLRPEAENNPGRppptlqemiqMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMT----- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  166 sklnneehNELREVDGTAKKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKE-PYENAICEQQLIMCIK 242
Cdd:cd05061 167 --------RDIYETDYYRKGGKGLLpvRWMAPESLKD--GVFTTSSDMWSFGVVLWEITSLAEqPYQGLSNEQVLKFVMD 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 3426027  243 SG--NRPdvdditEYCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05061 237 GGylDQP------DNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLK 276
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
22-286 1.30e-31

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: 124.50  E-value: 1.30e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSL--CFHRTQG----LMIMKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd05049  12 ELGEGAFGKVFLgeCYNLEPEqdkmLVAVKTL-KDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAE------MSTPLSVKGR--------IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaS 161
Cdd:cd05049  91 EHGDLNKFLRSHgpdaafLASEDSAPGEltlsqllhIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGM-S 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  162 FKMWSklnneehNELREVDGTAKKnggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMC 240
Cdd:cd05049 170 RDIYS-------TDYYRVGGHTML---PIRWMPPESI--LYRKFTTESDVWSFGVVLWEIFTyGKQPWFQ-LSNTEVIEC 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 3426027  241 IKSG---NRPdvdditEYCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05049 237 ITQGrllQRP------RTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
63-281 1.93e-31

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: 122.60  E-value: 1.93e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPE 142
Cdd:cd14059  31 DIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSP 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  143 NILVDNDFHIKIADLGlaSFKMWSklnneehnelrevDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAI 221
Cdd:cd14059 111 NVLVTYNDVLKISDFG--TSKELS-------------EKSTKMSfAGTVAWMAPEVIR--NEPCSEKVDIWSFGVVLWEL 173
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  222 FANKEPYENaICEQQLIMCIKSGN--RPdvddITEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14059 174 LTGEIPYKD-VDSSAIIWGVGSNSlqLP----VPSTCPDGFKLLMKQCWNSKPRNRPSFRQI 230
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
54-278 5.54e-31

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: 122.20  E-value: 5.54e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   54 IEHNEALLEEAKMMNRLRHSRVVKLLGVII-EEGKYSLVMEYMEKGNLMHVLKAEMSTPlSVKGRII--LEIIEGMCYLH 130
Cdd:cd05058  37 IEEVEQFLKEGIIMKDFSHPNVLSLLGICLpSEGSPLVVLPYMKHGDLRNFIRSETHNP-TVKDLIGfgLQVAKGMEYLA 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  131 GKGVIHKDLKPENILVDNDFHIKIADLGLASfKMWSKlnneehnelrEVDGTAKKNGGTL--YYMAPEHLNdvNAKPTEK 208
Cdd:cd05058 116 SKKFVHRDLAARNCMLDESFTVKVADFGLAR-DIYDK----------EYYSVHNHTGAKLpvKWMALESLQ--TQKFTTK 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  209 SDVYSFAVVLWAIFA-NKEPYenaiceqqlimciksgnrPDVD--DIT------------EYCPREIISLMKLCWEANPE 273
Cdd:cd05058 183 SDVWSFGVLLWELMTrGAPPY------------------PDVDsfDITvyllqgrrllqpEYCPDPLYEVMLSCWHPKPE 244

                ....*
gi 3426027  274 ARPTF 278
Cdd:cd05058 245 MRPTF 249
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
26-285 6.24e-31

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: 122.07  E-value: 6.24e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMImKTVYKGP--NCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd14146   5 GGFGKVYRATWKGQEVAV-KAARQDPdeDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGTLNRA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVKGRII---------LEIIEGMCYLHGKGV---IHKDLKPENIL----VDND----FHIKIADLGLAsfK 163
Cdd:cd14146  84 LAAANAAPGPRRARRIpphilvnwaVQIARGMLYLHEEAVvpiLHRDLKSSNILllekIEHDdicnKTLKITDFGLA--R 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 MWSKLnneehnelrevdgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEN--------AICEQ 235
Cdd:cd14146 162 EWHRT-------------TKMSAAGTYAWMAPEVIK--SSLFSKGSDIWSYGVLLWELLTGEVPYRGidglavayGVAVN 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  236 QLIMCIKSGnrpdvdditeyCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd14146 227 KLTLPIPST-----------CPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
62-281 1.96e-30

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: 120.06  E-value: 1.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRII--LEIIEGMCYLHGKG---VIH 136
Cdd:cd14060  31 KEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFDYLNSNESEEMDMDQIMTwaTDIAKGMHYLHMEApvkVIH 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFHIKIADLGLASFkmwsklnneeHNELREVDGTakkngGTLYYMAPEHLNDVnakPT-EKSDVYSFA 215
Cdd:cd14060 111 RDLKSRNVVIAADGVLKICDFGASRF----------HSHTTHMSLV-----GTFPWMAPEVIQSL---PVsETCDTYSYG 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  216 VVLWAIFANKEPYENAICEQQLIMCIKSGNRPDvddITEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14060 173 VVLWEMLTREVPFKGLEGLQVAWLVVEKNERPT---IPSSCPRSFAELMRRCWEADVKERPSFKQI 235
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
22-284 4.66e-30

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: 119.46  E-value: 4.66e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVyKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd05148  13 KLGSGYFGEVWEGLWKNRVRVAIKIL-KSDDLLKQQD-FQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELMEKGSLL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKA--EMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnneehneLREV 179
Cdd:cd05148  91 AFLRSpeGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARL-------------IKED 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAIcEQQLIMCIKSGNR---PdvdditEY 255
Cdd:cd05148 158 VYLSSDKKIPYKWTAPEAAS--HGTFSTKSDVWSFGILLYEMFTyGQVPYPGMN-NHEVYDQITAGYRmpcP------AK 228
                       250       260
                ....*....|....*....|....*....
gi 3426027  256 CPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd05148 229 CPQEIYKIMLECWAAEPEDRPSFKALREE 257
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
22-289 5.62e-30

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: 118.91  E-value: 5.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFH---RTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGvIIEEGKYSLVMEYMEKG 98
Cdd:cd05116   2 ELGSGNFGTVKKGYYqmkKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIG-ICEAESWMLVMEMAELG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLNNEEHNELRe 178
Cdd:cd05116  81 PLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGL------SKALRADENYYK- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdgtAKKNGG-TLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMcIKSGNRPDVddiTEYC 256
Cdd:cd05116 154 ----AQTHGKwPVKWYAPECMN--YYKFSSKSDVWSFGVLMWEAFSyGQKPYKGMKGNEVTQM-IEKGERMEC---PAGC 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  257 PREIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:cd05116 224 PPEMYDLMKLCWTYDVDERPGFAAVELRLRNYY 256
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
22-286 6.92e-30

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: 119.62  E-value: 6.92e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSL-CFHRTQ---GLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS--LVMEYM 95
Cdd:cd05080  11 DLGEGHFGKVSLyCYDPTNdgtGEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQGGKSlqLIMEYV 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwSKLNNEEHNE 175
Cdd:cd05080  91 PLGSLRDYL-PKHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAK----AVPEGHEYYR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 LREvDGTAKknggtLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYENA--------------ICEQQLIMCI 241
Cdd:cd05080 166 VRE-DGDSP-----VFWYAPECLKE--YKFYYASDVWSFGVTLYELLTHCDSSQSPptkflemigiaqgqMTVVRLIELL 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 3426027  242 KSGNR-PDVDDiteyCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05080 238 ERGERlPCPDK----CPQEVYHLMKNCWETEASFRPTFENLIPILK 279
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
23-277 7.61e-30

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: 118.73  E-value: 7.61e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLM-----IMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14098   8 LGSGTFAEVKKAVEVETGKMraikqIVKRKVAGND--KNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVMEYVEG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV--DNDFHIKIADLGLAsfKMwsklnneEHNe 175
Cdd:cd14098  86 GDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLA--KV-------IHT- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 lrevDGTAKKNGGTLYYMAPEHL--NDVNAKP--TEKSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKSGN---RPD 248
Cdd:cd14098 156 ----GTFLVTFCGTMAYLAPEILmsKEQNLQGgySNLVDMWSVGCLVYVMLTGALPFDGS-SQLPVEKRIRKGRytqPPL 230
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  249 VD-DITEycprEIISLMKLCWEANPEARPT 277
Cdd:cd14098 231 VDfNISE----EAIDFILRLLDVDPEKRMT 256
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
23-281 7.79e-30

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: 118.35  E-value: 7.79e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGP---NCIEHNeaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd14007   8 LGKGKFGNVYLAREKKSGFIVaLKVISKSQlqkSGLEHQ--LRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEYAPNG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmWS-KLNNEEHNELR 177
Cdd:cd14007  86 ELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG------WSvHAPSNRRKTFC 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdgtakkngGTLYYMAPEHlndVNAKP-TEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRpdvdDITEYC 256
Cdd:cd14007 160 ----------GTLDYLPPEM---VEGKEyDYKVDIWSLGVLCYELLVGKPPFE-SKSHQETYKRIQNVDI----KFPSSV 221
                       250       260
                ....*....|....*....|....*
gi 3426027  257 PREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14007 222 SPEAKDLISKLLQKDPSKRLSLEQV 246
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
15-277 8.73e-30

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: 118.93  E-value: 8.73e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGpNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd13996   6 NDFEEIELLGSGGFGSVYKVRNKVDGvTYAIKKIRLT-EKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQME 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVL-----KAEMSTPLSVkgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH-IKIADLGLASFkMWSK 167
Cdd:cd13996  85 LCEGGTLRDWIdrrnsSSKNDRKLAL--ELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDLqVKIGDFGLATS-IGNQ 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 LNNEEHNELREVDGTAKKN--GGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFAnkePYENAICEQQLIMCIKSGN 245
Cdd:cd13996 162 KRELNNLNNNNNGNTSNNSvgIGTPLYASPEQLDGENY--NEKADIYSLGIILFEMLH---PFKTAMERSTILTDLRNGI 236
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  246 RPdvDDITEYCPREiISLMKLCWEANPEARPT 277
Cdd:cd13996 237 LP--ESFKAKHPKE-ADLIQSLLSKNPEERPS 265
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
25-284 8.94e-30

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: 118.35  E-value: 8.94e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQG-LMIMKTvykgpNCIEHNEA-LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14155   3 SGFFSEVYKVRHRTSGqVMALKM-----NTLSSNRAnMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLEQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLAsfkmwSKL-NNEEHNELRE 178
Cdd:cd14155  78 LLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLA-----EKIpDYSDGKEKLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGTAkknggtlYYMAPEHLNDvnAKPTEKSDVYSFAVVLwaifankepyenaiCEqqLIMCIKSGnrPDVDDITEY--- 255
Cdd:cd14155 153 VVGSP-------YWMAPEVLRG--EPYNEKADVFSYGIIL--------------CE--IIARIQAD--PDYLPRTEDfgl 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 3426027  256 -----------CPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd14155 206 dydafqhmvgdCPPDFLQLAFNCCNMDPKSRPSFHDIVKT 245
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
61-281 1.60e-29

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: 117.86  E-value: 1.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKA--EMSTPLSVKGrIILEIIEGMCYLHGKGVIHKD 138
Cdd:cd05033  53 LTEASIMGQFDHPNVIRLEGVVTKSRPVMIVTEYMENGSLDKFLREndGKFTVTQLVG-MLRGIASGMKYLSEMNYVHRD 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  139 LKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGG--TLYYMAPEHLNdvNAKPTEKSDVYSFAV 216
Cdd:cd05033 132 LAARNILVNSDLVCKVSDFGLS-------------RRLEDSEATYTTKGGkiPIRWTAPEAIA--YRKFTSASDVWSFGI 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  217 VLWAIFANKE-PYENaICEQQLIMCIKSGNR--PDVDditeyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05033 197 VMWEVMSYGErPYWD-MSNQDVIKAVEDGYRlpPPMD-----CPSALYQLMLDCWQKDRNERPTFSQI 258
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
62-277 2.55e-29

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: 117.72  E-value: 2.55e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEegKYSLVMEYMEKGNLMHVLK--AEMSTPLS--VKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd14000  59 QELTVLSHLHHPSIVYLLGIGIH--PLMLVLELAPLGSLDHLLQqdSRSFASLGrtLQQRIALQVADGLRYLHSAMIIYR 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILV-----DNDFHIKIADLGLA--SFKMwsklnneehnelrevdgTAKKNGGTLYYMAPEhLNDVNAKPTEKSD 210
Cdd:cd14000 137 DLKSHNVLVwtlypNSAIIIKIADYGISrqCCRM-----------------GAKGSEGTPGFRAPE-IARGNVIYNEKVD 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  211 VYSFAVVLWAIFANKEPYENaicEQQLIMCIK--SGNRPDVDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14000 199 VFSFGMLLYEILSGGAPMVG---HLKFPNEFDihGGLRPPLKQYECAPWPEVEVLMKKCWKENPQQRPT 264
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
22-282 3.83e-29

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: 116.66  E-value: 3.83e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14069   8 TLGEGAFGEVFLAVNRnTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYASGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS-FKMwsklNNEEhnelREV 179
Cdd:cd14069  88 FDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATvFRY----KGKE----RLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAkkngGTLYYMAPEhlndVNAKPT---EKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDvdditeYC 256
Cdd:cd14069 160 NKMC----GTLPYVAPE----LLAKKKyraEPVDVWSCGIVLFAMLAGELPWDQPSDSCQEYSDWKENKKTY------LT 225
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  257 PREIIS------LMKLCWEaNPEARPTFPGIE 282
Cdd:cd14069 226 PWKKIDtaalslLRKILTE-NPNKRITIEDIK 256
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
23-292 5.02e-29

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: 116.58  E-value: 5.02e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKgpnCIEHNE-ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14222   1 LGKGFFGQAIKVTHKATGkVMVMKELIR---CDEETQkTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLN---NEEHNELR 177
Cdd:cd14222  78 KDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKpppDKPTTKKR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKNG----GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFAnkEPYENAICeqqLIMCIKSG--NRPDVDD 251
Cdd:cd14222 158 TLRKNDRKKRytvvGNPYWMAPEMLN--GKSYDEKVDIFSFGIVLCEIIG--QVYADPDC---LPRTLDFGlnVRLFWEK 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 3426027  252 -ITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLSQ 292
Cdd:cd14222 231 fVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEALSLYL 272
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
55-278 9.22e-29

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: 115.41  E-value: 9.22e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMStplSVKGRIILEIIE----GMCYLH 130
Cdd:cd05084  36 DLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFLTFLRTEGP---RLKVKELIRMVEnaaaGMEYLE 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  131 GKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnelREVDGTAKKNGGT----LYYMAPEHLNdvNAKPT 206
Cdd:cd05084 113 SKHCIHRDLAARNCLVTEKNVLKISDFGMSR---------------EEEDGVYAATGGMkqipVKWTAPEALN--YGRYS 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  207 EKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05084 176 SESDVWSFGILLWETFSlGAVPYAN-LSNQQTREAVEQGVRLPC---PENCPDEVYRLMEQCWEYDPRKRPSF 244
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
15-277 1.19e-28

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: 115.38  E-value: 1.19e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGLMI-MKTVYkGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRHKPTGKIYaLKKIH-VDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNNee 172
Cdd:cd06623  80 YMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKV-----LEN-- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelrevdGTAKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQL-IMC-IKSGNRPD 248
Cdd:cd06623 153 --------TLDQCNTfvGTVTYMSPERIQ--GESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFeLMQaICDGPPPS 222
                       250       260
                ....*....|....*....|....*....
gi 3426027  249 VDDITeyCPREIISLMKLCWEANPEARPT 277
Cdd:cd06623 223 LPAEE--FSPEFRDFISACLQKDPKKRPS 249
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
60-285 1.28e-28

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: 115.13  E-value: 1.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVIIEEgKYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKD 138
Cdd:cd05040  45 FLKEVNAMHSLDHPNLIRLYGVVLSS-PLMMVTELAPLGSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  139 LKPENILVDNDFHIKIADLGLasfkMWSKLNNEEH---NELREVdgtakknggTLYYMAPEHLNdvNAKPTEKSDVYSFA 215
Cdd:cd05040 124 LAARNILLASKDKVKIGDFGL----MRALPQNEDHyvmQEHRKV---------PFAWCAPESLK--TRKFSHASDVWMFG 188
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  216 VVLWAIFAN-KEPYEnAICEQQLIMCI-KSGNR---PDvdditeYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05040 189 VTLWEMFTYgEEPWL-GLNGSQILEKIdKEGERlerPD------DCPQDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
10-286 2.97e-28

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: 114.78  E-value: 2.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   10 IKMKSSDFLEsaELDSGGFGKV--------SLCFHRTQglMIMKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGV 81
Cdd:cd05048   2 IPLSAVRFLE--ELGEGAFGKVykgellgpSSEESAIS--VAIKTL-KENASPKTQQDFRREAELMSDLQHPNIVCLLGV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   82 IIEEGKYSLVMEYMEKGNL-----MHVLKAEMSTPLSVKG-----------RIILEIIEGMCYLHGKGVIHKDLKPENIL 145
Cdd:cd05048  77 CTKEQPQCMLFEYMAHGDLheflvRHSPHSDVGVSSDDDGtassldqsdflHIAIQIAAGMEYLSSHHYVHRDLAARNCL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  146 VDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDgtakknggtlyYMAPEHLndVNAKPTEKSDVYSFAVVLWAIF--- 222
Cdd:cd05048 157 VGDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVR-----------WMPPEAI--LYGKFTTESDVWSFGVVLWEIFsyg 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  223 -------ANKEPYEnAICEQQLIMCiksgnrpdvddiTEYCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05048 224 lqpyygySNQEVIE-MIRSRQLLPC------------PEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLR 281
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
23-277 3.01e-28

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: 114.04  E-value: 3.01e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEA---LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd06632   8 LGSGSFGSVYEGFNGDTGDFFaVKEVSLVDDDKKSRESvkqLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSklnneehnelre 178
Cdd:cd06632  88 SIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAF------------ 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENaiCEQQLIMcIKSGNRPDVDDITEYCPR 258
Cdd:cd06632 156 --SFAKSFKGSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQ--YEGVAAI-FKIGNSGELPPIPDHLSP 230
                       250
                ....*....|....*....
gi 3426027  259 EIISLMKLCWEANPEARPT 277
Cdd:cd06632 231 DAKDFIRLCLQRDPEDRPT 249
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
22-278 3.52e-28

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: 113.47  E-value: 3.52e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGNLM 101
Cdd:cd14203   2 KLGQGCFGEVWMGTWNGTTKVAIKTLKPG---TMSPEAFLEEAQIMKKLRHDKLVQLYAVVSEEPIY-IVTEFMSKGSLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneEHNELrev 179
Cdd:cd14203  78 DFLKDGEGKYLKLPQLVDMaaQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI--------EDNEY--- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 dgTAKKNGG-TLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFAN-KEPYEnAICEQQLIMCIKSGNRPDVddiTEYCP 257
Cdd:cd14203 147 --TARQGAKfPIKWTAPEAA--LYGRFTIKSDVWSFGILLTELVTKgRVPYP-GMNNREVLEQVERGYRMPC---PPGCP 218
                       250       260
                ....*....|....*....|.
gi 3426027  258 REIISLMKLCWEANPEARPTF 278
Cdd:cd14203 219 ESLHELMCQCWRKDPEERPTF 239
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
23-281 4.06e-28

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: 114.89  E-value: 4.06e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKV--SLCFHRTQGLMIMKTVYKGPNCIEH---NEALLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd05055  43 LGAGAFGKVveATAYGLSKSDAVMKVAVKMLKPTAHsseREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYCC 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneeHN 174
Cdd:cd05055 123 YGDLLNFLRRKRESFLTLEDLLSFsyQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIM--------ND 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 ELREVDGTAKKnggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNRPDVddiT 253
Cdd:cd05055 195 SNYVVKGNARL---PVKWMAPESI--FNCVYTFESDVWSYGILLWEIFSlGSNPYPGMPVDSKFYKLIKEGYRMAQ---P 266
                       250       260
                ....*....|....*....|....*...
gi 3426027  254 EYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05055 267 EHAPAEIYDIMKTCWDADPLKRPTFKQI 294
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
23-285 5.23e-28

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: 114.05  E-value: 5.23e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGkvslcfhrtqglmimkTVYKG-------PNCIE-------------HNEALLEEAKMMNRLRHSRVVKLLGVI 82
Cdd:cd05057  15 LGSGAFG----------------TVYKGvwipegeKVKIPvaikvlreetgpkANEEILDEAYVMASVDHPHLVRLLGIC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   83 IEEgKYSLVMEYMEKGNLMHVLKAEMSTplsVKGRIIL----EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLG 158
Cdd:cd05057  79 LSS-QVQLITQLMPLGCLLDYVRNHRDN---IGSQLLLnwcvQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  159 LAsfKMWSKLNNEEHNElrevdgtakknGGT--LYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQ 235
Cdd:cd05057 155 LA--KLLDVDEKEYHAE-----------GGKvpIKWMALESIQ--YRIYTHKSDVWSYGVTVWELMTfGAKPYEG-IPAV 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 3426027  236 QLIMCIKSGNR---PDVDDITEYCpreiisLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05057 219 EIPDLLEKGERlpqPPICTIDVYM------VLVKCWMIDAESRPTFKELANEF 265
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
27-277 5.31e-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: 113.68  E-value: 5.31e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   27 GFGKVSLCFH----RTQGLMIMKTVYKGPNCIEHN----EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd06630   9 GTGAFSSCYQardvKTGTLMAVKQVSFCRNSSSEQeevvEAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDND-FHIKIADLGLASfKMWSKLNneehnelr 177
Cdd:cd06630  89 SVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGAAA-RLASKGT-------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdGTAKKNG---GTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYEN-AICEQ-QLIMCIKSGNRPdvDDI 252
Cdd:cd06630 160 ---GAGEFQGqllGTIAFMAPEVLRGEQYG--RSCDVWSVGCVIIEMATAKPPWNAeKISNHlALIFKIASATTP--PPI 232
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd06630 233 PEHLSPGLRDVTLRCLELQPEDRPP 257
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
55-278 5.35e-28

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: 113.60  E-value: 5.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMeKGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGK 132
Cdd:cd14063  38 EQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLC-KGRTLYSLIHERKEKFDFNKtvQIAQQICQGMGYLHAK 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPENILVDNDfHIKIADLGLasFKMwSKLNNEehnelREVDGTAKKNGGTLYYMAPEHLNDVNA-------KP 205
Cdd:cd14063 117 GIIHKDLKSKNIFLENG-RVVITDFGL--FSL-SGLLQP-----GRREDTLVIPNGWLCYLAPEIIRALSPdldfeesLP 187
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  206 -TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMcIKSGNRPDVDDITEycPREIISLMKLCWEANPEARPTF 278
Cdd:cd14063 188 fTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQ-VGCGKKQSLSQLDI--GREVKDILMQCWAYDPEKRPTF 258
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
25-281 5.95e-28

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: 113.57  E-value: 5.95e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLC-FHRTQGLMIMKTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGkYSLVMEYMEKGNL--- 100
Cdd:cd14150  10 TGSFGTVFRGkWHGDVAVKILKVTEPTP---EQLQAFKNEMQVLRKTRHVNILLFMGFMTRPN-FAIITQWCEGSSLyrh 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKM-WSKLNNEEhnelrev 179
Cdd:cd14150  86 LHVTETRFDTMQLID--VARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTrWSGSQQVE------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 dgtakKNGGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGN-RPDVDDITEYCP 257
Cdd:cd14150 157 -----QPSGSILWMAPEVIRMQDTNPySFQSDVYAYGVVLYELMSGTLPYSNINNRDQIIFMVGRGYlSPDLSKLSSNCP 231
                       250       260
                ....*....|....*....|....
gi 3426027  258 REIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14150 232 KAMKRLLIDCLKFKREERPLFPQI 255
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
58-278 6.90e-28

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: 113.29  E-value: 6.90e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGNLMHVLKAEM-STPLSVKGRIILEIIEGMCYLHGKGVIH 136
Cdd:cd05056  52 EKFLQEAYIMRQFDHPHIVKLIGVITENPVW-IVMELAPLGELRSYLQVNKySLDLASLILYAYQLSTALAYLESKRFVH 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFHIKIADLGLASFkmwskLNNEEHNelrevdgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAV 216
Cdd:cd05056 131 RDIAARNVLVSSPDCVKLGDFGLSRY-----MEDESYY-------KASKGKLPIKWMAPESIN--FRRFTSASDVWMFGV 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  217 VLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPdvdDITEYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05056 197 CMWEILMlGVKPFQ-GVKNNDVIGRIENGERL---PMPPNCPPTLYSLMTKCWAYDPSKRPRF 255
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
25-287 9.88e-28

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: 112.62  E-value: 9.88e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE-GKYSLVMEYMEKGNLMHV 103
Cdd:cd14064   3 SGSFGKVYKGRCRNKIVAIKRYRANTYCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDpSQFAIVTQYVSGGSLFSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMST-PLSVKGRIILEIIEGMCYLHG--KGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklNNEEHNelrevd 180
Cdd:cd14064  83 LHEQKRViDLQSKLIIAVDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQ----SLDEDN------ 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  181 gtAKKNGGTLYYMAPEHLNDvNAKPTEKSDVYSFAVVLWAIFANKEPYEN-----AICEqqliMCIKSGNRPdvddITEY 255
Cdd:cd14064 153 --MTKQPGNLRWMAPEVFTQ-CTRYSIKADVFSYALCLWELLTGEIPFAHlkpaaAAAD----MAYHHIRPP----IGYS 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  256 CPREIISLMKLCWEANPEARPTFPGIEEKFRP 287
Cdd:cd14064 222 IPKPISSLLMRGWNAEPESRPSFVEIVALLEP 253
Pkinase pfam00069
Protein kinase domain;
22-279 1.09e-27

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 111.18  E-value: 1.09e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     22 ELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:pfam00069   6 KLGSGSFGTVYKAKHRdTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    101 MHVLKAEMSTPLSVKGRIILEIIEGMcylhgkgvihkdlkpenilvdndfhikiadlglasfkmwsklnnEEHNELREVD 180
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGL--------------------------------------------ESGSSLTTFV 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    181 gtakkngGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPdvDDITEYCPREI 260
Cdd:pfam00069 122 -------GTPWYMAPEVLGGNPY--GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAF--PELPSNLSEEA 190
                         250
                  ....*....|....*....
gi 3426027    261 ISLMKLCWEANPEARPTFP 279
Cdd:pfam00069 191 KDLLKKLLKKDPSKRLTAT 209
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
25-277 1.09e-27

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: 112.78  E-value: 1.09e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd06626  10 EGTFGKVYTAVNLDTGeLMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLEEL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLNNEEHNELREVDGTA 183
Cdd:cd06626  90 LRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG-SAVKLKNNTTTMAPGEVNSLVGTP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  184 KknggtlyYMAPEHLNdvNAKPTEK---SDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPrEI 260
Cdd:cd06626 169 A-------YMAPEVIT--GNKGEGHgraADIWSLGCVVLEMATGKRPWSELDNEWAIMYHVGMGHKPPIPDSLQLSP-EG 238
                       250
                ....*....|....*..
gi 3426027  261 ISLMKLCWEANPEARPT 277
Cdd:cd06626 239 KDFLSRCLESDPKKRPT 255
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
60-283 1.89e-27

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: 113.18  E-value: 1.89e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEM-----------STP---LSVKGRI--ILEI 122
Cdd:cd05098  65 LISEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRppgmeycynpsHNPeeqLSSKDLVscAYQV 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTL--YYMAPEHLND 200
Cdd:cd05098 145 ARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLA-------------RDIHHIDYYKKTTNGRLpvKWMAPEALFD 211
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  201 vnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEqQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd05098 212 --RIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVE-ELFKLLKEGHRMDK---PSNCTNELYMMMRDCWHAVPSQRPTFK 285

                ....
gi 3426027  280 GIEE 283
Cdd:cd05098 286 QLVE 289
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
22-278 2.85e-27

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: 111.49  E-value: 2.85e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCiehNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd05114  11 ELGSGLFGVVRLGKWRAQYKVAIKAIREGAMS---EEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVL---KAEMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneehnelre 178
Cdd:cd05114  88 NYLrqrRGKLSRDMLLS--MCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVL-------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vDGTAKKNGGTLY---YMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFAN-KEPYENAiCEQQLIMCIKSGNR---PDVdd 251
Cdd:cd05114 152 -DDQYTSSSGAKFpvkWSPPEVFN--YSKFSSKSDVWSFGVLMWEVFTEgKMPFESK-SNYEVVEMVSRGHRlyrPKL-- 225
                       250       260
                ....*....|....*....|....*..
gi 3426027  252 iteyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05114 226 ----ASKSVYEVMYSCWHEKPEGRPTF 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
23-277 7.18e-27

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: 110.28  E-value: 7.18e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVslcfhrTQGLMIMKTVY-----KGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14664   1 IGRGGAGTV------YKGVMPNGTLVavkrlKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVL--KAEMSTPL--SVKGRIILEIIEGMCYLH---GKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNN 170
Cdd:cd14664  75 GSLGELLhsRPESQPPLdwETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKL-----MDD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 EEHNELREVdgtakknGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIM----------- 239
Cdd:cd14664 150 KDSHVMSSV-------AGSYGYIAPEYAY--TGKVSEKSDVYSYGVVLLELITGKRPFDEAFLDDGVDIvdwvrglleek 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 3426027  240 CIKSGNRPDVDDIteYCPREIISLMK---LCWEANPEARPT 277
Cdd:cd14664 221 KVEALVDPDLQGV--YKLEEVEQVFQvalLCTQSSPMERPT 259
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
26-285 7.32e-27

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: 110.08  E-value: 7.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMImKTVYKGP--NCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd14148   5 GGFGKVYKGLWRGEEVAV-KAARQDPdeDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGALNRA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LkAEMSTPLSVKGRIILEIIEGMCYLHGKG---VIHKDLKPENIL----VDND----FHIKIADLGLAsfKMWSKLnnee 172
Cdd:cd14148  84 L-AGKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSNILilepIENDdlsgKTLKITDFGLA--REWHKT---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelrevdgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEN--------AICEQQLIMCIKSG 244
Cdd:cd14148 157 ---------TKMSAAGTYAWMAPEVIR--LSLFSKSSDVWSFGVLLWELLTGEVPYREidalavayGVAMNKLTLPIPST 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 3426027  245 nrpdvdditeyCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd14148 226 -----------CPEPFARLLEECWDPDPHGRPDFGSILKRL 255
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
20-278 7.47e-27

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 110.51  E-value: 7.47e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   20 SAELDSGGFGKV------SLCFHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd05062  11 SRELGQGSFGMVyegiakGVVKDEPETRVAIKTVNEAASMRERIE-FLNEASVMKEFNCHHVVRLLGVVSQGQPTLVIME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNL---MHVLKAEMS-----TPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfk 163
Cdd:cd05062  90 LMTRGDLksyLRSLRPEMEnnpvqAPPSLKKMIQMagEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFGMT--- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 mwsklnneehNELREVDGTAKKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMC 240
Cdd:cd05062 167 ----------RDIYETDYYRKGGKGLLpvRWMSPESLKD--GVFTTYSDVWSFGVVLWEIATlAEQPYQGMSNEQVLRFV 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 3426027  241 IKSG--NRPDvdditeYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05062 235 MEGGllDKPD------NCPDMLFELMRMCWQYNPKMRPSF 268
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
58-277 8.16e-27

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: 109.62  E-value: 8.16e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06627  44 KSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHR 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwSKLnNEEHNELREVDGTAkknggtlYYMAPEHLNDVNAkpTEKSDVYSFAVV 217
Cdd:cd06627 124 DIKGANILTTKDGLVKLADFGVA-----TKL-NEVEKDENSVVGTP-------YWMAPEVIEMSGV--TTASDIWSVGCT 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  218 LWAIFANKEPYENAiceQQL--IMCIKSGNRPdvdDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd06627 189 VIELLTGNPPYYDL---QPMaaLFRIVQDDHP---PLPENISPELRDFLLQCFQKDPTLRPS 244
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
22-281 1.21e-26

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: 110.31  E-value: 1.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKV------SLCFHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd05050  12 DIGQGAFGRVfqarapGLLPYEPFTMVAVKMLKEEASADMQAD-FQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKA------------------------EMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH 151
Cdd:cd05050  91 AYGDLNEFLRHrspraqcslshstssarkcglnplPLSCTEQLC--IAKQVAAGMAYLSERKFVHRDLATRNCLVGENMV 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  152 IKIADLGLaSFKMWS----KLNNEEHNELRevdgtakknggtlyYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKE 226
Cdd:cd05050 169 VKIADFGL-SRNIYSadyyKASENDAIPIR--------------WMPPESI--FYNRYTTESDVWAYGVVLWEIFSyGMQ 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  227 PYEnAICEQQLIMCIKSGNrpdVDDITEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05050 232 PYY-GMAHEEVIYYVRDGN---VLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
26-277 1.49e-26

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: 109.39  E-value: 1.49e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHN--------EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd06629  12 GTYGRVYLAMNATTGEMLaVKQVELPKTSSDRAdsrqktvvDALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIFLEYVP 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLNNEEHNEL 176
Cdd:cd06629  92 GGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFG-ISKKSDDIYGNNGATSM 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 RevdgtakkngGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENaicEQQLIMCIKSGN---RPDVDDIT 253
Cdd:cd06629 171 Q----------GSVFWMAPEVIHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSD---DEAIAAMFKLGNkrsAPPVPEDV 237
                       250       260
                ....*....|....*....|....
gi 3426027  254 EYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd06629 238 NLSP-EALDFLNACFAIDPRDRPT 260
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
67-286 1.63e-26

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-2D is allso called Retinal Guanylyl Cyclase 1 (RETGC-1) or Rod Outer Segment membrane Guanylate Cyclase (ROS-GC). It is found in the photoreceptors of the retina where it anchors the reciprocal feedback loop between calcium and cGMP, which regulates the dark, light, and recovery phases in phototransduction. It is also found in other sensory neurons and may be a universal transduction component that plays a role in the perception of all senses. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-2D subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 109.42  E-value: 1.63e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   67 MNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAE-MSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENIL 145
Cdd:cd14043  50 LRELRHENVNLFLGLFVDCGILAIVSEHCSRGSLEDLLRNDdMKLDWMFKSSLLLDLIKGMRYLHHRGIVHGRLKSRNCV 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  146 VDNDFHIKIADLGLASFKmwsklnnEEHNELREvdgtaKKNGGTLYYMAPEHLNDVNA--KPTEKSDVYSFAVVLWAIFA 223
Cdd:cd14043 130 VDGRFVLKITDYGYNEIL-------EAQNLPLP-----EPAPEELLWTAPELLRDPRLerRGTFPGDVFSFAIIMQEVIV 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  224 NKEPY-ENAICEQQLIMCIKSGN---RPDVDdiTEYCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd14043 198 RGAPYcMLGLSPEEIIEKVRSPPplcRPSVS--MDQAPLECIQLMKQCWSEAPERRPTFDQIFDQFK 262
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
60-295 2.41e-26

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: 110.10  E-value: 2.41e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKA------EMS--------TPLSVKGRI--ILEI 122
Cdd:cd05101  76 LVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRArrppgmEYSydinrvpeEQMTFKDLVscTYQL 155
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTL--YYMAPEHLND 200
Cdd:cd05101 156 ARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLA-------------RDINNIDYYKKTTNGRLpvKWMAPEALFD 222
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  201 vnAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd05101 223 --RVYTHQSDVWSFGVLMWEIFTlGGSPYP-GIPVEELFKLLKEGHRMDK---PANCTNELYMMMRDCWHAVPSQRPTFK 296
                       250
                ....*....|....*..
gi 3426027  280 GIEEKF-RPFYLSQLEE 295
Cdd:cd05101 297 QLVEDLdRILTLTTNEE 313
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
22-285 2.60e-26

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: 109.25  E-value: 2.60e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQG-----LMIMKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS--LVMEY 94
Cdd:cd05079  11 DLGEGHFGKVELCRYDPEGdntgeQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGikLIMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwSKLNNEEH 173
Cdd:cd05079  90 LPSGSLKEYLpRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK----AIETDKEY 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 NELREvdgtakKNGGTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAI--FANKE------------PYENAICEQQLIM 239
Cdd:cd05079 166 YTVKD------DLDSPVFWYAPECL--IQSKFYIASDVWSFGVTLYELltYCDSEsspmtlflkmigPTHGQMTVTRLVR 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 3426027  240 CIKSGNR-PDVDDiteyCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05079 238 VLEEGKRlPRPPN----CPEEVYQLMRKCWEFQPSKRTTFQNLIEGF 280
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
23-282 3.76e-26

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: 108.12  E-value: 3.76e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14221   1 LGKGCFGQAIKVTHRETGeVMVMKELIRFDE--ETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKA-EMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVD 180
Cdd:cd14221  79 GIIKSmDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKKPD 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  181 GTAKKN-GGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFA--NKEPyenaiceQQLIMCIKSGNRPDVdDITEYCP 257
Cdd:cd14221 159 RKKRYTvVGNPYWMAPEMINGRSYD--EKVDVFSFGIVLCEIIGrvNADP-------DYLPRTMDFGLNVRG-FLDRYCP 228
                       250       260
                ....*....|....*....|....*....
gi 3426027  258 RE----IISLMKLCWEANPEARPTFPGIE 282
Cdd:cd14221 229 PNcppsFFPIAVLCCDLDPEKRPSFSKLE 257
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
23-285 4.68e-26

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: 107.69  E-value: 4.68e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14009   1 IGRGSFATVWKGRHKQTGEVVaIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLASFkmwsklnneehnelRE 178
Cdd:cd14009  81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARS--------------LQ 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIKSGNRPDVDDITEYCPR 258
Cdd:cd14009 147 PASMAETLCGSPLYMAPEILQ--FQKYDAKADLWSVGAILFEMLVGKPPF-RGSNHVQLLRNIERSDAVIPFPIAAQLSP 223
                       250       260
                ....*....|....*....|....*..
gi 3426027  259 EIISLMKLCWEANPEARPTFpgiEEKF 285
Cdd:cd14009 224 DCKDLLRRLLRRDPAERISF---EEFF 247
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
60-285 5.03e-26

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: 107.40  E-value: 5.03e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL---KAEMSTPLSVKgrIILEIIEGMCYLHGKGVIH 136
Cdd:cd05085  40 FLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFLSFLrkkKDELKTKQLVK--FSLDAAAGMAYLESKNCIH 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNGG----TLYYMAPEHLNdvNAKPTEKSDVY 212
Cdd:cd05085 118 RDLAARNCLVGENNALKISDFGMS----------------RQEDDGVYSSSGlkqiPIKWTAPEALN--YGRYSSESDVW 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  213 SFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05085 180 SFGILLWETFSlGVCPYP-GMTNQQAREQVEKGYRMSA---PQRCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
12-286 5.30e-26

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: 108.13  E-value: 5.30e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   12 MKSSDFLESAELDSGGFGKVSL--CFHRT----QGLMIMKTVYKGPNCIEHNeaLLEEAKMMNRLRHSRVVKLLGVIIEE 85
Cdd:cd05092   2 IKRRDIVLKWELGEGAFGKVFLaeCHNLLpeqdKMLVAVKALKEATESARQD--FQREAELLTVLQHQHIVRFYGVCTEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEYMEKGNLMHVLKA-----------EMSTP----LSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF 150
Cdd:cd05092  80 EPLIMVFEYMRHGDLNRFLRShgpdakildggEGQAPgqltLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  151 HIKIADLGLAsfkmwsklnneehnelREVDGT--AKKNGGTLY---YMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-N 224
Cdd:cd05092 160 VVKIGDFGMS----------------RDIYSTdyYRVGGRTMLpirWMPPESI--LYRKFTTESDIWSFGVVLWEIFTyG 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  225 KEPYENaICEQQLIMCIKSG---NRPDVdditeyCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05092 222 KQPWYQ-LSNTEAIECITQGrelERPRT------CPPEVYAIMQGCWQREPQQRHSIKDIHSRLQ 279
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
23-277 5.37e-26

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: 107.44  E-value: 5.37e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIE---HNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd06625   8 LGQGAFGQVYLCYDAdTGRELAVKQVEIDPINTEaskEVKALECEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYMPGG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLNneeHNELRE 178
Cdd:cd06625  88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFG-ASKRLQTICS---STGMKS 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGTAkknggtlYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDV-DDITEYCP 257
Cdd:cd06625 164 VTGTP-------YWMSPEVIN--GEGYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIATQPTNPQLpPHVSEDAR 234
                       250       260
                ....*....|....*....|
gi 3426027  258 ReiisLMKLCWEANPEARPT 277
Cdd:cd06625 235 D----FLSLIFVRNKKQRPS 250
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
10-286 5.50e-26

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: 108.18  E-value: 5.50e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   10 IKMKSSDFLEsaELDSGGFGKV-------SLCFHRTQGLMImKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVI 82
Cdd:cd05091   3 INLSAVRFME--ELGEDRFGKVykghlfgTAPGEQTQAVAI-KTL-KDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   83 IEEGKYSLVMEYMEKGNLMHVLKaeMSTPLSVKG------------------RIILEIIEGMCYLHGKGVIHKDLKPENI 144
Cdd:cd05091  79 TKEQPMSMIFSYCSHGDLHEFLV--MRSPHSDVGstdddktvkstlepadflHIVTQIAAGMEYLSSHHVVHKDLATRNV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  145 LVDNDFHIKIADLGLasfkmwsklnneehneLREVDGT--AKKNGGTLY---YMAPEHLndVNAKPTEKSDVYSFAVVLW 219
Cdd:cd05091 157 LVFDKLNVKISDLGL----------------FREVYAAdyYKLMGNSLLpirWMSPEAI--MYGKFSIDSDIWSYGVVLW 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  220 AIFA-NKEPYeNAICEQQLIMCIKsgNR---PDVDDiteyCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05091 219 EVFSyGLQPY-CGYSNQDVIEMIR--NRqvlPCPDD----CPAWVYTLMLECWNEFPSRRPRFKDIHSRLR 282
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
23-279 5.87e-26

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: 107.82  E-value: 5.87e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFH-RTQGLMIMKTVYK-GPNCIEHNEAL----LEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd13993   8 IGEGAYGVVYLAVDlRTGRKYAIKCLYKsGPNSKDGNDFQklpqLREIDLHRRVsRHPNIITLHDVFETEVAIYIVLEYC 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLS---VKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF-HIKIADLGLASFKMWSklnne 171
Cdd:cd13993  88 PNGDLFEAITENRIYVGKtelIK-NVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCDFGLATTEKIS----- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelREVdgtakkNGGTLYYMAPEHLNDVNAK----PTEKSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKSGNRP 247
Cdd:cd13993 162 -----MDF------GVGSEFYMAPECFDEVGRSlkgyPCAAGDIWSLGIILLNLTFGRNPWKIA-SESDPIFYDYYLNSP 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  248 DVDDITEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd13993 230 NLFDVILPMSDDFYNLLRQIFTVNPNNRILLP 261
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
18-291 6.25e-26

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: 107.72  E-value: 6.25e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   18 LESAELDSGGFGKVSlcfhrtQGLMIMKT--------VYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGkYS 89
Cdd:cd05115   7 IDEVELGSGNFGCVK------KGVYKMRKkqidvaikVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMST-PLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKL 168
Cdd:cd05115  80 LVMEMASGGPLNKFLSGKKDEiTVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGL------SKA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 NNEEHNELrevdgTAKKNGG-TLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNR 246
Cdd:cd05115 154 LGADDSYY-----KARSAGKwPLKWYAPECIN--FRKFSSRSDVWSYGVTMWEAFSyGQKPYKK-MKGPEVMSFIEQGKR 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 3426027  247 PDVddiTEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLS 291
Cdd:cd05115 226 MDC---PAECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRTYYYS 267
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
23-285 6.64e-26

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: 108.13  E-value: 6.64e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCF-HRTQGL-----MIMKTVYKGPNCIEHnEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd05045   8 LGEGEFGKVVKATaFRLKGRagyttVAVKMLKENASSSEL-RDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLK----------------------AEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHI 152
Cdd:cd05045  87 YGSLRSFLResrkvgpsylgsdgnrnssyldNPDERALTMGDLISFawQISRGMQYLAEMKLVHRDLAARNVLVAEGRKM 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  153 KIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTL--YYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYE 229
Cdd:cd05045 167 KISDFGLS-------------RDVYEEDSYVKRSKGRIpvKWMAIESLFD--HIYTTQSDVWSFGVLLWEIVTlGGNPYP 231
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  230 nAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05045 232 -GIAPERLFNLLKTGYRMER---PENCSEEMYNLMLTCWKQEPDKRPTFADISKEL 283
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
21-282 9.02e-26

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: 107.67  E-value: 9.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFH-----RTQGLMIMKTVYKgpNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS--LVME 93
Cdd:cd05081  10 SQLGKGNFGSVELCRYdplgdNTGALVAVKQLQH--SGPDQQRDFQREIQILKALHSDFIVKYRGVSYGPGRRSlrLVME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTplsVKGRIIL----EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKln 169
Cdd:cd05081  88 YLPSGCLRDFLQRHRAR---LDASRLLlyssQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLPLDK-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neEHNELREvdgtakKNGGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIF--ANK--------------EPYENAIC 233
Cdd:cd05081 163 --DYYVVRE------PGQSPIFWYAPESLSD--NIFSRQSDVWSFGVVLYELFtyCDKscspsaeflrmmgcERDVPALC 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 3426027  234 eqQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGIE 282
Cdd:cd05081 233 --RLLELLEEGQRLPA---PPACPAEVHELMKLCWAPSPQDRPSFSALG 276
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
60-283 9.75e-26

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: 108.57  E-value: 9.75e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEM--------------STPLSVKGRI--ILEI 122
Cdd:cd05100  64 LVSEMEMMKMIgKHKNIINLLGACTQDGPLYVLVEYASKGNLREYLRARRppgmdysfdtcklpEEQLTFKDLVscAYQV 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnNEEHNelreVDGTAKKNGGTL--YYMAPEHLND 200
Cdd:cd05100 144 ARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLA---------RDVHN----IDYYKKTTNGRLpvKWMAPEALFD 210
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  201 vnAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd05100 211 --RVYTHQSDVWSFGVLLWEIFTlGGSPYP-GIPVEELFKLLKEGHRMDK---PANCTHELYMIMRECWHAVPSQRPTFK 284

                ....
gi 3426027  280 GIEE 283
Cdd:cd05100 285 QLVE 288
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
25-277 1.03e-25

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: 106.85  E-value: 1.03e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQG-LMIMKTVY----KGPNCIEHN---EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd06628  10 SGSFGSVYLGMNASSGeLMAVKQVElpsvSAENKDRKKsmlDALQREIALLRELQHENIVQYLGSSSDANHLNIFLEYVP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLnneEHNEL 176
Cdd:cd06628  90 GGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGIS-----KKL---EANSL 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 REVDGTAKKN-GGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYENaiCEQ-QLIMCIKSGNRPdvdDITE 254
Cdd:cd06628 162 STKNNGARPSlQGSVFWMAPEVVKQTSY--TRKADIWSLGCLVVEMLTGTHPFPD--CTQmQAIFKIGENASP---TIPS 234
                       250       260
                ....*....|....*....|...
gi 3426027  255 YCPREIISLMKLCWEANPEARPT 277
Cdd:cd06628 235 NISSEARDFLEKTFEIDHNKRPT 257
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
58-277 1.20e-25

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: 106.53  E-value: 1.20e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL---KAEMSTPLSvkGRIILEIIEGMCYLHGKGV 134
Cdd:cd06614  41 ELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLTDIItqnPVRMNESQI--AYVCREVLQGLEYLHSQNV 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEehnelrevdgTAKKNG--GTLYYMAPEHlndVNAKP-TEKSDV 211
Cdd:cd06614 119 IHRDIKSDNILLSKDGSVKLADFGFA-----AQLTKE----------KSKRNSvvGTPYWMAPEV---IKRKDyGPKVDI 180
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  212 YSFAVVLWAIFANKEPY--ENAIceqQLIMCIKSGNRPDVDDITEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd06614 181 WSLGIMCIEMAEGEPPYleEPPL---RALFLITTKGIPPLKNPEKWSP-EFKDFLNKCLVKDPEKRPS 244
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
586-665 1.32e-25

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 100.43  E-value: 1.32e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  586 HLDPIRENLGKHWKNCARKLGFTQSQIDEIDHDYeRDGLKEKVYQMLQKWVMREGiKGATVGKLAQALHQCSRIDLLSSL 665
Cdd:cd01670   1 YFDLVAEELGRDWKKLARKLGLSEGDIDQIEEDN-RDDLKEQAYQMLERWREREG-DEATLGRLIQALREIGRRDLAEKL 78
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
22-276 1.34e-25

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 106.65  E-value: 1.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCfhRTQGLMI---MKTVYKgpNCIEHNEALLEEAKMMNRL-RHSRVVKLLG--VIIEEGK--YSLVME 93
Cdd:cd13985   7 QLGEGGFSYVYLA--HDVNTGRryaLKRMYF--NDEEQLRVAIKEIEIMKRLcGHPNIVQYYDsaILSSEGRkeVLLLME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEkGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKG--VIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLN 169
Cdd:cd13985  83 YCP-GSLVDILEKSPPSPLSEEEvlRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHYPLER 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 NEEHNELREvdgTAKKNgGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPYenaicEQQLIMCIKSGNRPD 248
Cdd:cd13985 162 AEEVNIIEE---EIQKN-TTPMYRAPEMIDLYSKKPiGEKADIWALGCLLYKLCFFKLPF-----DESSKLAIVAGKYSI 232
                       250       260
                ....*....|....*....|....*...
gi 3426027  249 VDdiTEYCPREIISLMKLCWEANPEARP 276
Cdd:cd13985 233 PE--QPRYSPELHDLIRHMLTPDPAERP 258
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
58-285 1.49e-25

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: 106.35  E-value: 1.49e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKA--EMSTPLSVKGRIILEIIEGMCYLHGKGVI 135
Cdd:cd05052  47 EEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYGNLLDYLREcnREELNAVVLLYMATQIASAMEYLEKKNFI 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASFkmwsklnneehneLREVDGTAkKNGGT--LYYMAPEHLndVNAKPTEKSDVYS 213
Cdd:cd05052 127 HRDLAARNCLVGENHLVKVADFGLSRL-------------MTGDTYTA-HAGAKfpIKWTAPESL--AYNKFSIKSDVWA 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  214 FAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05052 191 FGVLLWEIATyGMSPYP-GIDLSQVYELLEKGYRMER---PEGCPPKVYELMRACWQWNPSDRPSFAEIHQAL 259
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
22-289 1.62e-25

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: 106.69  E-value: 1.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGNLM 101
Cdd:cd05069  19 KLGQGCFGEVWMGTWNGTTKVAIKTLKPG---TMMPEAFLQEAQIMKKLRHDKLVPLYAVVSEEPIY-IVTEFMGKGSLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneEHNELrev 179
Cdd:cd05069  95 DFLKEGDGKYLKLPQLVDMaaQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLI--------EDNEY--- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 dgTAKKNGG-TLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFAN-KEPYENAICEQQLIMCIKSGNRPdvddITEYCP 257
Cdd:cd05069 164 --TARQGAKfPIKWTAPEAA--LYGRFTIKSDVWSFGILLTELVTKgRVPYPGMVNREVLEQVERGYRMP----CPQGCP 235
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  258 REIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:cd05069 236 ESLHELMKLCWKKDPDERPTFEYIQSFLEDYF 267
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
58-289 2.07e-25

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: 105.95  E-value: 2.07e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTpLSVKGRIIL--EIIEGMCYLHGKGVI 135
Cdd:cd05068  48 EDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLLEYLQGKGRS-LQLPQLIDMaaQVASGMAYLESQNYI 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASFkmwskLNNEEHNELREvdgtakkngGT---LYYMAPEHLNdvNAKPTEKSDVY 212
Cdd:cd05068 127 HRDLAARNVLVGENNICKVADFGLARV-----IKVEDEYEARE---------GAkfpIKWTAPEAAN--YNRFSIKSDVW 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  213 SFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNR-PDVDDiteyCPREIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:cd05068 191 SFGILLTEIVTyGRIPYP-GMTNAEVLQQVERGYRmPCPPN----CPPQLYDIMLECWKADPMERPTFETLQWKLEDFF 264
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
23-278 2.24e-25

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: 106.39  E-value: 2.24e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHR------TQGLMIMKTVYKGPNciehNEALLE---EAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd05046  13 LGRGEFGEVFLAKAKgieeegGETLVLVKALQKTKD----ENLQSEfrrELDMFRKLSHKNVVRLLGLCREAEPHYMILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMST-------PLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKM 164
Cdd:cd05046  89 YTDLGDLKQFLRATKSKdeklkppPLSTKQKVALctQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVY 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  165 wsklnNEEHNELREVdgtakknGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKE-PYENaICEQQLIMCIKS 243
Cdd:cd05046 169 -----NSEYYKLRNA-------LIPLRWLAPEAVQEDDF--STKSDVWSFGVLMWEVFTQGElPFYG-LSDEEVLNRLQA 233
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 3426027  244 GnrpDVD-DITEYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05046 234 G---KLElPVPEGCPSRLYKLMTRCWAVNPKDRPSF 266
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
22-284 2.25e-25

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: 106.81  E-value: 2.25e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCfhRTQGLMIMKtvyKGPNCIEHnEALLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVM-EYMEKGN 99
Cdd:cd05054  25 QASAFGIDKSATC--RTVAVKMLK---EGATASEH-KALMTELKILIHIgHHLNVVNLLGACTKPGGPLMVIvEFCKFGN 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKA--EMSTPLSVKGRIILEIIE------------------------GMCYLHGKGVIHKDLKPENILVDNDFHIK 153
Cdd:cd05054  99 LSNYLRSkrEEFVPYRDKGARDVEEEEdddelykepltledlicysfqvarGMEFLASRKCIHRDLAARNILLSENNVVK 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  154 IADLGLAsfkmwsklnneehnelREV--DGTAKKNGGT---LYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEP 227
Cdd:cd05054 179 ICDFGLA----------------RDIykDPDYVRKGDArlpLKWMAPESIFD--KVYTTQSDVWSFGVLLWEIFSlGASP 240
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  228 YENAICEQQLIMCIKSGNR---PdvdditEYCPREIISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd05054 241 YPGVQMDEEFCRRLKEGTRmraP------EYTTPEIYQIMLDCWHGEPKERPTFSELVEK 294
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
26-281 2.45e-25

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


Pssm-ID: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 105.89  E-value: 2.45e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMImKTVYKGPN--CIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd14145  17 GGFGKVYRAIWIGDEVAV-KAARHDPDedISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFARGGPLNRV 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVKGRIIlEIIEGMCYLHGKG---VIHKDLKPENILV-----DNDFH---IKIADLGLAsfkmwsklnnee 172
Cdd:cd14145  96 LSGKRIPPDILVNWAV-QIARGMNYLHCEAivpVIHRDLKSSNILIlekveNGDLSnkiLKITDFGLA------------ 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelREVDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEN--------AICEQQLIMCIKS 243
Cdd:cd14145 163 ----REWHRTTKMSaAGTYAWMAPEVIR--SSMFSKGSDVWSYGVLLWELLTGEVPFRGidglavayGVAMNKLSLPIPS 236
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3426027  244 GnrpdvdditeyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14145 237 T-----------CPEPFARLMEDCWNPDPHSRPPFTNI 263
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
26-294 3.15e-25

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: 105.50  E-value: 3.15e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQgLMIMKTVYKGPN--CIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd14147  14 GGFGKVYRGSWRGE-LVAVKAARQDPDedISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LkAEMSTPLSVKGRIILEIIEGMCYLHGKG---VIHKDLKPENILVD--------NDFHIKIADLGLAsfKMWSKLnnee 172
Cdd:cd14147  93 L-AGRRVPPHVLVNWAVQIARGMHYLHCEAlvpVIHRDLKSNNILLLqpienddmEHKTLKITDFGLA--REWHKT---- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelrevdgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENaiceqqlIMCIKSGNRPDVDDI 252
Cdd:cd14147 166 ---------TQMSAAGTYAWMAPEVIK--ASTFSKGSDVWSFGVLLWELLTGEVPYRG-------IDCLAVAYGVAVNKL 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 3426027  253 T----EYCPREIISLMKLCWEANPEARPTFPGIeekfrpfyLSQLE 294
Cdd:cd14147 228 TlpipSTCPEPFAQLMADCWAQDPHRRPDFASI--------LQQLE 265
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
23-227 3.43e-25

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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: 105.64  E-value: 3.43e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFH-RTQGLMIMKTVyKGPNCIEH-NEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK--G 98
Cdd:cd07829   7 LGEGTYGVVYKAKDkKTGEIVALKKI-RLDNEEEGiPSTALREISLLKELKHPNIVKLLDVIHTENKLYLVFEYCDQdlK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLsVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA-SFKmwSKLNNEEHnelr 177
Cdd:cd07829  86 KYLDKRPGPLPPNL-IK-SIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLArAFG--IPLRTYTH---- 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  178 EVDgtakknggTLYYMAPEHLndvnakptEKSDVYSFAVVLWA---IFA---NKEP 227
Cdd:cd07829 158 EVV--------TLWYRAPEIL--------LGSKHYSTAVDIWSvgcIFAeliTGKP 197
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
22-286 3.65e-25

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 106.21  E-value: 3.65e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLC---------------FHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEG 86
Cdd:cd05097  12 KLGEGQFGEVHLCeaeglaeflgegapeFDGQPVLVAVKMLRADVTKTARND-FLKEIKIMSRLKNPNIIRLLGVCVSDD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   87 KYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGRI-----------ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKI 154
Cdd:cd05097  91 PLCMITEYMENGDLNQFLsQREIESTFTHANNIpsvsianllymAVQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  155 ADLGLAsfkmwsklNNEEHNELREVDGTAKKnggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA--NKEPYeNAI 232
Cdd:cd05097 171 ADFGMS--------RNLYSGDYYRIQGRAVL---PIRWMAWESI--LLGKFTTASDVWAFGVTLWEMFTlcKEQPY-SLL 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  233 CEQQLI----MCIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05097 237 SDEQVIentgEFFRNQGRQIYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLR 294
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
22-221 3.97e-25

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: 105.69  E-value: 3.97e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMI----MKTVYKGPN-CIEhnealLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd07830   6 QLGDGTFGSVYLARNKETGELVaikkMKKKFYSWEeCMN-----LREVKSLRKLnEHPNIVKLKEVFRENDELYFVFEYM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EkGNLMHVLKAEMSTPLS---VKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnnee 172
Cdd:cd07830  81 E-GNLYQLMKDRKGKPFSesvIRS-IIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLA------------ 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  173 hnelREVdgtakKNG-------GTLYYMAPEHLndvnakptEKSDVYSFAVVLWAI 221
Cdd:cd07830 147 ----REI-----RSRppytdyvSTRWYRAPEIL--------LRSTSYSSPVDIWAL 185
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
41-286 4.19e-25

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: 105.86  E-value: 4.19e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   41 LMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKaeMSTPLSVKG---- 116
Cdd:cd05090  36 LVAIKTLKDYNNPQQWNE-FQQEASLMTELHHPNIVCLLGVVTQEQPVCMLFEFMNQGDLHEFLI--MRSPHSDVGcssd 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  117 ---------------RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELRevdg 181
Cdd:cd05090 113 edgtvkssldhgdflHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLS-----REIYSSDYYRVQ---- 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 taKKNGGTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNRPDVDDiteyCPREI 260
Cdd:cd05090 184 --NKSLLPIRWMPPEAI--MYGKFSSDSDIWSFGVVLWEIFSfGLQPYYGFSNQEVIEMVRKRQLLPCSED----CPPRM 255
                       250       260
                ....*....|....*....|....*.
gi 3426027  261 ISLMKLCWEANPEARPTFPGIEEKFR 286
Cdd:cd05090 256 YSLMTECWQEIPSRRPRFKDIHARLR 281
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
58-277 5.00e-25

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: 105.13  E-value: 5.00e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMST---PLSVKGRIILEIIEGMCYLHGKGV 134
Cdd:cd06610  44 DELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLLSGGSLLDIMKSSYPRgglDEAIIATVLKEVLKGLEYLHSNGQ 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneehneLREVDGTAKKNG---GTLYYMAPEHLNDVNAKpTEKSDV 211
Cdd:cd06610 124 IHRDVKAGNILLGEDGSVKIADFGVSASL------------ATGGDRTRKVRKtfvGTPCWMAPEVMEQVRGY-DFKADI 190
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  212 YSFAVVLWAIFANKEPYENAICEQQLIMCIKSgNRPDVDDITEY--CPREIISLMKLCWEANPEARPT 277
Cdd:cd06610 191 WSFGITAIELATGAAPYSKYPPMKVLMLTLQN-DPPSLETGADYkkYSKSFRKMISLCLQKDPSKRPT 257
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
23-277 5.34e-25

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: 104.24  E-value: 5.34e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG----LMIMKTVykgpncIEHNEALLEEAKMMNRLR----HSRVVKLLGVI--IEEGKYSLVM 92
Cdd:cd05118   7 IGEGAFGTVWLARDKVTGekvaIKKIKND------FRHPKAALREIKLLKHLNdvegHPNIVKLLDVFehRGGNHLCLVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKgNLMHVLKAEMST-PLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDND-FHIKIADLGLASFkmwsklnn 170
Cdd:cd05118  81 ELMGM-NLYELIKDYPRGlPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLElGQLKLADFGLARS-------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eehnelrEVDGTAKKNGGTLYYMAPEHLndVNAKP-TEKSDVYSFAVVLWAIFANkepyenaiceqQLIMCIKSgnrpDV 249
Cdd:cd05118 152 -------FTSPPYTPYVATRWYRAPEVL--LGAKPyGSSIDIWSLGCILAELLTG-----------RPLFPGDS----EV 207
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  250 DDITEYC----PREIISLMKLCWEANPEARPT 277
Cdd:cd05118 208 DQLAKIVrllgTPEALDLLSKMLKYDPAKRIT 239
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
58-281 5.52e-25

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: 105.14  E-value: 5.52e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEgKYSLVMEYMEKGNLMHVLKAeMSTPLSVKGRIIL--EIIEGMCYLHGKGVI 135
Cdd:cd14151  49 QAFKNEVGVLRKTRHVNILLFMGYSTKP-QLAIVTQWCEGSSLYHHLHI-IETKFEMIKLIDIarQTAQGMDYLHAKSII 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASFK-MWSKLNNEEhnelrevdgtakKNGGTLYYMAPEHLNDVNAKPTE-KSDVYS 213
Cdd:cd14151 127 HRDLKSNNIFLHEDLTVKIGDFGLATVKsRWSGSHQFE------------QLSGSILWMAPEVIRMQDKNPYSfQSDVYA 194
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  214 FAVVLWAIFANKEPYENAICEQQLIMCIKSGN-RPDVDDITEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14151 195 FGIVLYELMTGQLPYSNINNRDQIIFMVGRGYlSPDLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQI 263
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
58-291 6.29e-25

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: 105.15  E-value: 6.29e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVMEYMEKGNLMHVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVI 135
Cdd:cd05071  49 EAFLQEAQVMKKLRHEKLVQLYAVVSEEPIY-IVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMaaQIASGMAYVERMNYV 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASFKmwsklnneEHNELrevdgTAKKNGG-TLYYMAPEHLndVNAKPTEKSDVYSF 214
Cdd:cd05071 128 HRDLRAANILVGENLVCKVADFGLARLI--------EDNEY-----TARQGAKfPIKWTAPEAA--LYGRFTIKSDVWSF 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  215 AVVLWAIFAN-KEPYENAICEQQLIMCIKSGNRPdvddITEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFYLS 291
Cdd:cd05071 193 GILLTELTTKgRVPYPGMVNREVLDQVERGYRMP----CPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDYFTS 266
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
15-228 9.22e-25

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: 104.60  E-value: 9.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGLMI-MKTVYKgpnciehnEALLEEAKM---------MNRLRHSRVVKLLGVIIE 84
Cdd:cd05581   1 NDFKFGKPLGEGSYSTVVLAKEKETGKEYaIKVLDK--------RHIIKEKKVkyvtiekevLSRLAHPGIVKLYYTFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EGKYSLVMEYMEKGNLMHVLKAEMStpLSVK-GRIIL-EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsf 162
Cdd:cd05581  73 ESKLYFVLEYAPNGDLLEYIRKYGS--LDEKcTRFYTaEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTA-- 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  163 KMWSKLNNEEHNELREVDGTAKKNG------GTLYYMAPEHLNDvnaKPTEK-SDVYSFAVVLWAIFANKEPY 228
Cdd:cd05581 149 KVLGPDSSPESTKGDADSQIAYNQAraasfvGTAEYVSPELLNE---KPAGKsSDLWALGCIIYQMLTGKPPF 218
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
23-277 1.80e-24

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: 103.02  E-value: 1.80e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKvslCFH----RTQGLMIMKTVYKGPNCIEHN-EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14099   9 LGKGGFAK---CYEvtdmSTGKVYAGKVVPKSSLTKPKQrEKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEmsTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNe 175
Cdd:cd14099  86 GSLMELLKRR--KALTEPevRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLA-----ARLEYDGER- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 lrevdgtaKKN-GGTLYYMAPEHLNDVNAKPTEkSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNR--PDVDDI 252
Cdd:cd14099 158 --------KKTlCGTPNYIAPEVLEKKKGHSFE-VDIWSLGVILYTLLVGKPPFE-TSDVKETYKRIKKNEYsfPSHLSI 227
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCPREIISLMKLcweaNPEARPT 277
Cdd:cd14099 228 SDEAKDLIRSMLQP----DPTKRPS 248
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
62-283 2.15e-24

Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 103.40  E-value: 2.15e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEmSTPLSVKGRI--ILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd14045  51 KEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDVLLNE-DIPLNWGFRFsfATDIARGMAYLHQHKIYHGRL 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  140 KPENILVDNDFHIKIADLGLASFKMWSKLNNEE--HNELREVdgtakknggtlyYMAPEHLNDVNAKPTEKSDVYSFAVV 217
Cdd:cd14045 130 KSSNCVIDDRWVCKIADYGLTTYRKEDGSENASgyQQRLMQV------------YLPPENHSNTDTEPTQATDVYSYAII 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  218 LWAIFANKEP-------YENAICE--QQLIMCiKSGNR-PdvdditeyCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14045 198 LLEIATRNDPvpeddysLDEAWCPplPELISG-KTENScP--------CPADYVELIRRCRKNNPAQRPTFEQIKK 264
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
56-277 2.77e-24

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: 103.51  E-value: 2.77e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   56 HNEALLEEAKMmnrLRHSRVVKLLGV-IIEEG---KYSLVMEYMEKGNLMHVLKaemSTPLSVKG--RIILEIIEGMCYL 129
Cdd:cd14056  35 FRETEIYQTVM---LRHENILGFIAAdIKSTGswtQLWLITEYHEHGSLYDYLQ---RNTLDTEEalRLAYSAASGLAHL 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  130 H-------GKGVI-HKDLKPENILVDNDFHIKIADLGLASFKMwSKLNNEEHNELREVdgtakkngGTLYYMAPEHLND- 200
Cdd:cd14056 109 HteivgtqGKPAIaHRDLKSKNILVKRDGTCCIADLGLAVRYD-SDTNTIDIPPNPRV--------GTKRYMAPEVLDDs 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  201 VNAKPTE---KSDVYSFAVVLWAI--------FAN--KEPYEN------AICEQQLIMCIKsGNRPDVDDITEYCP--RE 259
Cdd:cd14056 180 INPKSFEsfkMADIYSFGLVLWEIarrceiggIAEeyQLPYFGmvpsdpSFEEMRKVVCVE-KLRPPIPNRWKSDPvlRS 258
                       250
                ....*....|....*...
gi 3426027  260 IISLMKLCWEANPEARPT 277
Cdd:cd14056 259 MVKLMQECWSENPHARLT 276
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
23-283 2.89e-24

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: 102.48  E-value: 2.89e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHN--EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14663   8 LGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGmvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTGGEL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnneehNELREVD 180
Cdd:cd14663  88 FSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAL-----------SEQFRQD 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  181 GTAKKNGGTLYYMAPEHLNDvNAKPTEKSDVYSFAVVLWAIFANKEPYEnaicEQQLIMCIKSGNRPDVdDITEYCPREI 260
Cdd:cd14663 157 GLLHTTCGTPNYVAPEVLAR-RGYDGAKADIWSCGVILFVLLAGYLPFD----DENLMALYRKIMKGEF-EYPRWFSPGA 230
                       250       260
                ....*....|....*....|...
gi 3426027  261 ISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14663 231 KSLIKRILDPNPSTRITVEQIMA 253
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
12-275 3.03e-24

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: 103.17  E-value: 3.03e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   12 MKSSDFLESAELDSGGFGKVSL--CFH----RTQGLMIMKTVyKGPNcIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE 85
Cdd:cd05094   2 IKRRDIVLKRELGEGAFGKVFLaeCYNlsptKDKMLVAVKTL-KDPT-LAARKDFQREAELLTNLQHDHIVKFYGVCGDG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEYMEKGNLMHVLKAEM--------STPLSVKGRIIL--------EIIEGMCYLHGKGVIHKDLKPENILVDND 149
Cdd:cd05094  80 DPLIMVFEYMKHGDLNKFLRAHGpdamilvdGQPRQAKGELGLsqmlhiatQIASGMVYLASQHFVHRDLATRNCLVGAN 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  150 FHIKIADLGLAsfkmwsklnneehnelREVDGT--AKKNGGTLY---YMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA- 223
Cdd:cd05094 160 LLVKIGDFGMS----------------RDVYSTdyYRVGGHTMLpirWMPPESI--MYRKFTTESDVWSFGVILWEIFTy 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  224 NKEPYENaICEQQLIMCIKSG---NRPDVdditeyCPREIISLMKLCWEANPEAR 275
Cdd:cd05094 222 GKQPWFQ-LSNTEVIECITQGrvlERPRV------CPKEVYDIMLGCWQREPQQR 269
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
10-278 3.11e-24

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: 102.27  E-value: 3.11e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   10 IKMKSSDFLEsaELDSGGFGKVSLCFHRTQGLMIMKTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd05113   1 IDPKDLTFLK--ELGTGQFGVVKYGKWRGQYDVAIKMIKEGS---MSEDEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIF 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKgriILE----IIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMw 165
Cdd:cd05113  76 IITEYMANGCLLNYLREMRKRFQTQQ---LLEmckdVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVL- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  166 sklnneehnelrevDGTAKKNGGTLY---YMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCI 241
Cdd:cd05113 152 --------------DDEYTSSVGSKFpvrWSPPEVL--MYSKFSSKSDVWAFGVLMWEVYSlGKMPYER-FTNSETVEHV 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 3426027  242 KSGNRpdvdditEYCPR----EIISLMKLCWEANPEARPTF 278
Cdd:cd05113 215 SQGLR-------LYRPHlaseKVYTIMYSCWHEKADERPTF 248
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
43-289 3.23e-24

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: 102.91  E-value: 3.23e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   43 IMKTVYKGPNCIEHNeALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM-EYMEKGNLMHVLK----AEMSTPLSVKGR 117
Cdd:cd05043  38 LVKTVKDHASEIQVT-MLLQESSLLYGLSHQNLLPILHVCIEDGEKPMVLyPYMNWGNLKLFLQqcrlSEANNPQALSTQ 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  118 ----IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS--FKM-WSKLNNEEHNELRevdgtakknggtl 190
Cdd:cd05043 117 qlvhMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRdlFPMdYHCLGDNENRPIK------------- 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  191 yYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYENaICEQQLIMCIKSGNR---PDvdditeYCPREIISLMKL 266
Cdd:cd05043 184 -WMSLESL--VNKEYSSASDVWSFGVLLWELMTlGQTPYVE-IDPFEMAAYLKDGYRlaqPI------NCPDELFAVMAC 253
                       250       260
                ....*....|....*....|...
gi 3426027  267 CWEANPEARPTFPGIEEKFRPFY 289
Cdd:cd05043 254 CWALDPEERPSFQQLVQCLTDFH 276
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
13-278 3.29e-24

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: 102.84  E-value: 3.29e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   13 KSSDFLESaELDSGGFGKVSLCFHRTQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYsLVM 92
Cdd:cd05070   8 RESLQLIK-RLGNGQFGEVWMGTWNGNTKVAIKTLKPG---TMSPESFLEEAQIMKKLKHDKLVQLYAVVSEEPIY-IVT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnn 170
Cdd:cd05070  83 EYMSKGSLLDFLKDGEGRALKLPNLVDMaaQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLI------- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eEHNELrevdgTAKKNGG-TLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFAN-KEPYEnAICEQQLIMCIKSGNR-P 247
Cdd:cd05070 156 -EDNEY-----TARQGAKfPIKWTAPEAA--LYGRFTIKSDVWSFGILLTELVTKgRVPYP-GMNNREVLEQVERGYRmP 226
                       250       260       270
                ....*....|....*....|....*....|.
gi 3426027  248 DVDDiteyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05070 227 CPQD----CPISLHELMIHCWKKDPEERPTF 253
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
22-291 3.47e-24

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: 102.56  E-value: 3.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNE---ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd05611   3 PISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQvtnVKAERAIMMIQGESPYVAKLYYSFQSKDYLYLVMEYLNGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnELRE 178
Cdd:cd05611  83 DCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLS--------------RNGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGTAKKNGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIKSGNRPDVDDITEYCPR 258
Cdd:cd05611 149 EKRHNKKFVGTPDYLAPETILGVGD--DKMSDWWSLGCVIFEFLFGYPPF-HAETPDAVFDNILSRRINWPEEVKEFCSP 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  259 EIISLMKLCWEANPEARPTFPGIEE-KFRPFYLS 291
Cdd:cd05611 226 EAVDLINRLLCMDPAKRLGANGYQEiKSHPFFKS 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
69-231 3.47e-24

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: 102.39  E-value: 3.47e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   69 RLRHSRVVKLLGVII-EEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVD 147
Cdd:cd13994  53 KLHHPNIVKVLDLCQdLHGKWCLVMEYCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLD 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  148 NDFHIKIADLGLAsfkmwSKLNNEEHNELREVDGTakknGGTLYYMAPEHLN--DVNAKPtekSDVYSFAVVLWAIFANK 225
Cdd:cd13994 133 EDGVLKLTDFGTA-----EVFGMPAEKESPMSAGL----CGSEPYMAPEVFTsgSYDGRA---VDVWSCGIVLFALFTGR 200

                ....*.
gi 3426027  226 EPYENA 231
Cdd:cd13994 201 FPWRSA 206
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
23-289 3.87e-24

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: 101.95  E-value: 3.87e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLE-EAKMMNRLRHSRVVKLLGVIiEEGKY-SLVMEYMEKGN 99
Cdd:cd14081   9 LGKGQTGLVKLAKHCVTGqKVAIKIVNKEKLSKESVLMKVErEIAIMKLIEHPNVLKLYDVY-ENKKYlYLVLEYVSGGE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLnneehnelrev 179
Cdd:cd14081  88 LFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSL----------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 dgtAKKNGGTLYYMAPEhlnDVNAKPTE--KSDVYSFAVVLWAIFANKEPY--ENAiceQQLIMCIKSGnrpdVDDITEY 255
Cdd:cd14081 157 ---LETSCGSPHYACPE---VIKGEKYDgrKADIWSCGVILYALLVGALPFddDNL---RQLLEKVKRG----VFHIPHF 223
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  256 CPREIISLMKLCWEANPEARPTFPGIEEkfRPFY 289
Cdd:cd14081 224 ISPDAQDLLRRMLEVNPEKRITIEEIKK--HPWF 255
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
17-278 7.35e-24

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: 102.02  E-value: 7.35e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLEsaELDSGGFGKVSLCFH-----RTQGLMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSL- 90
Cdd:cd14205   8 FLQ--QLGKGNFGSVEMCRYdplqdNTGEVVAVKKLQHSTE--EHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLr 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 -VMEYMEKGNLMHVLKAEMSTPLSVKgrIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWS 166
Cdd:cd14205  84 lIMEYLPYGSLRDYLQKHKERIDHIK--LLQytsQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQD 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 KlnneEHNELREvdgtakKNGGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYENAICE------------ 234
Cdd:cd14205 162 K----EYYKVKE------PGESPIFWYAPESLTE--SKFSVASDVWSFGVVLYELFTYIEKSKSPPAEfmrmigndkqgq 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3426027  235 ---QQLIMCIKSGNR-PDVDDiteyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd14205 230 mivFHLIELLKNNGRlPRPDG----CPDEIYMIMTECWNNNVNQRPSF 273
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
87-288 7.62e-24

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: 102.13  E-value: 7.62e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   87 KYSLVMEYMEKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLH--------GKGVI-HKDLKPENILVDNDFHIKIADL 157
Cdd:cd13998  67 ELWLVTAFHPNGSL*DYLSLHTIDWVSL-CRLALSVARGLAHLHseipgctqGKPAIaHRDLKSKNILVKNDGTCCIADF 145
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  158 GLASfkMWSKLNNEEhnelrevDGTAKKNGGTLYYMAPEHLND-VNAKPTE---KSDVYSFAVVLWAIFAN--------- 224
Cdd:cd13998 146 GLAV--RLSPSTGEE-------DNANNGQVGTKRYMAPEVLEGaINLRDFEsfkRVDIYAMGLVLWEMASRctdlfgive 216
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  225 --KEPYEN------AICEQQLIMCIKSGnRPDVDDITEYCP--REIISLMKLCWEANPEARPTFPGIEEKFRPF 288
Cdd:cd13998 217 eyKPPFYSevpnhpSFEDMQEVVVRDKQ-RPNIPNRWLSHPglQSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
63-282 9.92e-24

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 101.11  E-value: 9.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPE 142
Cdd:cd14080  52 ELEILRKLRHPNIIQVYSIFERGSKVFIFMEYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCE 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  143 NILVDNDFHIKIADLGLAsfKMWSKlnneehnelREVDGTAKKNGGTLYYMAPEHLNDVNAKPTeKSDVYSFAVVLWaIF 222
Cdd:cd14080 132 NILLDSNNNVKLSDFGFA--RLCPD---------DDGDVLSKTFCGSAAYAAPEILQGIPYDPK-KYDIWSLGVILY-IM 198
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  223 ANKE-PYENA----ICEQQliMCIKSGNRPDVDDITEYCPREIISLMklcwEANPEARPTFPGIE 282
Cdd:cd14080 199 LCGSmPFDDSnikkMLKDQ--QNRKVRFPSSVKKLSPECKDLIDQLL----EPDPTKRATIEEIL 257
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
11-281 1.24e-23

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: 101.26  E-value: 1.24e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   11 KMKSSDFLESAELDSGGFGKVSLC-FHRTQGLMIMKTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEeGKYS 89
Cdd:cd14149   8 EIEASEVMLSTRIGSGSFGTVYKGkWHGDVAVKILKVVDPTP---EQFQAFRNEVAVLRKTRHVNILLFMGYMTK-DNLA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNL---MHVLKAEMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKM-W 165
Cdd:cd14149  84 IVTQWCEGSSLykhLHVQETKFQMFQLID--IARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSrW 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  166 SKLNNEEhnelrevdgtakKNGGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCI-KS 243
Cdd:cd14149 162 SGSQQVE------------QPTGSILWMAPEVIRMQDNNPfSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVgRG 229
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3426027  244 GNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14149 230 YASPDLSKLYKNCPKAMKRLVADCIKKVKEERPLFPQI 267
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
17-277 1.26e-23

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


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 101.35  E-value: 1.26e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEE--GKYSLVME 93
Cdd:cd06621   3 IVELSSLGEGAGGSVTKCRLRnTKTIFALKTITTDPNPDVQKQ-ILRELEINKSCASPYIVKYYGAFLDEqdSSIGIAME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNL----MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskln 169
Cdd:cd06621  82 YCEGGSLdsiyKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSG-------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neehnELreVDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQL--------IMCI 241
Cdd:cd06621 154 -----EL--VNSLAGTFTGTSYYMAPERIQ--GGPYSITSDVWSLGLTLLEVAQNRFPFP-PEGEPPLgpiellsyIVNM 223
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 3426027  242 KSGNRPDVDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd06621 224 PNPELKDEPENGIKWSESFKDFIEKCLEKDGTRRPG 259
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
16-277 1.43e-23

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: 100.69  E-value: 1.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLEsaELDSGGFGKVSLCFHRTQGLMImktVYKGPNCIEHNEA----LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSL- 90
Cdd:cd08217   3 EVLE--TIGKGSFGTVRKVRRKSDGKIL---VWKEIDYGKMSEKekqqLVSEVNILRELKHPNIVRYYDRIVDRANTTLy 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 -VMEYMEKGNLMHVLK--AEMSTPL--SVKGRIILEIIEGMCYLH-----GKGVIHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd08217  78 iVMEYCEGGDLAQLIKkcKKENQYIpeEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPANIFLDSDNNVKLGDFGLA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  161 sfKMwsklnneehneLREVDGTAKKNGGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMC 240
Cdd:cd08217 158 --RV-----------LSHDSSFAKTYVGTPYYMSPELLNE--QSYDEKSDIWSLGCLIYELCALHPPFQ-AANQLELAKK 221
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 3426027  241 IKSGNRPDVDDIteYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd08217 222 IKEGKFPRIPSR--YSS-ELNEVIKSMLNVDPDKRPS 255
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
20-228 1.72e-23

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: 100.55  E-value: 1.72e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   20 SAELDSGGFGKVSLCFHR-TQGLMIMKTVYK------GPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14084  11 SRTLGSGACGEVKLAYDKsTCKKVAIKIINKrkftigSRREINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYYIVL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLasfkmwSKLN 169
Cdd:cd14084  91 ELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGL------SKIL 164
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 NEehnelrevDGTAKKNGGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14084 165 GE--------TSLMKTLCGTPTYLAPEVLRSFGTEGyTRAVDCWSLGVILFICLSGYPPF 216
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
25-275 4.13e-23

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: 99.25  E-value: 4.13e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQGLMI-MKTVYKGpNCIEHNEA--LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL- 100
Cdd:cd05578  10 KGSFGKVCIVQKKDTKKMFaMKYMNKQ-KCIEKDSVrnVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGDLr 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEehnelrevd 180
Cdd:cd05578  89 YHLQQKVKFSEETVK-FYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATS--------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  181 gtakkNGGTLYYMAPEHLndvnakpteKSDVYSFAVVLWAI-------FANKEPYE---NAICEQQLIMCIKSGNrpdvd 250
Cdd:cd05578 159 -----TSGTKPYMAPEVF---------MRAGYSFAVDWWSLgvtayemLRGKRPYEihsRTSIEEIRAKFETASV----- 219
                       250       260
                ....*....|....*....|....*
gi 3426027  251 DITEYCPREIISLMKLCWEANPEAR 275
Cdd:cd05578 220 LYPAGWSEEAIDLINKLLERDPQKR 244
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
11-303 5.30e-23

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 99.44  E-value: 5.30e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   11 KMKSSDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVII-EEGKY 88
Cdd:cd06620   1 DLKNQDLETLKDLGAGNGGSVSKVLHIpTGTIMAKKVIHIDAKSSVRKQ-ILRELQILHECHSPYIVSFYGAFLnENNNI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   89 SLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwsk 167
Cdd:cd06620  80 IICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSG------ 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 lnneehnELreVDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY--ENAICEQQ--------L 237
Cdd:cd06620 154 -------EL--INSIADTFVGTSTYMSPERIQ--GGKYSVKSDVWSLGLSIIELALGEFPFagSNDDDDGYngpmgildL 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  238 IMCIKSGNRPDVDDITEYcPREIISLMKLCWEANPEARPTfpgIEEKFRPFYLSQLEESVEEDVKS 303
Cdd:cd06620 223 LQRIVNEPPPRLPKDRIF-PKDLRDFVDRCLLKDPRERPS---PQLLLDHDPFIQAVRASDVDLRA 284
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
25-281 5.43e-23

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: 99.28  E-value: 5.43e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQG----LMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd05063  15 AGEFGEVFRGILKMPGrkevAVAIKTLKPGYTEKQRQD-FLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITEYMENGAL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMS--TPLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnnEEHNElre 178
Cdd:cd05063  94 DKYLRDHDGefSSYQLVG-MLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVL-------EDDPE--- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdGTAKKNGGT--LYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKE-PYENaICEQQLIMCIKSGNR-PDVDDite 254
Cdd:cd05063 163 --GTYTTSGGKipIRWTAPEAIA--YRKFTSASDVWSFGIVMWEVMSFGErPYWD-MSNHEVMKAINDGFRlPAPMD--- 234
                       250       260
                ....*....|....*....|....*..
gi 3426027  255 yCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05063 235 -CPSAVYQLMLQCWQQDRARRPRFVDI 260
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
23-255 1.01e-22

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: 98.73  E-value: 1.01e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14158  23 LGEGGFGVVFKGYINDKNVAVKKLAAMVDISTEDLTKQFEqEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGSLL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLK-AEMSTPLSVKGR--IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA--SFKMWSKLNNEehnel 176
Cdd:cd14158 103 DRLAcLNDTPPLSWHMRckIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAraSEKFSQTIMTE----- 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 REVdgtakkngGTLYYMAPEHLndvNAKPTEKSDVYSFAVVLWAIFANKEPY-ENAicEQQLIMCIKSGNRPDVDDITEY 255
Cdd:cd14158 178 RIV--------GTTAYMAPEAL---RGEITPKSDIFSFGVVLLEIITGLPPVdENR--DPQLLLDIKEEIEDEEKTIEDY 244
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-277 1.13e-22

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: 98.53  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   13 KSSDFLESaeLDSGGFGKVSLCFHRTQG-LMIMKTVYKGPncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14166   3 ETFIFMEV--LGSGAFSEVYLVKQRSTGkLYALKCIKKSP--LSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLM-HVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLAsfKMwsk 167
Cdd:cd14166  79 MQLVSGGELFdRILERGVYTEKDAS-RVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLS--KM--- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 lnnEEHnelrevdGTAKKNGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEP-YENAicEQQLIMCIKSG- 244
Cdd:cd14166 153 ---EQN-------GIMSTACGTPGYVAPEVLAQ---KPYSKAvDCWSIGVITYILLCGYPPfYEET--ESRLFEKIKEGy 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 3426027  245 ---NRPDVDDITEYCPREIISLMklcwEANPEARPT 277
Cdd:cd14166 218 yefESPFWDDISESAKDFIRHLL----EKNPSKRYT 249
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
26-221 1.29e-22

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: 98.54  E-value: 1.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMIMKTVYKGpncIEHNEAL----LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKgNLM 101
Cdd:cd07833  12 GAYGVVLKCRNKATGEIVAIKKFKE---SEDDEDVkktaLREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYVER-TLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMS--TPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnnEEHNELREV 179
Cdd:cd07833  88 ELLEASPGglPPDAVR-SYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARAL-------TARPASPLT 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 3426027  180 DGTAkknggTLYYMAPEHL-NDVNakpteksdvYSFAVVLWAI 221
Cdd:cd07833 160 DYVA-----TRWYRAPELLvGDTN---------YGKPVDVWAI 188
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
12-290 1.57e-22

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: 98.19  E-value: 1.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   12 MKSSDFLESAELDSGGFGKV------SLCFHRTQGLMIMKTVYKGPNCIEHNeaLLEEAKMMNRLRHSRVVKLLGVIIEE 85
Cdd:cd05093   2 IKRHNIVLKRELGEGAFGKVflaecyNLCPEQDKILVAVKTLKDASDNARKD--FHREAELLTNLQHEHIVKFYGVCVEG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEYMEKGNLMHVLKA---------------EMSTPLSVkgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF 150
Cdd:cd05093  80 DPLIMVFEYMKHGDLNKFLRAhgpdavlmaegnrpaELTQSQML--HIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  151 HIKIADLGLAsfkmwsklnneehnelREVDGT--AKKNGGTLY---YMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-N 224
Cdd:cd05093 158 LVKIGDFGMS----------------RDVYSTdyYRVGGHTMLpirWMPPESI--MYRKFTTESDVWSLGVVLWEIFTyG 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  225 KEPYENaICEQQLIMCIKSG---NRPDVdditeyCPREIISLMKLCWEANPEARPTFPGIEE------KFRPFYL 290
Cdd:cd05093 220 KQPWYQ-LSNNEVIECITQGrvlQRPRT------CPKEVYDLMLGCWQREPHMRLNIKEIHSllqnlaKASPVYL 287
Death pfam00531
Death domain;
584-667 1.62e-22

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 92.04  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    584 DKHLDPIREN---LGKHWKNCARKLGFTQSQIDEIDHDYERdgLKEKVYQMLQKWVMREGiKGATVGKLAQALHQCSRID 660
Cdd:pfam00531   1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR--LRSQTYELLRLWEQREG-KNATVGTLLEALRKLGRRD 77

                  ....*..
gi 3426027    661 LLSSLIY 667
Cdd:pfam00531  78 AAEKIQS 84
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
15-228 2.59e-22

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: 97.65  E-value: 2.59e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGP----NCIEHneaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKdSGKYYALKILKKAKiiklKQVEH---VLNEKRILSEVRHPFIVNLLGSFQDDRNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskln 169
Cdd:cd05580  78 MVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFA--------- 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neehnelREVDGTAKKNGGTLYYMAPEHLndvNAKPTEKS-DVYSFAVVLWAIFANKEPY 228
Cdd:cd05580 149 -------KRVKDRTYTLCGTPEYLAPEII---LSKGHGKAvDWWALGILIYEMLAGYPPF 198
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
57-281 2.95e-22

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: 96.79  E-value: 2.95e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   57 NEALLEEAKMMNRLRHSRVVKLLGVIIEeGKYS--------LVMEYMEKgNLMHVLKAEMStpLSVKGRIILEIIEGMCY 128
Cdd:cd13975  42 NDLALEFHYTRSLPKHERIVSLHGSVID-YSYGggssiavlLIMERLHR-DLYTGIKAGLS--LEERLQIALDVVEGIRF 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  129 LHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneehnelrevdgtAKKNG---GTLYYMAPEHLndvNAKP 205
Cdd:cd13975 118 LHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPE-------------------AMMSGsivGTPIHMAPELF---SGKY 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  206 TEKSDVYSFAVVLWAIFANK----EPYENAICEQQLIMCIKSGNRPD-VDDITEYCPReiisLMKLCWEANPEARPtFPG 280
Cdd:cd13975 176 DNSVDVYAFGILFWYLCAGHvklpEAFEQCASKDHLWNNVRKGVRPErLPVFDEECWN----LMEACWSGDPSQRP-LLG 250

                .
gi 3426027  281 I 281
Cdd:cd13975 251 I 251
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
58-283 3.79e-22

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: 96.66  E-value: 3.79e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVI---IEEGKYsLVMEYMEKGNLMHVlkaEMSTPLSVKG--RIILEIIEGMCYLHGK 132
Cdd:cd14118  59 DRVYREIAILKKLDHPNVVKLVEVLddpNEDNLY-MVFELVDKGAVMEV---PTDNPLSEETarSYFRDIVLGIEYLHYQ 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKS-DV 211
Cdd:cd14118 135 KIIHRDIKPSNLLLGDDGHVKIADFGVS-------------NEFEGDDALLSSTAGTPAFMAPEALSESRKKFSGKAlDI 201
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  212 YSFAVVLWAIFANKEPYE--NAICEQQLImCIKSGNRPDVDDITEycprEIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14118 202 WAMGVTLYCFVFGRCPFEddHILGLHEKI-KTDPVVFPDDPVVSE----QLKDLILRMLDKNPSERITLPEIKE 270
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
23-283 5.22e-22

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: 95.79  E-value: 5.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKV-------SLCfHRTQGLMIMKTVYKGPNCiEHNeaLLEEAKMMNRLRHSRVVKLLGVII--EEGKYSLVME 93
Cdd:cd14119   1 LGEGSYGKVkevldteTLC-RRAVKILKKRKLRRIPNG-EAN--VKREIQILRRLNHRNVIKLVDVLYneEKQKLYMVME 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMeKGNLMHVLK--AEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnne 171
Cdd:cd14119  77 YC-VGGLQEMLDsaPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVA----------- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 EHNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYE--------NAICEQQLIMciks 243
Cdd:cd14119 145 EALDLFAEDDTCTTSQGSPAFQPPEIANGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEgdniyklfENIGKGEYTI---- 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 3426027  244 gnrPDvdditeYCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14119 221 ---PD------DVDPDLQDLLRGMLEKDPEKRFTIEQIRQ 251
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
52-276 8.31e-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: 95.85  E-value: 8.31e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   52 NCIEHneaLLEEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYL- 129
Cdd:cd13990  46 NYIKH---ALREYEIHKSLDHPRIVKLYDVFeIDTDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLn 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  130 -HGKGVIHKDLKPENILVDNDFH---IKIADLGLasfkmwSKLNNEEHNELREVDGTAkKNGGTLYYMAPE--HLNDVNA 203
Cdd:cd13990 123 eIKPPIIHYDLKPGNILLHSGNVsgeIKITDFGL------SKIMDDESYNSDGMELTS-QGAGTYWYLPPEcfVVGKTPP 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  204 KPTEKSDVYSFAVVLWAIFANKEPY-----ENAICEQQLIMCIKSGNRPDVDDITEYCPreiiSLMKLCWEANPEARP 276
Cdd:cd13990 196 KISSKVDVWSVGVIFYQMLYGRKPFghnqsQEAILEENTILKATEVEFPSKPVVSSEAK----DFIRRCLTYRKEDRP 269
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
23-231 8.44e-22

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: 95.47  E-value: 8.44e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEhneALLEEAKMMNRLRHSR-VVKLLGVIIE-EGKYSLVMEYMEKGN 99
Cdd:cd13987   1 LGEGTYGKVLLAVHKGSGtKMALKFVPKPSTKLK---DFLREYNISLELSVHPhIIKTYDVAFEtEDYYVFAQEYAPYGD 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV-DNDF-HIKIADLGLAsfkmwsklnneehnelR 177
Cdd:cd13987  78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDCrRVKLCDFGLT----------------R 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  178 EVDGTAKKNGGTLYYMAPEHLNDVNAKP--TEKS-DVYSFAVVLWAIFANKEPYENA 231
Cdd:cd13987 142 RVGSTVKRVSGTIPYTAPEVCEAKKNEGfvVDPSiDVWAFGVLLFCCLTGNFPWEKA 198
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
23-277 9.91e-22

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: 95.03  E-value: 9.91e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVykgpNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd06612  11 LGEGSYGSVYKAIHKETGQVVaIKVV----PVEEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEYCGAGSVS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAeMSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaSFKMwsklnneehnelreV 179
Cdd:cd06612  87 DIMKI-TNKTLTEEeiAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGV-SGQL--------------T 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNG--GTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMcIKSGNRPDVDDITEYCP 257
Cdd:cd06612 151 DTMAKRNTviGTPFWMAPEVIQEIGYN--NKADIWSLGITAIEMAEGKPPYSDIHPMRAIFM-IPNKPPPTLSDPEKWSP 227
                       250       260
                ....*....|....*....|
gi 3426027  258 rEIISLMKLCWEANPEARPT 277
Cdd:cd06612 228 -EFNDFVKKCLVKDPEERPS 246
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
23-228 1.37e-21

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: 95.09  E-value: 1.37e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGL-MIMKTVYKGPNCIEHNE---ALLEEAKMMNRLRHSRVVKLLGVI--IEEGKYSLVMEYME 96
Cdd:cd06653  10 LGRGAFGEVYLCYDADTGReLAVKQVPFDPDSQETSKevnALECEIQLLKNLRHDRIVQYYGCLrdPEEKKLSIFVEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLnneehnel 176
Cdd:cd06653  90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-ASKRIQTIC-------- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3426027  177 reVDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd06653 161 --MSGTGIKSvTGTPYWMSPEVIS--GEGYGRKADVWSVACTVVEMLTEKPPW 209
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
23-281 1.46e-21

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: 94.64  E-value: 1.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGL-----MIMKTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14079  10 LGVGSFGKVKLAEHELTGHkvavkILNRQKIKSL---DMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMVMEYVSG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMH--VLKAEMSTPLSVkgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkMwsklnneehne 175
Cdd:cd14079  87 GELFDyiVQKGRLSEDEAR--RFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNI-M----------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 lreVDGT-AKKNGGTLYYMAPEHLN-DVNAKPteKSDVYSFAVVLWAIFANKEPY--ENAiceQQLIMCIKSGNRPdvdd 251
Cdd:cd14079 153 ---RDGEfLKTSCGSPNYAAPEVISgKLYAGP--EVDVWSCGVILYALLCGSLPFddEHI---PNLFKKIKSGIYT---- 220
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  252 ITEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14079 221 IPSHLSPGARDLIKRMLVVDPLKRITIPEI 250
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
53-284 1.57e-21

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: 95.15  E-value: 1.57e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   53 CIEHNEA-LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL-----KAEMSTPLSVKG--RIILEIIE 124
Cdd:cd05036  48 CSEQDEMdFLMEALIMSKFNHPNIVRCIGVCFQRLPRFILLELMAGGDLKSFLrenrpRPEQPSSLTMLDllQLAQDVAK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  125 GMCYLHGKGVIHKDLKPENILVDN---DFHIKIADLGLAsfkmwsklnneehnelREV--DGTAKKNGGTLY---YMAPE 196
Cdd:cd05036 128 GCRYLEENHFIHRDIAARNCLLTCkgpGRVAKIGDFGMA----------------RDIyrADYYRKGGKAMLpvkWMPPE 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  197 HLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAiCEQQLIMCIKSGNRPDVDDiteYCPREIISLMKLCWEANPEAR 275
Cdd:cd05036 192 AFLD--GIFTSKTDVWSFGVLLWEIFSlGYMPYPGK-SNQEVMEFVTSGGRMDPPK---NCPGPVYRIMTQCWQHIPEDR 265

                ....*....
gi 3426027  276 PTFPGIEEK 284
Cdd:cd05036 266 PNFSTILER 274
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
23-278 1.83e-21

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: 94.98  E-value: 1.83e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYK----GPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIE---EGKYSLVM--- 92
Cdd:cd05074  17 LGKGEFGSVREAQLKSEDGSFQKVAVKmlkaDIFSSSDIEEFLREAACMKEFDHPNVIKLIGVSLRsraKGRLPIPMvil 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAE------MSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaSFKMWS 166
Cdd:cd05074  97 PFMKHGDLHTFLLMSrigeepFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGL-SKKIYS 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 KlnneehNELREvdGTAKKNggTLYYMAPEHLNDvNAKpTEKSDVYSFAVVLWAIFA-NKEPY---ENAICEQQLImcik 242
Cdd:cd05074 176 G------DYYRQ--GCASKL--PVKWLALESLAD-NVY-TTHSDVWAFGVTMWEIMTrGQTPYagvENSEIYNYLI---- 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 3426027  243 SGNR----PDvdditeyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05074 240 KGNRlkqpPD-------CLEDVYELMCQCWSPEPKCRPSF 272
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
26-223 1.94e-21

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 95.09  E-value: 1.94e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG-LMIMKTVY--KGPNCIEHNeaLLEEAKMMNRLR-HSRVVKLLGVIIEEGKYSLVMEYMEKGnLM 101
Cdd:cd07832  11 GAHGIVFKAKDRETGeTVALKKVAlrKLEGGIPNQ--ALREIKALQACQgHPYVVKLRDVFPHGTGFVLVFEYMLSS-LS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEmSTPLS---VKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEHNEL-- 176
Cdd:cd07832  88 EVLRDE-ERPLTeaqVK-RYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA------RLFSEEDPRLys 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 REVdgtakkngGTLYYMAPEHLNDvnakptekSDVYSFAVVLWA---IFA 223
Cdd:cd07832 160 HQV--------ATRWYRAPELLYG--------SRKYDEGVDLWAvgcIFA 193
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
63-281 2.18e-21

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: 94.29  E-value: 2.18e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPE 142
Cdd:cd14162  50 EIEVIKGLKHPNLICFYEAIETTSRVYIIMELAENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCE 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  143 NILVDNDFHIKIADLGLASFKMwsklnneehnelREVDGTAKKNG---GTLYYMAPEHLNDVNAKPTeKSDVYSFAVVLW 219
Cdd:cd14162 130 NLLLDKNNNLKITDFGFARGVM------------KTKDGKPKLSEtycGSYAYASPEILRGIPYDPF-LSDIWSMGVVLY 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  220 AIFANKEPYENaiceQQLIMCIKSGNR----PDVDDITEYCpREIISLMkLCWEanpEARPTFPGI 281
Cdd:cd14162 197 TMVYGRLPFDD----SNLKVLLKQVQRrvvfPKNPTVSEEC-KDLILRM-LSPV---KKRITIEEI 253
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
15-277 2.53e-21

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: 94.50  E-value: 2.53e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGLM--IMKTVYKGP---NCIEHnealLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd14049   6 NEFEEIARLGKGGYGKVYKVRNKLDGQYyaIKKILIKKVtkrDCMKV----LREVKVLAGLQHPNIVGYHTAWMEHVQLM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVM---------------------EYMEKGNLMHVLKAEMSTplsvkgRIILEIIEGMCYLHGKGVIHKDLKPENILVD- 147
Cdd:cd14049  82 LYIqmqlcelslwdwivernkrpcEEEFKSAPYTPVDVDVTT------KILQQLLEGVTYIHSMGIVHRDLKPRNIFLHg 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  148 NDFHIKIADLGLASFKMWSKLNNEEHNElREVDGTAKKNGGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFankEP 227
Cdd:cd14049 156 SDIHVRIGDFGLACPDILQDGNDSTTMS-RLNGLTHTSGVGTCLYAAPEQLEGSHYDF--KSDMYSIGVILLELF---QP 229
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  228 YENAICEQQLIMCIKSGNRPdvDDITEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd14049 230 FGTEMERAEVLTQLRNGQIP--KSLCKRWP-VQAKYIKLLTSTEPSERPS 276
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
16-303 3.70e-21

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: 94.03  E-value: 3.70e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06617   2 DLEVIEELGRGAYGVVDKMRHVPTGtIMAVKRIRATVNSQEQKRLLMDLDISMRSVDCPYTVTFYGALFREGDVWICMEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKgNL----MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASFKmwskln 169
Cdd:cd06617  82 MDT-SLdkfyKKVYDKGLTIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYL------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neehnelreVDGTAKK-NGGTLYYMAPEHLN-DVNAKPTE-KSDVYSFAVVLWAIFANKEPYEN-AICEQQLimciksgn 245
Cdd:cd06617 155 ---------VDSVAKTiDAGCKPYMAPERINpELNQKGYDvKSDVWSLGITMIELATGRFPYDSwKTPFQQL-------- 217
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  246 RPDVDDITEYCPREIISL-----MKLCWEANPEARPTFPGIEEkfRPFylSQLEESVEEDVKS 303
Cdd:cd06617 218 KQVVEEPSPQLPAEKFSPefqdfVNKCLKKNYKERPNYPELLQ--HPF--FELHLSKNTDVAS 276
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-277 3.90e-21

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: 93.83  E-value: 3.90e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   18 LESAELDSGGFGKVSLCFHRTQG----LMIMKTVYKGPNC---IEHNEALLEEAKmmnrlRHSRVVKLLGVIIEEGKYSL 90
Cdd:cd14198  11 LTSKELGRGKFAVVRQCISKSTGqeyaAKFLKKRRRGQDCraeILHEIAVLELAK-----SNPRVVNLHEVYETTSEIIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF---HIKIADLGLAsfkmw 165
Cdd:cd14198  86 ILEYAAGGEIFNLCVPDLAEMVSENDiiRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMS----- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  166 SKLNNEehNELREVDGTAKknggtlyYMAPEHLndvNAKP-TEKSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIKSG 244
Cdd:cd14198 161 RKIGHA--CELREIMGTPE-------YLAPEIL---NYDPiTTATDMWNIGVIAYMLLTHESPFVGED-NQETFLNISQV 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 3426027  245 N----RPDVDDITEYCPREIISLMKlcweANPEARPT 277
Cdd:cd14198 228 NvdysEETFSSVSQLATDFIQKLLV----KNPEKRPT 260
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
22-281 4.14e-21

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 94.29  E-value: 4.14e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLC----FHRTQG-------------LMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIE 84
Cdd:cd05095  12 KLGEGQFGEVHLCeaegMEKFMDkdfalevsenqpvLVAVKMLRADANKNARND-FLKEIKIMSRLKDPNIIRLLAVCIT 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EGKYSLVMEYMEKGNLMHVL---KAEMSTPLSVKGRII---------LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHI 152
Cdd:cd05095  91 DDPLCMITEYMENGDLNQFLsrqQPEGQLALPSNALTVsysdlrfmaAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTI 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  153 KIADLGLAsfkmwsklNNEEHNELREVDGTAKKnggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAI--FANKEPYeN 230
Cdd:cd05095 171 KIADFGMS--------RNLYSGDYYRIQGRAVL---PIRWMSWESI--LLGKFTTASDVWAFGVTLWETltFCREQPY-S 236
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  231 AICEQQLIMCIKSGNRPDVDDI----TEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05095 237 QLSDEQVIENTGEFFRDQGRQTylpqPALCPDSVYKLMLSCWRRDTKDRPSFQEI 291
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
58-282 4.98e-21

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: 93.88  E-value: 4.98e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIE--EGKYSLVMEYMEKGNLMHVlkaEMSTPLSV-KGRIILE-IIEGMCYLHGKG 133
Cdd:cd14199  70 ERVYQEIAILKKLDHPNVVKLVEVLDDpsEDHLYMVFELVKQGPVMEV---PTLKPLSEdQARFYFQdLIKGIEYLHYQK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKS-DVY 212
Cdd:cd14199 147 IIHRDVKPSNLLVGEDGHIKIADFGVS-------------NEFEGSDALLTNTVGTPAFMAPETLSETRKIFSGKAlDVW 213
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  213 SFAVVLWAIFANKEPYENaiceqQLIMCIKSGNR------PDVDDITEYCPREIISLMklcwEANPEARPTFPGIE 282
Cdd:cd14199 214 AMGVTLYCFVFGQCPFMD-----ERILSLHSKIKtqplefPDQPDISDDLKDLLFRML----DKNPESRISVPEIK 280
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
16-281 5.63e-21

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: 92.84  E-value: 5.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESaeLDSGGFGKVSLCFHRTQGLMI-MKTVYKgpNCIEHNEALL---EEAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14073   4 ELLET--LGKGTYGKVKLAIERATGREVaIKSIKK--DKIEDEQDMVrirREIEIMSSLNHPHIIRIYEVFENKDKIVIV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklNNE 171
Cdd:cd14073  80 MEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLS--------NLY 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 EHNELREVdgtakkNGGTLYYMAPEhlnDVNAKPTE--KSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKSGnrpdv 249
Cdd:cd14073 152 SKDKLLQT------FCGSPLYASPE---IVNGTPYQgpEVDCWSLGVLLYTLVYGTMPFDGS-DFKRLVKQISSG----- 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  250 dDITEYC-PREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd14073 217 -DYREPTqPSDASGLIRWMLTVNPKRRATIEDI 248
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
57-262 5.81e-21

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: 93.19  E-value: 5.81e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   57 NEALLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMStpLSVKG--RIILEIIEGMCYLHGKG 133
Cdd:cd14093  52 REATRREIEILRQVsGHPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEVVT--LSEKKtrRIMRQLFEAVEFLHSLN 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEhnELREVDGTAKknggtlyYMAPEHL----NDVNAKPTEKS 209
Cdd:cd14093 130 IVHRDLKPENILLDDNLNVKISDFGFA-----TRLDEGE--KLRELCGTPG-------YLAPEVLkcsmYDNAPGYGKEV 195
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  210 DVYSFAVVLWAIFANKEPYENaicEQQLIMC--IKSGN----RPDVDDITEyCPREIIS 262
Cdd:cd14093 196 DMWACGVIMYTLLAGCPPFWH---RKQMVMLrnIMEGKyefgSPEWDDISD-TAKDLIS 250
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
15-218 5.96e-21

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: 94.04  E-value: 5.96e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGL-MIMKTVYkgpncIEHNEA----LLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd06615   1 DDFEKLGELGAGNGGVVTKVLHRPSGLiMARKLIH-----LEIKPAirnqIIRELKVLHECNSPYIVGFYGAFYSDGEIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwskl 168
Cdd:cd06615  76 ICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSG------- 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 nneehnELreVDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVL 218
Cdd:cd06615 149 ------QL--IDSMANSFVGTRSYMSPERLQ--GTHYTVQSDIWSLGLSL 188
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
22-277 6.26e-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: 93.56  E-value: 6.26e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNcIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN-- 99
Cdd:cd06644  19 ELGDGAFGKVYKAKNKETGALAAAKVIETKS-EEELEDYMVEIEILATCNHPYIVKLLGAFYWDGKLWIMIEFCPGGAvd 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 -LMHVLKAEMSTP-LSVkgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnelR 177
Cdd:cd06644  98 aIMLELDRGLTEPqIQV---ICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSA---------------K 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKNG--GTLYYMAPEHLNDVNAKPTE---KSDVYSFAVVLWAIfANKEPYENAICEQQLIMCIKSGNRPDVDDI 252
Cdd:cd06644 160 NVKTLQRRDSfiGTPYWMAPEVVMCETMKDTPydyKADIWSLGITLIEM-AQIEPPHHELNPMRVLLKIAKSEPPTLSQP 238
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd06644 239 SKWSM-EFRDFLKTALDKHPETRPS 262
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
21-198 6.46e-21

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: 93.40  E-value: 6.46e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFHRTQGLMI-MKTVykgpncIEHNE------ALLEEAKMMNRLRHSRVVKLLGVIIEE------GK 87
Cdd:cd07840   5 AQIGEGTYGQVYKARNKKTGELVaLKKI------RMENEkegfpiTAIREIKLLQKLDHPNVVRLKEIVTSKgsakykGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEkgnlmHVLKAEMSTPLS------VKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS 161
Cdd:cd07840  79 IYMVFEYMD-----HDLTGLLDNPEVkftesqIKC-YMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLAR 152
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 3426027  162 FkmwskLNNEEHNEL--REVdgtakknggTLYYMAPEHL 198
Cdd:cd07840 153 P-----YTKENNADYtnRVI---------TLWYRPPELL 177
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
580-667 6.72e-21

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 87.47  E-value: 6.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     580 TSLTDKHLDPIREN-LGKHWKNCARKLGFTQSQIDEIDHDYERDgLKEKVYQMLQKWVMREGIKgATVGKLAQALHQCSR 658
Cdd:smart00005   1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRD-LAEQSVQLLRLWEQREGKN-ATLGTLLEALRKMGR 78

                   ....*....
gi 3426027     659 IDLLSSLIY 667
Cdd:smart00005  79 DDAVELLRS 87
PHA02988 PHA02988
hypothetical protein; Provisional
63-289 6.97e-21

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 93.27  E-value: 6.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    63 EAKMMNRLRHSRVVKLLGVIIEEG----KYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHK 137
Cdd:PHA02988  68 EIKNLRRIDSNNILKIYGFIIDIVddlpRLSLILEYCTRGYLREVLDKEKDLSFKTKLDMAIDCCKGLYNLYKYtNKPYK 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   138 DLKPENILVDNDFHIKIADLGLasFKMWSKlnneehnelrevdgTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVV 217
Cdd:PHA02988 148 NLTSVSFLVTENYKLKIICHGL--EKILSS--------------PPFKNVNFMVYFSYKMLNDIFSEYTIKDDIYSLGVV 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027   218 LWAIFANKEPYENAICEQQLIMCIKSGNRPDVDditEYCPREIISLMKLCWEANPEARPTFPGIEEKFRPFY 289
Cdd:PHA02988 212 LWEIFTGKIPFENLTTKEIYDLIINKNNSLKLP---LDCPLEIKCIVEACTSHDSIKRPNIKEILYNLSLYK 280
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
26-275 9.12e-21

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: 93.82  E-value: 9.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKgpnciehnEALLE----EAKMMNR------LRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd05570   6 GSFGKVMLAERKkTDELYAIKVLKK--------EVIIEdddvECTMTEKrvlalaNRHPFLTGLHACFQTEDRLYFVMEY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLM-HVLKAEMSTPlsVKGRI-ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSklnnee 172
Cdd:cd05570  78 VNGGDLMfHIQRARRFTE--ERARFyAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCKEGIWG------ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelrevDGTAKKNGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSgnrpdvDD 251
Cdd:cd05570 150 -------GNTTSTFCGTPDYIAPEILRE---QDYGFSvDWWALGVLLYEMLAGQSPFE-GDDEDELFEAILN------DE 212
                       250       260
                ....*....|....*....|....*.
gi 3426027  252 IT--EYCPREIISLMKLCWEANPEAR 275
Cdd:cd05570 213 VLypRWLSREAVSILKGLLTKDPARR 238
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
16-277 1.08e-20

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: 92.06  E-value: 1.08e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQGLM--IMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd13997   1 HFHELEQIGSGSFSEVFKVRSKVDGCLyaVKKSKKPFRGPKERARALREVEAHAALGQHPNIVRYYSSWEEGGHLYIQME 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKA---EMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfKMWSKLNN 170
Cdd:cd13997  81 LCENGSLQDALEElspISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT-RLETSGDV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 EEhnelrevdgtakkngGTLYYMAPEHLNDvNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLimciKSGNRPDVd 250
Cdd:cd13997 160 EE---------------GDSRYLAPELLNE-NYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQL----RQGKLPLP- 218
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  251 diteycPREIIS-----LMKLCWEANPEARPT 277
Cdd:cd13997 219 ------PGLVLSqeltrLLKVMLDPDPTRRPT 244
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
26-288 1.39e-20

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: 91.54  E-value: 1.39e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEkGNLMHVL 104
Cdd:cd14002  12 GSFGKVYKGRRKyTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYAQ-GELFQIL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklNNEEHNELreVDGTAK 184
Cdd:cd14002  91 EDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFA--------RAMSCNTL--VLTSIK 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  185 kngGTLYYMAPEHlndVNAKP-TEKSDVYSFAVVLWAIFANKEP-YENAICeqQLIMCIKSGNRPDVDDITEYCPreiiS 262
Cdd:cd14002 161 ---GTPLYMAPEL---VQEQPyDHTADLWSLGCILYELFVGQPPfYTNSIY--QLVQMIVKDPVKWPSNMSPEFK----S 228
                       250       260
                ....*....|....*....|....*.
gi 3426027  263 LMKLCWEANPEARPTFPGIEEkfRPF 288
Cdd:cd14002 229 FLQGLLNKDPSKRLSWPDLLE--HPF 252
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
22-281 1.47e-20

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 92.69  E-value: 1.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLC--------------FHRTQG---LMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIE 84
Cdd:cd05096  12 KLGEGQFGEVHLCevvnpqdlptlqfpFNVRKGrplLVAVKILRPDANKNARND-FLKEVKILSRLKDPNIIRLLGVCVD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EGKYSLVMEYMEKGNL-----MHVL--KAEMSTPLSVKG------------RIILEIIEGMCYLHGKGVIHKDLKPENIL 145
Cdd:cd05096  91 EDPLCMITEYMENGDLnqflsSHHLddKEENGNDAVPPAhclpaisyssllHVALQIASGMKYLSSLNFVHRDLATRNCL 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  146 VDNDFHIKIADLGLAsfkmwsklNNEEHNELREVDGTAKKnggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-- 223
Cdd:cd05096 171 VGENLTIKIADFGMS--------RNLYAGDYYRIQGRAVL---PIRWMAWECI--LMGKFTTASDVWAFGVTLWEILMlc 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  224 NKEPYeNAICEQQLI-----MCIKSGN-----RPDVdditeyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05096 238 KEQPY-GELTDEQVIenageFFRDQGRqvylfRPPP------CPQGLYELMLQCWSRDCRERPSFSDI 298
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
54-282 1.53e-20

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 91.87  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   54 IEHNEALLEEAKMMN-----RLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTP------LSVKGRIILEI 122
Cdd:cd14044  39 LKNNEGNFTEKQKIElnkllQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKISYPdgtfmdWEFKISVMYDI 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLH-GKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKlnneehnELrevdgtakknggtlyYMAPEHLNdv 201
Cdd:cd14044 119 AKGMSYLHsSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPSK-------DL---------------WTAPEHLR-- 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  202 NAKPTEKSDVYSFAVVLWAIFANKEPYENAICE--QQLIMCIKSGN-----RPDVD-DITEYCPREIISLMKLCWEANPE 273
Cdd:cd14044 175 QAGTSQKGDVYSYGIIAQEIILRKETFYTAACSdrKEKIYRVQNPKgmkpfRPDLNlESAGEREREVYGLVKNCWEEDPE 254

                ....*....
gi 3426027  274 ARPTFPGIE 282
Cdd:cd14044 255 KRPDFKKIE 263
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
22-277 2.19e-20

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: 91.73  E-value: 2.19e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGLMIMKTVykgpnCIEHNEALLE----EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd06611  12 ELGDGAFGKVYKAQHKETGLFAAAKI-----IQIESEEELEdfmvEIDILSECKHPNIVGLYEAYFYENKLWILIEFCDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 G---NLMHVLKAEMSTP-LSVKGRiilEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLNNEEH 173
Cdd:cd06611  87 GaldSIMLELERGLTEPqIRYVCR---QMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGV------SAKNKSTL 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 NelrevdgtaKKNG--GTLYYMAPEHLNDVNAKPTE---KSDVYSFAVVLWAIfANKEPYENAICEQQLIMCIKSGNRPD 248
Cdd:cd06611 158 Q---------KRDTfiGTPYWMAPEVVACETFKDNPydyKADIWSLGITLIEL-AQMEPPHHELNPMRVLLKILKSEPPT 227
                       250       260
                ....*....|....*....|....*....
gi 3426027  249 VDDITEYcPREIISLMKLCWEANPEARPT 277
Cdd:cd06611 228 LDQPSKW-SSSFNDFLKSCLVKDPDDRPT 255
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
69-284 2.27e-20

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 92.04  E-value: 2.27e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   69 RLRHSRVVKLLGV---IIEEG--KYSLVMEYMEKGNLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGK---------GV 134
Cdd:cd14054  45 LMEHSNILRFIGAderPTADGrmEYLLVLEYAPKGSLCSYLRENTLDWMSSC-RMALSLTRGLAYLHTDlrrgdqykpAI 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASFKMWSKLnneEHNELREVDGTAKKNGGTLYYMAPEHLND-VNAKPTEKS---- 209
Cdd:cd14054 124 AHRDLNSRNVLVKADGSCVICDFGLAMVLRGSSL---VRGRPGAAENASISEVGTLRYMAPEVLEGaVNLRDCESAlkqv 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  210 DVYSFAVVLWAI-------FANKE------PYE-----NAICEQQLIMCIKSGNRPDVDDI---TEYCPREIISLMKLCW 268
Cdd:cd14054 201 DVYALGLVLWEIamrcsdlYPGESvppyqmPYEaelgnHPTFEDMQLLVSREKARPKFPDAwkeNSLAVRSLKETIEDCW 280
                       250
                ....*....|....*.
gi 3426027  269 EANPEARPTFPGIEEK 284
Cdd:cd14054 281 DQDAEARLTALCVEER 296
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
16-303 2.30e-20

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: 92.05  E-value: 2.30e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06618  16 DLENLGEIGSGTCGQVYKMRHKKTGhVMAVKQMRRSGNKEENKRILMDLDVVLKSHDCPYIVKCYGYFITDSDVFICMEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MekGNLMHVLKAEMSTPL--SVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnne 171
Cdd:cd06618  96 M--STCLDKLLKRIQGPIpeDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISG---------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelREVDGTAK-KNGGTLYYMAPEHLnDVNAKPTE--KSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPD 248
Cdd:cd06618 164 -----RLVDSKAKtRSAGCAAYMAPERI-DPPDNPKYdiRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPS 237
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  249 VDDITEYCPrEIISLMKLCWEANPEARPTFPGIEEkfRPFYLSQleESVEEDVKS 303
Cdd:cd06618 238 LPPNEGFSP-DFCSFVDLCLTKDHRYRPKYRELLQ--HPFIRRY--ETAEVDVAS 287
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-288 2.34e-20

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: 91.17  E-value: 2.34e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLM-IMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd08225  11 GSFGKIYLAKAKSDSEHcVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYCDGGDLMKRI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSvKGRII---LEIIEGMCYLHGKGVIHKDLKPENI-LVDNDFHIKIADLGLAsfkmwSKLNNEehNELrevd 180
Cdd:cd08225  91 NRQRGVLFS-EDQILswfVQISLGLKHIHDRKILHRDIKSQNIfLSKNGMVAKLGDFGIA-----RQLNDS--MEL---- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  181 gtAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYE-NAIceQQLIMCIKSGNrpdVDDITEYCPRE 259
Cdd:cd08225 159 --AYTCVGTPYYLSPEICQ--NRPYNNKTDIWSLGCVLYELCTLKHPFEgNNL--HQLVLKICQGY---FAPISPNFSRD 229
                       250       260
                ....*....|....*....|....*....
gi 3426027  260 IISLMKLCWEANPEARPTFPGIEEkfRPF 288
Cdd:cd08225 230 LRSLISQLFKVSPRDRPSITSILK--RPF 256
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
60-281 2.47e-20

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: 91.47  E-value: 2.47e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAE--MSTPLSVKGrIILEIIEGMCYLHGKGVIHK 137
Cdd:cd05066  52 FLSEASIMGQFDHPNIIHLEGVVTRSKPVMIVTEYMENGSLDAFLRKHdgQFTVIQLVG-MLRGIASGMKYLSDMGYVHR 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnELREVDGTA--KKNGGTL--YYMAPEHLndVNAKPTEKSDVYS 213
Cdd:cd05066 131 DLAARNILVNSNLVCKVSDFGLS--------------RVLEDDPEAayTTRGGKIpiRWTAPEAI--AYRKFTSASDVWS 194
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  214 FAVVLWAIFANKE-PYENaICEQQLIMCIKSGNR--PDVDditeyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05066 195 YGIVMWEVMSYGErPYWE-MSNQDVIKAIEEGYRlpAPMD-----CPAALHQLMLDCWQKDRNERPKFEQI 259
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
17-228 2.92e-20

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 91.48  E-value: 2.92e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCFHRTQGLMIM--KTVYKGPNCIEHNEALLEEAKMMNRLrHSR-VVKLLGVIIEEGKYSLVME 93
Cdd:cd05608   3 FLDFRVLGKGGFGEVSACQMRATGKLYAckKLNKKRLKKRKGYEGAMVEKRILAKV-HSRfIVSLAYAFQTKTDLCLVMT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNL-MHVLKAEMSTPLSVKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskln 169
Cdd:cd05608  82 IMNGGDLrYHIYNVDEENPGFQEPRACFytaQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAV-------- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  170 neehnELREVDGTAKKNGGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05608 154 -----ELKDGQTKTKGYAGTPGFMAPELLLG--EEYDYSVDYFTLGVTLYEMIAARGPF 205
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
18-283 3.23e-20

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 91.22  E-value: 3.23e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   18 LESAEL-DSGGFGKVslcFH-RTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEyM 95
Cdd:cd14153   2 LEIGELiGKGRFGQV---YHgRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQTRHENVVLFMGACMSPPHLAIITS-L 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDfHIKIADLGLASFKMWSKLNNEEh 173
Cdd:cd14153  78 CKGRTLYSVVRDAKVVLDVNKtrQIAQEIVKGMGYLHAKGILHKDLKSKNVFYDNG-KVVITDFGLFTISGVLQAGRRE- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 NELRevdgtakKNGGTLYYMAPEHLNDVNAKPTE-------KSDVYSFAVVLWAIFANKEPYENAICEqQLIMCIKSGNR 246
Cdd:cd14153 156 DKLR-------IQSGWLCHLAPEIIRQLSPETEEdklpfskHSDVFAFGTIWYELHAREWPFKTQPAE-AIIWQVGSGMK 227
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 3426027  247 PDVDDITeyCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14153 228 PNLSQIG--MGKEISDILLFCWAYEQEERPTFSKLME 262
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
58-282 3.65e-20

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: 91.16  E-value: 3.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIE--EGKYSLVMEYMEKGNLMHVlkaEMSTPLSV-KGRIIL-EIIEGMCYLHGKG 133
Cdd:cd14200  68 ERVYQEIAILKKLDHVNIVKLIEVLDDpaEDNLYMVFDLLRKGPVMEV---PSDKPFSEdQARLYFrDIVLGIEYLHYQK 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKS-DVY 212
Cdd:cd14200 145 IVHRDIKPSNLLLGDDGHVKIADFGVS-------------NQFEGNDALLSSTAGTPAFMAPETLSDSGQSFSGKAlDVW 211
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  213 SFAVVLWAIFANKEPYenaICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGIE 282
Cdd:cd14200 212 AMGVTLYCFVYGKCPF---IDEFILALHNKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIK 278
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
26-278 5.86e-20

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 90.41  E-value: 5.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVslCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMeKGNLMHVLK 105
Cdd:cd14152  11 GRWGKV--HRGRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQTRHENVVLFMGACMHPPHLAIITSFC-KGRTLYSFV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  106 AEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDfHIKIADLGLASFKMWSKLNNEEhNELrevdgta 183
Cdd:cd14152  88 RDPKTSLDINKtrQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNG-KVVITDFGLFGISGVVQEGRRE-NEL------- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  184 KKNGGTLYYMAPEHL------NDVNAKPTEK-SDVYSFAVVLWAIFANKEPYENAICEqQLIMCIKSGNRPDVDDITEYC 256
Cdd:cd14152 159 KLPHDWLCYLAPEIVremtpgKDEDCLPFSKaADVYAFGTIWYELQARDWPLKNQPAE-ALIWQIGSGEGMKQVLTTISL 237
                       250       260
                ....*....|....*....|..
gi 3426027  257 PREIISLMKLCWEANPEARPTF 278
Cdd:cd14152 238 GKEVTEILSACWAFDLEERPSF 259
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
25-281 8.65e-20

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: 89.93  E-value: 8.65e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVslCFHR------TQGLMIMKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd05065  14 AGEFGEV--CRGRlklpgkREIFVAIKTL-KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRPVMIITEFMENG 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAE--MSTPLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNEL 176
Cdd:cd05065  91 ALDSFLRQNdgQFTVIQLVG-MLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDTSDPTYTSSL 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 revdgtakknGGTL--YYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKE-PYENaICEQQLIMCIKSGNR--PDVDd 251
Cdd:cd05065 170 ----------GGKIpiRWTAPEAI--AYRKFTSASDVWSYGIVMWEVMSYGErPYWD-MSNQDVINAIEQDYRlpPPMD- 235
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  252 iteyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05065 236 ----CPTALHQLMLDCWQKDRNLRPKFGQI 261
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-277 9.10e-20

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: 89.35  E-value: 9.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPncIEHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14083  11 LGTGAFSEVVLAEDKATGKLVaIKCIDKKA--LKGKEDSLEnEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELVTGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLasfkmwSKLNNEehnelr 177
Cdd:cd14083  89 FDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGL------SKMEDS------ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAkknGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPY--EN-AICEQQLIMCIKSGNRPDVDDIT 253
Cdd:cd14083 157 GVMSTA---CGTPGYVAPEVLAQ---KPYGKAvDCWSIGVISYILLCGYPPFydENdSKLFAQILKAEYEFDSPYWDDIS 230
                       250       260
                ....*....|....*....|....
gi 3426027  254 EYCPREIISLMklcwEANPEARPT 277
Cdd:cd14083 231 DSAKDFIRHLM----EKDPNKRYT 250
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
12-278 9.84e-20

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 90.47  E-value: 9.84e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   12 MKSSDFLESAELDSGGFGKVSLCFHRTQG----LMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEgK 87
Cdd:cd05108   4 LKETEFKKIKVLGSGAFGTVYKGLWIPEGekvkIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTS-T 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEKGNLMHVLKAEMStplSVKGRIIL----EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfK 163
Cdd:cd05108  83 VQLITQLMPFGCLLDYVREHKD---NIGSQYLLnwcvQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLA--K 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 MWSKLNNEEHNELREVdgtakknggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAI--FANKePYEnAICEQQLIMCI 241
Cdd:cd05108 158 LLGAEEKEYHAEGGKV---------PIKWMALESI--LHRIYTHQSDVWSYGVTVWELmtFGSK-PYD-GIPASEISSIL 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 3426027  242 KSGNRPDVDDIteyCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05108 225 EKGERLPQPPI---CTIDVYMIMVKCWMIDADSRPKF 258
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
26-277 1.05e-19

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: 89.31  E-value: 1.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKgPNCI--EHneaLLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14095  11 GNFAVVKECRDKaTDKEYALKIIDK-AKCKgkEH---MIEnEVAILRRVKHPNIVQLIEEYDTDTELYLVMELVKGGDLF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV----DNDFHIKIADLGLASfkmwsklnneehnelr 177
Cdd:cd14095  87 DAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLAT---------------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKNGGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFANKEPYENAICEQQ-LIMCIKSGN----RPDVDDI 252
Cdd:cd14095 151 EVKEPLFTVCGTPTYVAPEILAETGYGL--KVDIWAAGVITYILLCGFPPFRSPDRDQEeLFDLILAGEfeflSPYWDNI 228
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCpREIISLMklcWEANPEARPT 277
Cdd:cd14095 229 SDSA-KDLISRM---LVVDPEKRYS 249
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
23-277 1.12e-19

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: 88.86  E-value: 1.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIM-KTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14006   1 LGRGRFGVVKRCIEKATGREFAaKFIPKRD---KKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVL--KAEMSTPlSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVD--NDFHIKIADLGLAsfkmwSKLNNEEHnelr 177
Cdd:cd14006  78 DRLaeRGSLSEE-EVR-TYMRQLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLA-----RKLNPGEE---- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdgtAKKNGGTLYYMAPEHLNDVNAKPTekSDVYSFAVVLWAIFANKEPY--ENaicEQQLIMCIKSGN----RPDVDD 251
Cdd:cd14006 147 -----LKEIFGTPEFVAPEIVNGEPVSLA--TDMWSIGVLTYVLLSGLSPFlgED---DQETLANISACRvdfsEEYFSS 216
                       250       260
                ....*....|....*....|....*.
gi 3426027  252 ITEYCPREIISLMKlcweANPEARPT 277
Cdd:cd14006 217 VSQEAKDFIRKLLV----KEPRKRPT 238
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
23-199 1.45e-19

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: 88.44  E-value: 1.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEhNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14103   1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKD-REDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTpLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDN--DFHIKIADLGLASFkmwsklnneeHNElre 178
Cdd:cd14103  80 RVVDDDFE-LTERDCILFmrQICEGVQYMHKQGILHLDLKPENILCVSrtGNQIKIIDFGLARK----------YDP--- 145
                       170       180
                ....*....|....*....|.
gi 3426027  179 vDGTAKKNGGTLYYMAPEHLN 199
Cdd:cd14103 146 -DKKLKVLFGTPEFVAPEVVN 165
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
16-283 1.53e-19

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: 88.60  E-value: 1.53e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNC----IEH---NEALLEEAKM--MNRLRHSRVVKLLGVIIEE 85
Cdd:cd14004   1 DYTILKEMGEGAYGQVNLAIYKSKGkEVVIKFIFKERILvdtwVRDrklGTVPLEIHILdtLNKRSHPNIVKLLDFFEDD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEymEKGNLMHV-----LKAEMSTPLSvkGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd14004  81 EFYYLVME--KHGSGMDLfdfieRKPNMDEKEA--KYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  161 SFkmwsklnneehnelrevdgtaKKNG------GTLYYMAPEHL--NDVNAKPtekSDVYSFAVVLWAIFANKEPYENai 232
Cdd:cd14004 157 AY---------------------IKSGpfdtfvGTIDYAAPEVLrgNPYGGKE---QDIWALGVLLYTLVFKENPFYN-- 210
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 3426027  233 ceqqlimcIKSGNRPDVdDITEYCPREIISLMKLCWEANPEARPTfpgIEE 283
Cdd:cd14004 211 --------IEEILEADL-RIPYAVSEDLIDLISRMLNRDVGDRPT---IEE 249
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
58-278 1.56e-19

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: 89.13  E-value: 1.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIE-EGKYSL-----VMEYMEKGNL------MHVLKAEMSTPLSVKGRIILEIIEG 125
Cdd:cd05035  46 EEFLSEAACMKDFDHPNVMRLIGVCFTaSDLNKPpspmvILPFMKHGDLhsyllySRLGGLPEKLPLQTLLKFMVDIAKG 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  126 MCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVDGTAKKnggtlyYMAPEHLNDvnAKP 205
Cdd:cd05035 126 MEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS-----RKIYSGDYYRQGRISKMPVK------WIALESLAD--NVY 192
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  206 TEKSDVYSFAVVLWAIFA-NKEPY---ENAICEQQLImcikSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd05035 193 TSKSDVWSFGVTMWEIATrGQTPYpgvENHEIYDYLR----NGNRLKQ---PEDCLDEVYFLMYFCWTVDPKDRPTF 262
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
23-291 1.63e-19

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 89.77  E-value: 1.63e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRT----QGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd05582   3 LGQGSFGKVFLVRKITgpdaGTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAE-MSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKlnneehnELR 177
Cdd:cd05582  83 DLFTRLSKEvMFTEEDVK-FYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGL------SK-------ESI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKNGGTLYYMAPEhlnDVNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSG-NRPdvdditEY 255
Cdd:cd05582 149 DHEKKAYSFCGTVEYMAPE---VVNRRGhTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKlGMP------QF 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 3426027  256 CPREIISLMKLCWEANPEAR--PTFPGIEE-KFRPFYLS 291
Cdd:cd05582 220 LSPEAQSLLRALFKRNPANRlgAGPDGVEEiKRHPFFAT 258
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
55-289 1.75e-19

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: 89.20  E-value: 1.75e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLR-HSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKG 133
Cdd:cd14182  51 ELREATLKEIDILRKVSgHPNIIQLKDTYETNTFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwskLNNEEHNELREVDGTAKknggtlyYMAPE----HLNDVNAKPTEKS 209
Cdd:cd14182 131 IVHRDLKPENILLDDDMNIKLTDFGFS-------CQLDPGEKLREVCGTPG-------YLAPEiiecSMDDNHPGYGKEV 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  210 DVYSFAVVLWAIFANKEPYENaicEQQLIMC--IKSGN----RPDVDDITEYCpREIISLMKLcweANPEARptFPGIEE 283
Cdd:cd14182 197 DMWSTGVIMYTLLAGSPPFWH---RKQMLMLrmIMSGNyqfgSPEWDDRSDTV-KDLISRFLV---VQPQKR--YTAEEA 267

                ....*.
gi 3426027  284 KFRPFY 289
Cdd:cd14182 268 LAHPFF 273
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
60-223 1.82e-19

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 90.21  E-value: 1.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    60 LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEkGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:PTZ00024  67 TLRELKIMNEIKHENIMGLVDVYVEGDFINLVMDIMA-SDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   140 KPENILVDNDFHIKIADLGLAS---FKMWS-KLNNEEHNELREvDGTAKKNggTLYYMAPEHLNDvnakptekSDVYSFA 215
Cdd:PTZ00024 146 SPANIFINSKGICKIADFGLARrygYPPYSdTLSKDETMQRRE-EMTSKVV--TLWYRAPELLMG--------AEKYHFA 214
                        170
                 ....*....|.
gi 3426027   216 VVLWA---IFA 223
Cdd:PTZ00024 215 VDMWSvgcIFA 225
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
23-285 1.96e-19

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: 88.34  E-value: 1.96e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKgpNCIEHNeALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYK--NDVDQH-KIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLkAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLAsfkmwsklnnEEHNELR 177
Cdd:cd14156  78 LL-AREELPLSWREKVELacDISRGMVYLHSKNIYHRDLNSKNCLIrvtPRGREAVVTDFGLA----------REVGEMP 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKN-GGTLYYMAPEHLndvNAKP-TEKSDVYSFAVVLWAIFANkepyenaICEQQLIMCIKSGNRPDVDDITEY 255
Cdd:cd14156 147 ANDPERKLSlVGSAFWMAPEML---RGEPyDRKVDVFSFGIVLCEILAR-------IPADPEVLPRTGDFGLDVQAFKEM 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  256 ---CPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd14156 217 vpgCPEPFLDLAASCCRMDAFKRPSFAELLDEL 249
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
70-277 2.05e-19

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 89.07  E-value: 2.05e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   70 LRHSRVVKLLGV-IIEEGKYS---LVMEYMEKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLH-------GKGVI-HK 137
Cdd:cd14144  46 MRHENILGFIAAdIKGTGSWTqlyLITDYHENGSLYDFLRGNTLDTQSM-LKLAYSAACGLAHLHteifgtqGKPAIaHR 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwSKLNneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAK----PTEKSDVYS 213
Cdd:cd14144 125 DIKSKNILVKKNGTCCIADLGLA-----VKFI----SETNEVDLPPNTRVGTKRYMAPEVLDESLNRnhfdAYKMADMYS 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  214 FAVVLWAIfaNKEPYENAICEQ-QL-----------------IMCIKsGNRPDVDD--ITEYCPREIISLMKLCWEANPE 273
Cdd:cd14144 196 FGLVLWEI--ARRCISGGIVEEyQLpyydavpsdpsyedmrrVVCVE-RRRPSIPNrwSSDEVLRTMSKLMSECWAHNPA 272

                ....
gi 3426027  274 ARPT 277
Cdd:cd14144 273 ARLT 276
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
22-277 2.10e-19

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: 88.21  E-value: 2.10e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQG----LMIMKTVYKGPNCiehnEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14078  10 TIGSGGFAKVKLATHILTGekvaIKIMDKKALGDDL----PRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLEYCPG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMH--VLKAEMSTPlsvKGRIIL-EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehn 174
Cdd:cd14078  86 GELFDyiVAKDRLSED---EARVFFrQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLC-------------- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 elrevdgtAKKNGGTLY----------YMAPEHlndVNAKP--TEKSDVYSFAVVLWAIFANKEPYENAICeQQLIMCIK 242
Cdd:cd14078 149 --------AKPKGGMDHhletccgspaYAAPEL---IQGKPyiGSEADVWSMGVLLYALLCGFLPFDDDNV-MALYRKIQ 216
                       250       260       270
                ....*....|....*....|....*....|....*
gi 3426027  243 SGnrpdVDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14078 217 SG----KYEEPEWLSPSSKLLLDQMLQVDPKKRIT 247
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-227 2.12e-19

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: 89.73  E-value: 2.12e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   11 KMKSSDFLESAELDSGGFGKVSLCFHRTQGL-MIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd06650   1 ELKDDDFEKISELGAGNGGVVFKVSHKPSGLvMARKLIHLEIKPAIRNQ-IIRELQVLHECNSPYIVGFYGAFYSDGEIS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwskl 168
Cdd:cd06650  80 ICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSG------- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  169 nneehnelREVDGTAKKNGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEP 227
Cdd:cd06650 153 --------QLIDSMANSFVGTRSYMSPERLQGTHY--SVQSDIWSMGLSLVEMAVGRYP 201
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
70-277 2.14e-19

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 89.04  E-value: 2.14e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   70 LRHSRVvklLGVIIEEGKYS-------LVMEYMEKGNLMHVLKaemSTPLSVKG--RIILEIIEGMCYLH-------GKG 133
Cdd:cd14143  46 LRHENI---LGFIAADNKDNgtwtqlwLVSDYHEHGSLFDYLN---RYTVTVEGmiKLALSIASGLAHLHmeivgtqGKP 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VI-HKDLKPENILVDNDFHIKIADLGLASfkmwsklnneEHNELRE-VDGTAKKNGGTLYYMAPEHLND-VNAKPTE--- 207
Cdd:cd14143 120 AIaHRDLKSKNILVKKNGTCCIADLGLAV----------RHDSATDtIDIAPNHRVGTKRYMAPEVLDDtINMKHFEsfk 189
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  208 KSDVYSFAVVLWAI----------------FANKEPYENAICEQQLIMCIKsGNRPDVDDITEYCP--REIISLMKLCWE 269
Cdd:cd14143 190 RADIYALGLVFWEIarrcsiggihedyqlpYYDLVPSDPSIEEMRKVVCEQ-KLRPNIPNRWQSCEalRVMAKIMRECWY 268

                ....*...
gi 3426027  270 ANPEARPT 277
Cdd:cd14143 269 ANGAARLT 276
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
16-277 2.22e-19

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: 88.55  E-value: 2.22e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESaeLDSGGFGKVSLC-FHRTQGLMIMKTVYKgpNCIEHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd14167   6 DFREV--LGTGAFSEVVLAeEKRTQKLVAIKCIAK--KALEGKETSIEnEIAVLHKIKHPNIVALDDIYESGGHLYLIMQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENIL---VDNDFHIKIADLGLasfkmwSKLnn 170
Cdd:cd14167  82 LVSGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGL------SKI-- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eehnelrEVDGTAKKNG-GTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPY--EN-AICEQQLIMCIKSGN 245
Cdd:cd14167 154 -------EGSGSVMSTAcGTPGYVAPEVLAQ---KPYSKAvDCWSIGVIAYILLCGYPPFydENdAKLFEQILKAEYEFD 223
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  246 RPDVDDITEYCPREIISLMklcwEANPEARPT 277
Cdd:cd14167 224 SPYWDDISDSAKDFIQHLM----EKDPEKRFT 251
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
23-277 2.57e-19

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: 88.26  E-value: 2.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNE----ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd06631   9 LGKGAYGTVYCGLTSTGQLIAVKQVELDTSDKEKAEkeyeKLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFVPGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELRE 178
Cdd:cd06631  89 SIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKRLCINLSSGSQSQLLKS 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGTAkknggtlYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYENaICEQQLIMCIKSGNRPdVDDITEYCPR 258
Cdd:cd06631 169 MRGTP-------YWMAPEVINETGHG--RKSDIWSIGCTVFEMATGKPPWAD-MNPMAAIFAIGSGRKP-VPRLPDKFSP 237
                       250
                ....*....|....*....
gi 3426027  259 EIISLMKLCWEANPEARPT 277
Cdd:cd06631 238 EARDFVHACLTRDQDERPS 256
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
23-230 2.78e-19

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: 88.31  E-value: 2.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGL----------MIMKTVYKGPNcieHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14076   9 LGEGEFGKVKLGWPLPKANhrsgvqvaikLIRRDTQQENC---QTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS-FkmwsklnNE 171
Cdd:cd14076  86 EFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANtF-------DH 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  172 EHNELrevdgtAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd14076 159 FNGDL------MSTSCGSPCYAAPELVVSDSMYAGRKADIWSCGVILYAMLAGYLPFDD 211
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
11-245 4.66e-19

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: 88.83  E-value: 4.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   11 KMKSSDFLESAELDSGGFGKVSLC-FHRTQGLMIMKTVYKGPNCIEHN-EALLEEAKMMN-RLRHSRVVKLLGVIIEEGK 87
Cdd:cd05619   1 KLTIEDFVLHKMLGKGSFGKVFLAeLKGTNQFFAIKALKKDVVLMDDDvECTMVEKRVLSlAWEHPFLTHLFCTFQTKEN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWsk 167
Cdd:cd05619  81 LFFVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENML-- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 lnneehnelrevdGTAKKNG--GTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIKSGN 245
Cdd:cd05619 159 -------------GDAKTSTfcGTPDYIAPEIL--LGQKYNTSVDWWSFGVLLYEMLIGQSPF-HGQDEEELFQSIRMDN 222
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
66-298 4.70e-19

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: 88.50  E-value: 4.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   66 MMNR-LRHSRVVKLLGVIIE--EGKYSLVMEYMEKgNLMHVLK------AEMSTPLSVKgRIILEIIEGMCYLHGKGVIH 136
Cdd:cd07842  54 ALLReLKHENVVSLVEVFLEhaDKSVYLLFDYAEH-DLWQIIKfhrqakRVSIPPSMVK-SLLWQILNGIHYLHSNWVLH 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFH----IKIADLGLAsfkmwsKLNNEEHNELREVDGTAKknggTLYYMAPEHLndVNAKPteksdvY 212
Cdd:cd07842 132 RDLKPANILVMGEGPergvVKIGDLGLA------RLFNAPLKPLADLDPVVV----TIWYRAPELL--LGARH------Y 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  213 SFAVVLWA---IFAnkepyenaiceqqlimciksgnrpdvdditeycprEIISLmklcweanpeaRPTFPGIEEKFR--- 286
Cdd:cd07842 194 TKAIDIWAigcIFA-----------------------------------ELLTL-----------EPIFKGREAKIKksn 227
                       250
                ....*....|..
gi 3426027  287 PFYLSQLEESVE 298
Cdd:cd07842 228 PFQRDQLERIFE 239
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
58-278 4.90e-19

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: 87.76  E-value: 4.90e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIE----EGKYS--LVMEYMEKGNLMHVL------KAEMSTPLSVKGRIILEIIEG 125
Cdd:cd05075  46 EDFLSEAVCMKEFDHPNVMRLIGVCLQntesEGYPSpvVILPFMKHGDLHSFLlysrlgDCPVYLPTQMLVKFMTDIASG 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  126 MCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVDGTAKKnggtlyYMAPEHLNDvnAKP 205
Cdd:cd05075 126 MEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLS-----KKIYNGDYYRQGRISKMPVK------WIAIESLAD--RVY 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  206 TEKSDVYSFAVVLWAIFA-NKEPY---ENAiceqQLIMCIKSGNR----PDvdditeyCPREIISLMKLCWEANPEARPT 277
Cdd:cd05075 193 TTKSDVWSFGVTMWEIATrGQTPYpgvENS----EIYDYLRQGNRlkqpPD-------CLDGLYELMSSCWLLNPKDRPS 261

                .
gi 3426027  278 F 278
Cdd:cd05075 262 F 262
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
23-228 5.25e-19

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: 87.44  E-value: 5.25e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGL-MIMKTVYKGPNCIEHNE---ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLV--MEYME 96
Cdd:cd06651  15 LGQGAFGRVYLCYDVDTGReLAAKQVQFDPESPETSKevsALECEIQLLKNLQHERIVQYYGCLRDRAEKTLTifMEYMP 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLnneehnel 176
Cdd:cd06651  95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-ASKRLQTIC-------- 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3426027  177 reVDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd06651 166 --MSGTGIRSvTGTPYWMSPEVIS--GEGYGRKADVWSLGCTVVEMLTEKPPW 214
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
23-228 7.01e-19

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 87.02  E-value: 7.01e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGL-MIMKTVYKGPNCIEHNE---ALLEEAKMMNRLRHSRVVKLLGVI--IEEGKYSLVMEYME 96
Cdd:cd06652  10 LGQGAFGRVYLCYDADTGReLAVKQVQFDPESPETSKevnALECEIQLLKNLLHERIVQYYGCLrdPQERTLSIFMEYMP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMWSKLnneehnel 176
Cdd:cd06652  90 GGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG-ASKRLQTIC-------- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3426027  177 reVDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd06652 161 --LSGTGMKSvTGTPYWMSPEVIS--GEGYGRKADIWSVGCTVVEMLTEKPPW 209
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
23-277 7.56e-19

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: 87.12  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLEEAKMMNR-------------LRHSRVVKLLGVIIEEGKY 88
Cdd:cd14077   9 IGAGSMGKVKLAKHIRTGeKCAIKIIPRASNAGLKKEREKRLEKEISRdirtireaalsslLNHPHICRLRDFLRTPNHY 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   89 SLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKL 168
Cdd:cd14077  89 YMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNLYDPRRL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 nneehneLREVdgtakknGGTLYYMAPEHLndvNAKP--TEKSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKSGnr 246
Cdd:cd14077 169 -------LRTF-------CGSLYFAAPELL---QAQPytGPEVDVWSFGVVLYVLVCGKVPFDDE-NMPALHAKIKKG-- 228
                       250       260       270
                ....*....|....*....|....*....|.
gi 3426027  247 pDVdDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14077 229 -KV-EYPSYLSSECKSLISRMLVVDPKKRAT 257
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
22-277 8.32e-19

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 86.93  E-value: 8.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLC-----FHRTQGLMIMKTVYKGPncIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd14206   4 EIGNGWFGKVILGeifsdYTPAQVVVKELRVSAGP--LEQRK-FISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFCQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVL----KAEMSTP------LSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmws 166
Cdd:cd14206  81 LGDLKRYLraqrKADGMTPdlptrdLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLS------ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 klnneeHNELRE-VDGTAKKNGGTLYYMAPEHLNDVNAK-----PTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIM 239
Cdd:cd14206 155 ------HNNYKEdYYLTPDRLWIPLRWVAPELLDELHGNlivvdQSKESNVWSLGVTIWELFEfGAQPYRHLSDEEVLTF 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 3426027  240 CIKSgnrpdvDDITEYCPREIIS-------LMKLCWEAnPEARPT 277
Cdd:cd14206 229 VVRE------QQMKLAKPRLKLPyadywyeIMQSCWLP-PSQRPS 266
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
117-281 8.80e-19

Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. CSF-1R, also called c-Fms, is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of CSF-1R to its ligand, CSF-1, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. It leads to increases in gene transcription and protein translation, and induces cytoskeletal remodeling. CSF-1R signaling leads to a variety of cellular responses including survival, proliferation, and differentiation of target cells. It plays an important role in innate immunity, tissue development and function, and the pathogenesis of some diseases including atherosclerosis and cancer. CSF-1R signaling is also implicated in mammary gland development during pregnancy and lactation. Aberrant CSF-1/CSF-1R expression correlates with tumor cell invasiveness, poor clinical prognosis, and bone metastasis in breast cancer. Although the structure of the human CSF-1R catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. The CSF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 88.75  E-value: 8.80e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  117 RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklNNEEHnelrEVDGTAKKnggTLYYMAPE 196
Cdd:cd05106 216 RFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIM----NDSNY----VVKGNARL---PVKWMAPE 284
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  197 HLNDVNAkpTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSG---NRPDvdditeYCPREIISLMKLCWEANP 272
Cdd:cd05106 285 SIFDCVY--TVQSDVWSYGILLWEIFSlGKSPYPGILVNSKFYKMVKRGyqmSRPD------FAPPEIYSIMKMCWNLEP 356

                ....*....
gi 3426027  273 EARPTFPGI 281
Cdd:cd05106 357 TERPTFSQI 365
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
14-228 9.43e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 86.51  E-value: 9.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   14 SSDF-LESAELDSGG-FGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEeAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14190   1 SSTFsIHSKEVLGGGkFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLE-IQVMNQLNHRNLIQLYEAIETPNEIVLF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIIL-EIIEGMCYLHGKGVIHKDLKPENIL-VDNDFH-IKIADLGLAsfkmwSKL 168
Cdd:cd14190  80 MEYVEGGELFERIVDEDYHLTEVDAMVFVrQICEGIQFMHQMRVLHLDLKPENILcVNRTGHqVKIIDFGLA-----RRY 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  169 NNEEhnelrevdgTAKKNGGTLYYMAPEHLN-DVNAKPTeksDVYSFAVVLWAIFANKEPY 228
Cdd:cd14190 155 NPRE---------KLKVNFGTPEFLSPEVVNyDQVSFPT---DMWSMGVITYMLLSGLSPF 203
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
70-277 9.66e-19

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


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 87.02  E-value: 9.66e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   70 LRHSRVVKLLGVIIE-EGKYS---LVMEYMEKGNLMHVLKAemsTPLSVKG--RIILEIIEGMCYLH-------GKGVI- 135
Cdd:cd14220  46 MRHENILGFIAADIKgTGSWTqlyLITDYHENGSLYDFLKC---TTLDTRAllKLAYSAACGLCHLHteiygtqGKPAIa 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHnelrEVDGTAKKNGGTLYYMAP----EHLNDVNAKPTEKSDV 211
Cdd:cd14220 123 HRDLKSKNILIKKNGTCCIADLGLA-----VKFNSDTN----EVDVPLNTRVGTKRYMAPevldESLNKNHFQAYIMADI 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  212 YSFAVVLWAI----------------FANKEPYENAICEQQLIMCIKsGNRPDVDDI--TEYCPREIISLMKLCWEANPE 273
Cdd:cd14220 194 YSFGLIIWEMarrcvtggiveeyqlpYYDMVPSDPSYEDMREVVCVK-RLRPTVSNRwnSDECLRAVLKLMSECWAHNPA 272

                ....
gi 3426027  274 ARPT 277
Cdd:cd14220 273 SRLT 276
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-277 1.08e-18

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: 86.32  E-value: 1.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLC----FHRTQGLMIMKTVYKG---PNciEHNEALLEeAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd08222   8 LGSGNFGTVYLVsdlkATADEELKVLKEISVGelqPD--ETVDANRE-AKLLSKLDHPAIVKFHDSFVEKESFCIVTEYC 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVKGRIILE----IIEGMCYLHGKGVIHKDLKPENILVDNDFhIKIADLGLASFKMwsklnne 171
Cdd:cd08222  85 EGGDLDDKISEYKKSGTTIDENQILDwfiqLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILM------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelrevdGT---AKKNGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYENaiceQQLIMCIKSGNRPD 248
Cdd:cd08222 157 ---------GTsdlATTFTGTPYYMSPEVLKHEGY--NSKSDIWSLGCILYEMCCLKHAFDG----QNLLSVMYKIVEGE 221
                       250       260
                ....*....|....*....|....*....
gi 3426027  249 VDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd08222 222 TPSLPDKYSKELNAIYSRMLNKDPALRPS 250
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
71-281 1.15e-18

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 86.63  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   71 RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKA------------EMSTPLSVKGRIIL----EIIEGMCYLHGKGV 134
Cdd:cd05047  54 HHPNIINLLGACEHRGYLYLAIEYAPHGNLLDFLRKsrvletdpafaiANSTASTLSSQQLLhfaaDVARGMDYLSQKQF 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNGGTL--YYMAPEHLNdvNAKPTEKSDVY 212
Cdd:cd05047 134 IHRDLAARNILVGENYVAKIADFGLS----------------RGQEVYVKKTMGRLpvRWMAIESLN--YSVYTTNSDVW 195
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  213 SFAVVLWAIFA-NKEPYENAICeQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05047 196 SYGVLLWEIVSlGGTPYCGMTC-AELYEKLPQGYRLEK---PLNCDDEVYDLMRQCWREKPYERPSFAQI 261
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
26-229 1.29e-18

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: 86.03  E-value: 1.29e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd14072  11 GNFAKVKLARHVLTGREVaIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAE---MSTPLSVKGRiilEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS-FKMWSKLNNeehnelrevd 180
Cdd:cd14072  91 VAHgrmKEKEARAKFR---QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNeFTPGNKLDT---------- 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 3426027  181 gtakkNGGTLYYMAPEHLNDVNAKPTEkSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd14072 158 -----FCGSPPYAAPELFQGKKYDGPE-VDVWSLGVILYTLVSGSLPFD 200
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
15-255 1.33e-18

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: 86.47  E-value: 1.33e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFG-------KVSLCFHRTQGLMImktvykgPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIE--- 84
Cdd:cd14048   6 TDFEPIQCLGRGGFGvvfeaknKVDDCNYAVKRIRL-------PNNELAREKVLREVRALAKLDHPGIVRYFNAWLErpp 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 --------EGKYSLVMEYMEKGNL---MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIK 153
Cdd:cd14048  79 egwqekmdEVYLYIQMQLCRKENLkdwMNRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVK 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  154 IADLGLASfKMwsKLNNEEHNELREVDGTAK--KNGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLW------------ 219
Cdd:cd14048 159 VGDFGLVT-AM--DQGEPEQTVLTPMPAYAKhtGQVGTRLYMSPEQIHGNQY--SEKVDIFALGLILFeliysfstqmer 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 3426027  220 -------------AIFANKEPYENAICEQQLimCIKSGNRPDVDDITEY 255
Cdd:cd14048 234 irtltdvrklkfpALFTNKYPEERDMVQQML--SPSPSERPEAHEVIEH 280
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
23-228 1.63e-18

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: 85.78  E-value: 1.63e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14192  12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREE-VKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELFD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEmSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDNDF--HIKIADLGLA-SFKMWSKLnneehnelr 177
Cdd:cd14192  91 RITDE-SYQLTELDAILFtrQICEGVHYLHQHYILHLDLKPENILCVNSTgnQIKIIDFGLArRYKPREKL--------- 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  178 evdgtaKKNGGTLYYMAPEHLN-DVNAKPTeksDVYSFAVVLWAIFANKEPY 228
Cdd:cd14192 161 ------KVNFGTPEFLAPEVVNyDFVSFPT---DMWSVGVITYMLLSGLSPF 203
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
22-277 1.84e-18

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 85.72  E-value: 1.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSL---CFHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd05042   2 EIGNGWFGKVLLgeiYSGTSVAQVVVKELKASANPKEQDT-FLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFCDLG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAE-----MSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnNEEH 173
Cdd:cd05042  81 DLKAYLRSEreherGDSDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRY-----KEDY 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 NElrevdgTAKKNGGTLYYMAPEHLNDVN-----AKPTEKSDVYSFAVVLWAIFAN-KEPYENAICEQQLIMCIKSGN-- 245
Cdd:cd05042 156 IE------TDDKLWFPLRWTAPELVTEFHdrllvVDQTKYSNIWSLGVTLWELFENgAQPYSNLSDLDVLAQVVREQDtk 229
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  246 --RPDVDdiTEYCPReIISLMKLCWEAnPEARPT 277
Cdd:cd05042 230 lpKPQLE--LPYSDR-WYEVLQFCWLS-PEQRPA 259
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
60-231 2.08e-18

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: 85.60  E-value: 2.08e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKD 138
Cdd:cd14165  48 LPRELEILARLNHKSIIKTYEIFeTSDGKVYIVMELGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRD 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  139 LKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELRevdgTAKKNGGTLYYMAPEHLNDVNAKPtEKSDVYSFAVVL 218
Cdd:cd14165 128 LKCENLLLDKDFNIKLTDFGFS-----KRCLRDENGRIV----LSKTFCGSAAYAAPEVLQGIPYDP-RIYDIWSLGVIL 197
                       170
                ....*....|...
gi 3426027  219 WAIFANKEPYENA 231
Cdd:cd14165 198 YIMVCGSMPYDDS 210
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
58-304 2.16e-18

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: 86.14  E-value: 2.16e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEG-----KYSLVMEYMEKGNLMHVL---KAEMST---PLSVKGRIILEIIEGM 126
Cdd:cd14204  54 EEFLSEAACMKDFNHPNVIRLLGVCLEVGsqripKPMVILPFMKYGDLHSFLlrsRLGSGPqhvPLQTLLKFMIDIALGM 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  127 CYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaSFKMWSklnNEEHNELREVDGTAKknggtlyYMAPEHLNDvnAKPT 206
Cdd:cd14204 134 EYLSSRNFLHRDLAARNCMLRDDMTVCVADFGL-SKKIYS---GDYYRQGRIAKMPVK-------WIAVESLAD--RVYT 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  207 EKSDVYSFAVVLWAI----------FANKEPYENAICEQQLimciksgNRPdvdditEYCPREIISLMKLCWEANPEARP 276
Cdd:cd14204 201 VKSDVWAFGVTMWEIatrgmtpypgVQNHEIYDYLLHGHRL-------KQP------EDCLDELYDIMYSCWRSDPTDRP 267
                       250       260
                ....*....|....*....|....*...
gi 3426027  277 TFpgieekfrpfylSQLEESVEEDVKSL 304
Cdd:cd14204 268 TF------------TQLRENLEKLLESL 283
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
23-283 2.56e-18

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 86.57  E-value: 2.56e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKV--SLCFHRTQG----LMIMKTVYKGPNCIEHnEALLEEAKMMNRL-RHSRVVKLLGVIIE-EGKYSLVMEY 94
Cdd:cd05102  15 LGHGAFGKVveASAFGIDKSssceTVAVKMLKEGATASEH-KALMSELKILIHIgNHLNVVNLLGACTKpNGPLMVIVEF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLKAEMS----------------------------------------------------------TPLSVKG 116
Cdd:cd05102  94 CKYGNLSNFLRAKREgfspyrersprtrsqvrsmveavradrrsrqgsdrvasftestsstnqprqevddlwqSPLTMED 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  117 RII--LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneeHNELREVDGTAKKNGG-TLYYM 193
Cdd:cd05102 174 LICysFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLA------------RDIYKDPDYVRKGSARlPLKWM 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  194 APEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANP 272
Cdd:cd05102 242 APESIFD--KVYTTQSDVWSFGVLLWEIFSlGASPYPGVQINEEFCQRLKDGTRMRA---PEYATPEIYRIMLSCWHGDP 316
                       330
                ....*....|.
gi 3426027  273 EARPTFPGIEE 283
Cdd:cd05102 317 KERPTFSDLVE 327
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
58-279 3.24e-18

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: 84.96  E-value: 3.24e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHS-RVVKLLG--VIIEEGKYSLVMEYMEkGNLMHVLKAEMSTPLSVKGRIIL--EIIEGMCYLHGK 132
Cdd:cd14131  44 QSYKNEIELLKKLKGSdRIIQLYDyeVTDEDDYLYMVMECGE-IDLATILKKKRPKPIDPNFIRYYwkQMLEAVHTIHEE 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPEN-ILVDNdfHIKIADLGLASfkmwsKLNNEEHNELREVdgtakkNGGTLYYMAPEHLNDVNAKPTEK--- 208
Cdd:cd14131 123 GIVHSDLKPANfLLVKG--RLKLIDFGIAK-----AIQNDTTSIVRDS------QVGTLNYMSPEAIKDTSASGEGKpks 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  209 -----SDVYSFAVVLWAIFANKEPYENAICEQQLIMCIksgnrPDVDDITEY---CPREIISLMKLCWEANPEARPTFP 279
Cdd:cd14131 190 kigrpSDVWSLGCILYQMVYGKTPFQHITNPIAKLQAI-----IDPNHEIEFpdiPNPDLIDVMKRCLQRDPKKRPSIP 263
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
23-228 3.25e-18

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: 85.58  E-value: 3.25e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLM--IMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEY 94
Cdd:cd13989   1 LGSGGFGYVTLWKHQDTGEYvaIKKCRQELSPSDKNRERWCLEVQIMKKLNHPNVVSARDVPPELEKLSpndlplLAMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVL-KAEMSTPL-SVKGRIIL-EIIEGMCYLHGKGVIHKDLKPENIL---VDNDFHIKIADLGLAsfkmwskl 168
Cdd:cd13989  81 CSGGDLRKVLnQPENCCGLkESEVRTLLsDISSAISYLHENRIIHRDLKPENIVlqqGGGRVIYKLIDLGYA-------- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  169 nneehnelREVDGTAKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd13989 153 --------KELDQGSLCTSfvGTLQYLAPELFE--SKKYTCTVDYWSFGTLAFECITGYRPF 204
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
26-281 3.35e-18

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: 84.80  E-value: 3.35e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLM-IMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd08223  11 GSYGEVWLVRHKRDRKQyVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFeGEDGFLYIVMGFCEGGDLYTR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVKGRI--ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnnEEHNELrevdg 181
Cdd:cd08223  91 LKEQKGVLLEERQVVewFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVL-------ESSSDM----- 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 tAKKNGGTLYYMAPEHLNDvnaKP-TEKSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIKSGNRPDVDdiTEYCPrEI 260
Cdd:cd08223 159 -ATTLIGTPYYMSPELFSN---KPyNHKSDVWALGCCVYEMATLKHAF-NAKDMNSLVYKILEGKLPPMP--KQYSP-EL 230
                       250       260
                ....*....|....*....|.
gi 3426027  261 ISLMKLCWEANPEARPTFPGI 281
Cdd:cd08223 231 GELIKAMLHQDPEKRPSVKRI 251
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
58-229 3.76e-18

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 85.65  E-value: 3.76e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTP-LSVKGR--IILEIIEGMCYLHG--K 132
Cdd:cd14159  37 NSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVYLPNGSLEDRLHCQVSCPcLSWSQRlhVLLGTARAIQYLHSdsP 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREvdGTAKkngGTLYYMAPEHLNDvnAKPTEKSDVY 212
Cdd:cd14159 117 SLIHGDVKSSNILLDAALNPKLGDFGLARFSRRPKQPGMSSTLART--QTVR---GTLAYLPEEYVKT--GTLSVEIDVY 189
                       170
                ....*....|....*..
gi 3426027  213 SFAVVLWAIFANKEPYE 229
Cdd:cd14159 190 SFGVVLLELLTGRRAME 206
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
57-285 3.81e-18

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 85.08  E-value: 3.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   57 NEALLEEAKMMNRLRHSRVVKLLGVIIEEgKYSLVMEYMEKGNLMHVLKAEmstplsvKGRI--------ILEIIEGMCY 128
Cdd:cd05109  53 NKEILDEAYVMAGVGSPYVCRLLGICLTS-TVQLVTQLMPYGCLLDYVREN-------KDRIgsqdllnwCVQIAKGMSY 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  129 LHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnELREVDGTA-KKNGGT--LYYMAPEHLndVNAKP 205
Cdd:cd05109 125 LEEVRLVHRDLAARNVLVKSPNHVKITDFGLA--------------RLLDIDETEyHADGGKvpIKWMALESI--LHRRF 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  206 TEKSDVYSFAVVLWAIFA-NKEPYEnAICEQQLIMCIKSGNR---PDVdditeyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05109 189 THQSDVWSYGVTVWELMTfGAKPYD-GIPAREIPDLLEKGERlpqPPI------CTIDVYMIMVKCWMIDSECRPRFREL 261

                ....
gi 3426027  282 EEKF 285
Cdd:cd05109 262 VDEF 265
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
16-229 4.13e-18

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: 84.62  E-value: 4.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKG---PNCIEHNeaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14116   6 DFEIGRPLGKGKFGNVYLAREKqSKFILALKVLFKAqleKAGVEHQ--LRREVEIQSHLRHPNILRLYGYFHDATRVYLI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmWSklnne 171
Cdd:cd14116  84 LEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG------WS----- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  172 ehnelreVDGTAKKNG---GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd14116 153 -------VHAPSSRRTtlcGTLDYLPPEMIE--GRMHDEKVDLWSLGVLCYEFLVGKPPFE 204
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
22-277 4.68e-18

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: 84.28  E-value: 4.68e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd06613   7 RIGSGTYGDVYKARNIaTGELAAVKVIKLEPG--DDFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYCGGGSL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKaeMSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnelrE 178
Cdd:cd06613  85 QDIYQ--VTGPLSELqiAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSA----------------Q 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGT-AKKNG--GTLYYMAPEHLNdVNAKP--TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNR-PDVDDI 252
Cdd:cd06613 147 LTATiAKRKSfiGTPYWMAPEVAA-VERKGgyDGKCDIWALGITAIELAELQPPMFDLHPMRALFLIPKSNFDpPKLKDK 225
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd06613 226 EKWSP-DFHDFIKKCLTKNPKKRPT 249
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
61-223 6.70e-18

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: 85.27  E-value: 6.70e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYS-----LVMEYMEKgNLMHVLKaeMSTPLSVK--GRIILEIIEGMCYLHGKG 133
Cdd:cd07834  47 LREIKILRHLKHENIIGLLDILRPPSPEEfndvyIVTELMET-DLHKVIK--SPQPLTDDhiQYFLYQILRGLKYLHSAG 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNGGTLY-----YMAPEHLNDvnakptek 208
Cdd:cd07834 124 VIHRDLKPSNILVNSNCDLKICDFGLA----------------RGVDPDEDKGFLTEYvvtrwYRAPELLLS-------- 179
                       170
                ....*....|....*...
gi 3426027  209 SDVYSFAVVLWA---IFA 223
Cdd:cd07834 180 SKKYTKAIDIWSvgcIFA 197
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
43-277 7.03e-18

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: 83.98  E-value: 7.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   43 IMKTVyKGPNCIEHNEALLEEakmmNRLrhsrvvkllgviieegkySLVMEYMEKGNLMHVLK--AEMSTPLSVKG--RI 118
Cdd:cd08530  52 LLASV-NHPNIIRYKEAFLDG----NRL------------------CIVMEYAPFGDLSKLISkrKKKRRLFPEDDiwRI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  119 ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMWSKlnneehnelrevdGTAKKNGGTLYYMAPEHL 198
Cdd:cd08530 109 FIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGIS--KVLKK-------------NLAKTQIGTPLYAAPEVW 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  199 NDvnaKP-TEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVDDITEycpREIISLMKLCWEANPEARPT 277
Cdd:cd08530 174 KG---RPyDYKSDIWSLGCLLYEMATFRPPFE-ARTMQELRYKVCRGKFPPIPPVYS---QDLQQIIRSLLQVNPKKRPS 246
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
46-220 7.32e-18

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: 83.88  E-value: 7.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   46 TVYKGPN----------CIE--HNEALLEEAKMMNRLRHSRVVKLlgviieegkYS---------LVMEYMEKGNLMHVL 104
Cdd:cd14010  15 VVYKGRRkgtiefvaikCVDksKRPEVLNEVRLTHELKHPNVLKF---------YEwyetsnhlwLVVEYCTGGDLETLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA-----SFKMWSKLNNEEHNELREV 179
Cdd:cd14010  86 RQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLArregeILKELFGQFSDEGNVNKVS 165
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3426027  180 DGTAKKngGTLYYMAPEHLndvnakpteKSDVYSFAVVLWA 220
Cdd:cd14010 166 KKQAKR--GTPYYMAPELF---------QGGVHSFASDLWA 195
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
61-227 7.46e-18

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: 84.26  E-value: 7.46e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYmekgnLMHVLKAEM-STPLSVKGRIIL-----EIIEGMCYLHGKGV 134
Cdd:cd07835  46 IREISLLKELNHPNIVRLLDVVHSENKLYLVFEF-----LDLDLKKYMdSSPLTGLDPPLIksylyQLLQGIAFCHSHRV 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLA-SFKMwsKLNNEEHnelrEVDgtakknggTLYYMAPEHLndvnakptEKSDVYS 213
Cdd:cd07835 121 LHRDLKPQNLLIDTEGALKLADFGLArAFGV--PVRTYTH----EVV--------TLWYRAPEIL--------LGSKHYS 178
                       170       180
                ....*....|....*....|
gi 3426027  214 FAVVLWA---IFA---NKEP 227
Cdd:cd07835 179 TPVDIWSvgcIFAemvTRRP 198
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
22-306 7.69e-18

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: 84.40  E-value: 7.69e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGL----MIMKTvyKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14086   8 ELGKGAFSVVRRCVQKSTGQefaaKIINT--KKLSARDHQK-LEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLASfkmwsklnnEEHN 174
Cdd:cd14086  85 GELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAI---------EVQG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 ELREVDGTAkkngGTLYYMAPEHLNDVnakPTEKS-DVYSFAVVLWAIFANKEPY--ENaicEQQLIMCIKSGN----RP 247
Cdd:cd14086 156 DQQAWFGFA----GTPGYLSPEVLRKD---PYGKPvDIWACGVILYILLVGYPPFwdED---QHRLYAQIKAGAydypSP 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  248 DVDDITeycpREIISLMKLCWEANPEARPT------FPGIEEKFRPFYLSQLEESVEEdvksLKK 306
Cdd:cd14086 226 EWDTVT----PEAKDLINQMLTVNPAKRITaaealkHPWICQRDRVASMVHRQETVDC----LKK 282
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
22-277 7.75e-18

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 84.27  E-value: 7.75e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCfHRTQGLMIMKTVYK---GPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd05087   4 EIGHGWFGKVFLG-EVNSGLSSTQVVVKelkASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFCPLG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLM------HVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnnee 172
Cdd:cd05087  83 DLKgylrscRAAESMAPDPLTLQ-RMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCK--------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 HNELREVdgTAKKNGGTLYYMAPEHLNDVN-----AKPTEKSDVYSFAVVLWAIFA-NKEPYEN---------AICEQQL 237
Cdd:cd05087 153 YKEDYFV--TADQLWVPLRWIAPELVDEVHgnllvVDQTKQSNVWSLGVTIWELFElGNQPYRHysdrqvltyTVREQQL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 3426027  238 IMCIKSGNRPDVDDITEycpreiisLMKLCWeANPEARPT 277
Cdd:cd05087 231 KLPKPQLKLSLAERWYE--------VMQFCW-LQPEQRPT 261
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
2-160 8.08e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 85.25  E-value: 8.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     2 QPDMSlnviKMKSSDFLESAELDSGGFGKVSLCFHRTQGlmimktVYKGPNCIEHNEAL--------LEEAKMMNRLRHS 73
Cdd:PTZ00263   9 KPDTS----SWKLSDFEMGETLGTGSFGRVRIAKHKGTG------EYYAIKCLKKREILkmkqvqhvAQEKSILMELSHP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    74 RVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIK 153
Cdd:PTZ00263  79 FIVNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVK 158

                 ....*..
gi 3426027   154 IADLGLA 160
Cdd:PTZ00263 159 VTDFGFA 165
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
16-281 8.28e-18

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: 83.47  E-value: 8.28e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESaeLDSGGFGKVSLCFHRTQGLMIMKTVYKgpNCIEHNEALLE---EAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14161   6 EFLET--LGKGTYGRVKKARDSSGRLVAIKSIRK--DRIKDEQDLLHirrEIEIMSSLNHPHIISVYEVFENSSKIVIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnnee 172
Cdd:cd14161  82 EYASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSN----------- 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hneLREVDGTAKKNGGTLYYMAPEhlnDVNAKPTE--KSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIKSGNRPDVD 250
Cdd:cd14161 151 ---LYNQDKFLQTYCGSPLYASPE---IVNGRPYIgpEVDSWSLGVLLYILVHGTMPFDGHD-YKILVKQISSGAYREPT 223
                       250       260       270
                ....*....|....*....|....*....|.
gi 3426027  251 DITEYCpreiiSLMKLCWEANPEARPTFPGI 281
Cdd:cd14161 224 KPSDAC-----GLIRWLLMVNPERRATLEDV 249
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
23-315 8.84e-18

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 84.74  E-value: 8.84e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLC-FHRTQGLMIMKTVYKgpnciehnEALLE----EAKMMNR------LRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd05592   3 LGKGSFGKVMLAeLKGTNQYFAIKALKK--------DVVLEdddvECTMIERrvlalaSQHPFLTHLFCTFQTESHLFFV 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSklnne 171
Cdd:cd05592  75 MEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYG----- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelrevDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIksgnRPDVDD 251
Cdd:cd05592 150 --------ENKASTFCGTPDYIAPEILK--GQKYNQSVDWWSFGVLLYEMLIGQSPF-HGEDEDELFWSI----CNDTPH 214
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  252 ITEYCPREIISLMKLCWEANPEAR--------------PTFPGIE----EK------FRPFYLSQLeesveeDVKSLKKE 307
Cdd:cd05592 215 YPRWLTKEAASCLSLLLERNPEKRlgvpecpagdirdhPFFKTIDwdklERreidppFKPKVKSAN------DVSNFDPD 288

                ....*...
gi 3426027  308 YSNENAVV 315
Cdd:cd05592 289 FTMEKPVL 296
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
23-285 1.02e-17

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 83.88  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFH-RTQGLMIMKTVYkgpnC--IEHNEALLEEAKMMNRLRHSRVVKLLG-VIIEEGKYS----LVMEY 94
Cdd:cd13986   8 LGEGGFSFVYLVEDlSTGRLYALKKIL----ChsKEDVKEAMREIENYRLFNHPNILRLLDsQIVKEAGGKkevyLLLPY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLKAemstpLSVKG---------RIILEIIEGMCYLH---GKGVIHKDLKPENILVDNDFHIKIADLGLASF 162
Cdd:cd13986  84 YKRGSLQDEIER-----RLVKGtffpedrilHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDEPILMDLGSMNP 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  163 kmwSKLNNEEHNELREVDGTAKKNgGTLYYMAPEhLNDV--NAKPTEKSDVYSFAVVLWAIFANKEPYENAicEQQ---L 237
Cdd:cd13986 159 ---ARIEIEGRREALALQDWAAEH-CTMPYRAPE-LFDVksHCTIDEKTDIWSLGCTLYALMYGESPFERI--FQKgdsL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3426027  238 IMCIKSGNRPDVDDitEYCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd13986 232 ALAVLSGNYSFPDN--SRYSEELHQLVKSMLVVNPAERPSIDDLLSRV 277
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
11-227 1.08e-17

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: 84.72  E-value: 1.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   11 KMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSL 90
Cdd:cd06649   1 ELKDDDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwskln 169
Cdd:cd06649  81 CMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSG-------- 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  170 neehnelREVDGTAKKNGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEP 227
Cdd:cd06649 153 -------QLIDSMANSFVGTRSYMSPERLQGTHY--SVQSDIWSMGLSLVELAIGRYP 201
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
18-228 1.23e-17

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: 83.55  E-value: 1.23e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   18 LESAELDSGGFGKVSLCFHRTQGL----MIMKTVYKGPNC---IEHNEALLEEAKmmnrlRHSRVVKLLGVIIEEGKYSL 90
Cdd:cd14106  11 VESTPLGRGKFAVVRKCIHKETGKeyaaKFLRKRRRGQDCrneILHEIAVLELCK-----DCPRVVNLHEVYETRSELIL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF---HIKIADLGLASFKmwsk 167
Cdd:cd14106  86 ILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFplgDIKLCDFGISRVI---- 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  168 lnnEEHNELREVDGTAKknggtlyYMAPEHLndvNAKP-TEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14106 162 ---GEGEEIREILGTPD-------YVAPEIL---SYEPiSLATDMWSIGVLTYVLLTGHSPF 210
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
26-277 1.34e-17

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: 83.07  E-value: 1.34e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGPncIEHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd14185  11 GNFAVVKECRHWnENQEYAMKIIDKSK--LKGKEDMIEsEILIIKSLSHPNIVKLFEVYETEKEIYLILEYVRGGDLFDA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV----DNDFHIKIADLGLASFkmwsklnneehnelreV 179
Cdd:cd14185  89 IIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKY----------------V 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYENAICEQ-QLIMCIKSGN----RPDVDDITE 254
Cdd:cd14185 153 TGPIFTVCGTPTYVAPEILSEKGYG--LEVDMWAAGVILYILLCGFPPFRSPERDQeELFQIIQLGHyeflPPYWDNISE 230
                       250       260
                ....*....|....*....|...
gi 3426027  255 YCPREIISLMKLcweaNPEARPT 277
Cdd:cd14185 231 AAKDLISRLLVV----DPEKRYT 249
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
23-221 1.46e-17

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 83.35  E-value: 1.46e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIE-EGKYSLVMEYMEKGNL 100
Cdd:cd05577   1 LGRGGFGEVCACQVKATGKMYaCKKLDKKRIKKKKGETMALNEKIILEKVSSPFIVSLAYAFEtKDKLCLVLTLMNGGDL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 -MHVlkAEMSTPLSVKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnel 176
Cdd:cd05577  81 kYHI--YNVGTRGFSEARAIFyaaEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAV--------------- 143
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3426027  177 rEVDGTAKKNG--GTLYYMAPEHLndvnakptEKSDVYSFAVVLWAI 221
Cdd:cd05577 144 -EFKGGKKIKGrvGTHGYMAPEVL--------QKEVAYDFSVDWFAL 181
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
61-223 1.67e-17

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: 83.78  E-value: 1.67e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEkGNLMHVLKaEMSTPLS---VKGrIILEIIEGMCYLHGKGVIHK 137
Cdd:cd07841  50 LREIKLLQELKHPNIIGLLDVFGHKSNINLVFEFME-TDLEKVIK-DKSIVLTpadIKS-YMLMTLRGLEYLHSNWILHR 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLA-SFkmwsklnneehnelrevdGTAKKNGG----TLYYMAPEHLndVNAKpteksdVY 212
Cdd:cd07841 127 DLKPNNLLIASDGVLKLADFGLArSF------------------GSPNRKMThqvvTRWYRAPELL--FGAR------HY 180
                       170
                ....*....|....
gi 3426027  213 SFAVVLWA---IFA 223
Cdd:cd07841 181 GVGVDMWSvgcIFA 194
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
67-285 1.93e-17

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 83.20  E-value: 1.93e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   67 MNRLRHSRVVKLLGViiEEGK------YSLVMEYMEKGNLMHVLkaeMSTPLSVKG--RIILEIIEGMCYLH----GKG- 133
Cdd:cd14055  49 DASLKHENILQFLTA--EERGvgldrqYWLITAYHENGSLQDYL---TRHILSWEDlcKMAGSLARGLAHLHsdrtPCGr 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 ----VIHKDLKPENILVDNDFHIKIADLGLAsFKMWSKLNNEEHNELREVdgtakkngGTLYYMAPEHL----NDVNAKP 205
Cdd:cd14055 124 pkipIAHRDLKSSNILVKNDGTCVLADFGLA-LRLDPSLSVDELANSGQV--------GTARYMAPEALesrvNLEDLES 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  206 TEKSDVYSFAVVLWAIFAN----------KEPYENAICEQQLI-----MCIKSGNRPDVDD--ITEYCPREIISLMKLCW 268
Cdd:cd14055 195 FKQIDVYSMALVLWEMASRceasgevkpyELPFGSKVRERPCVesmkdLVLRDRGRPEIPDswLTHQGMCVLCDTITECW 274
                       250
                ....*....|....*..
gi 3426027  269 EANPEARPTFPGIEEKF 285
Cdd:cd14055 275 DHDPEARLTASCVAERF 291
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
26-277 1.96e-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: 83.24  E-value: 1.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd07846  12 GSYGMVMKCRHKETGQIVaIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEFVDHTVLDDLE 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNNEEHNELREVdgtak 184
Cdd:cd07846  92 KYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART-----LAAPGEVYTDYV----- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  185 kngGTLYYMAPEHL-NDVNakpteksdvYSFAVVLWAI------FANKEPY-----------------ENAICEQQLIMC 240
Cdd:cd07846 162 ---ATRWYRAPELLvGDTK---------YGKAVDVWAVgclvteMLTGEPLfpgdsdidqlyhiikclGNLIPRHQELFQ 229
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 3426027  241 ---IKSGNR-PDVDDITEYCPR------EIISLMKLCWEANPEARPT 277
Cdd:cd07846 230 knpLFAGVRlPEVKEVEPLERRypklsgVVIDLAKKCLHIDPDKRPS 276
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
17-276 1.99e-17

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: 82.56  E-value: 1.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCFHRTQG-----LMIMKTVYKGPNCIEHNeaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14070   4 YLIGRKLGEGSFAKVREGLHAVTGekvaiKVIDKKKAKKDSYVTKN--LRREGRIQQMIRHPNITQLLDILETENSYYLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNE 171
Cdd:cd14070  82 MELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDP 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 EHNELrevdgtakkngGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFANK-----EPYENAICEQQliMCIKSGNr 246
Cdd:cd14070 162 FSTQC-----------GSPAYAAPELLARKKYGP--KVDVWSIGVNMYAMLTGTlpftvEPFSLRALHQK--MVDKEMN- 225
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  247 PDVDDITEYCpreiISLMKLCWEANPEARP 276
Cdd:cd14070 226 PLPTDLSPGA----ISFLRSLLEPDPLKRP 251
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
14-222 2.22e-17

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 82.54  E-value: 2.22e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   14 SSDFLESAELDSGGFGKVSLCFHRTQGlmimKTvYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGV------------ 81
Cdd:cd14047   5 RQDFKEIELIGSGGFGQVFKAKHRIDG----KT-YAIKRVKLNNEKAEREVKALAKLDHPNIVRYNGCwdgfdydpetss 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   82 ----IIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLS--VKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIA 155
Cdd:cd14047  80 snssRSKTKCLFIQMEFCEKGTLESWIEKRNGEKLDkvLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIG 159
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  156 DLGLAsfkmwSKLNNeehnelrevDGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIF 222
Cdd:cd14047 160 DFGLV-----TSLKN---------DGKRTKSKGTLSYMSPEQISSQDYG--KEVDIYALGLILFELL 210
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
26-284 3.12e-17

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: 81.78  E-value: 3.12e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd08218  11 GSFGKALLVKSKEDGkQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYCDGGDLYKRI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSvKGRII---LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNNEehNELrevdg 181
Cdd:cd08218  91 NAQRGVLFP-EDQILdwfVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARV-----LNST--VEL----- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 tAKKNGGTLYYMAPEHLNDvnaKP-TEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVDDITEYcprEI 260
Cdd:cd08218 158 -ARTCIGTPYYLSPEICEN---KPyNNKSDIWALGCVLYEMCTLKHAFE-AGNMKNLVLKIIRGSYPPVPSRYSY---DL 229
                       250       260
                ....*....|....*....|....
gi 3426027  261 ISLMKLCWEANPEARPTFPGIEEK 284
Cdd:cd08218 230 RSLVSQLFKRNPRDRPSINSILEK 253
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
22-277 3.36e-17

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: 82.29  E-value: 3.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQG----LMIMKTVYKGPNC---IEHNEALLEEAKMmnrlrHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd14197  16 ELGRGKFAVVRKCVEKDSGkefaAKFMRKRRKGQDCrmeIIHEIAVLELAQA-----NPWVINLHEVYETASEMILVLEY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF---HIKIADLGLASFkmwskLN 169
Cdd:cd14197  91 AAGGEIFNQCVADREEAFKEKDvkRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRI-----LK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 NEEhnELREVDGTAKknggtlyYMAPEHLndvNAKP-TEKSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIKSGNRPD 248
Cdd:cd14197 166 NSE--ELREIMGTPE-------YVAPEIL---SYEPiSTATDMWSIGVLAYVMLTGISPFLGDD-KQETFLNISQMNVSY 232
                       250       260
                ....*....|....*....|....*....
gi 3426027  249 VDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14197 233 SEEEFEHLSESAIDFIKTLLIKKPENRAT 261
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
72-299 3.64e-17

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: 83.38  E-value: 3.64e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   72 HSRVVKLLGVI-IEEGK--YsLVMEYMEKgNLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDN 148
Cdd:cd07852  66 HPNIIKLLNVIrAENDKdiY-LVFEYMET-DLHAVIRANILEDIHKQ-YIMYQLLKALKYLHSGGVIHRDLKPSNILLNS 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  149 DFHIKIADLGLAsfKMWSKLNNEEHNELReVDGTAkknggTLYYMAPEHLndvnakptEKSDVYSFAVVLWAI------- 221
Cdd:cd07852 143 DCRVKLADFGLA--RSLSQLEEDDENPVL-TDYVA-----TRWYRAPEIL--------LGSTRYTKGVDMWSVgcilgem 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  222 FANKEPYENAICEQQLIMCIKSGNRPDVDDI-----------------------TEYCP---REIISLMKLCWEANPEAR 275
Cdd:cd07852 207 LLGKPLFPGTSTLNQLEKIIEVIGRPSAEDIesiqspfaatmleslppsrpkslDELFPkasPDALDLLKKLLVFNPNKR 286
                       250       260
                ....*....|....*....|....
gi 3426027  276 PTfpgIEEKFRPFYLSQLEESVEE 299
Cdd:cd07852 287 LT---AEEALRHPYVAQFHNPADE 307
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
26-218 3.95e-17

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: 83.49  E-value: 3.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKgpnciehneallEEAKMMNRLRHSR-------------VVKLLGVIIEEGKYSLV 91
Cdd:cd05573  12 GAFGEVWLVRDKdTGQVYAMKILRK------------SDMLKREQIAHVRaerdiladadspwIVRLHYAFQDEDHLYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMhvlkaemsTPLSVKGRI--------ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA--- 160
Cdd:cd05573  80 MEYMPGGDLM--------NLLIKYDVFpeetarfyIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCtkm 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  161 -----SFKMWSKLNNEEHNELREVDGTAKKNG--------GTLYYMAPEHLNDVnaKPTEKSDVYSFAVVL 218
Cdd:cd05573 152 nksgdRESYLNDSVNTLFQDNVLARRRPHKQRrvraysavGTPDYIAPEVLRGT--GYGPECDWWSLGVIL 220
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
45-277 4.06e-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: 81.50  E-value: 4.06e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   45 KTVYKGPNCIE-----------------HNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM--EYMEKGNLmhvlK 105
Cdd:cd13983  15 KTVYRAFDTEEgievawneiklrklpkaERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFitELMTSGTL----K 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  106 AEMSTPLSVKGRII----LEIIEGMCYLHGKG--VIHKDLKPENILVD-NDFHIKIADLGLASFKMWSKlnneehnelre 178
Cdd:cd13983  91 QYLKRFKRLKLKVIkswcRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQSF----------- 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdgtAKKNGGTLYYMAPEHLNDvnaKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPD-VDDITEYCP 257
Cdd:cd13983 160 ----AKSVIGTPEFMAPEMYEE---HYDEKVDIYAFGMCLLEMATGEYPYSECTNAAQIYKKVTSGIKPEsLSKVKDPEL 232
                       250       260
                ....*....|....*....|
gi 3426027  258 REIISlmkLCWEaNPEARPT 277
Cdd:cd13983 233 KDFIE---KCLK-PPDERPS 248
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
57-277 4.65e-17

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: 81.44  E-value: 4.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   57 NEALLEEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKgNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVI 135
Cdd:cd14164  44 QKFLPRELSILRRVNHPNIVQMFECIeVANGRLYIVMEAAAT-DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIV 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVD-NDFHIKIADLGLASFKmwsklnnEEHNELrevdgtAKKNGGTLYYMAPEHLNDVNAKPtEKSDVYSF 214
Cdd:cd14164 123 HRDLKCENILLSaDDRKIKIADFGFARFV-------EDYPEL------STTFCGSRAYTPPEVILGTPYDP-KKYDVWSL 188
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  215 AVVLWAIFANKEPYENAICeqQLIMCIKSG-NRPDVDDITEYCPREIISLMKLcweaNPEARPT 277
Cdd:cd14164 189 GVVLYVMVTGTMPFDETNV--RRLRLQQRGvLYPSGVALEEPCRALIRTLLQF----NPSTRPS 246
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
23-277 6.33e-17

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: 81.15  E-value: 6.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVslcfhrtqglmiMKTVYKGPNC---IEHNEA----LLEEAKMMNRLRHSRVVKLLGVIIEegKYSLVMEYM 95
Cdd:cd14068   2 LGDGGFGSV------------YRAVYRGEDVavkIFNKHTsfrlLRQELVVLSHLHHPSLVALLAAGTA--PRMLVMELA 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAE-MSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV-----DNDFHIKIADLGLASF--KMwsk 167
Cdd:cd14068  68 PKGSLDALLQQDnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYccRM--- 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 lnneehnelrevdgTAKKNGGTLYYMAPEhLNDVNAKPTEKSDVYSFAVVLWAIFAnkepyenaiCEQQLIMCIKSGNRP 247
Cdd:cd14068 145 --------------GIKTSEGTPGFRAPE-VARGNVIYNQQADVYSFGLLLYDILT---------CGERIVEGLKFPNEF 200
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 3426027  248 D--------VDDITEY-CP--REIISLMKLCWEANPEARPT 277
Cdd:cd14068 201 DelaiqgklPDPVKEYgCApwPGVEALIKDCLKENPQCRPT 241
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
71-281 6.58e-17

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: 81.97  E-value: 6.58e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   71 RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKA------------EMSTPLSVKGRIIL----EIIEGMCYLHGKGV 134
Cdd:cd05089  61 HHPNIINLLGACENRGYLYIAIEYAPYGNLLDFLRKsrvletdpafakEHGTASTLTSQQLLqfasDVAKGMQYLSEKQF 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNGGTL--YYMAPEHLNdvNAKPTEKSDVY 212
Cdd:cd05089 141 IHRDLAARNVLVGENLVSKIADFGLS----------------RGEEVYVKKTMGRLpvRWMAIESLN--YSVYTTKSDVW 202
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  213 SFAVVLWAIFA-NKEPYENAICeQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05089 203 SFGVLLWEIVSlGGTPYCGMTC-AELYEKLPQGYRMEK---PRNCDDEVYELMRQCWRDRPYERPPFSQI 268
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
26-230 6.90e-17

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: 81.04  E-value: 6.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQ----GLMIMKTVYKGPNCIEhneallEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14087  12 GSFSRVVRVEHRVTrqpyAIKMIETKCRGREVCE------SELNVLRRVRHTNIIQLIEVFETKERVYMVMELATGGELF 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLASFKmwsklNNEEHNELRE 178
Cdd:cd14087  86 DRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTR-----KKGPNCLMKT 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  179 VDGTAKknggtlyYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd14087 161 TCGTPE-------YIAPEIL--LRKPYTQSVDMWAVGVIAYILLSGTMPFDD 203
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
26-236 7.32e-17

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 80.80  E-value: 7.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCF-HRTQGLMIMKTVYKGPNCIEHNEALL-EEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14163  11 GTYSKVKEAFsKKHQRKVAIKIIDKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLeSADGKIYLVMELAEDGDVFD 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNdFHIKIADLGLAsfkmwsKLNNEEHNELrevdgt 182
Cdd:cd14163  91 CVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQG-FTLKLTDFGFA------KQLPKGGREL------ 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  183 AKKNGGTLYYMAPEHLNDVnAKPTEKSDVYSFAVVLWAIFANKEPYENA-----ICEQQ 236
Cdd:cd14163 158 SQTFCGSTAYAAPEVLQGV-PHDSRKGDIWSMGVVLYVMLCAQLPFDDTdipkmLCQQQ 215
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
22-291 7.77e-17

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: 81.43  E-value: 7.77e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGL-MIMKTVYkgpncIEHNEA----LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd06622   8 ELGKGNYGSVYKVLHRPTGVtMAMKEIR-----LELDESkfnqIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMST---PLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnnee 172
Cdd:cd06622  83 AGSLDKLYAGGVATegiPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSG----------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnelREVDGTAKKNGGTLYYMAPEHLNDVNAKP----TEKSDVYSFAVVLWAIFANKEPYE----NAICEQqlIMCIKSG 244
Cdd:cd06622 152 ----NLVASLAKTNIGCQSYMAPERIKSGGPNQnptyTVQSDVWSLGLSILEMALGRYPYPpetyANIFAQ--LSAIVDG 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 3426027  245 NRPDVDDitEYCPrEIISLMKLCWEANPEARPTFPGIEEkfRPFYLS 291
Cdd:cd06622 226 DPPTLPS--GYSD-DAQDFVAKCLNKIPNRRPTYAQLLE--HPWLVK 267
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
23-229 7.87e-17

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: 81.22  E-value: 7.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIM-KTVYKGPNCIEHNEAL-LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd05630   8 LGKGGFGEVCACQVRATGKMYAcKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 -MHVLkaEMSTPLSVKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskLNNEEhnel 176
Cdd:cd05630  88 kFHIY--HMGQAGFPEARAVFyaaEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA-------VHVPE---- 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3426027  177 revDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd05630 155 ---GQTIKGRVGTVGYMAPEVVK--NERYTFSPDWWALGCLLYEMIAGQSPFQ 202
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
15-196 1.00e-16

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: 81.33  E-value: 1.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCI--EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIrlKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnnee 172
Cdd:cd05612  81 EYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFA------------ 148
                       170       180
                ....*....|....*....|....
gi 3426027  173 hNELREVDGTAkknGGTLYYMAPE 196
Cdd:cd05612 149 -KKLRDRTWTL---CGTPEYLAPE 168
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
15-276 1.04e-16

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: 80.84  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVslcfHRTQGLMIMKTV-YKGPNCIEHNEA-----LLEEAKMMNRLRHSRVVKLLGVIIEEGKY 88
Cdd:cd08228   2 ANFQIEKKIGRGQFSEV----YRATCLLDRKPVaLKKVQIFEMMDAkarqdCVKEIDLLKQLNHPNVIKYLDSFIEDNEL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   89 SLVMEYMEKGNL----MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkm 164
Cdd:cd08228  78 NIVLELADAGDLsqmiKYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRF-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  165 WSKLNNEEHNELrevdgtakkngGTLYYMAPE--HLNDVNAkpteKSDVYSFAVVLWAIFANKEP-YENAICEQQLIMCI 241
Cdd:cd08228 156 FSSKTTAAHSLV-----------GTPYYMSPEriHENGYNF----KSDIWSLGCLLYEMAALQSPfYGDKMNLFSLCQKI 220
                       250       260       270
                ....*....|....*....|....*....|....*
gi 3426027  242 KSGNRPDVDdiTEYCPREIISLMKLCWEANPEARP 276
Cdd:cd08228 221 EQCDYPPLP--TEHYSEKLRELVSMCIYPDPDQRP 253
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
23-277 1.19e-16

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: 80.40  E-value: 1.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd08219   8 VGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYCDGGDLMQ 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEmstplsvKGRI-----ILEIIEGMC----YLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnneeh 173
Cdd:cd08219  88 KIKLQ-------RGKLfpedtILQWFVQMClgvqHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARL----------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 neLREVDGTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGNRPDVDDIT 253
Cdd:cd08219 150 --LTSPGAYACTYVGTPYYVPPEIWE--NMPYNNKSDIWSLGCILYELCTLKHPFQ-ANSWKNLILKVCQGSYKPLPSHY 224
                       250       260
                ....*....|....*....|....
gi 3426027  254 EYcprEIISLMKLCWEANPEARPT 277
Cdd:cd08219 225 SY---ELRSLIKQMFKRNPRSRPS 245
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
121-284 1.22e-16

Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. Kit signaling is involved in major cellular functions including cell survival, proliferation, differentiation, adhesion, and chemotaxis. Mutations in Kit, which result in constitutive ligand-independent activation, are found in human cancers such as gastrointestinal stromal tumor (GIST) and testicular germ cell tumor (TGCT). The aberrant expression of Kit and/or SCF is associated with other tumor types such as systemic mastocytosis and cancers of the breast, neurons, lung, prostate, colon, and rectum. Although the structure of the human Kit catalytic domain is known, it is excluded from this specific alignment model because it contains a deletion in its sequence. Kit is a member of the Platelet Derived Growth Factor Receptor (PDGFR) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of Kit to its ligand, the stem-cell factor (SCF), leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. The Kit subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 82.26  E-value: 1.22e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  121 EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsKLNNEEHnelREVDGTAKKnggTLYYMAPEHLnd 200
Cdd:cd05104 222 QVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLAR-----DIRNDSN---YVVKGNARL---PVKWMAPESI-- 288
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  201 VNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFP 279
Cdd:cd05104 289 FECVYTFESDVWSYGILLWEIFSlGSSPYPGMPVDSKFYKMIKEGYRMDS---PEFAPSEMYDIMRSCWDADPLKRPTFK 365

                ....*
gi 3426027  280 GIEEK 284
Cdd:cd05104 366 QIVQL 370
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
23-275 1.37e-16

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: 80.35  E-value: 1.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLM-IMKTVYK----GPNCIEHneaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd05572   1 LGVGGFGRVELVQLKSKGRTfALKCVKKrhivQTRQQEH---IFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLglasfkmwsklnneehnelr 177
Cdd:cd05572  78 GELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDF-------------------- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdGTAKKNG---------GTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIM-CIKSGNrp 247
Cdd:cd05572 138 ---GFAKKLGsgrktwtfcGTPEYVAPEII--LNKGYDFSVDYWSLGILLYELLTGRPPFGGDDEDPMKIYnIILKGI-- 210
                       250       260
                ....*....|....*....|....*....
gi 3426027  248 DVDDITEYCPREIISLMK-LCwEANPEAR 275
Cdd:cd05572 211 DKIEFPKYIDKNAKNLIKqLL-RRNPEER 238
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
58-277 1.41e-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: 80.10  E-value: 1.41e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKmmnRLRHSRVVKLLGVIIEE------GKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHG 131
Cdd:cd14012  46 EKELESLK---KLRHPNLVSYLAFSIERrgrsdgWKVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLHR 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  132 KGVIHKDLKPENILVDNDFH---IKIADLGlasfkmwskLNNEEHNELREVDGTAKKNggtLYYMAPEhLNDVNAKPTEK 208
Cdd:cd14012 123 NGVVHKSLHAGNVLLDRDAGtgiVKLTDYS---------LGKTLLDMCSRGSLDEFKQ---TYWLPPE-LAQGSKSPTRK 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  209 SDVYSFAVVLWAIFANKEPYENAICEQQLImcIKSGNRPDVDDiteycpreiisLMKLCWEANPEARPT 277
Cdd:cd14012 190 TDVWDLGLLFLQMLFGLDVLEKYTSPNPVL--VSLDLSASLQD-----------FLSKCLSLDPKKRPT 245
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
98-283 1.48e-16

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR alpha is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR alpha forms homodimers or heterodimers with PDGFR beta, depending on the nature of the PDGF ligand. PDGF-AA, PDGF-AB, and PDGF-CC induce PDGFR alpha homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR alpha signaling is important in the formation of lung alveoli, intestinal villi, mesenchymal dermis, and hair follicles, as well as in the development of oligodendrocytes, retinal astrocytes, neural crest cells, and testicular cells. Aberrant PDGFR alpha expression is associated with some human cancers. Mutations in PDGFR alpha have been found within a subset of gastrointestinal stromal tumors (GISTs). An active fusion protein FIP1L1-PDGFR alpha, derived from interstitial deletion, is associated with idiopathic hypereosinophilic syndrome and chronic eosinophilic leukemia. The PDGFR alpha subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 82.38  E-value: 1.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRI--ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneeHne 175
Cdd:cd05105 220 SEVKNLLSDDGSEGLTTLDLLsfTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIM--------H-- 289
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 lrevDGTAKKNGGTLY---YMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNR---PD 248
Cdd:cd05105 290 ----DSNYVSKGSTFLpvkWMAPESIFD--NLYTTLSDVWSYGILLWEIFSlGGTPYPGMIVDSTFYNKIKSGYRmakPD 363
                       170       180       190
                ....*....|....*....|....*....|....*
gi 3426027  249 vdditeYCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd05105 364 ------HATQEVYDIMVKCWNSEPEKRPSFLHLSD 392
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
52-229 1.74e-16

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


Pssm-ID: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 80.05  E-value: 1.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   52 NCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAeMSTPLSVKGRIILEIIEG-MCYLH 130
Cdd:cd14202  40 NLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDLADYLHT-MRTLSEDTIRLFLQQIAGaMKMLH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  131 GKGVIHKDLKPENILVD---------NDFHIKIADLGLASFkmwskLNNeehnelrevDGTAKKNGGTLYYMAPEHLNDV 201
Cdd:cd14202 119 SKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARY-----LQN---------NMMAATLCGSPMYMAPEVIMSQ 184
                       170       180
                ....*....|....*....|....*...
gi 3426027  202 NAKPteKSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd14202 185 HYDA--KADLWSIGTIIYQCLTGKAPFQ 210
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
23-229 1.79e-16

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: 80.81  E-value: 1.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEAlleEAKMMNRlrhsRVVKLLG----------VIIEEGKYSLVM 92
Cdd:cd05616   8 LGKGSFGKVMLAERKGTDELYAVKILKKDVVIQDDDV---ECTMVEK----RVLALSGkppfltqlhsCFQTMDRLYFVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLK--AEMSTPLSVkgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWsklnn 170
Cdd:cd05616  81 EYVNGGDLMYHIQqvGRFKEPHAV--FYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIW----- 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  171 eehnelrevDG-TAKKNGGTLYYMAPEhlnDVNAKPTEKS-DVYSFAVVLWAIFANKEPYE 229
Cdd:cd05616 154 ---------DGvTTKTFCGTPDYIAPE---IIAYQPYGKSvDWWAFGVLLYEMLAGQAPFE 202
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
19-223 2.12e-16

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: 80.01  E-value: 2.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   19 ESAELDSGGFGKVSLCFHRTQGLMI-MKTVYkgpncIEHNE-----------ALLeeaKMMNRLRHSRVVKLLGV----- 81
Cdd:cd07838   3 EVAEIGEGAYGTVYKARDLQDGRFVaLKKVR-----VPLSEegiplstireiALL---KQLESFEHPNVVRLLDVchgpr 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   82 IIEEGKYSLVMEYMEK---GNLMHVLKAEMSTPLsVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLG 158
Cdd:cd07838  75 TDRELKLTLVFEHVDQdlaTYLDKCPKPGLPPET-IK-DLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  159 LA---SFKMwsklnneehnELREVdgtakknGGTLYYMAPEHLndvnakpteKSDVYSFAVVLWA---IFA 223
Cdd:cd07838 153 LAriySFEM----------ALTSV-------VVTLWYRAPEVL---------LQSSYATPVDMWSvgcIFA 197
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
16-277 2.30e-16

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: 80.07  E-value: 2.30e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLE-SAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNcIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06643   5 DFWEiVGELGDGAFGKVYKAQNKETGILAAAKVIDTKS-EEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEF 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLkAEMSTPLS-VKGRIIL-EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnnEE 172
Cdd:cd06643  84 CAGGAVDAVM-LELERPLTePQIRVVCkQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSA---------KN 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 HNELREVDGTAkkngGTLYYMAPEHLNDVNAK--PTE-KSDVYSFAVVLWAIfANKEPYENAICEQQLIMCIKSGNRPDV 249
Cdd:cd06643 154 TRTLQRRDSFI----GTPYWMAPEVVMCETSKdrPYDyKADVWSLGVTLIEM-AQIEPPHHELNPMRVLLKIAKSEPPTL 228
                       250       260
                ....*....|....*....|....*...
gi 3426027  250 DDITEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd06643 229 AQPSRWSP-EFKDFLRKCLEKNVDARWT 255
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
17-285 2.39e-16

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 80.80  E-value: 2.39e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCfhRTQGLMIMKtvyKGPNCIEHNeALLEEAKMMNRL-RHSRVVKLLGVIIEEG-KYSLVMEY 94
Cdd:cd05103  20 FGQVIEADAFGIDKTATC--RTVAVKMLK---EGATHSEHR-ALMSELKILIHIgHHLNVVNLLGACTKPGgPLMVIVEF 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLKAEMS---------------------TPLSVKGRI----------------------------------- 118
Cdd:cd05103  94 CKFGNLSAYLRSKRSefvpyktkgarfrqgkdyvgdISVDLKRRLdsitssqssassgfveekslsdveeeeagqedlyk 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  119 -----------ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS--FKmwsklnneEHNELREVDGTAKk 185
Cdd:cd05103 174 dfltledlicySFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARdiYK--------DPDYVRKGDARLP- 244
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  186 nggtLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNRPDVDDiteYCPREIISLM 264
Cdd:cd05103 245 ----LKWMAPETIFD--RVYTIQSDVWSFGVLLWEIFSlGASPYPGVKIDEEFCRRLKEGTRMRAPD---YTTPEMYQTM 315
                       330       340
                ....*....|....*....|.
gi 3426027  265 KLCWEANPEARPTFPGIEEKF 285
Cdd:cd05103 316 LDCWHGEPSQRPTFSELVEHL 336
pknD PRK13184
serine/threonine-protein kinase PknD;
61-230 2.51e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 83.28  E-value: 2.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKA-----EMSTPL----SVKG--RIILEIIEGMCYL 129
Cdd:PRK13184  50 LREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTLKSLLKSvwqkeSLSKELaektSVGAflSIFHKICATIEYV 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   130 HGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnNEEHNELREVDGTAK-----------KNGGTLYYMAPEHL 198
Cdd:PRK13184 130 HSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFK------KLEEEDLLDIDVDERnicyssmtipgKIVGTPDYMAPERL 203
                        170       180       190
                 ....*....|....*....|....*....|..
gi 3426027   199 NDVNAkpTEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:PRK13184 204 LGVPA--SESTDIYALGVILYQMLTLSFPYRR 233
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
58-228 3.37e-16

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: 78.87  E-value: 3.37e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd14121  40 ENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHM 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVD--NDFHIKIADLGLASFKMwsklNNEEHNELRevdgtakkngGTLYYMAPEHLndVNAKPTEKSDVYSFA 215
Cdd:cd14121 120 DLKPQNLLLSsrYNPVLKLADFGFAQHLK----PNDEAHSLR----------GSPLYMAPEMI--LKKKYDARVDLWSVG 183
                       170
                ....*....|...
gi 3426027  216 VVLWAIFANKEPY 228
Cdd:cd14121 184 VILYECLFGRAPF 196
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
26-230 3.47e-16

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: 78.71  E-value: 3.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMIMKTVYkgPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLK 105
Cdd:cd14111  14 GRFGVIRRCRENATGKNFPAKIV--PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFCSGKELLHSLI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  106 AEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA-SFKMWSklnneehneLREVDgtak 184
Cdd:cd14111  92 DRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAqSFNPLS---------LRQLG---- 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 3426027  185 KNGGTLYYMAPEHLN-DVNAKPTeksDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd14111 159 RRTGTLEYMAPEMVKgEPVGPPA---DIWSIGVLTYIMLSGRSPFED 202
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
26-277 3.51e-16

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: 78.92  E-value: 3.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGL-MIMKTVYKGPNCieHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHV 103
Cdd:cd14184  12 GNFAVVKECVERSTGKeFALKIIDKAKCC--GKEHLIEnEVSILRRVKHPNIIMLIEEMDTPAELYLVMELVKGGDLFDA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV----DNDFHIKIADLGLASFkmwsklnneehnelreV 179
Cdd:cd14184  90 ITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATV----------------V 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  180 DGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPY--ENAICE---QQLIMCIKSGNRPDVDDITE 254
Cdd:cd14184 154 EGPLYTVCGTPTYVAPEIIAETGYG--LKVDIWAAGVITYILLCGFPPFrsENNLQEdlfDQILLGKLEFPSPYWDNITD 231
                       250       260
                ....*....|....*....|...
gi 3426027  255 yCPREIISLMklcWEANPEARPT 277
Cdd:cd14184 232 -SAKELISHM---LQVNVEARYT 250
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
17-281 3.71e-16

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 78.68  E-value: 3.71e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESaeLDSGGFGKVSLCFHRTQGL-------MIMKTVYKGPNCIehNEALLEEAKMMNRLRHSRVVKLLGVIIEEGkYS 89
Cdd:cd05037   3 FHEH--LGQGTFTNIYDGILREVGDgrvqeveVLLKVLDSDHRDI--SESFFETASLMSQISHKHLVKLYGVCVADE-NI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNL-MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV------DNDFHIKIADLGLAsf 162
Cdd:cd05037  78 MVQEYVRYGPLdKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLaregldGYPPFIKLSDPGVP-- 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  163 kmwSKLNNEEHNELRevdgtakknggtLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFAN-KEPYeNAICEQQLIMCI 241
Cdd:cd05037 156 ---ITVLSREERVDR------------IPWIAPECLRNLQANLTIAADKWSFGTTLWEICSGgEEPL-SALSSQEKLQFY 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 3426027  242 KSGNRPDVDDITeycprEIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05037 220 EDQHQLPAPDCA-----ELAELIMQCWTYEPTKRPSFRAI 254
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
25-277 3.72e-16

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: 79.21  E-value: 3.72e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVslcfhrtqglmiMKTVYKGPN------CIEHNEA------LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd06609  11 KGSFGEV------------YKGIDKRTNqvvaikVIDLEEAedeiedIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKA----EMSTplsvkGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskl 168
Cdd:cd06609  79 EYCGGGSVLDLLKPgpldETYI-----AFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG------- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 nneehnelrEVDGTAKKNG---GTLYYMAPEHLndVNAKPTEKSDVYSFAVVlwAI-FANKEPYENAICEQQLIMCIKSG 244
Cdd:cd06609 147 ---------QLTSTMSKRNtfvGTPFWMAPEVI--KQSGYDEKADIWSLGIT--AIeLAKGEPPLSDLHPMRVLFLIPKN 213
                       250       260       270
                ....*....|....*....|....*....|....*
gi 3426027  245 NRPDVDDiTEYCP--REIISlmkLCWEANPEARPT 277
Cdd:cd06609 214 NPPSLEG-NKFSKpfKDFVE---LCLNKDPKERPS 244
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
58-277 3.96e-16

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: 78.99  E-value: 3.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMStPLSVKGRIIL----EIIEGMCYLHGKG 133
Cdd:cd06624  50 QPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLSALLRSKWG-PLKDNENTIGyytkQILEGLKYLHDNK 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVdNDFH--IKIADLGLasfkmwSKlnneehnELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDV 211
Cdd:cd06624 129 IVHRDIKGDNVLV-NTYSgvVKISDFGT------SK-------RLAGINPCTETFTGTLQYMAPEVIDKGQRGYGPPADI 194
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  212 YSFAVVLWAIFANKEP-YEnaICEQQLIMcIKSGNRPDVDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd06624 195 WSLGCTIIEMATGKPPfIE--LGEPQAAM-FKVGMFKIHPEIPESLSEEAKSFILRCFEPDPDKRAT 258
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
19-228 4.33e-16

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: 78.80  E-value: 4.33e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   19 ESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd14193   8 KEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEE-VKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEYVDGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVL------KAEMSTPLSVKgriilEIIEGMCYLHGKGVIHKDLKPENILVDN--DFHIKIADLGLA-SFKMWSKLn 169
Cdd:cd14193  87 ELFDRIidenynLTELDTILFIK-----QICEGIQYMHQMYILHLDLKPENILCVSreANQVKIIDFGLArRYKPREKL- 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neehnelrevdgtaKKNGGTLYYMAPEHLN-DVNAKPTeksDVYSFAVVLWAIFANKEPY 228
Cdd:cd14193 161 --------------RVNFGTPEFLAPEVVNyEFVSFPT---DMWSLGVIAYMLLSGLSPF 203
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
59-281 4.75e-16

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 78.81  E-value: 4.75e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   59 ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd05064  52 GFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEYMSNGALDSFLrKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHK 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLG-LASFKMwsklnneehnelrEVDGTAKKNGGTLYYMAPEHLNDVNAKPTekSDVYSFAV 216
Cdd:cd05064 132 GLAAHKVLVNSDLVCKISGFRrLQEDKS-------------EAIYTTMSGKSPVLWAAPEAIQYHHFSSA--SDVWSFGI 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  217 VLWAIFANKE-PYENaICEQQLIMCIKSGNR--PDVDditeyCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05064 197 VMWEVMSYGErPYWD-MSGQDVIKAVEDGFRlpAPRN-----CPNLLHQLMLDCWQKERGERPRFSQI 258
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
14-301 4.79e-16

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 79.33  E-value: 4.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   14 SSDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd06616   5 AEDLKDLGEIGRGAFGTVNKMLHKpSGTIMAVKRIRSTVDEKEQKRLLMDLDVVMRSSDCPYIVKFYGALFREGDCWICM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYM----EKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGK-GVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSK 167
Cdd:cd06616  85 ELMdislDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGIS-----GQ 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 LnneehnelreVDGTAK-KNGGTLYYMAPEHLNDVNAKPTE--KSDVYSFAVVLWAIFANKEPYE--NAICEqQLIMCIK 242
Cdd:cd06616 160 L----------VDSIAKtRDAGCRPYMAPERIDPSASRDGYdvRSDVWSLGITLYEVATGKFPYPkwNSVFD-QLTQVVK 228
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  243 sGNRP--DVDDITEYCPrEIISLMKLCWEANPEARPTFPGIEEkfRPFYlsQLEESVEEDV 301
Cdd:cd06616 229 -GDPPilSNSEEREFSP-SFVNFVNLCLIKDESKRPKYKELLK--HPFI--KMYEERNVDV 283
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
120-285 4.92e-16

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: 80.05  E-value: 4.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  120 LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwSKLNNEEHneLREVDGTAKknggtLYYMAPEHLN 199
Cdd:cd14207 187 FQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLAR----DIYKNPDY--VRKGDARLP-----LKWMAPESIF 255
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  200 DvnAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTF 278
Cdd:cd14207 256 D--KIYSTKSDVWSYGVLLWEIFSlGASPYPGVQIDEDFCSKLKEGIRMRA---PEFATSEIYQIMLDCWQGDPNERPRF 330

                ....*..
gi 3426027  279 PGIEEKF 285
Cdd:cd14207 331 SELVERL 337
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
26-277 5.66e-16

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: 78.24  E-value: 5.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRT-QGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd08220  11 GAYGTVYLCRRKDdNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYI 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSVKG--RIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHI-KIADLGLasfkmwSKLNNEEHNELREVdg 181
Cdd:cd08220  91 QQRKGSLLSEEEilHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGI------SKILSSKSKAYTVV-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 takkngGTLYYMAPEHlndVNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEqQLIMCIKSGN-RPDVDDITEYCPRE 259
Cdd:cd08220 163 ------GTPCYISPEL---CEGKPyNQKSDIWALGCVLYELASLKRAFEAANLP-ALVLKIMRGTfAPISDRYSEELRHL 232
                       250
                ....*....|....*...
gi 3426027  260 IISLMKLcweaNPEARPT 277
Cdd:cd08220 233 ILSMLHL----DPNKRPT 246
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
23-228 5.74e-16

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: 78.94  E-value: 5.74e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLM-IMKTVYKGPNCIEHNEAL-LEEAKMMNRLrHSRVVKLLGVIIEEgKYSL--VMEYMEKG 98
Cdd:cd05605   8 LGKGGFGEVCACQVRATGKMyACKKLEKKRIKKRKGEAMaLNEKQILEKV-NSRFVVSLAYAYET-KDALclVLTIMNGG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NL-MHVLKaeMSTPLSVKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehn 174
Cdd:cd05605  86 DLkFHIYN--MGNPGFEEERAVFyaaEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAV------------- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3426027  175 ELREVDgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05605 151 EIPEGE-TIRGRVGTVGYMAPEVVK--NERYTFSPDWWGLGCLIYEMIEGQAPF 201
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
15-160 5.96e-16

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 79.28  E-value: 5.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVykgpncIEHNE------ALLEEAKMMNRLRHSRVVKLLGVIIEEGK 87
Cdd:cd07866   8 RDYEILGKLGEGTFGEVYKARQIkTGRVVALKKI------LMHNEkdgfpiTALREIKILKKLKHPNVVPLIDMAVERPD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YS--------LVMEYMEKgNLMHVL-----KAEMStplSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKI 154
Cdd:cd07866  82 KSkrkrgsvyMVTPYMDH-DLSGLLenpsvKLTES---QIKC-YMLQLLEGINYLHENHILHRDIKAANILIDNQGILKI 156

                ....*.
gi 3426027  155 ADLGLA 160
Cdd:cd07866 157 ADFGLA 162
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
63-218 6.24e-16

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 81.38  E-value: 6.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    63 EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEmsTPLSVkgRIILEIIEGMC----YLHGKGVIHKD 138
Cdd:NF033483  57 EAQSAASLSHPNIVSVYDVGEDGGIPYIVMEYVDGRTLKDYIREH--GPLSP--EEAVEIMIQILsaleHAHRNGIVHRD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   139 LKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNG----GTLYYMAPEHLNDVNAkpTEKSDVYSF 214
Cdd:NF033483 133 IKPQNILITKDGRVKVTDFGIA----------------RALSSTTMTQTnsvlGTVHYLSPEQARGGTV--DARSDIYSL 194

                 ....
gi 3426027   215 AVVL 218
Cdd:NF033483 195 GIVL 198
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
61-227 6.66e-16

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: 78.81  E-value: 6.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEG--KYSLVMEYMEkgnlmHVLKA---EMSTPLSVKGR--IILEIIEGMCYLHGKG 133
Cdd:cd07843  52 LREINILLKLQHPNIVTVKEVVVGSNldKIYMVMEYVE-----HDLKSlmeTMKQPFLQSEVkcLMLQLLSGVAHLHDNW 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKK---NGGTLYYMAPEHLNDvnakptekSD 210
Cdd:cd07843 127 ILHRDLKTSNLLLNNRGILKICDFGLA----------------REYGSPLKPytqLVVTLWYRAPELLLG--------AK 182
                       170       180
                ....*....|....*....|...
gi 3426027  211 VYSFAVVLWA---IFA---NKEP 227
Cdd:cd07843 183 EYSTAIDMWSvgcIFAellTKKP 205
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
61-221 7.48e-16

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: 78.32  E-value: 7.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGnlmhvLKAEMST------PLSVKGRIILEIIEGMCYLHGKGV 134
Cdd:cd07860  47 IREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQD-----LKKFMDAsaltgiPLPLIKSYLFQLLQGLAFCHSHRV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLA-SFKMwsKLNNEEHnelrEVdgtakkngGTLYYMAPEHLndvnakptEKSDVYS 213
Cdd:cd07860 122 LHRDLKPQNLLINTEGAIKLADFGLArAFGV--PVRTYTH----EV--------VTLWYRAPEIL--------LGCKYYS 179

                ....*...
gi 3426027  214 FAVVLWAI 221
Cdd:cd07860 180 TAVDIWSL 187
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
23-230 7.51e-16

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: 79.28  E-value: 7.51e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEA--LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd05595   3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVahTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 M-HVLKAEMSTplSVKGRII-LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwSKLNNEehnelre 178
Cdd:cd05595  83 FfHLSRERVFT--EDRARFYgAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCK----EGITDG------- 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  179 vdGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd05595 150 --ATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYN 197
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
60-228 7.95e-16

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


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 77.79  E-value: 7.95e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd14120  39 LGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDL 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  140 KPENILVD---------NDFHIKIADLGLASFkmwskLNNEEhnelrevdgTAKKNGGTLYYMAPEHLndVNAKPTEKSD 210
Cdd:cd14120 119 KPQNILLShnsgrkpspNDIRLKIADFGFARF-----LQDGM---------MAATLCGSPMYMAPEVI--MSLQYDAKAD 182
                       170
                ....*....|....*...
gi 3426027  211 VYSFAVVLWAIFANKEPY 228
Cdd:cd14120 183 LWSIGTIVYQCLTGKAPF 200
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-275 8.07e-16

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


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 78.39  E-value: 8.07e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHR-TQGLMIMKTVYKgpNCIEHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14169  11 LGEGAFSEVVLAQERgSQRLVALKCIPK--KALRGKEAMVEnEIAVLRRINHENIVSLEDIYESPTHLYLAMELVTGGEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH---IKIADLGLASFkmwsklnneehnelr 177
Cdd:cd14169  89 FDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATPFEdskIMISDFGLSKI--------------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 EVDGTAKKNGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSG---NRPDVDDIT 253
Cdd:cd14169 154 EAQGMLSTACGTPGYVAPELLEQ---KPYGKAvDVWAIGVISYILLCGYPPFYDENDSELFNQILKAEyefDSPYWDDIS 230
                       250       260
                ....*....|....*....|..
gi 3426027  254 EYCPREIISLMklcwEANPEAR 275
Cdd:cd14169 231 ESAKDFIRHLL----ERDPEKR 248
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
31-277 1.09e-15

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: 77.70  E-value: 1.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   31 VSLCFHRTQG----LMIMKTVYKGPNCIEHNEALLEEAKMMNRLR----HSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd14181  26 VRRCVHRHTGqefaVKIIEVTAERLSPEQLEEVRSSTLKEIHILRqvsgHPSIITLIDSYESSTFIFLVFDLMRRGELFD 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskLNNEEHNELREVDGT 182
Cdd:cd14181 106 YLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFS-------CHLEPGEKLRELCGT 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKknggtlyYMAPEHL----NDVNAKPTEKSDVYSFAVVLWAIFANKEPYENaicEQQLIMC--IKSG----NRPDVDDI 252
Cdd:cd14181 179 PG-------YLAPEILkcsmDETHPGYGKEVDLWACGVILFTLLAGSPPFWH---RRQMLMLrmIMEGryqfSSPEWDDR 248
                       250       260
                ....*....|....*....|....*
gi 3426027  253 TEYCPREIISLMKLCweanPEARPT 277
Cdd:cd14181 249 SSTVKDLISRLLVVD----PEIRLT 269
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
58-281 1.17e-15

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: 77.27  E-value: 1.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEmSTPLSVKGRIIL-EIIEGMCYLHGKGVIH 136
Cdd:cd14189  46 EKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSLAHIWKAR-HTLLEPEVRYYLkQIISGLKYLHLKGILH 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFHIKIADLGLASFkmwsklnneehneLREVDGTAKKNGGTLYYMAPEHLNDVNAKPteKSDVYSFAV 216
Cdd:cd14189 125 RDLKLGNFFINENMELKVGDFGLAAR-------------LEPPEQRKKTICGTPNYLAPEVLLRQGHGP--ESDVWSLGC 189
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  217 VLWAIFANKEPYENAICEQQLiMCIKSGNRPDVDDITEYCPREIISLMKlcweANPEARPTFPGI 281
Cdd:cd14189 190 VMYTLLCGNPPFETLDLKETY-RCIKQVKYTLPASLSLPARHLLAGILK----RNPGDRLTLDQI 249
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
62-276 1.19e-15

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: 77.70  E-value: 1.19e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGKYSLvmEYMEKGNLMHVL----KAEMSTPLS--VKGRIILEIIEGMCYLHGKGVI 135
Cdd:cd14067  59 QEASMLHSLQHPCIVYLIGISIHPLCFAL--ELAPLGSLNTVLeenhKGSSFMPLGhmLTFKIAYQIAAGLAYLHKKNII 136
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILV-----DNDFHIKIADLGLA--SFkmwsklnneeHNELREVDGTAKknggtlyYMAPEhlndvnAKP--- 205
Cdd:cd14067 137 FCDLKSDNILVwsldvQEHINIKLSDYGISrqSF----------HEGALGVEGTPG-------YQAPE------IRPriv 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  206 -TEKSDVYSFAVVLWAIFANKEPyenAICEQQLIMCIK--SGNRPDVDDITEYCPREIISLMKLCWEANPEARP 276
Cdd:cd14067 194 yDEKVDMFSYGMVLYELLSGQRP---SLGHHQLQIAKKlsKGIRPVLGQPEEVQFFRLQALMMECWDTKPEKRP 264
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
23-277 1.59e-15

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: 77.28  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKvslCFHRTQ--------GLMIMKTVYKGPNcieHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd14187  15 LGKGGFAK---CYEITDadtkevfaGKIVPKSLLLKPH---QKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLEL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLM--HVLKAEMSTPlsvKGRIIL-EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLnne 171
Cdd:cd14187  89 CRRRSLLelHKRRKALTEP---EARYYLrQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLA-----TKV--- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelrEVDGTAKKN-GGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKSgnrpdvd 250
Cdd:cd14187 158 ------EYDGERKKTlCGTPNYIAPEVLS--KKGHSFEVDIWSIGCIMYTLLVGKPPFETS-CLKETYLRIKK------- 221
                       250       260       270
                ....*....|....*....|....*....|..
gi 3426027  251 diTEYC-PREI----ISLMKLCWEANPEARPT 277
Cdd:cd14187 222 --NEYSiPKHInpvaASLIQKMLQTDPTARPT 251
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
90-277 1.63e-15

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 77.87  E-value: 1.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKaemSTPLSVKG--RIILEIIEGMCYLH-------GKGVI-HKDLKPENILVDNDFHIKIADLGL 159
Cdd:cd14142  80 LITHYHENGSLYDYLQ---RTTLDHQEmlRLALSAASGLVHLHteifgtqGKPAIaHRDLKSKNILVKSNGQCCIADLGL 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  160 ASfkmwskLNNEEHNELrevDGTAKKNGGTLYYMAPEHLND-VNAKPTE---KSDVYSFAVVLWAI-------------- 221
Cdd:cd14142 157 AV------THSQETNQL---DVGNNPRVGTKRYMAPEVLDEtINTDCFEsykRVDIYAFGLVLWEVarrcvsggiveeyk 227
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  222 --FANKEPYENAICEQQLIMCIkSGNRPDV------DDITEycprEIISLMKLCWEANPEARPT 277
Cdd:cd14142 228 ppFYDVVPSDPSFEDMRKVVCV-DQQRPNIpnrwssDPTLT----AMAKLMKECWYQNPSARLT 286
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
23-228 1.78e-15

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: 77.70  E-value: 1.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIM-KTVYKGPNCIEHNEAL-LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd05632  10 LGKGGFGEVCACQVRATGKMYAcKRLEKKRIKKRKGESMaLNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 -MHVLKaeMSTPLSVKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskLNNEEHNEL 176
Cdd:cd05632  90 kFHIYN--MGNPGFEEERALFyaaEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA-------VKIPEGESI 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  177 RevdgtakKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05632 161 R-------GRVGTVGYMAPEVLN--NQRYTLSPDYWGLGCLIYEMIEGQSPF 203
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
69-285 1.85e-15

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 77.37  E-value: 1.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   69 RLRHSRVVKLLGV-IIEEGKYS---LVMEYMEKGNLMHVLKA-EMStpLSVKGRIILEIIEGMCYLHG----------KG 133
Cdd:cd14053  45 GMKHENILQFIGAeKHGESLEAeywLITEFHERGSLCDYLKGnVIS--WNELCKIAESMARGLAYLHEdipatngghkPS 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELrevdgtakkngGTLYYMAPEHLND-VNAKPTE--KSD 210
Cdd:cd14053 123 IAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCGDTHGQV-----------GTRRYMAPEVLEGaINFTRDAflRID 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  211 VYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYC------PR------------EIISLMKLCWEANP 272
Cdd:cd14053 192 MYAMGLVLWELLSRCSVHDGPVDEYQLPFEEEVGQHPTLEDMQECVvhkklrPQirdewrkhpglaQLCETIEECWDHDA 271
                       250
                ....*....|...
gi 3426027  273 EARPTFPGIEEKF 285
Cdd:cd14053 272 EARLSAGCVEERL 284
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
23-200 1.86e-15

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: 77.78  E-value: 1.86e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG-LMIMKtVYKGPNCIEHNEA--LLEEAKMMNRLRHSRVVKLlgviieegKYSL--------V 91
Cdd:cd05571   3 LGKGTFGKVILCREKATGeLYAIK-ILKKEVIIAKDEVahTLTENRVLQNTRHPFLTSL--------KYSFqtndrlcfV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAE--MSTPlsvKGRI-ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwskl 168
Cdd:cd05571  74 MEYVNGGELFFHLSRErvFSED---RTRFyGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEI---- 146
                       170       180       190
                ....*....|....*....|....*....|...
gi 3426027  169 nneehnelreVDG-TAKKNGGTLYYMAPEHLND 200
Cdd:cd05571 147 ----------SYGaTTKTFCGTPEYLAPEVLED 169
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
60-275 1.91e-15

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: 77.48  E-value: 1.91e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH--VLKAEMSTPLSvkGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd14096  53 ILKEVQIMKRLSHPNIVKLLDFQESDEYYYIVLELADGGEIFHqiVRLTYFSEDLS--RHVITQVASAVKYLHEIGVVHR 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILV-----------------DND------F----------HIKIADLGLASfKMWSKlnneehnelrevdgTAK 184
Cdd:cd14096 131 DIKPENLLFepipfipsivklrkaddDETkvdegeFipgvggggigIVKLADFGLSK-QVWDS--------------NTK 195
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  185 KNGGTLYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEP-YENAIceQQLIMCIKSGN----RPDVDDITEYCPRE 259
Cdd:cd14096 196 TPCGTVGYTAPEVVKD--ERYSKKVDMWALGCVLYTLLCGFPPfYDESI--ETLTEKISRGDytflSPWWDEISKSAKDL 271
                       250
                ....*....|....*.
gi 3426027  260 IISLMklcwEANPEAR 275
Cdd:cd14096 272 ISHLL----TVDPAKR 283
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
13-228 2.12e-15

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: 76.92  E-value: 2.12e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   13 KSSDFLESA-ELDSGGFGKVSLCFHRTQGL-----MIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEG 86
Cdd:cd14196   2 KVEDFYDIGeELGSGQFAIVKKCREKSTGLeyaakFIKKRQSRASRRGVSREEIEREVSILRQVLHPNIITLHDVYENRT 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   87 KYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENI-LVDNDF---HIKIADLGLASf 162
Cdd:cd14196  82 DVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENImLLDKNIpipHIKLIDFGLAH- 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  163 kmwsklNNEEHNELREVDGTAKknggtlyYMAPEhlnDVNAKPTE-KSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14196 161 ------EIEDGVEFKNIFGTPE-------FVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
18-228 2.18e-15

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: 76.99  E-value: 2.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   18 LESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNeaLLEEAKMMNRLR-HSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd14173   5 LQEEVLGEGAYARVQTCINLiTNKEYAVKIIEKRPGHSRSR--VFREVEMLYQCQgHRNVLELIEFFEEEDKFYLVFEKM 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLM-HVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHI---KIADLGLAS-FKMWSKLNN 170
Cdd:cd14173  83 RGGSILsHIHRRRHFNELEAS-VVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSgIKLNSDCSP 161
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  171 EEHNELREVDGTAKknggtlyYMAPEHLNDVNAKPT---EKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14173 162 ISTPELLTPCGSAE-------YMAPEVVEAFNEEASiydKRCDLWSLGVILYIMLSGYPPF 215
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
61-223 2.18e-15

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: 77.41  E-value: 2.18e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYS--LVMEYMEKgNLMHVLKaEMSTPLS---VKGrIILEIIEGMCYLHGKGVI 135
Cdd:cd07845  54 LREITLLLNLRHPNIVELKEVVVGKHLDSifLVMEYCEQ-DLASLLD-NMPTPFSesqVKC-LMLQLLRGLQYLHENFII 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASfkmwsklnNEEHnelreVDGTAKKNGGTLYYMAPEHLndvnakptEKSDVYSFA 215
Cdd:cd07845 131 HRDLKVSNLLLTDKGCLKIADFGLAR--------TYGL-----PAKPMTPKVVTLWYRAPELL--------LGCTTYTTA 189
                       170
                ....*....|.
gi 3426027  216 VVLWA---IFA 223
Cdd:cd07845 190 IDMWAvgcILA 200
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
12-285 2.38e-15

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: 77.41  E-value: 2.38e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   12 MKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTV-------YKGPNCiehNEALLEEAKMMNRLRHSRVVKLLGVIIE 84
Cdd:cd05110   4 LKETELKRVKVLGSGAFGTVYKGIWVPEGETVKIPVaikilneTTGPKA---NVEFMDEALIMASMDHPHLVRLLGVCLS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EgKYSLVMEYMEKGNLM---HVLKAEMSTPLSVKGriILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAs 161
Cdd:cd05110  81 P-TIQLVTQLMPHGCLLdyvHEHKDNIGSQLLLNW--CVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLA- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  162 fkmwsklnneehnelREVDGTAKK---NGGTL--YYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYEnAICEQ 235
Cdd:cd05110 157 ---------------RLLEGDEKEynaDGGKMpiKWMALECIH--YRKFTHQSDVWSYGVTIWELMTfGGKPYD-GIPTR 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  236 QLIMCIKSGNRPDVDDIteyCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05110 219 EIPDLLEKGERLPQPPI---CTIDVYMVMVKCWMIDADSRPKFKELAAEF 265
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
16-227 2.53e-15

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: 77.07  E-value: 2.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYkgpncIEHNE-----ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd07861   1 DYTKIEKIGEGTYGVVYKGRNKkTGQIVAMKKIR-----LESEEegvpsTAIREISLLKELQHPNIVCLEDVLMQENRLY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEY--MEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA-SFKMWS 166
Cdd:cd07861  76 LVFEFlsMDLKKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLArAFGIPV 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  167 KLNNEEHNelrevdgtakknggTLYYMAPEHLndvnakptEKSDVYSFAVVLWAI------FANKEP 227
Cdd:cd07861 156 RVYTHEVV--------------TLWYRAPEVL--------LGSPRYSTPVDIWSIgtifaeMATKKP 200
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
10-221 2.66e-15

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: 78.15  E-value: 2.66e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   10 IKMKSSDFLESAELDSGGFGKVSLCFHRTQG----LMIM-KTVYKGPNCIEHneaLLEEAKMMNRLRHSRVVKLLGVIIE 84
Cdd:cd05600   6 TRLKLSDFQILTQVGQGGYGSVFLARKKDTGeicaLKIMkKKVLFKLNEVNH---VLTERDILTTTNSPWLVKLLYAFQD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EGKYSLVMEYMEKGnlmhvlkaEMSTPLSVKGRI--------ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIAD 156
Cdd:cd05600  83 PENVYLAMEYVPGG--------DFRTLLNNSGILseeharfyIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTD 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  157 LGLASFKM------WSKLNNEE----------HNELREVDGTAKKNG--------GTLYYMAPEHLNDVNakpteksdvY 212
Cdd:cd05600 155 FGLASGTLspkkieSMKIRLEEvkntafleltAKERRNIYRAMRKEDqnyansvvGSPDYMAPEVLRGEG---------Y 225

                ....*....
gi 3426027  213 SFAVVLWAI 221
Cdd:cd05600 226 DLTVDYWSL 234
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
61-277 3.11e-15

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: 75.81  E-value: 3.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKgNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd14050  48 LEEVERHEKLgEHPNCVRFIKAWEEKGILYIQTELCDT-SLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDI 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  140 KPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVDGTakknggtlyYMAPEHLndvNAKPTEKSDVYSFAVVLW 219
Cdd:cd14050 127 KPANIFLSKDGVCKLGDFGLV-----VELDKEDIHDAQEGDPR---------YMAPELL---QGSFTKAADIFSLGITIL 189
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  220 AIFANKEPYENAICEQQLimciKSGNRPdvDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14050 190 ELACNLELPSGGDGWHQL----RQGYLP--EEFTAGLSPELRSIIKLMMDPDPERRPT 241
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
72-245 3.36e-15

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: 76.96  E-value: 3.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   72 HSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DN 148
Cdd:cd14092  58 HPNIVKLHEVFQDELHTYLVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDD 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  149 DFHIKIADLGLASFKmwsklnnEEHNELrevdgtaKKNGGTLYYMAPEHLNDVNAKP--TEKSDVYSFAVVLWAIFANKE 226
Cdd:cd14092 138 DAEIKIVDFGFARLK-------PENQPL-------KTPCFTLPYAAPEVLKQALSTQgyDESCDLWSLGVILYTMLSGQV 203
                       170       180
                ....*....|....*....|....*
gi 3426027  227 PY------ENAIceqQLIMCIKSGN 245
Cdd:cd14092 204 PFqspsrnESAA---EIMKRIKSGD 225
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
46-160 3.71e-15

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: 76.37  E-value: 3.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   46 TVYKGPNcIEHNE--ALLE---------------EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGnlmhvLKAEM 108
Cdd:cd07836  15 TVYKGRN-RTTGEivALKEihldaeegtpstairEISLMKELKHENIVRLHDVIHTENKLMLVFEYMDKD-----LKKYM 88
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  109 ST--------PLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd07836  89 DThgvrgaldPNTVKS-FTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLA 147
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
23-228 3.79e-15

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: 76.57  E-value: 3.79e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIM-KTVYKGPNCIEHNEAL-LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd05631   8 LGKGGFGEVCACQVRATGKMYAcKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 -MHVLKaeMSTPLSVKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnEL 176
Cdd:cd05631  88 kFHIYN--MGNPGFDEQRAIFyaaELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAV-------------QI 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  177 REVDgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05631 153 PEGE-TVRGRVGTVGYMAPEVIN--NEKYTFSPDWWGLGCLIYEMIQGQSPF 201
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
25-158 3.87e-15

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: 76.16  E-value: 3.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQGLMI----MKTVYKGPNCIEHnealLEEAKMMNRLR-HSRVVKLLGVIIEE--GKYSLVMEYMEk 97
Cdd:cd07831   9 EGTFSEVLKAQSRKTGKYYaikcMKKHFKSLEQVNN----LREIQALRRLSpHPNILRLIEVLFDRktGRLALVFELMD- 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027   98 GNLMHVLKAEmSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDfHIKIADLG 158
Cdd:cd07831  84 MNLYELIKGR-KRPLPEKrvKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG 144
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
23-277 4.29e-15

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 76.07  E-value: 4.29e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLmh 102
Cdd:cd06619   9 LGHGNGGTVYKAYHLLTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGGSL-- 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 vlKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnelREVDGT 182
Cdd:cd06619  87 --DVYRKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVST---------------QLVNSI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY------ENAICEQQLIMCIKSGNRPdVDDITEYC 256
Cdd:cd06619 150 AKTYVGTNAYMAPERIS--GEQYGIHSDVWSLGISFMELALGRFPYpqiqknQGSLMPLQLLQCIVDEDPP-VLPVGQFS 226
                       250       260
                ....*....|....*....|.
gi 3426027  257 PReIISLMKLCWEANPEARPT 277
Cdd:cd06619 227 EK-FVHFITQCMRKQPKERPA 246
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
588-656 4.54e-15

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 70.79  E-value: 4.54e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  588 DPIRENLGKHWKNCARKLGFTQSQIDEIDHDYERDgLKEKVYQMLQKWVMREGiKGATVGKLAQALHQC 656
Cdd:cd08306   6 DVICENLGRDWRQLARKLGLSETKIESISEAHPRN-LREQVRQSLREWKKIKK-AEATVADLIKALRDC 72
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
21-314 4.85e-15

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: 76.57  E-value: 4.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFHRTQG-LMIMKTVYKGpNCIEHNE--ALLEEAKMM---NRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd05589   5 AVLGRGHFGKVLLAEYKPTGeLFAIKALKKG-DIIARDEveSLMCEKRIFetvNSARHPFLVNLFACFQTPEHVCFVMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLM-HVLKAEMSTPLSV--KGRIILeiieGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnne 171
Cdd:cd05589  84 AAGGDLMmHIHEDVFSEPRAVfyAACVVL----GLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGM------- 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelrevdGTAKKNG---GTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIksgnrpd 248
Cdd:cd05589 153 ---------GFGDRTStfcGTPEFLAPEVLTDTSY--TRAVDWWGLGVLIYEMLVGESPFPGDD-EEEVFDSI------- 213
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  249 VDDITEYcPR----EIISLMKLCWEANPEAR--------------PTFPGIE------EKFRPFYLSQLEESveEDVKSL 304
Cdd:cd05589 214 VNDEVRY-PRflstEAISIMRRLLRKNPERRlgaserdaedvkkqPFFRNIDweallaRKIKPPFVPTIKSP--EDVSNF 290
                       330
                ....*....|
gi 3426027  305 KKEYSNENAV 314
Cdd:cd05589 291 DEEFTSEKPV 300
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
44-253 5.10e-15

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: 75.92  E-value: 5.10e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   44 MKTVYKGPNcieHNEALLEEAKMMNRLR---HSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkAEmstpLSVKGR--- 117
Cdd:cd14052  34 LKPNYAGAK---DRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQTELCENGSLDVFL-SE----LGLLGRlde 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  118 -----IILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkMWSKLNNEEHNELREvdgtakknggtlyY 192
Cdd:cd14052 106 frvwkILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMAT--VWPLIRGIEREGDRE-------------Y 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  193 MAPEHLNDVN-AKPtekSDVYSFAVVLWAIFANKEPYENAICEQQLimciKSGNRPDVDDIT 253
Cdd:cd14052 171 IAPEILSEHMyDKP---ADIFSLGLILLEAAANVVLPDNGDAWQKL----RSGDLSDAPRLS 225
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
91-229 5.87e-15

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: 76.28  E-value: 5.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSklnn 170
Cdd:cd05587  75 VMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIFG---- 150
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eehnelrevDGTAKKNGGTLYYMAPEHlndVNAKPTEKS-DVYSFAVVLWAIFANKEPYE 229
Cdd:cd05587 151 ---------GKTTRTFCGTPDYIAPEI---IAYQPYGKSvDWWAYGVLLYEMLAGQPPFD 198
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
25-239 6.02e-15

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: 76.62  E-value: 6.02e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVI-----IEEGKYSLVMEYMEKG 98
Cdd:cd07877  27 SGAYGSVCAAFDTKTGLRVaVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFtparsLEEFNDVYLVTHLMGA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelRE 178
Cdd:cd07877 107 DLNNIVKCQKLTDDHVQ-FLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLA----------------RH 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  179 VDGTAKKNGGTLYYMAPE-HLNDVNAKPTekSDVYSFAVVLWAIFANKE--PYENAICEQQLIM 239
Cdd:cd07877 170 TDDEMTGYVATRWYRAPEiMLNWMHYNQT--VDIWSVGCIMAELLTGRTlfPGTDHIDQLKLIL 231
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
16-277 6.47e-15

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: 75.31  E-value: 6.47e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLEsaELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEhNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd14114   5 DILE--ELGTGAFGVVHRCTERATGNNFAAKFIMTPHESD-KETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAE---MSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVD--NDFHIKIADLGLAsfkmwSKLNN 170
Cdd:cd14114  82 SGGELFERIAAEhykMSEAEVIN--YMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLA-----THLDP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 EEhnelrevdgTAKKNGGTLYYMAPEhlnDVNAKPTE-KSDVYSFAVVLWAIFANKEPY--ENaicEQQLIMCIKSGNRP 247
Cdd:cd14114 155 KE---------SVKVTTGTAEFAAPE---IVEREPVGfYTDMWAVGVLSYVLLSGLSPFagEN---DDETLRNVKSCDWN 219
                       250       260       270
                ....*....|....*....|....*....|
gi 3426027  248 DVDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14114 220 FDDSAFSGISEEAKDFIRKLLLADPNKRMT 249
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
22-277 6.93e-15

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: 75.18  E-value: 6.93e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRT--QGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM--EK 97
Cdd:cd06607   8 EIGHGSFGAVYYARNKRtsEVVAIKKMSYSGKQSTEKWQDIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLVMEYClgSA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTpLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwsklnneehnelr 177
Cdd:cd06607  88 SDIVEVHKKPLQE-VEIAA-ICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLV-------------- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  178 evdGTAKKNGGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMcIKSGNRPDVDDITeyC 256
Cdd:cd06607 152 ---CPANSFVGTPYWMAPEVILAMDEGQyDGKVDVWSLGITCIELAERKPPLFNMNAMSALYH-IAQNDSPTLSSGE--W 225
                       250       260
                ....*....|....*....|.
gi 3426027  257 PREIISLMKLCWEANPEARPT 277
Cdd:cd06607 226 SDDFRNFVDSCLQKIPQDRPS 246
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
57-281 7.36e-15

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: 75.51  E-value: 7.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   57 NEALLEEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKgNLMHVLKAEMST-----PLSVKGRIILEIIEGMCYLH 130
Cdd:cd14001  49 QERLKEEAKILKSLNHPNIVGFRAFTkSEDGSLCLAMEYGGK-SLNDLIEERYEAglgpfPAATILKVALSIARALEYLH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  131 G-KGVIHKDLKPENILVDNDFH-IKIADLGLaSFKMWSKLNNEEHNELREVdgtakkngGTLYYMAPEHLNDvNAKPTEK 208
Cdd:cd14001 128 NeKKILHGDIKSGNVLIKGDFEsVKLCDFGV-SLPLTENLEVDSDPKAQYV--------GTEPWKAKEALEE-GGVITDK 197
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  209 SDVYSFAVVLWAIFANKEPYenaiceqqlimcIKSGNRPDvDDITEYCPReiislMKLCWEANPEARPTFPGI 281
Cdd:cd14001 198 ADIFAYGLVLWEMMTLSVPH------------LNLLDIED-DDEDESFDE-----DEEDEEAYYGTLGTRPAL 252
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
70-302 1.17e-14

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


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 75.09  E-value: 1.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   70 LRHSRVVKLLGVIIE-EGKYS---LVMEYMEKGNLMHVLKaemSTPLSVKGRIILEI--IEGMCYLH-------GKGVI- 135
Cdd:cd14219  56 MRHENILGFIAADIKgTGSWTqlyLITDYHENGSLYDYLK---STTLDTKAMLKLAYssVSGLCHLHteifstqGKPAIa 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLAsFKMWSKLNneehnelrEVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKS----DV 211
Cdd:cd14219 133 HRDLKSKNILVKKNGTCCIADLGLA-VKFISDTN--------EVDIPPNTRVGTKRYMPPEVLDESLNRNHFQSyimaDM 203
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  212 YSFAVVLWAI----------------FANKEPYENAICEQQLIMCIKSgNRPDVDD--ITEYCPREIISLMKLCWEANPE 273
Cdd:cd14219 204 YSFGLILWEVarrcvsggiveeyqlpYHDLVPSDPSYEDMREIVCIKR-LRPSFPNrwSSDECLRQMGKLMTECWAHNPA 282
                       250       260
                ....*....|....*....|....*....
gi 3426027  274 ARPTFPGIEEKfrpfyLSQLEESveEDVK 302
Cdd:cd14219 283 SRLTALRVKKT-----LAKMSES--QDIK 304
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
17-230 1.20e-14

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: 75.46  E-value: 1.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCF--HRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06633  23 FVDLHEIGHGSFGAVYFATnsHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEY 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 M--EKGNLMHVLKAEMStplSVK-GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnne 171
Cdd:cd06633 103 ClgSASDLLEVHKKPLQ---EVEiAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSAS---------- 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 ehnelreVDGTAKKNGGTLYYMAPEHLNDVNAKPTE-KSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd06633 170 -------IASPANSFVGTPYWMAPEVILAMDEGQYDgKVDIWSLGITCIELAERKPPLFN 222
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
23-198 1.43e-14

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: 75.13  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG----LMIMKtVYKGPNCIE------HNEAlleEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd05584   4 LGKGGYGKVFQVRKTTGSdkgkIFAMK-VLKKASIVRnqkdtaHTKA---ERNILEAVKHPFIVDLHYAFQTGGKLYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnnEE 172
Cdd:cd05584  80 EYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLC----------KE 149
                       170       180
                ....*....|....*....|....*.
gi 3426027  173 HNELREVDGTAkknGGTLYYMAPEHL 198
Cdd:cd05584 150 SIHDGTVTHTF---CGTIEYMAPEIL 172
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
61-276 1.57e-14

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 74.68  E-value: 1.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL----MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIH 136
Cdd:cd08229  72 IKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLsrmiKHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRRVMH 151
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFHIKIADLGLASFkmWSKLNNEEHNELrevdgtakkngGTLYYMAPE--HLNDVNAkpteKSDVYSF 214
Cdd:cd08229 152 RDIKPANVFITATGVVKLGDLGLGRF--FSSKTTAAHSLV-----------GTPYYMSPEriHENGYNF----KSDIWSL 214
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  215 AVVLWAIFANKEP-YENAICEQQLIMCIKSGNRPDVDdiTEYCPREIISLMKLCWEANPEARP 276
Cdd:cd08229 215 GCLLYEMAALQSPfYGDKMNLYSLCKKIEQCDYPPLP--SDHYSEELRQLVNMCINPDPEKRP 275
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
25-277 1.85e-14

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 75.25  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    25 SGGFGKVSLCFHRTQG-LMIMKTVYKgpnciEHNEALL----EEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:PLN00034  84 SGAGGTVYKVIHRPTGrLYALKVIYG-----NHEDTVRrqicREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   100 L--MHVLKAEMSTPLSvkgriiLEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwsklnneehneLR 177
Cdd:PLN00034 159 LegTHIADEQFLADVA------RQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRI-------------LA 219
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   178 EVDGTAKKNGGTLYYMAPEHLN-DVN--AKPTEKSDVYSFAVVLWAIFANKEPYenAICEQ---QLIMCIKSGNRPDVDD 251
Cdd:PLN00034 220 QTMDPCNSSVGTIAYMSPERINtDLNhgAYDGYAGDIWSLGVSILEFYLGRFPF--GVGRQgdwASLMCAICMSQPPEAP 297
                        250       260
                 ....*....|....*....|....*.
gi 3426027   252 ITeyCPREIISLMKLCWEANPEARPT 277
Cdd:PLN00034 298 AT--ASREFRHFISCCLQREPAKRWS 321
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
61-277 1.89e-14

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: 73.84  E-value: 1.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLK--AEMSTPLSVKG--RIILEIIEGMCYLHGKGVIH 136
Cdd:cd08224  48 LKEIDLLQQLNHPNIIKYLASFIENNELNIVLELADAGDLSRLIKhfKKQKRLIPERTiwKYFVQLCSALEHMHSKRIMH 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFHIKIADLGLASFkmWSKLNNEEHNELrevdgtakkngGTLYYMAPEHLNDvnaKPTE-KSDVYSFA 215
Cdd:cd08224 128 RDIKPANVFITANGVVKLGDLGLGRF--FSSKTTAAHSLV-----------GTPYYMSPERIRE---QGYDfKSDIWSLG 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  216 VVLWAIFANKEPYEN------AICEQqlimcIKSGNRPDVDDitEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd08224 192 CLLYEMAALQSPFYGekmnlySLCKK-----IEKCEYPPLPA--DLYSQELRDLVAACIQPDPEKRPD 252
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
23-281 2.00e-14

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 74.65  E-value: 2.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEA--LLEEAKMMNRL-RHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd05088  15 IGEGNFGQVLKARIKKDGLRMDAAIKRMKEYASKDDHrdFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYAPHGN 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEM------------STPLSVKGRIIL----EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfk 163
Cdd:cd05088  95 LLDFLRKSRvletdpafaianSTASTLSSQQLLhfaaDVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLS--- 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 mwsklnneehnelREVDGTAKKNGGTL--YYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICeQQLIMC 240
Cdd:cd05088 172 -------------RGQEVYVKKTMGRLpvRWMAIESLN--YSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTC-AELYEK 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 3426027  241 IKSGNRPDVddiTEYCPREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05088 236 LPQGYRLEK---PLNCDDEVYDLMRQCWREKPYERPSFAQI 273
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
23-277 2.06e-14

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: 73.86  E-value: 2.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLC-FHRTQGLMIMKTVYkgpncIEHNEALLE---EAKMMNRLR-HSRVVKLLG---VIIEEGKYS--LVM 92
Cdd:cd14037  11 LAEGGFAHVYLVkTSNGGNRAALKRVY-----VNDEHDLNVckrEIEIMKRLSgHKNIVGYIDssaNRSGNGVYEvlLLM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLS----VKgrIILEIIEGMCYLHG--KGVIHKDLKPENILVDNDFHIKIADLGLASFKMws 166
Cdd:cd14037  86 EYCKGGGVIDLMNQRLQTGLTeseiLK--IFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGSATTKI-- 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 kLNNEEHNELREVDGTAKKNgGTLYYMAPEHLNDVNAKP-TEKSDVYSFAVVLWAIFANKEPYenaicEQQLIMCIKSGN 245
Cdd:cd14037 162 -LPPQTKQGVTYVEEDIKKY-TTLQYRAPEMIDLYRGKPiTEKSDIWALGCLLYKLCFYTTPF-----EESGQLAILNGN 234
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  246 R--PDVddiTEYCPReIISLMKLCWEANPEARPT 277
Cdd:cd14037 235 FtfPDN---SRYSKR-LHKLIRYMLEEDPEKRPN 264
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
72-240 2.17e-14

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: 74.69  E-value: 2.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   72 HSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DN 148
Cdd:cd14179  61 HPNIVKLHEVYHDQLHTFLVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSD 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  149 DFHIKIADLGLASFKmwsklnnEEHNELrevdgtAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14179 141 NSEIKIIDFGFARLK-------PPDNQP------LKTPCFTLHYAAPELLNYNGYD--ESCDLWSLGVILYTMLSGQVPF 205
                       170
                ....*....|..
gi 3426027  229 EnaiCEQQLIMC 240
Cdd:cd14179 206 Q---CHDKSLTC 214
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
90-310 2.57e-14

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: 74.21  E-value: 2.57e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAemstplsvKGRIIL--------EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS 161
Cdd:cd05620  73 FVMEFLNGGDLMFHIQD--------KGRFDLyratfyaaEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCK 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  162 FKMWSklnneehnelrevDGTAKKNGGTLYYMAPEHLNDVnaKPTEKSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCI 241
Cdd:cd05620 145 ENVFG-------------DNRASTFCGTPDYIAPEILQGL--KYTFSVDWWSFGVLLYEMLIGQSPFHGDD-EDELFESI 208
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  242 ksgnRPDVDDITEYCPREIISLMKLCWEANPEARPTFPGiEEKFRPFYLS---------QLEESVEEDVKSlKKEYSN 310
Cdd:cd05620 209 ----RVDTPHYPRWITKESKDILEKLFERDPTRRLGVVG-NIRGHPFFKTinwtalekrELDPPFKPKVKS-PSDYSN 280
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
6-229 2.84e-14

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: 74.65  E-value: 2.84e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    6 SLNVIKMKSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNE---ALLEEAKMMNRLRHSRVVKLLGVI 82
Cdd:cd05615   1 SNNLDRVRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVVIQDDDvecTMVEKRVLALQDKPPFLTQLHSCF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   83 IEEGKYSLVMEYMEKGNLMHVLK--AEMSTPLSVkgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd05615  81 QTVDRLYFVMEYVNGGDLMYHIQqvGKFKEPQAV--FYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMC 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  161 SFKMwsklnneehnelreVDG-TAKKNGGTLYYMAPEhlnDVNAKPTEKS-DVYSFAVVLWAIFANKEPYE 229
Cdd:cd05615 159 KEHM--------------VEGvTTRTFCGTPDYIAPE---IIAYQPYGRSvDWWAYGVLLYEMLAGQPPFD 212
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
22-228 3.02e-14

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: 73.51  E-value: 3.02e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGL-----MIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd14194  12 ELGSGQFAVVKKCREKSTGLqyaakFIKKRRTKSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVILILELVA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENI-LVDNDF---HIKIADLGLASfkmwsklNNEE 172
Cdd:cd14194  92 GGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENImLLDRNVpkpRIKIIDFGLAH-------KIDF 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  173 HNELREVDGTAKknggtlyYMAPEhlnDVNAKPTE-KSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14194 165 GNEFKNIFGTPE-------FVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-312 3.60e-14

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: 74.65  E-value: 3.60e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   10 IKMKSSDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALL-EEAKMMNRLRHSRVVKLLGVIIEEGK 87
Cdd:cd05621  47 LQMKAEDYDVVKVIGRGAFGEVQLVRHKaSQKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFCAFQDDKY 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEKGNLMHvLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASFKMwsk 167
Cdd:cd05621 127 LYMVMEYMPGGDLVN-LMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFG-TCMKM--- 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 lnneEHNELREVDGTAkkngGTLYYMAPEHLNDVNAKP--TEKSDVYSFAVVLWAIFANKEPY--ENAICEQQLIMCIK- 242
Cdd:cd05621 202 ----DETGMVHCDTAV----GTPDYISPEVLKSQGGDGyyGRECDWWSVGVFLFEMLVGDTPFyaDSLVGTYSKIMDHKn 273
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  243 SGNRPDVDDITEYCPREIISLMklcweANPEARPTFPGIEE-KFRPFY------LSQLEESVEEDVKSLKKEYSNEN 312
Cdd:cd05621 274 SLNFPDDVEISKHAKNLICAFL-----TDREVRLGRNGVEEiKQHPFFrndqwnWDNIRETAAPVVPELSSDIDTSN 345
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
121-278 3.92e-14

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


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 74.66  E-value: 3.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  121 EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneeHNELREVDGTAKknGGT---LYYMAPEH 197
Cdd:cd05107 247 QVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLA------------RDIMRDSNYISK--GSTflpLKWMAPES 312
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  198 LndVNAKPTEKSDVYSFAVVLWAIFA-NKEPYENAICEQQLIMCIKSGNR---PdvdditEYCPREIISLMKLCWEANPE 273
Cdd:cd05107 313 I--FNNLYTTLSDVWSFGILLWEIFTlGGTPYPELPMNEQFYNAIKRGYRmakP------AHASDEIYEIMQKCWEEKFE 384

                ....*
gi 3426027  274 ARPTF 278
Cdd:cd05107 385 IRPDF 389
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
26-229 4.00e-14

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: 72.81  E-value: 4.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd14071  11 GNFAVVKLARHRiTKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEYASNGEIFDYL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNNEEHnelrevdgtAK 184
Cdd:cd14071  91 AQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNF-----FKPGEL---------LK 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 3426027  185 KNGGTLYYMAPEhLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd14071 157 TWCGSPPYAAPE-VFEGKEYEGPQLDIWSLGVVLYVLVCGALPFD 200
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
22-169 4.01e-14

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: 72.76  E-value: 4.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14075   9 ELGSGNFSQVKLGIHQlTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVMEYASGGEL 88
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASF-KMWSKLN 169
Cdd:cd14075  89 YTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHaKRGETLN 158
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
16-219 4.15e-14

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: 73.21  E-value: 4.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKgPNCIEHN--EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd05609   1 DFETIKLISNGAYGAVYLVRHReTRQRFAMKKINK-QNLILRNqiQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNN-- 170
Cdd:cd05609  80 EYVEGGDCATLLKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMSLTTNly 159
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 EEHNELREVDGTAKKNGGTLYYMAPEH-LNDVNAKPTeksDVYSFAVVLW 219
Cdd:cd05609 160 EGHIEKDTREFLDKQVCGTPEYIAPEViLRQGYGKPV---DWWAMGIILY 206
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
62-258 4.94e-14

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: 72.73  E-value: 4.94e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLL----GVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKG--VI 135
Cdd:cd14033  49 EEVEMLKGLQHPNIVRFYdswkSTVRGHKCIILVTELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCppIL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDN-DFHIKIADLGLASFKMWSklnneehnelrevdgTAKKNGGTLYYMAPEHLNDvnaKPTEKSDVYSF 214
Cdd:cd14033 129 HRDLKCDNIFITGpTGSVKIGDLGLATLKRAS---------------FAKSVIGTPEFMAPEMYEE---KYDEAVDVYAF 190
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 3426027  215 AVVLWAIFANKEPYENAICEQQLIMCIKSGNRPD---------VDDITEYCPR 258
Cdd:cd14033 191 GMCILEMATSEYPYSECQNAAQIYRKVTSGIKPDsfykvkvpeLKEIIEGCIR 243
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
61-323 5.16e-14

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: 73.55  E-value: 5.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEYMEkGNLMHVLKAemSTPLSVKG-RIIL-EIIEGMCYLHGK 132
Cdd:cd07855  52 LRELKILRHFKHDNIIAIRDILRPKVPYAdfkdvyVVLDLME-SDLHHIIHS--DQPLTLEHiRYFLyQLLRGLKYIHSA 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKlnnEEHNELrevdgtAKKNGGTLYYMAPEHLndvnakptEKSDVY 212
Cdd:cd07855 129 NVIHRDLKPSNLLVNENCELKIGDFGMARGLCTSP---EEHKYF------MTEYVATRWYRAPELM--------LSLPEY 191
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  213 SFAVVLWA---IFAN----KE--PYENAICEQQLIM---------------------CIKS-GNRPDVD--DITEYCPRE 259
Cdd:cd07855 192 TQAIDMWSvgcIFAEmlgrRQlfPGKNYVHQLQLILtvlgtpsqavinaigadrvrrYIQNlPNKQPVPweTLYPKADQQ 271
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  260 IISLMKLCWEANPEARPTfpgIEEKFRPFYLSQLEESVEEDVKSLKKEYSNENAVVKRMQSLQL 323
Cdd:cd07855 272 ALDLLSQMLRFDPSERIT---VAEALQHPFLAKYHDPDDEPDCAPPFDFDFDAEALTREALKEA 332
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
67-285 5.77e-14

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 72.68  E-value: 5.77e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   67 MNRLRHSRVVKLLGvIIEEGKYSLVMEYMEKGNLM-HVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENIL 145
Cdd:cd05111  63 IGSLDHAYIVRLLG-ICPGASLQLVTQLLPLGSLLdHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVL 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  146 VDNDFHIKIADLGLASFkMWSKLNNEEHNELREvdgtakknggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFA-N 224
Cdd:cd05111 142 LKSPSQVQVADFGVADL-LYPDDKKYFYSEAKT----------PIKWMALESI--HFGKYTHQSDVWSYGVTVWEMMTfG 208
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  225 KEPYEnAICEQQLIMCIKSGNRPDVDDIteyCPREIISLMKLCWEANPEARPTFPGIEEKF 285
Cdd:cd05111 209 AEPYA-GMRLAEVPDLLEKGERLAQPQI---CTIDVYMVMVKCWMIDENIRPTFKELANEF 265
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
63-160 6.17e-14

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: 72.92  E-value: 6.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEGK------YSLVMEYMEKgNL----MHVLKAEMSTPLS-VKgRIILEIIEGMCYLHG 131
Cdd:cd14137  47 ELQIMRRLKHPNIVKLKYFFYSSGEkkdevyLNLVMEYMPE-TLyrviRHYSKNKQTIPIIyVK-LYSYQLFRGLAYLHS 124
                        90       100       110
                ....*....|....*....|....*....|
gi 3426027  132 KGVIHKDLKPENILVDNDFHI-KIADLGLA 160
Cdd:cd14137 125 LGICHRDIKPQNLLVDPETGVlKLCDFGSA 154
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
13-228 6.71e-14

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: 73.51  E-value: 6.71e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   13 KSSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEA---LLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd05602   5 KPSDFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEkhiMSERNVLLKNVKHPFLVGLHFSFQTTDKLY 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTpLSVKGRIIL-EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskl 168
Cdd:cd05602  85 FVLDYINGGELFYHLQRERCF-LEPRARFYAaEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCK------- 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  169 NNEEHNelrevdGTAKKNGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPY 228
Cdd:cd05602 157 ENIEPN------GTTSTFCGTPEYLAPEVLHK---QPYDRTvDWWCLGAVLYEMLYGLPPF 208
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
22-221 7.05e-14

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: 72.73  E-value: 7.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFH----RTQGLMIMKTVYkgpncIEHNEAL----LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd07871   9 KLDKLGEGTYATVFKgrskLTENLVALKEIR-----LEHEEGApctaIREVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEK---------GNLMHVLKAEMstplsvkgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKm 164
Cdd:cd07871  84 YLDSdlkqyldncGNLMSMHNVKI---------FMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAK- 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  165 wSKLNNEEHNELRevdgtakknggTLYYMAPehlnDVNAKPTEksdvYSFAVVLWAI 221
Cdd:cd07871 154 -SVPTKTYSNEVV-----------TLWYRPP----DVLLGSTE----YSTPIDMWGV 190
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
16-229 7.30e-14

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: 72.35  E-value: 7.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFlESAELDSGGFGKVSLCF---HR--TQGLMIMKTVYKgPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSL 90
Cdd:cd14201   5 DF-EYSRKDLVGHGAFAVVFkgrHRkkTDWEVAIKSINK-KNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVD---------NDFHIKIADLGLAS 161
Cdd:cd14201  83 VMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFAR 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  162 FkmwsklnneehnelREVDGTAKKNGGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd14201 163 Y--------------LQSNMMAATLCGSPMYMAPEVIMSQHYDA--KADLWSIGTVIYQCLVGKPPFQ 214
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
15-289 7.31e-14

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: 73.89  E-value: 7.31e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSL-CFHRTQGLMIMKTVYK----GPNCIEHNEAlleEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd05626   1 SMFVKIKTLGIGAFGEVCLaCKVDTHALYAMKTLRKkdvlNRNQVAHVKA---ERDILAEADNEWVVKLYYSFQDKDNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAS-FK----- 163
Cdd:cd05626  78 FVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTgFRwthns 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 ------------------MWSKLNN-EEHNELREVDGTAKKNG---------GTLYYMAPEHLndVNAKPTEKSDVYSFA 215
Cdd:cd05626 158 kyyqkgshirqdsmepsdLWDDVSNcRCGDRLKTLEQRATKQHqrclahslvGTPNYIAPEVL--LRKGYTQLCDWWSVG 235
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  216 VVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCWEAnpEARPTFPGIEE-KFRPFY 289
Cdd:cd05626 236 VILFEMLVGQPPFLAPTPTETQLKVINWENTLHIPPQVKLSPEAVDLITKLCCSA--EERLGRNGADDiKAHPFF 308
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
26-218 9.81e-14

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: 72.34  E-value: 9.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKgNLMHVL 104
Cdd:cd07848  12 GAYGVVLKCRHKeTKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYVEK-NMLELL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KaEMST---PLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMWSKLNNEEHNELRevdg 181
Cdd:cd07848  91 E-EMPNgvpPEKVRS-YIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFA--RNLSEGSNANYTEYV---- 162
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 3426027  182 takkngGTLYYMAPEHLndVNAKPTEKSDVYSFAVVL 218
Cdd:cd07848 163 ------ATRWYRSPELL--LGAPYGKAVDMWSVGCIL 191
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
46-237 1.10e-13

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: 72.34  E-value: 1.10e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   46 TVYKGPNCI------------EHNEAL----LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK---------GNL 100
Cdd:cd07873  17 TVYKGRSKLtdnlvalkeirlEHEEGApctaIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKdlkqylddcGNS 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMstplsvkgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKmwSKLNNEEHNELRevd 180
Cdd:cd07873  97 INMHNVKL---------FLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAK--SIPTKTYSNEVV--- 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  181 gtakknggTLYYMAPehlnDVNAKPTEKS---DVYSFAVVLWAIFANKEPYENAICEQQL 237
Cdd:cd07873 163 --------TLWYRPP----DILLGSTDYStqiDMWGVGCIFYEMSTGRPLFPGSTVEEQL 210
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
12-230 1.18e-13

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: 72.81  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   12 MKSSDFLESaeLDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEA--LLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd05593  14 MNDFDYLKL--LGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVahTLTESRVLKNTRHPFLTSLKYSFQTKDRLC 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKln 169
Cdd:cd05593  92 FVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEGITDA-- 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  170 neehnelrevdGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd05593 170 -----------ATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYN 217
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
23-196 1.20e-13

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: 72.27  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHR-TQGLMIMKTVYKgpNC-IEHNEA--LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd05574   9 LGKGDVGRVYLVRLKgTGKLFAMKVLDK--EEmIKRNKVkrVLTEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKaemSTPlsvKGRI--------ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGL----------- 159
Cdd:cd05574  87 ELFRLLQ---KQP---GKRLpeevarfyAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLskqssvtpppv 160
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 3426027  160 ---ASFKMWSKLNNEEHNELREVDGTAKKNG--GTLYYMAPE 196
Cdd:cd05574 161 rksLRKGSRRSSVKSIEKETFVAEPSARSNSfvGTEEYIAPE 202
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
52-218 1.30e-13

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 71.84  E-value: 1.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   52 NCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGR--IILEIIEGMCY 128
Cdd:cd14160  31 QWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEKFCLVYPYMQNGTLFDRLqCHGVTKPLSWHERinILIGIAKAIHY 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  129 LHGK---GVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklNNEEHNELREVDGTAKKNggtLYYMAPEHLNDvnAKP 205
Cdd:cd14160 111 LHNSqpcTVICGNISSANILLDDQMQPKLTDFALAHFRP----HLEDQSCTINMTTALHKH---LWYMPEEYIRQ--GKL 181
                       170
                ....*....|...
gi 3426027  206 TEKSDVYSFAVVL 218
Cdd:cd14160 182 SVKTDVYSFGIVI 194
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
23-244 1.44e-13

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: 71.68  E-value: 1.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGL-MIMKTVYKGPNcieHNEA-LLEEAKMMNRLR-HSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd14090  10 LGEGAYASVQTCINLYTGKeYAVKIIEKHPG---HSRSrVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFEKMRGGP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LM-HVLKAEMSTPLSVkGRIILEIIEGMCYLHGKGVIHKDLKPENIL---VDNDFHIKIADLGLASfkmWSKLNNEEHN- 174
Cdd:cd14090  87 LLsHIEKRVHFTEQEA-SLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGS---GIKLSSTSMTp 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 ----ELREVDGTAKknggtlyYMAPEhlnDVNAKPTE------KSDVYSFAVVLWAIFANKEPYENA------------- 231
Cdd:cd14090 163 vttpELLTPVGSAE-------YMAPE---VVDAFVGEalsydkRCDLWSLGVILYIMLCGYPPFYGRcgedcgwdrgeac 232
                       250
                ....*....|....
gi 3426027  232 -ICEQQLIMCIKSG 244
Cdd:cd14090 233 qDCQELLFHSIQEG 246
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
15-198 1.45e-13

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: 72.35  E-value: 1.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSL-CFHRTQGLMIMKTVYKGpNCIEHNEA--------LLEEAKmmnrlrHSRVVKLLGVIIEE 85
Cdd:cd05598   1 SMFEKIKTIGVGAFGEVSLvRKKDTNALYAMKTLRKK-DVLKRNQVahvkaerdILAEAD------NEWVVKLYYSFQDK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   86 GKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMW 165
Cdd:cd05598  74 ENLYFVMDYIPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRW 153
                       170       180       190
                ....*....|....*....|....*....|...
gi 3426027  166 SklnneeHNELREVdgtAKKNGGTLYYMAPEHL 198
Cdd:cd05598 154 T------HDSKYYL---AHSLVGTPNYIAPEVL 177
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
15-228 1.72e-13

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: 70.80  E-value: 1.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAE-LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEhNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd14191   1 SDFYDIEErLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKE-KENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVL---KAEMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF--HIKIADLGLAsfkmwSKL 168
Cdd:cd14191  80 MVSGGELFERIideDFELTERECIK--YMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtKIKLIDFGLA-----RRL 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  169 NNEehnelrevdGTAKKNGGTLYYMAPEHlndVNAKPTE-KSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14191 153 ENA---------GSLKVLFGTPEFVAPEV---INYEPIGyATDMWSIGVICYILVSGLSPF 201
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-221 1.76e-13

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: 71.27  E-value: 1.76e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSL----CFHRTQGLMIMK-----TVYKGPNCIEHNEAlleEAKMMNRLRHSR-VVKLLGVIIEEGKYSLVM 92
Cdd:cd05583   2 LGTGAYGKVFLvrkvGGHDAGKLYAMKvlkkaTIVQKAKTAEHTMT---ERQVLEAVRQSPfLVTLHYAFQTDAKLHLIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLM-HVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSK--LN 169
Cdd:cd05583  79 DYVNGGELFtHLYQREHFTESEVR-IYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGL------SKefLP 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  170 NEEHNelrevdgtAKKNGGTLYYMAPEHLNDvnakpteKSDVYSFAVVLWAI 221
Cdd:cd05583 152 GENDR--------AYSFCGTIEYMAPEVVRG-------GSDGHDKAVDWWSL 188
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
23-193 1.83e-13

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: 70.95  E-value: 1.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFH-RTQGLMIMKtvykgpncIEHNEA----LLEEAKMMNRLRHSR-VVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd14016   8 IGSGSFGEVYLGIDlKTGEEVAIK--------IEKKDSkhpqLEYEAKVYKLLQGGPgIPRLYWFGQEGDYNVMVMDLLG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KgNLMHVLKaEMSTPLSVK-----GRIILEIIEgmcYLHGKGVIHKDLKPENILVDNDFHIK---IADLGLAsfKMWSKL 168
Cdd:cd14016  80 P-SLEDLFN-KCGRKFSLKtvlmlADQMISRLE---YLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLA--KKYRDP 152
                       170       180
                ....*....|....*....|....*.
gi 3426027  169 NNEEHNELREvdgtaKKNG-GTLYYM 193
Cdd:cd14016 153 RTGKHIPYRE-----GKSLtGTARYA 173
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
23-276 2.04e-13

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: 70.99  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKV-SLCFHRTQG-LMIMKTVYK-----GPNCIEHNEA---LLEEAKMM-NRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd08528   8 LGSGAFGCVyKVRKKSNGQtLLALKEINMtnpafGRTEQERDKSvgdIISEVNIIkEQLRHPNIVRYYKTFLENDRLYIV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEK---GNLMHVLKAE-MSTPLSVKGRIILEIIEGMCYLHG-KGVIHKDLKPENILVDNDFHIKIADLGLASFKMWs 166
Cdd:cd08528  88 MELIEGaplGEHFSSLKEKnEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQKGP- 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 klnneEHNELREVdgtakknGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSGnr 246
Cdd:cd08528 167 -----ESSKMTSV-------VGTILYSCPEIVQ--NEPYGEKADIWALGCILYQMCTLQPPFY-STNMLTLATKIVEA-- 229
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 3426027  247 pdvdditEYCP-------REIISLMKLCWEANPEARP 276
Cdd:cd08528 230 -------EYEPlpegmysDDITFVIRSCLTPDPEARP 259
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
16-251 2.15e-13

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: 70.98  E-value: 2.15e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAE-LDSGGFGKVSLCFHRTQGL-----MIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd14105   5 DFYDIGEeLGSGQFAVVKKCREKSTGLeyaakFIKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVL--KAEMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENI-LVDNDF---HIKIADLGLASfk 163
Cdd:cd14105  85 LILELVAGGELFDFLaeKESLSEEEATE--FLKQILDGVNYLHTKNIAHFDLKPENImLLDKNVpipRIKLIDFGLAH-- 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  164 mwsklNNEEHNELREVDGTAKknggtlyYMAPEhlnDVNAKPTE-KSDVYSFAVVLWAIFANKEPYENAIcEQQLIMCIK 242
Cdd:cd14105 161 -----KIEDGNEFKNIFGTPE-------FVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPFLGDT-KQETLANIT 224

                ....*....
gi 3426027  243 SGNRpDVDD 251
Cdd:cd14105 225 AVNY-DFDD 232
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
59-243 2.23e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.22  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    59 ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMeKGNLMHVLKAEMsTPLSVK--GRIILEIIEGMCYLHGKGVIH 136
Cdd:PHA03209 103 TTLIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHY-SSDLYTYLTKRS-RPLPIDqaLIIEKQILEGLRYLHAQRIIH 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   137 KDLKPENILVDNDFHIKIADLGLASFkmwsklNNEEHNELrevdGTAkkngGTLYYMAPEHLndVNAKPTEKSDVYSFAV 216
Cdd:PHA03209 181 RDVKTENIFINDVDQVCIGDLGAAQF------PVVAPAFL----GLA----GTVETNAPEVL--ARDKYNSKADIWSAGI 244
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 3426027   217 VLWAIFA---------NKEPYENAI-CEQQLIMCIKS 243
Cdd:PHA03209 245 VLFEMLAypstifedpPSTPEEYVKsCHSHLLKIIST 281
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
16-277 2.42e-13

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: 70.84  E-value: 2.42e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06645  12 DFELIQRIGSGTYGDVYKARNVNTGeLAAIKVIKLEPG--EDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEF 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLkaEMSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnnee 172
Cdd:cd06645  90 CGGGSLQDIY--HVTGPLSESqiAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSA----------- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hnELREVDGTAKKNGGTLYYMAPEhlndvnAKPTEKSDVYSFAVVLWAI------FANKEP--YENAICEQQLIMCIKSG 244
Cdd:cd06645 157 --QITATIAKRKSFIGTPYWMAPE------VAAVERKGGYNQLCDIWAVgitaieLAELQPpmFDLHPMRALFLMTKSNF 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  245 NRPDVDDITEYCpREIISLMKLCWEANPEARPT 277
Cdd:cd06645 229 QPPKLKDKMKWS-NSFHHFVKMALTKNPKKRPT 260
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
62-229 2.94e-13

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: 70.27  E-value: 2.94e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIIL-EIIEGMCYLHGKGVIHKDLK 140
Cdd:cd14186  50 NEVEIHCQLKHPSILELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRKKPFTEDEARHFMhQIVTGMLYLHSHGILHRDLT 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  141 PENILVDNDFHIKIADLGLASfkmWSKLNNEEHNELrevdgtakknGGTLYYMAPEhLNDVNAKPTEkSDVYSFAVVLWA 220
Cdd:cd14186 130 LSNLLLTRNMNIKIADFGLAT---QLKMPHEKHFTM----------CGTPNYISPE-IATRSAHGLE-SDVWSLGCMFYT 194

                ....*....
gi 3426027  221 IFANKEPYE 229
Cdd:cd14186 195 LLVGRPPFD 203
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
16-169 3.29e-13

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: 71.45  E-value: 3.29e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHN--EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd05610   5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNmvHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVME 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027   94 YMEKGNLMHVLK--AEMSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLN 169
Cdd:cd05610  85 YLIGGDVKSLLHiyGYFDEEMAVK--YISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRELN 160
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
26-225 3.45e-13

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: 71.18  E-value: 3.45e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLmimKTVYKGPNCIEHN---EALLEEAKMMNRLRHSRVVKLLGVI----IEEGK--YsLVMEYME 96
Cdd:cd07849  16 GAYGMVCSAVHKPTGQ---KVAIKKISPFEHQtycLRTLREIKILLRFKHENIIGILDIQrpptFESFKdvY-IVQELME 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KgNLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwSKLNNEEHNel 176
Cdd:cd07849  92 T-DLYKLIKTQHLSNDHIQ-YFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAR----IADPEHDHT-- 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  177 revdGTAKKNGGTLYYMAPEHLndVNAKPTEKS-DVYSFAVVLWAIFANK 225
Cdd:cd07849 164 ----GFLTEYVATRWYRAPEIM--LNSKGYTKAiDIWSVGCILAEMLSNR 207
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
15-277 3.51e-13

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: 70.00  E-value: 3.51e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVME 93
Cdd:cd14113   7 SFYSEVAELGRGRFSVVKKCDQRgTKRAVATKFVNKK---LMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLM-HVLKAEMSTplsvKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFH---IKIADLGLAsfkmwS 166
Cdd:cd14113  84 MADQGRLLdYVVRWGNLT----EEKIRFylrEILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDA-----V 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 KLNNEEHneLREVDGTAKknggtlyYMAPEHL--NDVNAkpteKSDVYSFAVVLWAIFANKEPY-ENAICEQQLIMCIKS 243
Cdd:cd14113 155 QLNTTYY--IHQLLGSPE-------FAAPEIIlgNPVSL----TSDLWSIGVLTYVLLSGVSPFlDESVEETCLNICRLD 221
                       250       260       270
                ....*....|....*....|....*....|....
gi 3426027  244 GNRPdvDDITEYCPREIISLMKLCWEANPEARPT 277
Cdd:cd14113 222 FSFP--DDYFKGVSQKAKDFVCFLLQMDPAKRPS 253
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
25-249 4.71e-13

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: 70.85  E-value: 4.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFH-RTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVI-----IEEGKYSLVMEYMEKG 98
Cdd:cd07878  25 SGAYGSVCSAYDtRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFtpatsIENFNEVYLVTNLMGA 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelRE 178
Cdd:cd07878 105 DLNNIVKCQKLSDEHVQ-FLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLA----------------RQ 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  179 VDGTAKKNGGTLYYMAPE-HLNDVNAKPTekSDVYSFAVVLWAIFANKE--PYENAICEQQLIMCIKSGNRPDV 249
Cdd:cd07878 168 ADDEMTGYVATRWYRAPEiMLNWMHYNQT--VDIWSVGCIMAELLKGKAlfPGNDYIDQLKRIMEVVGTPSPEV 239
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
10-289 5.08e-13

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: 71.19  E-value: 5.08e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   10 IKMKSSDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALL-EEAKMMNRLRHSRVVKLLGVIIEEGK 87
Cdd:cd05622  68 LRMKAEDYEVVKVIGRGAFGEVQLVRHKsTRKVYAMKLLSKFEMIKRSDSAFFwEERDIMAFANSPWVVQLFYAFQDDRY 147
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSK 167
Cdd:cd05622 148 LYMVMEYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTC-----MK 221
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  168 LNNEEHNELREVDGTAKknggtlyYMAPEHLNDVNAKP--TEKSDVYSFAVVLWAIFANKEPY--ENAICEQQLIMCIKS 243
Cdd:cd05622 222 MNKEGMVRCDTAVGTPD-------YISPEVLKSQGGDGyyGRECDWWSVGVFLYEMLVGDTPFyaDSLVGTYSKIMNHKN 294
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3426027  244 G-NRPDVDDITEYCPREIISLMklcweANPEARPTFPGIEE-KFRPFY 289
Cdd:cd05622 295 SlTFPDDNDISKEAKNLICAFL-----TDREVRLGRNGVEEiKRHLFF 337
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
26-221 5.25e-13

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: 70.09  E-value: 5.25e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG--LMIMKTVYKGPNCIEHNEALlEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKgNLMHV 103
Cdd:cd07847  12 GSYGVVFKCRNRETGqiVAIKKFVESEDDPVIKKIAL-REIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEYCDH-TVLNE 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMS--TPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNNEEHNELREVdg 181
Cdd:cd07847  90 LEKNPRgvPEHLIK-KIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARI-----LTGPGDDYTDYV-- 161
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3426027  182 takkngGTLYYMAPEHL-NDVnakpteksdVYSFAVVLWAI 221
Cdd:cd07847 162 ------ATRWYRAPELLvGDT---------QYGPPVDVWAI 187
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
23-277 5.71e-13

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: 69.60  E-value: 5.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQG----LMIMKtvykgpNCIEHNEALLEEAKMMNRLR------HSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14133   7 LGKGTFGQVVKCYDLLTGeevaLKIIK------NNKDYLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLCIVF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKgNLMHVLKAEMSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDN--DFHIKIADLGLASFkmwskL 168
Cdd:cd14133  81 ELLSQ-NLYEFLKQNKFQYLSLPriRKIAQQILEALVFLHSLGLIHCDLKPENILLASysRCQIKIIDFGSSCF-----L 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 NNEEHNELRevdgtakknggTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPYENAiCEQQLIMCIKS--GNR 246
Cdd:cd14133 155 TQRLYSYIQ-----------SRYYRAPEVI--LGLPYDEKIDMWSLGCILAELYTGEPLFPGA-SEVDQLARIIGtiGIP 220
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 3426027  247 PD-------VDDiteycpREIISLMKLCWEANPEARPT 277
Cdd:cd14133 221 PAhmldqgkADD------ELFVDFLKKLLEIDPKERPT 252
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
23-241 6.26e-13

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: 70.32  E-value: 6.26e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHN--EALLEEAKMMNRLR-HSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd05590   3 LGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDdvECTMTEKRILSLARnHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LM-HVLKAEMSTplSVKGRII-LEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehNELR 177
Cdd:cd05590  83 LMfHIQKSRRFD--EARARFYaAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK------------EGIF 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  178 EVDGTAkKNGGTLYYMAPEHLNDVNAKPTekSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCI 241
Cdd:cd05590 149 NGKTTS-TFCGTPDYIAPEILQEMLYGPS--VDWWAMGVLLYEMLCGHAPFE-AENEDDLFEAI 208
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
63-275 6.64e-13

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: 69.43  E-value: 6.64e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSR---VVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEmstPLSVK--GRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06917  49 EVALLSQLKLGQpknIIKYYGSYLKGPSLWIIMDYCEGGSIRTLMRAG---PIAERyiAVIMREVLVALKFIHKDGIIHR 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTeKSDVYSFAVV 217
Cdd:cd06917 126 DIKAANILVTNTGNVKLCDFGVAA-------------SLNQNSSKRSTFVGTPYWMAPEVITEGKYYDT-KADIWSLGIT 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  218 LWAIFANKEPYenaiCEQ---QLIMCIKSGNRPDVDDiTEYCP--REIISlmkLCWEANPEAR 275
Cdd:cd06917 192 TYEMATGNPPY----SDVdalRAVMLIPKSKPPRLEG-NGYSPllKEFVA---ACLDEEPKDR 246
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
23-228 7.13e-13

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: 69.56  E-value: 7.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIiEEGKYS------LVMEYME 96
Cdd:cd14039   1 LGTGGFGNVCLYQNQETGEKIAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVP-EEMNFLvndvplLAMEYCS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVL-KAEMSTPL--SVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDND----FHiKIADLGLAsfkmwskln 169
Cdd:cd14039  80 GGDLRKLLnKPENCCGLkeSQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEIngkiVH-KIIDLGYA--------- 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  170 neehnelREVDGTAKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14039 150 -------KDLDQGSLCTSfvGTLQYLAPELFE--NKSYTVTVDYWSFGTMVFECIAGFRPF 201
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
16-231 7.71e-13

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: 69.12  E-value: 7.71e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKG---PNCIEHNeaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14117   7 DFDIGRPLGKGKFGNVYLAREKqSKFIVALKVLFKSqieKEGVEHQ--LRREIEIQSHLRHPNILRLYNYFHDRKRIYLI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmWSKlnne 171
Cdd:cd14117  85 LEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFG------WSV---- 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  172 EHNELREvdgtaKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYENA 231
Cdd:cd14117 155 HAPSLRR-----RTMCGTLDYLPPEMIE--GRTHDEKVDLWCIGVLCYELLVGMPPFESA 207
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
46-163 8.44e-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: 69.33  E-value: 8.44e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   46 TVYKGPNCI------------EHNEAL----LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK---------GNL 100
Cdd:cd07844  15 TVYKGRSKLtgqlvalkeirlEHEEGApftaIREASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDTdlkqymddcGGG 94
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  101 MHvlkaemstPLSVkgRIIL-EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFK 163
Cdd:cd07844  95 LS--------MHNV--RLFLfQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAK 148
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
17-277 8.75e-13

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: 69.31  E-value: 8.75e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCF-HRTQGLMIMKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd06640   6 FTKLERIGKGSFGEVFKGIdNRTQQVVAIKII-DLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehne 175
Cdd:cd06640  85 GGGSALDLLRAGPFDEFQI-ATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAG-------------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  176 lREVDGTAKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVlwAI-FANKEPYENAICEQQLIMCIKSGNRPD-VDD 251
Cdd:cd06640 150 -QLTDTQIKRNTfvGTPFWMAPEVIQ--QSAYDSKADIWSLGIT--AIeLAKGEPPNSDMHPMRVLFLIPKNNPPTlVGD 224
                       250       260
                ....*....|....*....|....*.
gi 3426027  252 ITeycpREIISLMKLCWEANPEARPT 277
Cdd:cd06640 225 FS----KPFKEFIDACLNKDPSFRPT 246
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
22-231 9.82e-13

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: 69.20  E-value: 9.82e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQGL-----MIMKTVYkgpNCIEHNEALLEEAkmmnrlRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd14091   7 EIGKGSYSVCKRCIHKATGKeyavkIIDKSKR---DPSEEIEILLRYG------QHPNIITLRDVYDDGNSVYLVTELLR 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH----IKIADLGLAsfkmwsklnnee 172
Cdd:cd14091  78 GGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICDFGFA------------ 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  173 hNELREVDG-------TAKknggtlyYMAPEHLN----DVNAkpteksDVYSFAVVLWAIFANKEPYENA 231
Cdd:cd14091 146 -KQLRAENGllmtpcyTAN-------FVAPEVLKkqgyDAAC------DIWSLGVLLYTMLAGYTPFASG 201
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
3-230 1.03e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 68.73  E-value: 1.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     3 PDMSLNVIkmksSDFLESAE------LDSGGFGKVSLCFHR-TQGLMIMKTV-YKGPNCIEHNEALLeeakMMNrlrHSR 74
Cdd:PHA03390   2 MDKSLSEL----VQFLKNCEivkklkLIDGKFGKVSVLKHKpTQKLFVQKIIkAKNFNAIEPMVHQL----MKD---NPN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    75 VVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAE--MSTPLSVKgrIILEIIEGMCYLHGKGVIHKDLKPENILVD-NDFH 151
Cdd:PHA03390  71 FIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEgkLSEAEVKK--IIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDR 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027   152 IKIADLGLAsfkmwsklnneehnelrEVDGTAKKNGGTLYYMAPEHLNDVNAkpTEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:PHA03390 149 IYLCDYGLC-----------------KIIGTPSCYDGTLDYFSPEKIKGHNY--DVSFDWWAVGVLTYELLTGKHPFKE 208
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
23-281 1.18e-12

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: 68.50  E-value: 1.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKvslCFHRTQglMIMKTVYKGpNCIEHN--------EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd14188   9 LGKGGFAK---CYEMTD--LTTNKVYAA-KIIPHSrvskphqrEKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 MEKGNLMHVLKA-EMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEH 173
Cdd:cd14188  83 CSRRSMAHILKArKVLTEPEVR-YYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLA-----ARLEPLEH 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 NElrevdgtaKKNGGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFANKEPYENAICEQQLiMCIKSGNRPDVDDIT 253
Cdd:cd14188 157 RR--------RTICGTPNYLSPEVLNKQGHGC--ESDIWALGCVMYTMLLGRPPFETTNLKETY-RCIREARYSLPSSLL 225
                       250       260
                ....*....|....*....|....*...
gi 3426027  254 EYCPREIISLMklcwEANPEARPTFPGI 281
Cdd:cd14188 226 APAKHLIASML----SKNPEDRPSLDEI 249
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
23-264 1.22e-12

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: 68.59  E-value: 1.22e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM 101
Cdd:cd14074  11 LGRGHFAVVKLARHVFTGEKVaVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILELGDGGDMY 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 -HVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV-DNDFHIKIADLGLA-SFKMWSKLNNeehnelre 178
Cdd:cd14074  91 dYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSnKFQPGEKLET-------- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdgtakkNGGTLYYMAPE-HLNDVNAKPteKSDVYSFAVVLWAIFANKEPYENAICEQQLIMcIKSGNRPDVDDITEYCp 257
Cdd:cd14074 163 -------SCGSLAYSAPEiLLGDEYDAP--AVDIWSLGVILYMLVCGQPPFQEANDSETLTM-IMDCKYTVPAHVSPEC- 231

                ....*..
gi 3426027  258 REIISLM 264
Cdd:cd14074 232 KDLIRRM 238
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-228 1.24e-12

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: 68.87  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCF----HRTQGLMIMK-----TVYKGPNCIEHNEAlleEAKMMNRLRHSR-VVKLLGVIIEEGKYSLVM 92
Cdd:cd05613   8 LGTGAYGKVFLVRkvsgHDAGKLYAMKvlkkaTIVQKAKTAEHTRT---ERQVLEHIRQSPfLVTLHYAFQTDTKLHLIL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLM-HVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLNNE 171
Cdd:cd05613  85 DYINGGELFtHLSQRERFTENEVQ-IYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGL------SKEFLL 157
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  172 EHNElrevdgTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05613 158 DENE------RAYSFCGTIEYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPF 208
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
62-277 1.25e-12

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: 68.52  E-value: 1.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkaEMSTPLS--VKGRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd06646  55 QEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIY--HVTGPLSelQIAYVCRETLQGLAYLHSKGKMHRDI 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  140 KPENILVDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEhlndvnAKPTEKSDVYSFAVVLW 219
Cdd:cd06646 133 KGANILLTDNGDVKLADFGVAA-------------KITATIAKRKSFIGTPYWMAPE------VAAVEKNGGYNQLCDIW 193
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  220 AI------FANKEP--YENAICEQQLIMCIKSGNRPDVDDITEYCPrEIISLMKLCWEANPEARPT 277
Cdd:cd06646 194 AVgitaieLAELQPpmFDLHPMRALFLMSKSNFQPPKLKDKTKWSS-TFHNFVKISLTKNPKKRPT 258
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
61-225 1.48e-12

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: 69.06  E-value: 1.48e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVII----------EEGKYSLVMEYMEKgNLMHVLKAEMS--TPLSVKGrIILEIIEGMCY 128
Cdd:cd07864  54 IREIKILRQLNHRSVVNLKEIVTdkqdaldfkkDKGAFYLVFEYMDH-DLMGLLESGLVhfSEDHIKS-FMKQLLEGLNY 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  129 LHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMWSKlnneehNELREVDGTAKknggTLYYMAPEHLNDvNAKPTEK 208
Cdd:cd07864 132 CHKKNFLHRDIKCSNILLNNKGQIKLADFGLA--RLYNS------EESRPYTNKVI----TLWYRPPELLLG-EERYGPA 198
                       170
                ....*....|....*..
gi 3426027  209 SDVYSFAVVLWAIFANK 225
Cdd:cd07864 199 IDVWSCGCILGELFTKK 215
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
17-277 1.63e-12

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: 68.56  E-value: 1.63e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCF-HRTQGLMIMKTVyKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd06641   6 FTKLEKIGKGSFGEVFKGIdNRTQKVVAIKII-DLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAemsTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneeh 173
Cdd:cd06641  85 GGGSALDLLEP---GPLDETqiATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAG------------ 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  174 nelREVDGTAKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIfANKEPYENAICEQQLIMCIKSGNRPDVDD 251
Cdd:cd06641 150 ---QLTDTQIKRN*fvGTPFWMAPEVIK--QSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLIPKNNPPTLEG 223
                       250       260
                ....*....|....*....|....*.
gi 3426027  252 ITEYCPREIIslmKLCWEANPEARPT 277
Cdd:cd06641 224 NYSKPLKEFV---EACLNKEPSFRPT 246
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
61-238 1.69e-12

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: 68.71  E-value: 1.69e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHS-RVVKLLGV--IIEEGK--YSLVMEYMEKG--NLMHVLKAEMSTPLSVK--GRIILEIIEGMCYLHG 131
Cdd:cd07837  48 LREVSLLQMLSQSiYIVRLLDVehVEENGKplLYLVFEYLDTDlkKFIDSYGRGPHNPLPAKtiQSFMYQLCKGVAHCHS 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  132 KGVIHKDLKPENILVDNDFHI-KIADLGLA-SFKMWSKLNNEEHNelrevdgtakknggTLYYMAPEHLndvnakptEKS 209
Cdd:cd07837 128 HGVMHRDLKPQNLLVDKQKGLlKIADLGLGrAFTIPIKSYTHEIV--------------TLWYRAPEVL--------LGS 185
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 3426027  210 DVYSFAVVLWA---IFAN---KEPYENAICE-QQLI 238
Cdd:cd07837 186 THYSTPVDMWSvgcIFAEmsrKQPLFPGDSElQQLL 221
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
26-277 1.71e-12

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: 68.11  E-value: 1.71e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVykgPncIEHNEAllEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHvl 104
Cdd:cd13995  15 GAFGKVYLAQDTkTKKRMACKLI---P--VEQFKP--SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLE-- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  105 KAEMSTPLSvKGRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIkIADLGLaSFKMWSKLNNEEhnELRevdg 181
Cdd:cd13995  86 KLESCGPMR-EFEIIWvtkHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGL-SVQMTEDVYVPK--DLR---- 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 takkngGTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQL--IMCIKSGNRPDVDDITEYCPRE 259
Cdd:cd13995 157 ------GTEIYMSPEVI--LCRGHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYpsYLYIIHKQAPPLEDIAQDCSPA 228
                       250
                ....*....|....*...
gi 3426027  260 IISLMKLCWEANPEARPT 277
Cdd:cd13995 229 MRELLEAALERNPNHRSS 246
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
61-277 2.11e-12

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: 67.84  E-value: 2.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRI--ILEIIEGMCYLHGKGVIHKD 138
Cdd:cd08221  47 LNEIDILSLLNHDNIITYYNHFLDGESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLwyLYQIVSAVSHIHKAGILHRD 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  139 LKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHnelrevdgTAKKNGGTLYYMAPEHLNDVnaKPTEKSDVYSFAVVL 218
Cdd:cd08221 127 IKTLNIFLTKADLVKLGDFGIS-----KVLDSESS--------MAESIVGTPYYMSPELVQGV--KYNFKSDIWAVGCVL 191
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  219 WAIFANKEPYeNAICEQQLIMCIKSGNRPDVDDITEycpREIISLMKLCWEANPEARPT 277
Cdd:cd08221 192 YELLTLKRTF-DATNPLRLAVKIVQGEYEDIDEQYS---EEIIQLVHDCLHQDPEDRPT 246
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
23-158 2.18e-12

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 64.77  E-value: 2.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFH--RTQGLM--IMKTVYKGPNciehnEALLEEAKMMNRLRHSR--VVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd13968   1 MGEGASAKVFWAEGecTTIGVAvkIGDDVNNEEG-----EDLESEMDILRRLKGLElnIPKVLVTEDVDGPNILLMELVK 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027   97 KGNLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLG 158
Cdd:cd13968  76 GGTLIAYTQEEELDEKDVE-SIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
26-228 2.53e-12

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: 68.46  E-value: 2.53e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG------LMIMKTVYKGPnciEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd05603   6 GSFGKVLLAKRKCDGkfyavkVLQKKTILKKK---EQNHIMAERNVLLKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEMSTpLSVKGRI-ILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneehnelrE 178
Cdd:cd05603  83 LFFHLQRERCF-LEPRARFyAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGM-------------E 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 3426027  179 VDGTAKKNGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPY 228
Cdd:cd05603 149 PEETTSTFCGTPEYLAPEVLRK---EPYDRTvDWWCLGAVLYEMLYGLPPF 196
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
15-291 2.59e-12

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: 68.92  E-value: 2.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVslCFHR---TQGLMIMKTVYKGP----NCIEHNEAlleEAKMMNRLRHSRVVKLLGVIIEEGK 87
Cdd:cd05625   1 SMFVKIKTLGIGAFGEV--CLARkvdTKALYATKTLRKKDvllrNQVAHVKA---ERDILAEADNEWVVRLYYSFQDKDN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWS- 166
Cdd:cd05625  76 LYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTh 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  167 ----------------KLNNEE--------HNELREVDGTAKKNG---------GTLYYMAPEHLndVNAKPTEKSDVYS 213
Cdd:cd05625 156 dskyyqsgdhlrqdsmDFSNEWgdpencrcGDRLKPLERRAARQHqrclahslvGTPNYIAPEVL--LRTGYTQLCDWWS 233
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  214 FAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIISLMKLCweANPEARPTFPGIEE-KFRPFYLS 291
Cdd:cd05625 234 VGVILFEMLVGQPPFLAQTPLETQMKVINWQTSLHIPPQAKLSPEASDLIIKLC--RGPEDRLGKNGADEiKAHPFFKT 310
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
26-198 2.98e-12

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: 68.16  E-value: 2.98e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVykgpncIEHNE------ALLEEAKMMNRLRHSRVVKLLGVIIEE--------GKYSL 90
Cdd:cd07865  23 GTFGEVFKARHRkTGQIVALKKV------LMENEkegfpiTALREIKILQLLKHENVVNLIEICRTKatpynrykGSIYL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEkgnlmHVLKAEMSTP-----LSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMW 165
Cdd:cd07865  97 VFEFCE-----HDLAGLLSNKnvkftLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLA--RAF 169
                       170       180       190
                ....*....|....*....|....*....|....*
gi 3426027  166 SKLNNEEHNEL--REVdgtakknggTLYYMAPEHL 198
Cdd:cd07865 170 SLAKNSQPNRYtnRVV---------TLWYRPPELL 195
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
23-219 3.21e-12

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: 67.05  E-value: 3.21e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMeKGNLM 101
Cdd:cd14082  11 LGSGQFGIVYGGKHRKTGRDVaIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKL-HGDML 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  102 HVLKAemstplSVKGRI--------ILEIIEGMCYLHGKGVIHKDLKPENILV--DNDF-HIKIADLGLASFKmwsklnn 170
Cdd:cd14082  90 EMILS------SEKGRLperitkflVTQILVALRYLHSKNIVHCDLKPENVLLasAEPFpQVKLCDFGFARII------- 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 EEHNELREVDGTAKknggtlyYMAPEHLNDvnaKPTEKS-DVYSFAVVLW 219
Cdd:cd14082 157 GEKSFRRSVVGTPA-------YLAPEVLRN---KGYNRSlDMWSVGVIIY 196
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
16-228 3.47e-12

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: 67.34  E-value: 3.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLE-SAELDSGGFGKVSLCFHRTQGL-----MIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS 89
Cdd:cd14195   5 DHYEmGEELGSGQFAIVRKCREKGTGKeyaakFIKKRRLSSSRRGVSREEIEREVNILREIQHPNIITLHDIFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENI-LVDNDF---HIKIADLGLASfkmw 165
Cdd:cd14195  85 LILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENImLLDKNVpnpRIKLIDFGIAH---- 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  166 sklNNEEHNELREVDGTAKknggtlyYMAPEhlnDVNAKPTE-KSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14195 161 ---KIEAGNEFKNIFGTPE-------FVAPE---IVNYEPLGlEADMWSIGVITYILLSGASPF 211
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
55-216 3.76e-12

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: 67.33  E-value: 3.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRL-RHSRVVKLLGVII------EEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVK----GRIILEII 123
Cdd:cd06608  44 DEEEEIKLEINILRKFsNHPNIATFYGAFIkkdppgGDDQLWLVMEYCGGGSVTDLVKGLRKKGKRLKeewiAYILRETL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  124 EGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNG---GTLYYMAPEHLN- 199
Cdd:cd06608 124 RGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVS----------------AQLDSTLGRRNtfiGTPYWMAPEVIAc 187
                       170
                ....*....|....*....
gi 3426027  200 DVNAKPT--EKSDVYSFAV 216
Cdd:cd06608 188 DQQPDASydARCDVWSLGI 206
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
17-230 3.99e-12

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: 67.77  E-value: 3.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLC--FHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06635  27 FSDLREIGHGSFGAVYFArdVRTSEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEY 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 M--EKGNLMHVLKAEMSTpLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnnee 172
Cdd:cd06635 107 ClgSASDLLEVHKKPLQE-IEIAA-ITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSAS----------- 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  173 hnelreVDGTAKKNGGTLYYMAPEHLNDVNAKPTE-KSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd06635 174 ------IASPANSFVGTPYWMAPEVILAMDEGQYDgKVDVWSLGITCIELAERKPPLFN 226
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
58-160 6.70e-12

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


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 67.22  E-value: 6.70e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHS--------RVVKLLG---VIIEEGKY-SLVMEYMekG-NLMHVLK--AEMSTPLSVKGRIILEI 122
Cdd:cd14136  51 EAALDEIKLLKCVREAdpkdpgreHVVQLLDdfkHTGPNGTHvCMVFEVL--GpNLLKLIKryNYRGIPLPLVKKIARQV 128
                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLHGK-GVIHKDLKPENILVD-NDFHIKIADLGLA 160
Cdd:cd14136 129 LQGLDYLHTKcGIIHTDIKPENVLLCiSKIEVKIADLGNA 168
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
58-299 7.18e-12

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: 66.80  E-value: 7.18e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH--VLKAEMSTPLS--VKGRIILEIIEGMCYLHGKG 133
Cdd:cd14094  50 EDLKREASICHMLKHPHIVELLETYSSDGMLYMVFEFMDGADLCFeiVKRADAGFVYSeaVASHYMRQILEALRYCHDNN 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENIL---VDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEhlnDVNAKPTEKS- 209
Cdd:cd14094 130 IIHRDVKPHCVLlasKENSAPVKLGGFGVAI-------------QLGESGLVAGGRVGTPHFMAPE---VVKREPYGKPv 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  210 DVYSFAVVLWAIFANKEPYENAICE-QQLIMCIK-SGNRPDVDDITEYCpREIISLMklcWEANPEARPTF------PGI 281
Cdd:cd14094 194 DVWGCGVILFILLSGCLPFYGTKERlFEGIIKGKyKMNPRQWSHISESA-KDLVRRM---LMLDPAERITVyealnhPWI 269
                       250
                ....*....|....*...
gi 3426027  282 EEKFRPFYLSQLEESVEE 299
Cdd:cd14094 270 KERDRYAYRIHLPETVEQ 287
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
17-230 7.54e-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: 66.97  E-value: 7.54e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLC--FHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEY 94
Cdd:cd06634  17 FSDLREIGHGSFGAVYFArdVRNNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   95 M--EKGNLMHVLKA---EMSTPLSVKGriileIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskln 169
Cdd:cd06634  97 ClgSASDLLEVHKKplqEVEIAAITHG-----ALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSAS-------- 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  170 neehnelreVDGTAKKNGGTLYYMAPEHLNDVNAKPTE-KSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd06634 164 ---------IMAPANSFVGTPYWMAPEVILAMDEGQYDgKVDVWSLGITCIELAERKPPLFN 216
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
58-230 7.91e-12

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: 66.10  E-value: 7.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06647  49 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHR 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVdgtakkngGTLYYMAPEHLNDVNAKPteKSDVYSFAVV 217
Cdd:cd06647 128 DIKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV--------GTPYWMAPEVVTRKAYGP--KVDIWSLGIM 192
                       170
                ....*....|...
gi 3426027  218 LWAIFANKEPYEN 230
Cdd:cd06647 193 AIEMVEGEPPYLN 205
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
23-228 8.79e-12

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: 66.52  E-value: 8.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEYME 96
Cdd:cd14038   2 LGTGGFGNVLRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEGLQKLApndlplLAMEYCQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVL-KAEMSTPLSVKGRIIL--EIIEGMCYLHGKGVIHKDLKPENILVDND----FHiKIADLGLAsfkmwskln 169
Cdd:cd14038  82 GGDLRKYLnQFENCCGLREGAILTLlsDISSALRYLHENRIIHRDLKPENIVLQQGeqrlIH-KIIDLGYA--------- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  170 neehnelREVDGTAKKNG--GTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14038 152 -------KELDQGSLCTSfvGTLQYLAPELLE--QQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
21-225 1.10e-11

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: 66.14  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFHRTQGLMI-MKTVYkgpncIEHNE-----ALLEEAKMMNRLR---HSRVVKLLGVII-----EEG 86
Cdd:cd07863   6 AEIGVGAYGTVYKARDPHSGHFVaLKSVR-----VQTNEdglplSTVREVALLKRLEafdHPNIVRLMDVCAtsrtdRET 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   87 KYSLVMEYMEKGNLMHVLKAEM-STPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKMW 165
Cdd:cd07863  81 KVTLVFEHVDQDLRTYLDKVPPpGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLA--RIY 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  166 SKlnneeHNELREVdgtakknGGTLYYMAPE-HLNDVNAKPTeksDVYSFAVVLWAIFANK 225
Cdd:cd07863 159 SC-----QMALTPV-------VVTLWYRAPEvLLQSTYATPV---DMWSVGCIFAEMFRRK 204
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
22-277 1.16e-11

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


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 65.66  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSL--CFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd05086   4 EIGNGWFGKVLLgeIYTGTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGD 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVLKAEM-----STPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnNEEHN 174
Cdd:cd05086  84 LKTYLANQQeklrgDSQIMLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRY-----KEDYI 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 ElrevdgTAKKNGGTLYYMAPEHLND-----VNAKPTEKSDVYSFAVVLWAIFAN-KEPYENAICEQQLIMCIKSGN--- 245
Cdd:cd05086 159 E------TDDKKYAPLRWTAPELVTSfqdglLAAEQTKYSNIWSLGVTLWELFENaAQPYSDLSDREVLNHVIKERQvkl 232
                       250       260       270
                ....*....|....*....|....*....|...
gi 3426027  246 -RPDVDdiTEYCPReIISLMKLCWeANPEARPT 277
Cdd:cd05086 233 fKPHLE--QPYSDR-WYEVLQFCW-LSPEKRPT 261
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
4-230 1.16e-11

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: 66.59  E-value: 1.16e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    4 DMSLNVIKMKS----SDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEA--LLEEAKMMNRLRHSRVVK 77
Cdd:cd05594  10 EMEVSLTKPKHkvtmNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVahTLTENRVLQNSRHPFLTA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   78 LLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHG-KGVIHKDLKPENILVDNDFHIKIAD 156
Cdd:cd05594  90 LKYSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITD 169
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  157 LGLAsfkmwsklnneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd05594 170 FGLC-------------KEGIKDGATMKTFCGTPEYLAPEVLEDNDYG--RAVDWWGLGVVMYEMMCGRLPFYN 228
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
21-245 1.31e-11

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 65.65  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFH-RTQGLMIMKTVYKgPNCIEHNEALLE-EAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd14097   7 RKLGQGSFGVVIEATHkETQTKWAIKKINR-EKAGSSAVKLLErEVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDG 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDND-------FHIKIADLGLASFKMWSklnNE 171
Cdd:cd14097  86 ELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSSiidnndkLNIKVTDFGLSVQKYGL---GE 162
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  172 EHnelrevdgtAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKEPYeNAICEQQLIMCIKSGN 245
Cdd:cd14097 163 DM---------LQETCGTPIYMAPEVIS--AHGYSQQCDIWSIGVIMYMLLCGEPPF-VAKSEEKLFEEIRKGD 224
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
15-229 1.32e-11

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: 66.18  E-value: 1.32e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLESAELDSGGFGKVSLCFHRTQG-LMIMKTVYKGPNCIEHNEALLEEAK-MMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd05601   1 KDFEVKNVIGRGHFGEVQVVKEKATGdIYAMKVLKKSETLAQEEVSFFEEERdIMAKANSPWITKLQYAFQDSENLYLVM 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNE 171
Cdd:cd05601  81 EYHPGGDLLSLLsRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSA-----AKLSSD 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  172 EHnelrevdGTAKKNGGTLYYMAPEHLNDVNAKPTE----KSDVYSFAVVLWAIFANKEPYE 229
Cdd:cd05601 156 KT-------VTSKMPVGTPDYIAPEVLTSMNGGSKGtygvECDWWSLGIVAYEMLYGKTPFT 210
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
89-343 1.52e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 67.20  E-value: 1.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    89 SLVMEYMEKGNLMHVLKAEMSTPLSVK----GRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfKM 164
Cdd:PTZ00283 115 ALVLDYANAGDLRQEIKSRAKTNRTFReheaGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFS--KM 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   165 WSKLNNeehnelrevDGTAKKNGGTLYYMAPEHLndvNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKS 243
Cdd:PTZ00283 193 YAATVS---------DDVGRTFCGTPYYVAPEIW---RRKPySKKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAG 260
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   244 GNRPDVDDITEYCpREIISLMkLCWEanPEARPT-------------FPGIEE--KFRPFYLSQLEESVEEDVKSLKKEY 308
Cdd:PTZ00283 261 RYDPLPPSISPEM-QEIVTAL-LSSD--PKRRPSsskllnmpicklfISGLLEivQTQPGFSGPLRDTISRQIQQTKQLL 336
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 3426027   309 SNEN-AVVKRMQSLQLDCVAVPSSRSNSATEQPGSL 343
Cdd:PTZ00283 337 QVERrRIVRQMEESLSTAASTTILEGATPLTTLGGL 372
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
63-228 1.61e-11

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: 65.64  E-value: 1.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLR-HSRVVKLLGVIIEE--GKYSLVMEYMEKGN---LMHVLkaemsTPLSVKgRIILEIIEGMCYLHGKGVIH 136
Cdd:cd14132  62 EIKILQNLRgGPNIVKLLDVVKDPqsKTPSLIFEYVNNTDfktLYPTL-----TDYDIR-YYMYELLKALDYCHSKGIMH 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  137 KDLKPENILVDNDFH-IKIADLGLASFkmwsKLNNEEHNeLReVdgtakkngGTLYYMAPEHLndVNAKPTEKS-DVYSF 214
Cdd:cd14132 136 RDVKPHNIMIDHEKRkLRLIDWGLAEF----YHPGQEYN-VR-V--------ASRYYKGPELL--VDYQYYDYSlDMWSL 199
                       170
                ....*....|....
gi 3426027  215 AVVLWAIFANKEPY 228
Cdd:cd14132 200 GCMLASMIFRKEPF 213
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
17-230 1.73e-11

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: 65.31  E-value: 1.73e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   17 FLESAELDSGGFGKVSLCFHRTQGLM-----IMKTVYKGPNciEHNEALLEEaKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd05607   4 FYEFRVLGKGGFGEVCAVQVKNTGQMyackkLDKKRLKKKS--GEKMALLEK-EILEKVNSPFIVSLAYAFETKTHLCLV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKgRIIL---EIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskl 168
Cdd:cd05607  81 MSLMNGGDLKYHIYNVGERGIEME-RVIFysaQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAV------- 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  169 nneehnELREVDGTAKKnGGTLYYMAPEHLNDVNakpteksdvYSFAVVLWAI-------FANKEPYEN 230
Cdd:cd05607 153 ------EVKEGKPITQR-AGTNGYMAPEILKEES---------YSYPVDWFAMgcsiyemVAGRTPFRD 205
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
11-228 2.09e-11

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 65.77  E-value: 2.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    11 KMKSSDFLESAELDSGGFGKVSLCFHRTQGLM-IMKTVYKGPNCIEHNEA--LLEEAKMMNRLRHSRVVKLLGVIIEEGK 87
Cdd:PTZ00426  26 KMKYEDFNFIRTLGTGSFGRVILATYKNEDFPpVAIKRFEKSKIIKQKQVdhVFSERKILNYINHPFCVNLYGSFKDESY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    88 YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsk 167
Cdd:PTZ00426 106 LYLVLEFVIGGEFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFA------- 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027   168 lnneehnelREVDGTAKKNGGTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:PTZ00426 179 ---------KVVDTRTYTLCGTPEYIAPEIL--LNVGHGKAADWWTLGIFIYEILVGCPPF 228
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
16-228 2.18e-11

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: 65.12  E-value: 2.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGP----NCIEHneaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSL 90
Cdd:cd14209   2 DFDRIKTLGTGSFGRVMLVRHKeTGNYYAMKILDKQKvvklKQVEH---TLNEKRILQAINFPFLVKLEYSFKDNSNLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLK--AEMSTPLS--VKGRIILEIIegmcYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmws 166
Cdd:cd14209  79 VMEYVPGGEMFSHLRriGRFSEPHArfYAAQIVLAFE----YLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFA------ 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  167 klnneehnelREVDGTAKKNGGTLYYMAPEHlndVNAKPTEKS-DVYSFAVVLWAIFANKEPY 228
Cdd:cd14209 149 ----------KRVKGRTWTLCGTPEYLAPEI---ILSKGYNKAvDWWALGVLIYEMAAGYPPF 198
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
26-198 2.51e-11

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: 65.42  E-value: 2.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG-LMIMKTVYKgPNCIEHNEA---LLEEAKMMNRLRHSRVVKLlgviieegKYSL--------VME 93
Cdd:cd05575   6 GSFGKVLLARHKAEGkLYAVKVLQK-KAILKRNEVkhiMAERNVLLKNVKHPFLVGL--------HYSFqtkdklyfVLD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   94 YMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMwsklnneeh 173
Cdd:cd05575  77 YVNGGELFFHLQRERHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEGI--------- 147
                       170       180
                ....*....|....*....|....*
gi 3426027  174 nelrEVDGTAKKNGGTLYYMAPEHL 198
Cdd:cd05575 148 ----EPSDTTSTFCGTPEYLAPEVL 168
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
22-249 2.84e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 67.07  E-value: 2.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     22 ELDSGGFGKVSLCFH-RTQGLMIMKTV-YKGPNCIEHNEaLLEEAKMMNRLRHSRVVKLLGVIIEEG--KYSLVMEYMEK 97
Cdd:PTZ00266   20 KIGNGRFGEVFLVKHkRTQEFFCWKAIsYRGLKEREKSQ-LVIEVNVMRELKHKNIVRYIDRFLNKAnqKLYILMEFCDA 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027     98 GNLMHVLKAEMSTPLSVKGRIILEI----IEGMCYLH-------GKGVIHKDLKPENILVDNDfhikIADLGlasfKMWS 166
Cdd:PTZ00266   99 GDLSRNIQKCYKMFGKIEEHAIVDItrqlLHALAYCHnlkdgpnGERVLHRDLKPQNIFLSTG----IRHIG----KITA 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    167 KLNNEEHNELREVD--GTAKKNG---------GTLYYMAPEHLNDVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQ 235
Cdd:PTZ00266  171 QANNLNGRPIAKIGdfGLSKNIGiesmahscvGTPYYWSPELLLHETKSYDDKSDMWALGCIIYELCSGKTPFHKANNFS 250
                         250
                  ....*....|....
gi 3426027    236 QLIMCIKSGnrPDV 249
Cdd:PTZ00266  251 QLISELKRG--PDL 262
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
38-163 3.14e-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: 65.01  E-value: 3.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   38 TQGLMIMKTVYkgpncIEHNEAL----LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK---------GNLMHVL 104
Cdd:cd07872  30 TENLVALKEIR-----LEHEEGApctaIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYLDKdlkqymddcGNIMSMH 104
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  105 KAEMstplsvkgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFK 163
Cdd:cd07872 105 NVKI---------FLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAK 154
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
58-277 3.38e-11

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: 64.31  E-value: 3.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKaemSTPL--SVKGRIILEIIEGMCYLHGKGVI 135
Cdd:cd06642  47 EDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSALDLLK---PGPLeeTYIATILREILKGLDYLHSERKI 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnelREVDGTAKKNG--GTLYYMAPEHLndvnakpteKSDVYS 213
Cdd:cd06642 124 HRDIKAANVLLSEQGDVKLADFGVAG---------------QLTDTQIKRNTfvGTPFWMAPEVI---------KQSAYD 179
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  214 FAVVLWAI------FANKEPYENAICEQQLIMCIKSGNRPDVDDITEYCPREIIslmKLCWEANPEARPT 277
Cdd:cd06642 180 FKADIWSLgitaieLAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFV---EACLNKDPRFRPT 246
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
26-228 3.52e-11

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: 64.90  E-value: 3.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGpNCIEHNEA--LLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd05585   5 GSFGKVMQVRKKdTSRIYALKTIRKA-HIVSRSEVthTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGELFH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEhnelrevDGT 182
Cdd:cd05585  84 HLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLC------KLNMKD-------DDK 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 3426027  183 AKKNGGTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05585 151 TNTFCGTPEYLAPELL--LGHGYTKAVDWWTLGVLLYEMLTGLPPF 194
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
65-164 3.57e-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: 64.67  E-value: 3.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   65 KMMNRLRHSRVVKLLGVII-----EEGKYSLVMEYMEKGNLMHVLKA-EMSTPLSVKGRIILEIIEGMCYLHGKGVIHKD 138
Cdd:cd07862  56 RHLETFEHPNVVRLFDVCTvsrtdRETKLTLVFEHVDQDLTTYLDKVpEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRD 135
                        90       100
                ....*....|....*....|....*....
gi 3426027  139 LKPENILVDNDFHIKIADLGLA---SFKM 164
Cdd:cd07862 136 LKPQNILVTSSGQIKLADFGLAriySFQM 164
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
55-230 3.70e-11

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: 64.66  E-value: 3.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLHGKGV 134
Cdd:cd06657  59 QRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQI-AAVCLAVLKALSVLHAQGV 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVdgtakkngGTLYYMAPEHLNDVNAKPteKSDVYSF 214
Cdd:cd06657 138 IHRDIKSDSILLTHDGRVKLSDFGFC-----AQVSKEVPRRKSLV--------GTPYWMAPELISRLPYGP--EVDIWSL 202
                       170
                ....*....|....*.
gi 3426027  215 AVVLWAIFANKEPYEN 230
Cdd:cd06657 203 GIMVIEMVDGEPPYFN 218
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
117-277 4.54e-11

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: 63.83  E-value: 4.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  117 RIILEIIEGMCYLHGKGVIHKDLKPENILVD-----NDFHIKIADLGLAsfkmwSKLNNEEHNeLREVDGTAkkngGTLY 191
Cdd:cd13982 103 RLLRQIASGLAHLHSLNIVHRDLKPQNILIStpnahGNVRAMISDFGLC-----KKLDVGRSS-FSRRSGVA----GTSG 172
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  192 YMAPEHLN-DVNAKPTEKSDVYSFAVVLWAIFAN-KEPY-ENAICEqqliMCIKSG--NRPDVDDITEYCP--REIISLM 264
Cdd:cd13982 173 WIAPEMLSgSTKRRQTRAVDIFSLGCVFYYVLSGgSHPFgDKLERE----ANILKGkySLDKLLSLGEHGPeaQDLIERM 248
                       170
                ....*....|...
gi 3426027  265 klcWEANPEARPT 277
Cdd:cd13982 249 ---IDFDPEKRPS 258
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
62-259 5.02e-11

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: 63.97  E-value: 5.02e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGV--IIEEGKYSLVM--EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKG--VI 135
Cdd:cd14031  58 EEAEMLKGLQHPNIVRFYDSweSVLKGKKCIVLvtELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppII 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDF-HIKIADLGLASFKMWSklnneehnelrevdgTAKKNGGTLYYMAPEHLNDvnaKPTEKSDVYSF 214
Cdd:cd14031 138 HRDLKCDNIFITGPTgSVKIGDLGLATLMRTS---------------FAKSVIGTPEFMAPEMYEE---HYDESVDVYAF 199
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3426027  215 AVVLWAIFANKEPYENAICEQQLIMCIKSGNR---------PDVDDITEYCPRE 259
Cdd:cd14031 200 GMCMLEMATSEYPYSECQNAAQIYRKVTSGIKpasfnkvtdPEVKEIIEGCIRQ 253
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
26-159 5.39e-11

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: 64.56  E-value: 5.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG-LMIMKTVYKGP----NCIEHNEA---LLEEAKmmnrlrHSRVVKLlgviieegKYS-------- 89
Cdd:cd05599  12 GAFGEVRLVRKKDTGhVYAMKKLRKSEmlekEQVAHVRAerdILAEAD------NPWVVKL--------YYSfqdeenly 77
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGL 159
Cdd:cd05599  78 LIMEFLPGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL 147
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
26-264 5.75e-11

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: 63.48  E-value: 5.75e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLK 105
Cdd:cd14183  17 GNFAVVKECVERSTGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELVKGGDLFDAIT 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  106 AEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV----DNDFHIKIADLGLASFkmwsklnneehnelreVDG 181
Cdd:cd14183  97 STNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATV----------------VDG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  182 TAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYENAICEQ-----QLIMCIKSGNRPDVDDITEyC 256
Cdd:cd14183 161 PLYTVCGTPTYVAPEIIAETGYG--LKVDIWAAGVITYILLCGFPPFRGSGDDQevlfdQILMGQVDFPSPYWDNVSD-S 237

                ....*...
gi 3426027  257 PREIISLM 264
Cdd:cd14183 238 AKELITMM 245
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
55-276 6.87e-11

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 63.68  E-value: 6.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLR-HSRVVKLLGV--IIEEGKYSLVMEYME-----KGNLMHVLKaEMSTPLSVKGRIILEIIEGM 126
Cdd:cd14036  39 EKNKAIIQEINFMKKLSgHPNIVQFCSAasIGKEESDQGQAEYLLltelcKGQLVDFVK-KVEAPGPFSPDTVLKIFYQT 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  127 C----YLHGKG--VIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLNNEEHNELREVDGTAKKNgGTLYYMAPEHLND 200
Cdd:cd14036 118 CravqHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAHYPDYSWSAQKRSLVEDEITRN-TTPMYRTPEMIDL 196
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  201 VNAKP-TEKSDVYSFAVVLWAIFANKEPYENAICEQqlimcIKSGNRPDVDDITEYcpREIISLMKLCWEANPEARP 276
Cdd:cd14036 197 YSNYPiGEKQDIWALGCILYLLCFRKHPFEDGAKLR-----IINAKYTIPPNDTQY--TVFHDLIRSTLKVNPEERL 266
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
13-228 6.89e-11

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 63.01  E-value: 6.89e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   13 KSSDFLesAELDSGGFGKVSLCFHRTQGLMIMKTVYkgPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14110   3 KTYAFQ--TEINRGRFSVVRQCEEKRSGQMLAAKII--PYKPEDKQLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLkAEMSTPLSVKGRIILE-IIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLNNE 171
Cdd:cd14110  79 ELCSGPELLYNL-AERNSYSEAEVTDYLWqILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQP-----FNQG 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  172 ehnelrEVDGTAKKnGGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14110 153 ------KVLMTDKK-GDYVETMAPELLEGQGAGP--QTDIWAIGVTAFIMLSADYPV 200
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
25-160 7.91e-11

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: 64.24  E-value: 7.91e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCF-HRTQGLMIMKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEYMEK 97
Cdd:cd07851  25 SGAYGQVCSAFdTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLEdfqdvyLVTHLMGA 104
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027   98 gNLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd07851 105 -DLNNIVKCQKLSDDHIQ-FLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLA 165
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
62-259 8.97e-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: 63.15  E-value: 8.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGK----YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKG--VI 135
Cdd:cd14030  73 EEAGMLKGLQHPNIVRFYDSWESTVKgkkcIVLVTELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppII 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDF-HIKIADLGLASFKMWSklnneehnelrevdgTAKKNGGTLYYMAPEHLNDvnaKPTEKSDVYSF 214
Cdd:cd14030 153 HRDLKCDNIFITGPTgSVKIGDLGLATLKRAS---------------FAKSVIGTPEFMAPEMYEE---KYDESVDVYAF 214
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 3426027  215 AVVLWAIFANKEPYENAICEQQLIMCIKSGNR---------PDVDDITEYCPRE 259
Cdd:cd14030 215 GMCMLEMATSEYPYSECQNAAQIYRRVTSGVKpasfdkvaiPEVKEIIEGCIRQ 268
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
63-164 1.00e-10

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: 63.59  E-value: 1.00e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEYMEkGNLMHVLKAEMS-TPLSVkgrIILEIIEGMCYLHGKGVI 135
Cdd:cd07850  49 ELVLMKLVNHKNIIGLLNVFTPQKSLEefqdvyLVMELMD-ANLCQVIQMDLDhERMSY---LLYQMLCGIKHLHSAGII 124
                        90       100       110
                ....*....|....*....|....*....|....
gi 3426027  136 HKDLKPENILVDNDFHIKIADLGLA-----SFKM 164
Cdd:cd07850 125 HRDLKPSNIVVKSDCTLKILDFGLArtagtSFMM 158
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
62-231 1.14e-10

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: 63.11  E-value: 1.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRL-RHSRVVKLLGVIiEEGKYS-LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd14178  45 EEIEILLRYgQHPNIITLKDVY-DDGKFVyLVMELMRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDL 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  140 KPENIL-VD---NDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTekSDVYSFA 215
Cdd:cd14178 124 KPSNILyMDesgNPESIRICDFGFA-------------KQLRAENGLLMTPCYTANFVAPEVLKRQGYDAA--CDIWSLG 188
                       170
                ....*....|....*.
gi 3426027  216 VVLWAIFANKEPYENA 231
Cdd:cd14178 189 ILLYTMLAGFTPFANG 204
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
22-282 1.17e-10

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: 62.48  E-value: 1.17e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHneallEEAKMMNR--LRHSRVVKLLGVIIEEGKYSLVMEYMEKG 98
Cdd:cd14662   7 DIGSGNFGVARLMRNKeTKELVAVKYIERGLKIDEN-----VQREIINHrsLRHPNIIRFKEVVLTPTHLAIVMEYAAGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 nlmhvlkaEMSTPLSVKGRI--------ILEIIEGMCYLHGKGVIHKDLKPENILVDNDF--HIKIADLGlasfkmWSKl 168
Cdd:cd14662  82 --------ELFERICNAGRFsedearyfFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG------YSK- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 NNEEHNElrevdgtAKKNGGTLYYMAPEHLN--DVNAKpteKSDVYSFAVVLWAIFANKEPYE------NAICEQQLIMC 240
Cdd:cd14662 147 SSVLHSQ-------PKSTVGTPAYIAPEVLSrkEYDGK---VADVWSCGVTLYVMLVGAYPFEdpddpkNFRKTIQRIMS 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 3426027  241 IKSgNRPDVDDITEYCpREIISLMklcWEANPEARPTFPGIE 282
Cdd:cd14662 217 VQY-KIPDYVRVSQDC-RHLLSRI---FVANPAKRITIPEIK 253
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
55-230 1.25e-10

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: 62.75  E-value: 1.25e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLHGKGV 134
Cdd:cd06658  61 QRRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQI-ATVCLSVLRALSYLHNQGV 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSF 214
Cdd:cd06658 140 IHRDIKSDSILLTSDGRIKLSDFGFCA-------------QVSKEVPKRKSLVGTPYWMAPEVISRLPYG--TEVDIWSL 204
                       170
                ....*....|....*.
gi 3426027  215 AVVLWAIFANKEPYEN 230
Cdd:cd06658 205 GIMVIEMIDGEPPYFN 220
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
62-244 1.39e-10

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: 62.74  E-value: 1.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRL-RHSRVVKLLGVIiEEGKY-SLVMEYMEKGNLM-HVLKAEMSTPLSVKGrIILEIIEGMCYLHGKGVIHKD 138
Cdd:cd14175  43 EEIEILLRYgQHPNIITLKDVY-DDGKHvYLVTELMRGGELLdKILRQKFFSEREASS-VLHTICKTVEYLHSQGVVHRD 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  139 LKPENIL-VD---NDFHIKIADLGLAsfkmwsklnneehNELREVDGTAKKNGGTLYYMAPEHLNDVNAKptEKSDVYSF 214
Cdd:cd14175 121 LKPSNILyVDesgNPESLRICDFGFA-------------KQLRAENGLLMTPCYTANFVAPEVLKRQGYD--EGCDIWSL 185
                       170       180       190
                ....*....|....*....|....*....|..
gi 3426027  215 AVVLWAIFANKEPYENAICE--QQLIMCIKSG 244
Cdd:cd14175 186 GILLYTMLAGYTPFANGPSDtpEEILTRIGSG 217
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
75-228 1.52e-10

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: 62.74  E-value: 1.52e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   75 VVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFH 151
Cdd:cd14174  62 ILELIEFFEDDTRFYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSP 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  152 IKIADLGLAS-FKMWSKLNNEEHNELREVDGTAKknggtlyYMAPEHLNDVNAKPT---EKSDVYSFAVVLWAIFANKEP 227
Cdd:cd14174 142 VKICDFDLGSgVKLNSACTPITTPELTTPCGSAE-------YMAPEVVEVFTDEATfydKRCDLWSLGVILYIMLSGYPP 214

                .
gi 3426027  228 Y 228
Cdd:cd14174 215 F 215
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
25-250 1.54e-10

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: 63.05  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   25 SGGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEE------GKYSLVMEYMEK 97
Cdd:cd07880  25 SGAYGTVCSALDRRTGAKVaIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDlsldrfHDFYLVMPFMGT 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 gNLMHVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehnelR 177
Cdd:cd07880 105 -DLGKLMKHEKLSEDRIQ-FLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA----------------R 166
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 3426027  178 EVDGTAKKNGGTLYYMAPEH-LNDVNAkpTEKSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVD 250
Cdd:cd07880 167 QTDSEMTGYVVTRWYRAPEViLNWMHY--TQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKE 238
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
61-160 1.54e-10

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: 62.45  E-value: 1.54e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKgNLMHVLKAEMSTP-LSVKGRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd07839  47 LREICLLKELKHKNIVRLYDVLHSDKKLTLVFEYCDQ-DLKKYFDSCNGDIdPEIVKSFMFQLLKGLAFCHSHNVLHRDL 125
                        90       100
                ....*....|....*....|.
gi 3426027  140 KPENILVDNDFHIKIADLGLA 160
Cdd:cd07839 126 KPQNLLINKNGELKLADFGLA 146
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
21-283 1.55e-10

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: 62.25  E-value: 1.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   21 AELDSGGFGKVSLCFHRTQGLMI-MKTVYKGPNC----IEHNEALLEEAKMM---NRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14005   6 DLLGKGGFGTVYSGVRIRDGLPVaVKFVPKSRVTewamINGPVPVPLEIALLlkaSKPGVPGVIRLLDWYERPDGFLLIM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EY-----------MEKGnlmhVLKAEMStplsvkgRIILE-IIEGMCYLHGKGVIHKDLKPENILVDNDFH-IKIADLGL 159
Cdd:cd14005  86 ERpepcqdlfdfiTERG----ALSENLA-------RIIFRqVVEAVRHCHQRGVLHRDIKDENLLINLRTGeVKLIDFGC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  160 ASFkmwsklnneehneLRevDGTAKKNGGTLYYMAPEHLND--VNAKPtekSDVYSFAVVLWAIFANKEPYEN--AICEQ 235
Cdd:cd14005 155 GAL-------------LK--DSVYTDFDGTRVYSPPEWIRHgrYHGRP---ATVWSLGILLYDMLCGDIPFENdeQILRG 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 3426027  236 QLImcIKSGNRPDVDDiteycpreiisLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14005 217 NVL--FRPRLSKECCD-----------LISRCLQFDPSKRPSLEQILS 251
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
51-221 1.71e-10

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: 62.96  E-value: 1.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   51 PNCIEHNEALLEEAKMMNRLRH-SRVVKLLGVIIE---EGKYSL----------VMEYMEKGNLMHVLKAEMSTPLSVKG 116
Cdd:cd13977  59 PNVIQLEECVLQRDGLAQRMSHgSSKSDLYLLLVEtslKGERCFdprsacylwfVMEFCDGGDMNEYLLSRRPDRQTNTS 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  117 rIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH---IKIADLGLASFKMWSKLNNEEHNELREVDGTAKknGGTLYYM 193
Cdd:cd13977 139 -FMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGepiLKVADFGLSKVCSGSGLNPEEPANVNKHFLSSA--CGSDFYM 215
                       170       180       190
                ....*....|....*....|....*....|..
gi 3426027  194 APE----HLndvnakpTEKSDVYSFAVVLWAI 221
Cdd:cd13977 216 APEvwegHY-------TAKADIFALGIIIWAM 240
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
15-237 1.72e-10

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: 62.54  E-value: 1.72e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   15 SDFLE-SAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNciehNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVM 92
Cdd:cd14085   2 EDFFEiESELGRGATSVVYRCRQKgTQKPYAVKKLKKTVD----KKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   93 EYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDN---DFHIKIADLGLAsfkmwskln 169
Cdd:cd14085  78 ELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLS--------- 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  170 neehnELREVDGTAKKNGGTLYYMAPEHLNDVNAKPteKSDVYSFAVVLWAIFANKEPYENAICEQQL 237
Cdd:cd14085 149 -----KIVDQQVTMKTVCGTPGYCAPEILRGCAYGP--EVDMWSVGVITYILLCGFEPFYDERGDQYM 209
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
23-238 1.91e-10

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: 62.38  E-value: 1.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLMIMKTV------YKGPNCIEHNEALLEEAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYM 95
Cdd:cd14041  14 LGRGGFSEVYKAFDLTEQRYVAVKIhqlnknWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDSFCTVLEYC 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLH--GKGVIHKDLKPENILVDNDF---HIKIADLGLASFkmwskLNN 170
Cdd:cd14041  94 EGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGTacgEIKITDFGLSKI-----MDD 168
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 EEHNELREVDGTAkKNGGTLYYMAPEHLNDVNAKP--TEKSDVYSFAVVLWAIFANKEPYENAICEQQLI 238
Cdd:cd14041 169 DSYNSVDGMELTS-QGAGTYWYLPPECFVVGKEPPkiSNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDIL 237
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
11-158 1.99e-10

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: 62.78  E-value: 1.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   11 KMKSSDFLESAELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCIEHNEALL-EEAKMMNRLRHSRVVKLLGVIIEEGKY 88
Cdd:cd05596  22 RMNAEDFDVIKVIGRGAFGEVQLVRHKsTKKVYAMKLLSKFEMIKRSDSAFFwEERDIMAHANSEWIVQLHYAFQDDKYL 101
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   89 SLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLG 158
Cdd:cd05596 102 YMVMDYMPGGDLVNLM-SNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFG 170
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
61-163 2.31e-10

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: 61.90  E-value: 2.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGnlmhvLKAEMST------PLSVKgRIILEIIEGMCYLHGKGV 134
Cdd:cd07870  46 IREASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHTD-----LAQYMIQhpgglhPYNVR-LFMFQLLRGLAYIHGQHI 119
                        90       100
                ....*....|....*....|....*....
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASFK 163
Cdd:cd07870 120 LHRDLKPQNLLISYLGELKLADFGLARAK 148
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
23-277 2.48e-10

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: 61.99  E-value: 2.48e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHRTQGLM-----IMKTVYKGpncieHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd14168  18 LGTGAFSEVVLAEERATGKLfavkcIPKKALKG-----KESSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLVSG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLAsfKMWSKlnneehn 174
Cdd:cd14168  93 GELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLS--KMEGK------- 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  175 elREVDGTAkknGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAIFANKEPY---ENAICEQQLIMCIKSGNRPDVD 250
Cdd:cd14168 164 --GDVMSTA---CGTPGYVAPEVLAQ---KPYSKAvDCWSIGVIAYILLCGYPPFydeNDSKLFEQILKADYEFDSPYWD 235
                       250       260
                ....*....|....*....|....*..
gi 3426027  251 DITEYCPREIISLMklcwEANPEARPT 277
Cdd:cd14168 236 DISDSAKDFIRNLM----EKDPNKRYT 258
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
63-196 2.79e-10

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: 62.20  E-value: 2.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIE--EGKYsLVMEYMekGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLK 140
Cdd:cd07856  59 ELKLLKHLRHENIISLSDIFISplEDIY-FVTELL--GTDLHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLK 135
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 3426027  141 PENILVDNDFHIKIADLGLAsfkmwsklnneehnelREVDGTAKKNGGTLYYMAPE 196
Cdd:cd07856 136 PSNILVNENCDLKICDFGLA----------------RIQDPQMTGYVSTRYYRAPE 175
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
23-241 2.80e-10

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: 62.18  E-value: 2.80e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCF-HRTQGLMIMKtVYKGPNCIeHNEALLEeAKMMNRLRH------SRVVKLLGVIIEEGKYSLVMEYM 95
Cdd:cd14210  21 LGKGSFGQVVKCLdHKTGQLVAIK-IIRNKKRF-HQQALVE-VKILKHLNDndpddkHNIVRYKDSFIFRGHLCIVFELL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   96 EKgNLMHVLKAE----MSTPLsVKgRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH--IKIADLGLASFkmwskln 169
Cdd:cd14210  98 SI-NLYELLKSNnfqgLSLSL-IR-KFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKssIKVIDFGSSCF------- 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  170 neehnelrevdgtakkNGGTLY-------YMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKE--PYENaicEQQLIMC 240
Cdd:cd14210 168 ----------------EGEKVYtyiqsrfYRAPEVI--LGLPYDTAIDMWSLGCILAELYTGYPlfPGEN---EEEQLAC 226

                .
gi 3426027  241 I 241
Cdd:cd14210 227 I 227
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
61-160 2.86e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 61.76  E-value: 2.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGnlmhvLKAEM-STP-LSVKGRII----LEIIEGMCYLHGKGV 134
Cdd:PLN00009  49 IREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYLDLD-----LKKHMdSSPdFAKNPRLIktylYQILRGIAYCHSHRV 123
                         90       100
                 ....*....|....*....|....*..
gi 3426027   135 IHKDLKPENILVDNDFH-IKIADLGLA 160
Cdd:PLN00009 124 LHRDLKPQNLLIDRRTNaLKLADFGLA 150
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
22-281 3.09e-10

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: 61.15  E-value: 3.09e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCiehNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL 100
Cdd:cd14665   7 DIGSGNFGVARLMRDKqTKELVAVKYIERGEKI---DENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEYAAGGEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  101 MHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF--HIKIADLGlasfkmWSKlNNEEHNElre 178
Cdd:cd14665  84 FERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFG------YSK-SSVLHSQ--- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 vdgtAKKNGGTLYYMAPEHL--NDVNAKpteKSDVYSFAVVLWAIFANKEPYENAICEQ------QLIMCIKSgNRPDVD 250
Cdd:cd14665 154 ----PKSTVGTPAYIAPEVLlkKEYDGK---IADVWSCGVTLYVMLVGAYPFEDPEEPRnfrktiQRILSVQY-SIPDYV 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 3426027  251 DITEYCpREIISLMklcWEANPEARPTFPGI 281
Cdd:cd14665 226 HISPEC-RHLISRI---FVADPATRITIPEI 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
61-225 3.14e-10

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: 62.04  E-value: 3.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLR-HSRVVKLLGV-IIEEGKYSLVMEYME--KGNLMHVLKAEMstPLSVK--GRIILEIIEGMCYLHGKGV 134
Cdd:cd07857  49 LRELKLLRHFRgHKNITCLYDMdIVFPGNFNELYLYEElmEADLHQIIRSGQ--PLTDAhfQSFIYQILCGLKYIHSANV 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLA-SFkmwsklnneeHNELREVDGTAKKNGGTLYYMAPEHLndVNAKPTEKS-DVY 212
Cdd:cd07857 127 LHRDLKPGNLLVNADCELKICDFGLArGF----------SENPGENAGFMTEYVATRWYRAPEIM--LSFQSYTKAiDVW 194
                       170
                ....*....|...
gi 3426027  213 SFAVVLWAIFANK 225
Cdd:cd07857 195 SVGCILAELLGRK 207
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
91-275 3.18e-10

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: 62.12  E-value: 3.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSklnn 170
Cdd:cd05591  74 VMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILN---- 149
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  171 eehnelrevDGTAKKNGGTLYYMAPEHLNDVNAKPTekSDVYSFAVVLWAIFANKEPYEnAICEQQLIMCIKSgnrpdvD 250
Cdd:cd05591 150 ---------GKTTTTFCGTPDYIAPEILQELEYGPS--VDWWALGVLMYEMMAGQPPFE-ADNEDDLFESILH------D 211
                       170       180
                ....*....|....*....|....*..
gi 3426027  251 DITE--YCPREIISLMKLCWEANPEAR 275
Cdd:cd05591 212 DVLYpvWLSKEAVSILKAFMTKNPAKR 238
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
62-247 3.55e-10

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: 61.25  E-value: 3.55e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGK----YSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKG--VI 135
Cdd:cd14032  49 EEAEMLKGLQHPNIVRFYDFWESCAKgkrcIVLVTELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppII 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILVDNDF-HIKIADLGLASFKMWSklnneehnelrevdgTAKKNGGTLYYMAPEHLNDvnaKPTEKSDVYSF 214
Cdd:cd14032 129 HRDLKCDNIFITGPTgSVKIGDLGLATLKRAS---------------FAKSVIGTPEFMAPEMYEE---HYDESVDVYAF 190
                       170       180       190
                ....*....|....*....|....*....|...
gi 3426027  215 AVVLWAIFANKEPYENAICEQQLIMCIKSGNRP 247
Cdd:cd14032 191 GMCMLEMATSEYPYSECQNAAQIYRKVTCGIKP 223
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
26-311 3.63e-10

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: 61.90  E-value: 3.63e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQG-LMIMKTVYKGP--NCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMH 102
Cdd:cd05604   7 GSFGKVLLAKRKRDGkYYAVKVLQKKVilNRKEQKHIMAERNVLLKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGELFF 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  103 VLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnneehNELREVDGT 182
Cdd:cd05604  87 HLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLC-------------KEGISNSDT 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  183 AKKNGGTLYYMAPEHLNDvnaKPTEKS-DVYSFAVVLWAI------FANK---EPYENaICEQQLIMciksgnRPDVDDI 252
Cdd:cd05604 154 TTTFCGTPEYLAPEVIRK---QPYDNTvDWWCLGSVLYEMlyglppFYCRdtaEMYEN-ILHKPLVL------RPGISLT 223
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  253 TeycpreiISLMKLCWEANPEARptfPGIEEKF-----RPFYLS----QLEE---------SVE--EDVKSLKKEYSNE 311
Cdd:cd05604 224 A-------WSILEELLEKDRQLR---LGAKEDFleiknHPFFESinwtDLVQkkipppfnpNVNgpDDISNFDAEFTEE 292
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
85-296 3.75e-10

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 61.58  E-value: 3.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EGKYSLVMEYMEKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLH-------GKG----VIHKDLKPENILVDNDFHIK 153
Cdd:cd14140  65 EMELWLITAFHDKGSLTDYLKGNIVSWNEL-CHIAETMARGLSYLHedvprckGEGhkpaIAHRDFKSKNVLLKNDLTAV 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  154 IADLGLASFKMWSKLNNEEHNELrevdgtakkngGTLYYMAPEHLND-VNAKPTE--KSDVYSFAVVLWAIFANKEPYEN 230
Cdd:cd14140 144 LADFGLAVRFEPGKPPGDTHGQV-----------GTRRYMAPEVLEGaINFQRDSflRIDMYAMGLVLWELVSRCKAADG 212
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  231 AICEQQLIMCIKSGNRPDVDDITEYCPR------------------EIISLMKLCWEANPEARPTFPGIEEKfrpfyLSQ 292
Cdd:cd14140 213 PVDEYMLPFEEEIGQHPSLEDLQEVVVHkkmrpvfkdhwlkhpglaQLCVTIEECWDHDAEARLSAGCVEER-----ISQ 287

                ....
gi 3426027  293 LEES 296
Cdd:cd14140 288 IRRS 291
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
63-286 3.78e-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: 61.62  E-value: 3.78e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEG--KYSLVMEYMEKgNLMHVLK---------AEMSTPLSVKGRIILEIIEGMCYLHG 131
Cdd:cd07867  49 EIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH-DLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLHA 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  132 KGVIHKDLKPENILVDND----FHIKIADLGLAsfkmwsKLNNEEHNELREVDGTAKknggTLYYMAPEHLndVNAKPte 207
Cdd:cd07867 128 NWVLHRDLKPANILVMGEgperGRVKIADMGFA------RLFNSPLKPLADLDPVVV----TFWYRAPELL--LGARH-- 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  208 ksdvYSFAVVLWA---IFA---NKEPYENaiCEQQlimCIKSGNRPDVDDITeycprEIISLMKLC----WEaNPEARPT 277
Cdd:cd07867 194 ----YTKAIDIWAigcIFAellTSEPIFH--CRQE---DIKTSNPFHHDQLD-----RIFSVMGFPadkdWE-DIRKMPE 258

                ....*....
gi 3426027  278 FPGIEEKFR 286
Cdd:cd07867 259 YPTLQKDFR 267
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
26-245 3.93e-10

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: 61.57  E-value: 3.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGL----MIMKTVYKGPNciehneallEEAKMMNRL-RHSRVVKLLGVIiEEGKYS-LVMEYMEKGN 99
Cdd:cd14177  15 GSYSVCKRCIHRATNMefavKIIDKSKRDPS---------EEIEILMRYgQHPNIITLKDVY-DDGRYVyLVTELMKGGE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LM-HVLKAEMSTPLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF----HIKIADLGLAsfkmwsklnneehN 174
Cdd:cd14177  85 LLdRILRQKFFSEREASA-VLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSanadSIRICDFGFA-------------K 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  175 ELREVDGTAKKNGGTLYYMAPEHLndVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICE--QQLIMCIKSGN 245
Cdd:cd14177 151 QLRGENGLLLTPCYTANFVAPEVL--MRQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDtpEEILLRIGSGK 221
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
58-230 4.33e-10

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: 60.92  E-value: 4.33e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVkGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06648  49 ELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQI-ATVCRAVLKALSFLHSQGVIHR 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEHlndVNAKP--TEkSDVYSFA 215
Cdd:cd06648 128 DIKSDSILLTSDGRVKLSDFGFCA-------------QVSKEVPRRKSLVGTPYWMAPEV---ISRLPygTE-VDIWSLG 190
                       170
                ....*....|....*
gi 3426027  216 VVLWAIFANKEPYEN 230
Cdd:cd06648 191 IMVIEMVDGEPPYFN 205
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
58-275 4.93e-10

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: 61.28  E-value: 4.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06655  61 ELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLTDVV-TETCMDEAQIAAVCRECLQALEFLHANQVIHR 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVdgtakkngGTLYYMAPEHLNDVNAKPteKSDVYSFAVV 217
Cdd:cd06655 140 DIKSDNVLLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV--------GTPYWMAPEVVTRKAYGP--KVDIWSLGIM 204
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 3426027  218 LWAIFANKEPYENAICEQQLIMCIKSGNrPDVDDITEYCPReIISLMKLCWEANPEAR 275
Cdd:cd06655 205 AIEMVEGEPPYLNENPLRALYLIATNGT-PELQNPEKLSPI-FRDFLNRCLEMDVEKR 260
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
90-283 4.99e-10

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 61.21  E-value: 4.99e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTpLSVKGRIILEIIEGMCYLHGK----------GVIHKDLKPENILVDNDFHIKIADLGL 159
Cdd:cd14141  70 LITAFHEKGSLTDYLKANVVS-WNELCHIAQTMARGLAYLHEDipglkdghkpAIAHRDIKSKNVLLKNNLTACIADFGL 148
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  160 ASFKMWSKLNNEEHNELrevdgtakkngGTLYYMAPEHLN---DVNAKPTEKSDVYSFAVVLWAIFANKEPYENAICEQQ 236
Cdd:cd14141 149 ALKFEAGKSAGDTHGQV-----------GTRRYMAPEVLEgaiNFQRDAFLRIDMYAMGLVLWELASRCTASDGPVDEYM 217
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 3426027  237 LIMCIKSGNRPDVDDITE-YCPREIISLMKLCWEANPEARPTFPGIEE 283
Cdd:cd14141 218 LPFEEEVGQHPSLEDMQEvVVHKKKRPVLRECWQKHAGMAMLCETIEE 265
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
22-162 5.65e-10

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: 61.43  E-value: 5.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   22 ELDSGGFGKVSLCFHRTQG----LMIMKTVYKgpncieHNEALLEEAKMMNRLRH------SRVVKLLGVIIEEGKYSLV 91
Cdd:cd14134  19 LLGEGTFGKVLECWDRKRKryvaVKIIRNVEK------YREAAKIEIDVLETLAEkdpngkSHCVQLRDWFDYRGHMCIV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYME-------KGNLMHVLkaemstPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENIL-VDNDF------------- 150
Cdd:cd14134  93 FELLGpslydflKKNNYGPF------PLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILlVDSDYvkvynpkkkrqir 166
                       170
                ....*....|....*..
gi 3426027  151 -----HIKIADLGLASF 162
Cdd:cd14134 167 vpkstDIKLIDFGSATF 183
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
60-238 6.27e-10

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: 61.34  E-value: 6.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   60 LLEEAKMMNRLRHSRVVKLLGVIIEEGKYS-----LVMEYMEKgNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGV 134
Cdd:cd07859  46 ILREIKLLRLLRHPDIVEIKHIMLPPSRREfkdiyVVFELMES-DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANV 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASFKMwsklnNEEHNELREVDGTAkknggTLYYMAPEHLNDVNAKPTEKSDVYSF 214
Cdd:cd07859 125 FHRDLKPKNILANADCKLKICDFGLARVAF-----NDTPTAIFWTDYVA-----TRWYRAPELCGSFFSKYTPAIDIWSI 194
                       170       180
                ....*....|....*....|....*.
gi 3426027  215 AVVLWAIFANKE--PYENAICEQQLI 238
Cdd:cd07859 195 GCIFAEVLTGKPlfPGKNVVHQLDLI 220
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
62-277 6.42e-10

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: 60.29  E-value: 6.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   62 EEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLM-HVLKAEMSTPLSVKgRIILEIIEGMCYLHGKGVIHKDLK 140
Cdd:cd14107  47 QERDILARLSHRRLTCLLDQFETRKTLILILELCSSEELLdRLFLKGVVTEAEVK-LYIQQVLEGIGYLHGMNILHLDIK 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  141 PENILVDNDFH--IKIADLGLAsfkmwSKLNNEEHNELREvdgtakkngGTLYYMAPE--HLNDVnakpTEKSDVYSFAV 216
Cdd:cd14107 126 PDNILMVSPTRedIKICDFGFA-----QEITPSEHQFSKY---------GSPEFVAPEivHQEPV----SAATDIWALGV 187
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  217 VLWAIFANKEPY--ENaicEQQLIMCIKSG----NRPDVDDITEycprEIISLMKLCWEANPEARPT 277
Cdd:cd14107 188 IAYLSLTCHSPFagEN---DRATLLNVAEGvvswDTPEITHLSE----DAKDFIKRVLQPDPEKRPS 247
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
26-231 6.81e-10

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: 61.19  E-value: 6.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGL----MIMKTVYKGPNciehneallEEAKMMNRL-RHSRVVKLLGVIiEEGKYS-LVMEYMEKGN 99
Cdd:cd14176  30 GSYSVCKRCIHKATNMefavKIIDKSKRDPT---------EEIEILLRYgQHPNIITLKDVY-DDGKYVyVVTELMKGGE 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LM-HVLKAEMSTPLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENIL-VD---NDFHIKIADLGLAsfkmwsklnneehN 174
Cdd:cd14176 100 LLdKILRQKFFSEREASA-VLFTITKTVEYLHAQGVVHRDLKPSNILyVDesgNPESIRICDFGFA-------------K 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 3426027  175 ELREVDGTAKKNGGTLYYMAPEHLNDVNAKPTekSDVYSFAVVLWAIFANKEPYENA 231
Cdd:cd14176 166 QLRAENGLLMTPCYTANFVAPEVLERQGYDAA--CDIWSLGVLLYTMLTGYTPFANG 220
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
59-281 7.89e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; 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 cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 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: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 60.34  E-value: 7.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   59 ALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNL---MHVLKAEMSTPLsvKGRIILEIIEGMCYLHGKGVI 135
Cdd:cd05077  54 AFFETASMMRQVSHKHIVLLYGVCVRDVENIMVEEFVEFGPLdlfMHRKSDVLTTPW--KFKVAKQLASALSYLEDKDLV 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  136 HKDLKPENILV-----DNDF--HIKIADLGLASfkmwSKLNNEEHNElrevdgtakknggTLYYMAPEHLNDvNAKPTEK 208
Cdd:cd05077 132 HGNVCTKNILLaregiDGECgpFIKLSDPGIPI----TVLSRQECVE-------------RIPWIAPECVED-SKNLSIA 193
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  209 SDVYSFAVVLWAIFANKE-PYEN-AICEQQLIMciKSGNRPdvddITEYCpREIISLMKLCWEANPEARPTFPGI 281
Cdd:cd05077 194 ADKWSFGTTLWEICYNGEiPLKDkTLAEKERFY--EGQCML----VTPSC-KELADLMTHCMNYDPNQRPFFRAI 261
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
61-223 8.02e-10

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: 61.30  E-value: 8.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGvIIEEGKYSLVMEYMEKGNLMH------VLKAEMSTPLSVKgRIILEIIEGMCYLHGKGV 134
Cdd:cd07853  47 FRELKMLCFFKHDNVLSALD-ILQPPHIDPFEEIYVVTELMQsdlhkiIVSPQPLSSDHVK-VFLYQILRGLKYLHSAGI 124
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASFkmwsklnnEEHNELREVdgTAKKNggTLYYMAPEHLNDvnakptekSDVYSF 214
Cdd:cd07853 125 LHRDIKPGNLLVNSNCVLKICDFGLARV--------EEPDESKHM--TQEVV--TQYYRAPEILMG--------SRHYTS 184
                       170
                ....*....|..
gi 3426027  215 AVVLWA---IFA 223
Cdd:cd07853 185 AVDIWSvgcIFA 196
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-228 9.15e-10

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: 60.70  E-value: 9.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCF----HRTQGLMIMKTVYKGpnciehneALLEEAKMMNRLRHSR-----------VVKLLGVIIEEGK 87
Cdd:cd05614   8 LGTGAYGKVFLVRkvsgHDANKLYAMKVLRKA--------ALVQKAKTVEHTRTERnvlehvrqspfLVTLHYAFQTDAK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   88 YSLVMEYMEKGNLM-HVLKAEMSTPLSVK---GRIILeiieGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfk 163
Cdd:cd05614  80 LHLILDYVSGGELFtHLYQRDHFSEDEVRfysGEIIL----ALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGL---- 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 3426027  164 mwSKLNNEEHNElrevdgTAKKNGGTLYYMAPEHLNDVNAKpTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05614 152 --SKEFLTEEKE------RTYSFCGTIEYMAPEIIRGKSGH-GKAVDWWSLGILMFELLTGASPF 207
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
18-231 9.21e-10

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: 60.66  E-value: 9.21e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   18 LESAELDSGGFGKVSLCFHRTQGL-MIMKTVYKGpncIEHNEALlEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYME 96
Cdd:cd14180   9 LEEPALGEGSFSVCRKCRHRQSGQeYAVKIISRR---MEANTQR-EVAALRLCQSHPNIVALHEVLHDQYHTYLVMELLR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   97 KGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFH---IKIADLGLAsfkmwsklnneeh 173
Cdd:cd14180  85 GGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFA------------- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  174 nELREVDGTAKKNGG-TLYYMAPEHLNDVNAKptEKSDVYSFAVVLWAIFANKEPYENA 231
Cdd:cd14180 152 -RLRPQGSRPLQTPCfTLQYAAPELFSNQGYD--ESCDLWSLGVILYTMLSGQVPFQSK 207
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
55-228 1.05e-09

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: 60.00  E-value: 1.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGV 134
Cdd:cd06659  60 QRRELLFNEVVIMRDYQHPNVVEMYKSYLVGEELWVLMEYLQGGALTDIV-SQTRLNEEQIATVCEAVLQALAYLHSQGV 138
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLASfkMWSKlnneehnelrevDGTAKKN-GGTLYYMAPEHLNDVNAkpTEKSDVYS 213
Cdd:cd06659 139 IHRDIKSDSILLTLDGRVKLSDFGFCA--QISK------------DVPKRKSlVGTPYWMAPEVISRCPY--GTEVDIWS 202
                       170
                ....*....|....*
gi 3426027  214 FAVVLWAIFANKEPY 228
Cdd:cd06659 203 LGIMVIEMVDGEPPY 217
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
23-213 1.25e-09

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: 59.78  E-value: 1.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   23 LDSGGFGKVSLCFHR-TQGLMIMKTVYKGPNCieHNEALLEeakmMNRLRHSRVVKLLGVIIEEGKYS----------LV 91
Cdd:cd14171  14 LGTGISGPVRVCVKKsTGERFALKILLDRPKA--RTEVRLH----MMCSGHPNIVQIYDVYANSVQFPgessprarllIV 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDN---DFHIKIADLGLAsfkmwskl 168
Cdd:cd14171  88 MELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDnseDAPIKLCDFGFA-------- 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 3426027  169 nneehnelREVDGTAKKNGGTLYYMAPEHLNDVNAKPTEKSDVYS 213
Cdd:cd14171 160 --------KVDQGDLMTPQFTPYYVAPQVLEAQRRHRKERSGIPT 196
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
29-219 1.26e-09

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: 59.61  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   29 GKVSLCFHRTQG----LMIMKTVYKGPNCIEHNealleeakmMNRLRHSRVVKLLGVIieEGKYS------LVMEYMEKG 98
Cdd:cd14089  15 GKVLECFHKKTGekfaLKVLRDNPKARREVELH---------WRASGCPHIVRIIDVY--ENTYQgrkcllVVMECMEGG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   99 NLMHVLKAEMSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENIL-VDNDFH--IKIADLGLAsfkmwsklnneeh 173
Cdd:cd14089  84 ELFSRIQERADSAFTEReaAEIMRQIGSAVAHLHSMNIAHRDLKPENLLySSKGPNaiLKLTDFGFA------------- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 3426027  174 nelREVDGTAKKNGG--TLYYMAPEHLndvNAKPTEKS-DVYSFAVVLW 219
Cdd:cd14089 151 ---KETTTKKSLQTPcyTPYYVAPEVL---GPEKYDKScDMWSLGVIMY 193
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
16-228 1.31e-09

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: 60.06  E-value: 1.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   16 DFLESAELDSGGFGKVSLCFHRTQGLM-IMKTVYKGPNCIEHNEALLEEAKMMNRLRHSR----VVKLLGVIIEEGKYSL 90
Cdd:cd14223   1 DFSVHRIIGRGGFGEVYGCRKADTGKMyAMKCLDKKRIKMKQGETLALNERIMLSLVSTGdcpfIVCMSYAFHTPDKLSF 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   91 VMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnn 170
Cdd:cd14223  81 ILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLA---------- 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  171 eehnelreVDGTAKK---NGGTLYYMAPEHLNDVNAKPTEkSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14223 151 --------CDFSKKKphaSVGTHGYMAPEVLQKGVAYDSS-ADWFSLGCMLFKLLRGHSPF 202
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
63-164 1.39e-09

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


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 57.28  E-value: 1.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHS--RVVKLLGViiEEGKYSLVMEYMEKGNLMHVLKAEMSTPlsvkgRIILEIIEGMCYLHGKGVIHKDLK 140
Cdd:COG3642   6 EARLLRELREAgvPVPKVLDV--DPDDADLVMEYIEGETLADLLEEGELPP-----ELLRELGRLLARLHRAGIVHGDLT 78
                        90       100
                ....*....|....*....|....
gi 3426027  141 PENILVDNDfHIKIADLGLASFKM 164
Cdd:COG3642  79 TSNILVDDG-GVYLIDFGLARYSD 101
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
43-160 1.47e-09

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: 60.18  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   43 IMKTVYKGPNCIEHneaLLEEAKMMNRLRHSRVVKLLGVIIEEGK--------------YSLVMEYMEKgNLMHVLkaEM 108
Cdd:cd07854  35 VKKIVLTDPQSVKH---ALREIKIIRRLDHDNIVKVYEVLGPSGSdltedvgsltelnsVYIVQEYMET-DLANVL--EQ 108
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 3426027  109 STPLSVKGRIIL-EIIEGMCYLHGKGVIHKDLKPENILVD-NDFHIKIADLGLA 160
Cdd:cd07854 109 GPLSEEHARLFMyQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLA 162
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
61-252 1.54e-09

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: 60.08  E-value: 1.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYS-----LVMEYMEKgNLMHVLKAemSTPLSVK--GRIILEIIEGMCYLHGKG 133
Cdd:cd07858  52 LREIKLLRHLDHENVIAIKDIMPPPHREAfndvyIVYELMDT-DLHQIIRS--SQTLSDDhcQYFLYQLLRGLKYIHSAN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  134 VIHKDLKPENILVDNDFHIKIADLGLAsfkmwsKLNNEEHNELRE--VdgtakknggTLYYMAPEHLNDVNaKPTEKSDV 211
Cdd:cd07858 129 VLHRDLKPSNLLLNANCDLKICDFGLA------RTTSEKGDFMTEyvV---------TRWYRAPELLLNCS-EYTTAIDV 192
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 3426027  212 YSFAVVLWAIFANKEPYENAICEQQLIMCIKSGNRPDVDDI 252
Cdd:cd07858 193 WSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGSPSEEDL 233
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
26-229 1.55e-09

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: 60.05  E-value: 1.55e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLC-FHRTQGLMIMKTVYK-------GPNCIEHNEALLEEAKmmnrlRHSRVVKLLGVIIEEGKYSLVMEYMEK 97
Cdd:cd05618  31 GSYAKVLLVrLKKTERIYAMKVVKKelvnddeDIDWVQTEKHVFEQAS-----NHPFLVGLHSCFQTESRLFFVIEYVNG 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   98 GNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehNELR 177
Cdd:cd05618 106 GDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCK------------EGLR 173
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  178 EVDgTAKKNGGTLYYMAPEHLndvnakpteKSDVYSFAVVLWAI-------FANKEPYE 229
Cdd:cd05618 174 PGD-TTSTFCGTPNYIAPEIL---------RGEDYGFSVDWWALgvlmfemMAGRSPFD 222
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
594-666 1.55e-09

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 54.96  E-value: 1.55e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 3426027  594 LGKHWKNCARKLGFTQSQIDEIDHDYERDgLKEKVYQMLQKWVMREGIKgATVGKLAQALHQCSRIDLLSSLI 666
Cdd:cd08317  14 LGSDWPELARELGVSEEDIDLIRSENPNS-LAQQAMAMLRLWLEREGEK-ATGNALESALKKIGRDDIVEKCE 84
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
14-277 1.68e-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: 59.27  E-value: 1.68e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   14 SSDFLESAELDSGGFGKVSLCFHRTQGLMIMKTVYKGP--NCIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLV 91
Cdd:cd14138   4 ATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPlaGSVDEQNALREVYAHAVLGQHSHVVRYYSAWAEDDHMLIQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   92 MEYMEKGNLMHVLKAE---MS--TPLSVKGrIILEIIEGMCYLHGKGVIHKDLKPENILVD------------------- 147
Cdd:cd14138  84 NEYCNGGSLADAISENyriMSyfTEPELKD-LLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaseegdedewas 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  148 NDFHIKIADLGLASfkmwsKLNNEEHNElrevdgtakkngGTLYYMAPEHLNDvNAKPTEKSDVYSFAVVLWAIfANKEP 227
Cdd:cd14138 163 NKVIFKIGDLGHVT-----RVSSPQVEE------------GDSRFLANEVLQE-NYTHLPKADIFALALTVVCA-AGAEP 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 3426027  228 Y-ENAICEQQlimcIKSGNRPDVDDITEycpREIISLMKLCWEANPEARPT 277
Cdd:cd14138 224 LpTNGDQWHE----IRQGKLPRIPQVLS---QEFLDLLKVMIHPDPERRPS 267
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
63-160 1.98e-09

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: 59.92  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEYMEKGnlmhvLKAEMSTPLSVKG--RIILEIIEGMCYLHGKGV 134
Cdd:cd07879  64 ELTLLKHMQHENVIGLLDVFTSAVSGDefqdfyLVMPYMQTD-----LQKIMGHPLSEDKvqYLVYQMLCGLKYIHSAGI 138
                        90       100
                ....*....|....*....|....*.
gi 3426027  135 IHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd07879 139 IHRDLKPGNLAVNEDCELKILDFGLA 164
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
85-229 2.10e-09

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: 59.65  E-value: 2.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   85 EGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkm 164
Cdd:cd05617  88 TSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCK--- 164
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  165 wsklnneehNELREVDgTAKKNGGTLYYMAPEHLndvnakpteKSDVYSFAVVLWAI-------FANKEPYE 229
Cdd:cd05617 165 ---------EGLGPGD-TTSTFCGTPNYIAPEIL---------RGEEYGFSVDWWALgvlmfemMAGRSPFD 217
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
71-277 2.65e-09

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 60.03  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    71 RHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVK----GRIILEIIEGMCYLHGKGVIHKDLKPENILV 146
Cdd:PTZ00267 123 DHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNKQIKQRLKEHLPFQeyevGLLFYQIVLALDEVHSRKMMHRDLKSANIFL 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   147 DNDFHIKIADLGLAsfkmwsklnnEEHNELREVDgTAKKNGGTLYYMAPEHLNdvNAKPTEKSDVYSFAVVLWAIFANKE 226
Cdd:PTZ00267 203 MPTGIIKLGDFGFS----------KQYSDSVSLD-VASSFCGTPYYLAPELWE--RKRYSKKADMWSLGVILYELLTLHR 269
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 3426027   227 PYENAiCEQQLIMCIKSGNrpdvddiTEYCPREIISLMKLCWE----ANPEARPT 277
Cdd:PTZ00267 270 PFKGP-SQREIMQQVLYGK-------YDPFPCPVSSGMKALLDpllsKNPALRPT 316
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
61-163 2.94e-09

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: 58.94  E-value: 2.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMST-PLSVKgRIILEIIEGMCYLHGKGVIHKDL 139
Cdd:cd07869  51 IREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLhPENVK-LFLFQLLRGLSYIHQRYILHRDL 129
                        90       100
                ....*....|....*....|....
gi 3426027  140 KPENILVDNDFHIKIADLGLASFK 163
Cdd:cd07869 130 KPQNLLISDTGELKLADFGLARAK 153
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
63-238 3.02e-09

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: 58.91  E-value: 3.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVI-IEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLH--GKGVIHKDL 139
Cdd:cd14040  60 EYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDL 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  140 KPENI-LVDNDF--HIKIADLGLasfkmwSKLNNEEHNELREVDGTAkKNGGTLYYMAPEHLNDVNAKP--TEKSDVYSF 214
Cdd:cd14040 140 KPGNIlLVDGTAcgEIKITDFGL------SKIMDDDSYGVDGMDLTS-QGAGTYWYLPPECFVVGKEPPkiSNKVDVWSV 212
                       170       180
                ....*....|....*....|....
gi 3426027  215 AVVLWAIFANKEPYENAICEQQLI 238
Cdd:cd14040 213 GVIFFQCLYGRKPFGHNQSQQDIL 236
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
90-228 3.39e-09

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: 58.74  E-value: 3.39e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLN 169
Cdd:cd05586  73 LVTDYMSGGELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGL------SKAD 146
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  170 NEEhnelrevDGTAKKNGGTLYYMAPEHLNDvNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05586 147 LTD-------NKTTNTFCGTTEYLAPEVLLD-EKGYTKMVDFWSLGVLVFEMCCGWSPF 197
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
90-221 3.95e-09

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: 58.59  E-value: 3.95e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwskln 169
Cdd:cd05588  73 FVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCK-------- 144
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 3426027  170 neehNELREVDGTAkKNGGTLYYMAPEHLndvnakpteKSDVYSFAVVLWAI 221
Cdd:cd05588 145 ----EGLRPGDTTS-TFCGTPNYIAPEIL---------RGEDYGFSVDWWAL 182
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
58-230 3.98e-09

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: 58.58  E-value: 3.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06654  62 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALEFLHSNQVIHR 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVdgtakkngGTLYYMAPEHLNDVNAKPteKSDVYSFAVV 217
Cdd:cd06654 141 DIKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV--------GTPYWMAPEVVTRKAYGP--KVDIWSLGIM 205
                       170
                ....*....|...
gi 3426027  218 LWAIFANKEPYEN 230
Cdd:cd06654 206 AIEMIEGEPPYLN 218
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
84-228 4.66e-09

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: 58.87  E-value: 4.66e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   84 EEGKYSLVMEYMEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlASF 162
Cdd:cd05624 143 DENYLYLVMDYYVGGDLLTLLsKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFG-SCL 221
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 3426027  163 KMwsklnNEehnelrevDGTAKKN--GGTLYYMAPEHLN---DVNAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05624 222 KM-----ND--------DGTVQSSvaVGTPDYISPEILQameDGMGKYGPECDWWSLGVCMYEMLYGETPF 279
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
58-230 4.69e-09

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: 58.19  E-value: 4.69e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLkAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHK 137
Cdd:cd06656  61 ELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLTDVV-TETCMDEGQIAAVCRECLQALDFLHSNQVIHR 139
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  138 DLKPENILVDNDFHIKIADLGLAsfkmwSKLNNEEHNELREVdgtakkngGTLYYMAPEHLNDVNAKPteKSDVYSFAVV 217
Cdd:cd06656 140 DIKSDNILLGMDGSVKLTDFGFC-----AQITPEQSKRSTMV--------GTPYWMAPEVVTRKAYGP--KVDIWSLGIM 204
                       170
                ....*....|...
gi 3426027  218 LWAIFANKEPYEN 230
Cdd:cd06656 205 AIEMVEGEPPYLN 217
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
26-160 4.70e-09

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: 57.66  E-value: 4.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHR-TQGLMIMKTVYKGpncIEHNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVL 104
Cdd:cd14115   4 GRFSIVKKCLHKaTRKDVAVKFVSKK---MKKKEQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL 80
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 3426027  105 KAE---MSTPLSVkgrIILEIIEGMCYLHGKGVIHKDLKPENILVDNDF---HIKIADLGLA 160
Cdd:cd14115  81 MNHdelMEEKVAF---YIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEDA 139
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
55-216 4.91e-09

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 58.09  E-value: 4.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSR-VVKLLGVIIEEG------KYSLVMEYMEKGNLMHVLKAEMSTPLSVK--GRIILEIIEG 125
Cdd:cd06636  54 DEEEEIKLEINMLKKYSHHRnIATYYGAFIKKSppghddQLWLVMEFCGAGSVTDLVKNTKGNALKEDwiAYICREILRG 133
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  126 MCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEHLN-DVNAK 204
Cdd:cd06636 134 LAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSA-------------QLDRTVGRRNTFIGTPYWMAPEVIAcDENPD 200
                       170
                ....*....|....
gi 3426027  205 PT--EKSDVYSFAV 216
Cdd:cd06636 201 ATydYRSDIWSLGI 214
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
26-228 5.00e-09

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: 57.83  E-value: 5.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   26 GGFGKVSLCFHRTQGLMI-MKTVYKGPNCIEHNEAL-LEEAKMMNRLRHSR----VVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:cd05606   5 GGFGEVYGCRKADTGKMYaMKCLDKKRIKMKQGETLaLNERIMLSLVSTGGdcpfIVCMTYAFQTPDKLCFILDLMNGGD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  100 LMHVL-------KAEMSTPLSvkgriilEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwsklnnee 172
Cdd:cd05606  85 LHYHLsqhgvfsEAEMRFYAA-------EVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLA------------ 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 3426027  173 hnelreVDGTAKK---NGGTLYYMAPEHLNDVNAKPTEkSDVYSFAVVLWAIFANKEPY 228
Cdd:cd05606 146 ------CDFSKKKphaSVGTHGYMAPEVLQKGVAYDSS-ADWFSLGCMLYKLLKGHSPF 197
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
90-189 5.54e-09

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: 58.71  E-value: 5.54e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLaSFKMWSKLN 169
Cdd:cd05629  78 LIMEFLPGGDLMTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGL-STGFHKQHD 156
                        90       100
                ....*....|....*....|
gi 3426027  170 NEEHNELREvdGTAKKNGGT 189
Cdd:cd05629 157 SAYYQKLLQ--GKSNKNRID 174
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
29-228 5.59e-09

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: 57.69  E-value: 5.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   29 GKVSLCFHRTQGLMI-MKTVYKGPnciehnEALLEEAKMMNRLRHSRVVKLLGVI--IEEGKYSL--VMEYMEKGNLMHV 103
Cdd:cd14172  18 GKVLECFHRRTGQKCaLKLLYDSP------KARREVEHHWRASGGPHIVHILDVYenMHHGKRCLliIMECMEGGELFSR 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  104 LKAEMSTPLSVK--GRIILEIIEGMCYLHGKGVIHKDLKPENILV---DNDFHIKIADLGLASfkmwsklNNEEHNELRE 178
Cdd:cd14172  92 IQERGDQAFTEReaSEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAK-------ETTVQNALQT 164
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 3426027  179 VDGTAkknggtlYYMAPEHLNDvnAKPTEKSDVYSFAVVLWAIFANKEPY 228
Cdd:cd14172 165 PCYTP-------YYVAPEVLGP--EKYDKSCDMWSLGVIMYILLCGFPPF 205
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
55-216 6.40e-09

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: 57.81  E-value: 6.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   55 EHNEALLEEAKMMNRLRHSR-VVKLLGVIIEEG------KYSLVMEYMEKGNLMHVLKAEMSTPLSVK--GRIILEIIEG 125
Cdd:cd06637  44 DEEEEIKQEINMLKKYSHHRnIATYYGAFIKKNppgmddQLWLVMEFCGAGSVTDLIKNTKGNTLKEEwiAYICREILRG 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  126 MCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnELREVDGTAKKNGGTLYYMAPEHLN-DVNAK 204
Cdd:cd06637 124 LSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSA-------------QLDRTVGRRNTFIGTPYWMAPEVIAcDENPD 190
                       170
                ....*....|....
gi 3426027  205 PTE--KSDVYSFAV 216
Cdd:cd06637 191 ATYdfKSDLWSLGI 204
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
41-281 6.70e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit, common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. Jaks are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271110 [Multi-domain]  Cd Length: 260  Bit Score: 57.22  E-value: 6.70e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   41 LMIMKTVYKgpNCiehNEALLEEAKMMNRLRHSRVVKLLGVIIeeGKYS-LVMEYMEKGNLMHVLKAEMS---TPLSVKG 116
Cdd:cd14208  35 LKVMDPTHG--NC---QESFLEAASIMSQISHKHLVLLHGVCV--GKDSiMVQEFVCHGALDLYLKKQQQkgpVAISWKL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  117 RIILEIIEGMCYLHGKGVIHKDLKPENILV------DNDFHIKIADLGLASFKMWSKLNNEEhnelrevdgtakknggtL 190
Cdd:cd14208 108 QVVKQLAYALNYLEDKQLVHGNVSAKKVLLsregdkGSPPFIKLSDPGVSIKVLDEELLAER-----------------I 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  191 YYMAPEHLNDVNAKPTEkSDVYSFAVVLWAIFANKEPYENAICEQQLIMCIKsgnrpdvDDITEYCPR--EIISLMKLCW 268
Cdd:cd14208 171 PWVAPECLSDPQNLALE-ADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYN-------DRKQLPAPHwiELASLIQQCM 242
                       250
                ....*....|...
gi 3426027  269 EANPEARPTFPGI 281
Cdd:cd14208 243 SYNPLLRPSFRAI 255
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
58-276 7.22e-09

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: 57.33  E-value: 7.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   58 EALLEEAKMMNRLRHSRVVKLLGVIiEEGKYSL--------------VMEYMEKGNLMHVLKA-EMSTPLSVKGriILEI 122
Cdd:cd14011  47 ELLKRGVKQLTRLRHPRILTVQHPL-EESRESLafatepvfaslanvLGERDNMPSPPPELQDyKLYDVEIKYG--LLQI 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  123 IEGMCYLHG-KGVIHKDLKPENILVDNDFHIKIADLGLAS--------FKMWSKLNNEEHNELREvdgtakknggTLYYM 193
Cdd:cd14011 124 SEALSFLHNdVKLVHGNICPESVVINSNGEWKLAGFDFCIsseqatdqFPYFREYDPNLPPLAQP----------NLNYL 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  194 APEHLNDVNAKPteKSDVYSFAVVLWAIFAN-KEPYENA-------ICEQQL-IMCIKSGNRPdvdditeycPREIISLM 264
Cdd:cd14011 194 APEYILSKTCDP--ASDMFSLGVLIYAIYNKgKPLFDCVnnllsykKNSNQLrQLSLSLLEKV---------PEELRDHV 262
                       250
                ....*....|..
gi 3426027  265 KLCWEANPEARP 276
Cdd:cd14011 263 KTLLNVTPEVRP 274
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
23-227 7.67e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 58.32  E-value: 7.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027    23 LDSGGFGKVSLCFHR---TQGLMIMKTVYKGPNciehneaLLEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGN 99
Cdd:PHA03207 100 LTPGSEGEVFVCTKHgdeQRKKVIVKAVTGGKT-------PGREIDILKTISHRAIINLIHAYRWKSTVCMVMPKYKCDL 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   100 LMHVlkaEMSTPLSVKGRIILE--IIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASfkmwsklnneehnELR 177
Cdd:PHA03207 173 FTYV---DRSGPLPLEQAITIQrrLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAAC-------------KLD 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 3426027   178 EVDGTAKKNG--GTLYYMAPEHLndvnAKPT--EKSDVYSFAVVLWAIFANKEP 227
Cdd:PHA03207 237 AHPDTPQCYGwsGTLETNSPELL----ALDPycAKTDIWSAGLVLFEMSVKNVT 286
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
63-221 7.92e-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: 57.76  E-value: 7.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   63 EAKMMNRLRHSRVVKLLGVIIEEG--KYSLVMEYMEKgNLMHVLKAEMST---------PLSVKGRIILEIIEGMCYLHG 131
Cdd:cd07868  64 EIALLRELKHPNVISLQKVFLSHAdrKVWLLFDYAEH-DLWHIIKFHRASkankkpvqlPRGMVKSLLYQILDGIHYLHA 142
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  132 KGVIHKDLKPENILVDND----FHIKIADLGLAsfkmwsKLNNEEHNELREVDGTAKknggTLYYMAPEHLndVNAKPte 207
Cdd:cd07868 143 NWVLHRDLKPANILVMGEgperGRVKIADMGFA------RLFNSPLKPLADLDPVVV----TFWYRAPELL--LGARH-- 208
                       170
                ....*....|....
gi 3426027  208 ksdvYSFAVVLWAI 221
Cdd:cd07868 209 ----YTKAIDIWAI 218
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
56-160 8.91e-09

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: 57.79  E-value: 8.91e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   56 HNEALLEEAKMMNRLRHSRVVKLLGVIIEEGKYS------LVMEYMEkGNLMHVLKAEMSTplSVKGRIILEIIEGMCYL 129
Cdd:cd07874  59 HAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEefqdvyLVMELMD-ANLCQVIQMELDH--ERMSYLLYQMLCGIKHL 135
                        90       100       110
                ....*....|....*....|....*....|.
gi 3426027  130 HGKGVIHKDLKPENILVDNDFHIKIADLGLA 160
Cdd:cd07874 136 HSAGIIHRDLKPSNIVVKSDCTLKILDFGLA 166
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
75-289 8.93e-09

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: 56.79  E-value: 8.93e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   75 VVKLLGVIIEEGKYSLVMEYMEKGNL------------MHVLKAEMSTPLSVKGRIIL----------EIIEGMCYLHGK 132
Cdd:cd05576  53 MVCLRKYIISEESVFLVLQHAEGGKLwsylskflndkeIHQLFADLDERLAAASRFYIpeeciqrwaaEMVVALDALHRE 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  133 GVIHKDLKPENILVDNDFHIKiadlgLASFKMWSKLNNeehnelrEVDGTAKKNggtlYYMAPEhlndVNA--KPTEKSD 210
Cdd:cd05576 133 GIVCRDLNPNNILLNDRGHIQ-----LTYFSRWSEVED-------SCDSDAIEN----MYCAPE----VGGisEETEACD 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  211 VYSFAVVLWAIFANKepyenaiceqQLIMCIKSG-NRPDVDDITEYCPREIISLMKLCWEANPEAR--PTFPGIEE-KFR 286
Cdd:cd05576 193 WWSLGALLFELLTGK----------ALVECHPAGiNTHTTLNIPEWVSEEARSLLQQLLQFNPTERlgAGVAGVEDiKSH 262

                ...
gi 3426027  287 PFY 289
Cdd:cd05576 263 PFF 265
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
61-213 9.16e-09

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: 57.14  E-value: 9.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   61 LEEAKMMNRLRHSRVVKLLGVIIEEGKYSLVMEYMEKGNLMHVLKAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLK 140
Cdd:cd13991  46 AEELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVK 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  141 PENILVDND-FHIKIADLGlasfkmwsklnneeHNELREVDGTAKKN------GGTLYYMAPEhlnDVNAKPTE-KSDVY 212
Cdd:cd13991 126 ADNVLLSSDgSDAFLCDFG--------------HAECLDPDGLGKSLftgdyiPGTETHMAPE---VVLGKPCDaKVDVW 188

                .
gi 3426027  213 S 213
Cdd:cd13991 189 S 189
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
90-289 1.11e-08

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: 57.36  E-value: 1.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027   90 LVMEYMEKGNLMHVL-KAEMSTPLSVKGRIILEIIEGMCYLHGKGVIHKDLKPENILVDNDFHIKIADLGlasfkmwSKL 168
Cdd:cd05597  78 LVMDYYCGGDLLTLLsKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-------SCL 150
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 3426027  169 nneehnELREvDGTAKKNG--GTLYYMAPEHL---NDVNAKPTEKSDVYSFAVVLWAIFANKEPY--ENAICEQQLIMCI 241
Cdd:cd05597 151 ------KLRE-DGTVQSSVavGTPDYISPEILqamEDGKGRYGPECDWWSLGVCMYEMLYGETPFyaESLVETYGKIMNH 223
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 3426027  242 KSGNR--PDVDDITEYCpREIISLMkLCweaNPEARPTFPGIEE-KFRPFY 289
Cdd:cd05597 224 KEHFSfpDDEDDVSEEA-KDLIRRL-IC---SRERRLGQNGIDDfKKHPFF 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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