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Conserved domains on  [gi|15225456|ref|NP_182059|]
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Leucine-rich repeat protein kinase family protein [Arabidopsis thaliana]

Protein Classification

leucine-rich repeat receptor-like protein kinase family protein( domain architecture ID 13746061)

leucine-rich repeat (LRR) receptor-like protein kinase (LRR-RLK) family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates, and may play crucial roles in a variety of different physiological processes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
423-687 3.63e-104

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: 318.45  E-value: 3.63e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskGRGECFLIYEFVPNGNLL 502
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCL--ESDEKLLVYEYMPNGSLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDvKDETGEVLEWATRVSIINGIARGIVYLHGEngNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFT-DDIVFSK 581
Cdd:cd14066  79 DRLH-CHKGSPPLPWPQRLKIAKGIARGLEYLHEE--CPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPpSESVSKT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 LKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISH-------LMILQAVES--GRLNEDFMDPNLRKNFP 652
Cdd:cd14066 156 SAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDEnrenasrKDLVEWVESkgKEELEDILDKRLVDDDG 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15225456 653 --EVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14066 236 veEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
PLN00113 super family cl33413
leucine-rich repeat receptor-like protein kinase; Provisional
80-684 3.98e-41

leucine-rich repeat receptor-like protein kinase; Provisional


The actual alignment was detected with superfamily member PLN00113:

Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 161.55  E-value: 3.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   80 LTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPLLTDLYLNVNNLSG-------EIPPL----------IGNL--- 139
Cdd:PLN00113 392 LEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGrinsrkwDMPSLqmlslarnkfFGGLpds 471
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  140 ---DNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNLFGPVPVKLAGAPLLEV 216
Cdd:PLN00113 472 fgsKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQ 551
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  217 LDIRNNSFSGFVPSALKRLNNGFQY--SNNHglcgdgftdlkactgLNGPNPnrpdPTNPtnFTTVDVKPESA--DLQRS 292
Cdd:PLN00113 552 LDLSQNQLSGEIPKNLGNVESLVQVniSHNH---------------LHGSLP----STGA--FLAINASAVAGniDLCGG 610
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  293 NCSNNNGGCSSKSLKSSPLGIVMGLIGSILAVAIfGGSTFTWYRRRKQKIGSSLDAMDGRISTEYNFKEVSRRKSSSPLI 372
Cdd:PLN00113 611 DTTSGLPPCKRVRKTPSWWFYITCTLGAFLVLAL-VAFGFVFIRGRNNLELKRVENEDGTWELQFFDSKVSKSITINDIL 689
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  373 SleyasgwdplgrgqssnnnsalsqevfesfmfnleeieratqSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSC 452
Cdd:PLN00113 690 S------------------------------------------SLKEENVISRGKKGASYKGKSIKNGMQFVVKEINDVN 727
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  453 KSDESEFLKGLKmltlLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLdvkdetgEVLEWATRVSIINGIARGIV 532
Cdd:PLN00113 728 SIPSSEIADMGK----LQHPNIVKLIGLCRSEK--GAYLIHEYIEGKNLSEVL-------RNLSWERRRKIAIGIAKALR 794
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  533 YLHGENgnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDdivFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGM 612
Cdd:PLN00113 795 FLHCRC--SPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTD---TKCFISSA---YVAPETRETKDITEKSDIYGFGL 866
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  613 ILLQILSGK--SKISHLMILQAVESGRLN------EDFMDPNLRKNFP--EVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:PLN00113 867 ILIELLTGKspADAEFGVHGSIVEWARYCysdchlDMWIDPSIRGDVSvnQNEIVEVMNLALHCTATDPTARPCANDVLK 946

                 ..
gi 15225456  683 EL 684
Cdd:PLN00113 947 TL 948
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
28-65 2.74e-05

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


:

Pssm-ID: 462411 [Multi-domain]  Cd Length: 41  Bit Score: 41.51  E-value: 2.74e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 15225456    28 DILLDIKSSLDPEKRFLTSWT-PDADPCssgSFDGVACD 65
Cdd:pfam08263   6 QALLAFKSSLNDPPGALSSWNsSSSDPC---SWTGVTCD 41
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
423-687 3.63e-104

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: 318.45  E-value: 3.63e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskGRGECFLIYEFVPNGNLL 502
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCL--ESDEKLLVYEYMPNGSLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDvKDETGEVLEWATRVSIINGIARGIVYLHGEngNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFT-DDIVFSK 581
Cdd:cd14066  79 DRLH-CHKGSPPLPWPQRLKIAKGIARGLEYLHEE--CPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPpSESVSKT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 LKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISH-------LMILQAVES--GRLNEDFMDPNLRKNFP 652
Cdd:cd14066 156 SAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDEnrenasrKDLVEWVESkgKEELEDILDKRLVDDDG 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15225456 653 --EVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14066 236 veEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
80-684 3.98e-41

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 161.55  E-value: 3.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   80 LTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPLLTDLYLNVNNLSG-------EIPPL----------IGNL--- 139
Cdd:PLN00113 392 LEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGrinsrkwDMPSLqmlslarnkfFGGLpds 471
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  140 ---DNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNLFGPVPVKLAGAPLLEV 216
Cdd:PLN00113 472 fgsKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQ 551
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  217 LDIRNNSFSGFVPSALKRLNNGFQY--SNNHglcgdgftdlkactgLNGPNPnrpdPTNPtnFTTVDVKPESA--DLQRS 292
Cdd:PLN00113 552 LDLSQNQLSGEIPKNLGNVESLVQVniSHNH---------------LHGSLP----STGA--FLAINASAVAGniDLCGG 610
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  293 NCSNNNGGCSSKSLKSSPLGIVMGLIGSILAVAIfGGSTFTWYRRRKQKIGSSLDAMDGRISTEYNFKEVSRRKSSSPLI 372
Cdd:PLN00113 611 DTTSGLPPCKRVRKTPSWWFYITCTLGAFLVLAL-VAFGFVFIRGRNNLELKRVENEDGTWELQFFDSKVSKSITINDIL 689
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  373 SleyasgwdplgrgqssnnnsalsqevfesfmfnleeieratqSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSC 452
Cdd:PLN00113 690 S------------------------------------------SLKEENVISRGKKGASYKGKSIKNGMQFVVKEINDVN 727
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  453 KSDESEFLKGLKmltlLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLdvkdetgEVLEWATRVSIINGIARGIV 532
Cdd:PLN00113 728 SIPSSEIADMGK----LQHPNIVKLIGLCRSEK--GAYLIHEYIEGKNLSEVL-------RNLSWERRRKIAIGIAKALR 794
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  533 YLHGENgnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDdivFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGM 612
Cdd:PLN00113 795 FLHCRC--SPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTD---TKCFISSA---YVAPETRETKDITEKSDIYGFGL 866
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  613 ILLQILSGK--SKISHLMILQAVESGRLN------EDFMDPNLRKNFP--EVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:PLN00113 867 ILIELLTGKspADAEFGVHGSIVEWARYCysdchlDMWIDPSIRGDVSvnQNEIVEVMNLALHCTATDPTARPCANDVLK 946

                 ..
gi 15225456  683 EL 684
Cdd:PLN00113 947 TL 948
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
423-684 1.95e-37

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 140.38  E-value: 1.95e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    423 LGKSNVSSVYKGILRDGSV-----AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGecFLIYEFVP 497
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGDgkeveVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPL--MIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    498 NGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:smart00221  85 GGDLLDYL--RKNRPKELSLSDLLSFALQIARGMEYLESKN-----FIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    578 VFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRlnedFMDPnlrknfPE 653
Cdd:smart00221 158 YYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEpypGMSNAEVLEYLKKGY----RLPK------PP 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 15225456    654 VEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:smart00221 228 NCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
420-684 1.98e-31

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: 123.38  E-value: 1.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   420 INLLGKSNVSSVYKGILRDGS-----VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcsKGRGECFLIYE 494
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTLKGEGentkiKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVC--TQGEPLYIVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   495 FVPNGNLLQYLDvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFT 574
Cdd:pfam07714  82 YMPGGDLLDFLR---KHKRKLTLKDLLSMALQIAKGMEYLESKN-----FVHRDLAARNCLVSENLVVKISDFGLSRDIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   575 DDIVFSKlkasAAMGYL-----APEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRlnedfmdp 645
Cdd:pfam07714 154 DDDYYRK----RGGGKLpikwmAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQpypGMSNEEVLEFLEDGY-------- 221
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 15225456   646 nlRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:pfam07714 222 --RLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
83-348 1.13e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.16  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  83 TIPPSIGLLTSLTGLYLHFNSLTGhIPKDISNLPLLTDLYLNVNNLSgEIPPLIGNLDNLQVIQLCYNKLSgSIPTQFGS 162
Cdd:COG4886 150 DLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLAN 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 163 LKKITVLALQYNQLSgAIPaSLGDIDTLTRLDLSFNNLFGpVPvKLAGAPLLEVLDIRNNSFSGFVPSALKRLNNGFQYS 242
Cdd:COG4886 227 LTNLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQLTD-LP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLL 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 243 NNHGLCGDGFTDLKACTGLNGPNPNRPDPTNPTNFTTVDVKPESADLQRSNCSNNNGGCSSKSLKSSPLGIVMGLIGSIL 322
Cdd:COG4886 303 LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTL 382
                       250       260
                ....*....|....*....|....*.
gi 15225456 323 AVAIFGGSTFTWYRRRKQKIGSSLDA 348
Cdd:COG4886 383 ALLLLTLLLLLLTTTAGVLLLTLALL 408
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
420-690 2.44e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 97.78  E-value: 2.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESE--FLKGLKMLTLLKHENLARLRGFccSKGRGECFLIYEFV 496
Cdd:COG0515  12 LRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEARerFRREARALARLNHPNIVRVYDV--GEEDGRPYLVMEYV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD 576
Cdd:COG0515  90 EGESLADLL----RRRGPLPPAEALRILAQLAEALAAAHAAG-----IVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 IVfskLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---SKISHLMILQAVESGRLnedfmdPNLRKN 650
Cdd:COG0515 161 TL---TQTGTVVGtpgYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRppfDGDSPAELLRAHLREPP------PPPSEL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 651 FPEVeAAQLARLGLLCTHESSNQRP-SMEDVIQELNNLAAD 690
Cdd:COG0515 232 RPDL-PPALDAIVLRALAKDPEERYqSAAELAAALRAVLRS 271
PHA02988 PHA02988
hypothetical protein; Provisional
401-684 3.72e-10

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 61.30  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  401 ESFMFNLEEIERATQSFSEINLLGKSNVSSVYKGILRDGSVAaIKCIAKSS--CKSDESEFLKGLKMLTLLKHENLARLR 478
Cdd:PHA02988   6 RSYINDIKCIESDDIDKYTSVLIKENDQNSIYKGIFNNKEVI-IRTFKKFHkgHKVLIDITENEIKNLRRIDSNNILKIY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  479 GFCCSKGRGECF--LIYEFVPNGNLLQYLDVKDEtgevLEWATRVSIINGIARGIVYLHgENGNKPaivHQNLSAEKILI 556
Cdd:PHA02988  85 GFIIDIVDDLPRlsLILEYCTRGYLREVLDKEKD----LSFKTKLDMAIDCCKGLYNLY-KYTNKP---YKNLTSVSFLV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  557 DHWYNPSLADSGLHKLFTDdivfSKLKASAAMGYLAPEYITT--GRFTDKSDVYAFGMILLQILSGKSKISHL------- 627
Cdd:PHA02988 157 TENYKLKIICHGLEKILSS----PPFKNVNFMVYFSYKMLNDifSEYTIKDDIYSLGVVLWEIFTGKIPFENLttkeiyd 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456  628 MILQAVESGRLNEDfmDPNLRKNFpeVEAaqlarlgllCTHESSNQRPSMEDVIQEL 684
Cdd:PHA02988 233 LIINKNNSLKLPLD--CPLEIKCI--VEA---------CTSHDSIKRPNIKEILYNL 276
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
68-227 1.28e-08

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 55.95  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  68 RRVANISLQGMGLTgtippSIGLL---TSLTGLYLHFNSLTgHIPKdISNLPLLTDLYLNVNNLSgEIPPLiGNLDNLQV 144
Cdd:cd21340   2 KRITHLYLNDKNIT-----KIDNLslcKNLKVLYLYDNKIT-KIEN-LEFLTNLTHLYLQNNQIE-KIENL-ENLVNLKK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 145 IQLCYNKLS---GsiptqFGSLKKITVLALQYNQL-SGAI----PASLGDI-DTLTRLDLSFNNLFGPVPvkLAGAPLLE 215
Cdd:cd21340  73 LYLGGNRISvveG-----LENLTNLEELHIENQRLpPGEKltfdPRSLAALsNSLRVLNISGNNIDSLEP--LAPLRNLE 145
                       170
                ....*....|..
gi 15225456 216 VLDIRNNSFSGF 227
Cdd:cd21340 146 QLDASNNQISDL 157
LRR_8 pfam13855
Leucine rich repeat;
141-200 5.55e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.05  E-value: 5.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   141 NLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNL 200
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
28-65 2.74e-05

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 462411 [Multi-domain]  Cd Length: 41  Bit Score: 41.51  E-value: 2.74e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 15225456    28 DILLDIKSSLDPEKRFLTSWT-PDADPCssgSFDGVACD 65
Cdd:pfam08263   6 QALLAFKSSLNDPPGALSSWNsSSSDPC---SWTGVTCD 41
 
Name Accession Description Interval E-value
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
423-687 3.63e-104

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: 318.45  E-value: 3.63e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskGRGECFLIYEFVPNGNLL 502
Cdd:cd14066   1 IGSGGFGTVYKGVLENGTVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCL--ESDEKLLVYEYMPNGSLE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDvKDETGEVLEWATRVSIINGIARGIVYLHGEngNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFT-DDIVFSK 581
Cdd:cd14066  79 DRLH-CHKGSPPLPWPQRLKIAKGIARGLEYLHEE--CPPPIIHGDIKSSNILLDEDFEPKLTDFGLARLIPpSESVSKT 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 LKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISH-------LMILQAVES--GRLNEDFMDPNLRKNFP 652
Cdd:cd14066 156 SAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLTGKPAVDEnrenasrKDLVEWVESkgKEELEDILDKRLVDDDG 235
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15225456 653 --EVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14066 236 veEEEVEALLRLALLCTRSDPSLRPSMKEVVQMLEKL 272
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
423-686 6.09e-54

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: 186.16  E-value: 6.09e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLL 502
Cdd:cd14664   1 IGRGGAGTVYKGVMPNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPT--TNLLVYEYMPNGSLG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENgnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd14664  79 ELLHSRPESQPPLDWETRQRIALGSARGLAYLHHDC--SPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMS 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISH------LMILQAV----ESGRLnEDFMDPNLRKNFP 652
Cdd:cd14664 157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELITGKRPFDEaflddgVDIVDWVrgllEEKKV-EALVDPDLQGVYK 235
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 653 EVEAAQLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd14664 236 LEEVEQVFQVALLCTQSSPMERPTMREVVRMLEG 269
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
431-684 4.53e-43

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 155.77  E-value: 4.53e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 431 VYKGILRDGSVAaIKCI-AKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcsKGRGECFLIYEFVPNGNLLQYLDVKD 509
Cdd:cd13999   9 VYKGKWRGTDVA-IKKLkVEDDNDELLKEFRREVSILSKLRHPNIVQFIGAC--LSPPPLCIVTEYMPGGSLYDLLHKKK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 510 EtgeVLEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDdivfSKLKASAAMG 589
Cdd:cd13999  86 I---PLSWSLRLKIALDIARGMNYLH-----SPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNS----TTEKMTGVVG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 590 ---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---SKISHLMILQAVesgrlNEDFMDPNLRKNFPEveaaQLARLG 663
Cdd:cd13999 154 tprWMAPEVLRGEPYTEKADVYSFGIVLWELLTGEvpfKELSPIQIAAAV-----VQKGLRPPIPPDCPP----ELSKLI 224
                       250       260
                ....*....|....*....|.
gi 15225456 664 LLCTHESSNQRPSMEDVIQEL 684
Cdd:cd13999 225 KRCWNEDPEKRPSFSEIVKRL 245
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
80-684 3.98e-41

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 161.55  E-value: 3.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   80 LTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPLLTDLYLNVNNLSG-------EIPPL----------IGNL--- 139
Cdd:PLN00113 392 LEGEIPKSLGACRSLRRVRLQDNSFSGELPSEFTKLPLVYFLDISNNNLQGrinsrkwDMPSLqmlslarnkfFGGLpds 471
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  140 ---DNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNLFGPVPVKLAGAPLLEV 216
Cdd:PLN00113 472 fgsKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLSGQIPASFSEMPVLSQ 551
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  217 LDIRNNSFSGFVPSALKRLNNGFQY--SNNHglcgdgftdlkactgLNGPNPnrpdPTNPtnFTTVDVKPESA--DLQRS 292
Cdd:PLN00113 552 LDLSQNQLSGEIPKNLGNVESLVQVniSHNH---------------LHGSLP----STGA--FLAINASAVAGniDLCGG 610
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  293 NCSNNNGGCSSKSLKSSPLGIVMGLIGSILAVAIfGGSTFTWYRRRKQKIGSSLDAMDGRISTEYNFKEVSRRKSSSPLI 372
Cdd:PLN00113 611 DTTSGLPPCKRVRKTPSWWFYITCTLGAFLVLAL-VAFGFVFIRGRNNLELKRVENEDGTWELQFFDSKVSKSITINDIL 689
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  373 SleyasgwdplgrgqssnnnsalsqevfesfmfnleeieratqSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSC 452
Cdd:PLN00113 690 S------------------------------------------SLKEENVISRGKKGASYKGKSIKNGMQFVVKEINDVN 727
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  453 KSDESEFLKGLKmltlLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLdvkdetgEVLEWATRVSIINGIARGIV 532
Cdd:PLN00113 728 SIPSSEIADMGK----LQHPNIVKLIGLCRSEK--GAYLIHEYIEGKNLSEVL-------RNLSWERRRKIAIGIAKALR 794
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  533 YLHGENgnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDdivFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGM 612
Cdd:PLN00113 795 FLHCRC--SPAVVVGNLSPEKIIIDGKDEPHLRLSLPGLLCTD---TKCFISSA---YVAPETRETKDITEKSDIYGFGL 866
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  613 ILLQILSGK--SKISHLMILQAVESGRLN------EDFMDPNLRKNFP--EVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:PLN00113 867 ILIELLTGKspADAEFGVHGSIVEWARYCysdchlDMWIDPSIRGDVSvnQNEIVEVMNLALHCTATDPTARPCANDVLK 946

                 ..
gi 15225456  683 EL 684
Cdd:PLN00113 947 TL 948
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
423-684 1.95e-37

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


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 140.38  E-value: 1.95e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    423 LGKSNVSSVYKGILRDGSV-----AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGecFLIYEFVP 497
Cdd:smart00221   7 LGEGAFGEVYKGTLKGKGDgkeveVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPL--MIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    498 NGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:smart00221  85 GGDLLDYL--RKNRPKELSLSDLLSFALQIARGMEYLESKN-----FIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    578 VFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRlnedFMDPnlrknfPE 653
Cdd:smart00221 158 YYKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEEpypGMSNAEVLEYLKKGY----RLPK------PP 227
                          250       260       270
                   ....*....|....*....|....*....|.
gi 15225456    654 VEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:smart00221 228 NCPPELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
423-684 6.24e-37

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 138.82  E-value: 6.24e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    423 LGKSNVSSVYKGILRDGSVA-----AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGecFLIYEFVP 497
Cdd:smart00219   7 LGEGAFGEVYKGKLKGKGGKkkvevAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPL--YIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    498 NGNLLQYLdvKDeTGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:smart00219  85 GGDLLSYL--RK-NRPKLSLSDLLSFALQIARGMEYLESKN-----FIHRDLAARNCLVGENLVVKISDFGLSRDLYDDD 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    578 VFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRlnedfmdpnlRKNFPE 653
Cdd:smart00219 157 YYRKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTlGEQpypGMSNEEVLEYLKNGY----------RLPQPP 226
                          250       260       270
                   ....*....|....*....|....*....|.
gi 15225456    654 VEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:smart00219 227 NCPPELYDLMLQCWAEDPEDRPTFSELVEIL 257
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
421-684 5.43e-36

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: 136.51  E-value: 5.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRDGS----VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFV 496
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGDgktvDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEE--PLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL-----DVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL-H 570
Cdd:cd00192  79 EGGDLLDFLrksrpVFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKK-----FVHRDLAARNCLVGEDLVVKISDFGLsR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESG-RLnedfmdp 645
Cdd:cd00192 154 DIYDDDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTlGATpypGLSNEEVLEYLRKGyRL------- 226
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15225456 646 nlrkNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd00192 227 ----PKPENCPDELYELMLSCWQLDPEDRPTFSELVERL 261
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
407-687 3.77e-35

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: 134.93  E-value: 3.77e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 407 LEEIERATQSFSEI------NLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDE--SEFLKGLKMLTLLKHENLARLR 478
Cdd:cd14158   1 FHELKNMTNNFDERpisvggNKLGEGGFGVVFKGYINDKNVAVKKLAAMVDISTEDltKQFEQEIQVMAKCQHENLVELL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 479 GFCCSkGRGECfLIYEFVPNGNLLQYLDVKDETgEVLEWATRVSIINGIARGIVYLHgENgnkpAIVHQNLSAEKILIDH 558
Cdd:cd14158  81 GYSCD-GPQLC-LVYTYMPNGSLLDRLACLNDT-PPLSWHMRCKIAQGTANGINYLH-EN----NHIHRDIKSANILLDE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 559 WYNPSLADSGLHKL---FTDDIVFSKLKASAAmgYLAPEYITtGRFTDKSDVYAFGMILLQILSG-----KSKISHLM-- 628
Cdd:cd14158 153 TFVPKISDFGLARAsekFSQTIMTERIVGTTA--YMAPEALR-GEITPKSDIFSFGVVLLEIITGlppvdENRDPQLLld 229
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 629 ILQAVESGRLN-EDFMDPNLrKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14158 230 IKEEIEDEEKTiEDYVDKKM-GDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
423-617 1.18e-31

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: 122.38  E-value: 1.18e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcsKGRGECFLIYEFVPNGNL 501
Cdd:cd00180   1 LGKGSFGKVYKARDKeTGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVF--ETENFLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL-HKLFTDDIVFS 580
Cdd:cd00180  79 KDLLKENKGP---LSEEEALSILRQLLSALEYLHSNG-----IIHRDLKPENILLDSDGTVKLADFGLaKDLDSDDSLLK 150
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 15225456 581 KLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQI 617
Cdd:cd00180 151 TTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
420-684 1.98e-31

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: 123.38  E-value: 1.98e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   420 INLLGKSNVSSVYKGILRDGS-----VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcsKGRGECFLIYE 494
Cdd:pfam07714   4 GEKLGEGAFGEVYKGTLKGEGentkiKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVC--TQGEPLYIVTE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   495 FVPNGNLLQYLDvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFT 574
Cdd:pfam07714  82 YMPGGDLLDFLR---KHKRKLTLKDLLSMALQIAKGMEYLESKN-----FVHRDLAARNCLVSENLVVKISDFGLSRDIY 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   575 DDIVFSKlkasAAMGYL-----APEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRlnedfmdp 645
Cdd:pfam07714 154 DDDYYRK----RGGGKLpikwmAPESLKDGKFTSKSDVWSFGVLLWEIFTlGEQpypGMSNEEVLEFLEDGY-------- 221
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 15225456   646 nlRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:pfam07714 222 --RLPQPENCPDELYDLMKQCWAYDPEDRPTFSELVEDL 258
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
28-243 4.91e-30

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 126.89  E-value: 4.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   28 DILLDIKSSLDPEKRFLTSWTPDADPCssgSFDGVACDGNRRVANISLQGMGLTGTIPPSIGLLTSLTGLYLHFNSLTGH 107
Cdd:PLN00113  32 ELLLSFKSSINDPLKYLSNWNSSADVC---LWQGITCNNSSRVVSIDLSGKNISGKISSAIFRLPYIQTINLSNNQLSGP 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  108 IPKDI------------SN-----------LPLLTDLYLNVNNLSGEIPPLIGNLDNLQVIQLCYNKLSGSIPTQFGSLK 164
Cdd:PLN00113 109 IPDDIfttssslrylnlSNnnftgsiprgsIPNLETLDLSNNMLSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLT 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  165 KITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNLFGPVPVKLAGAPLLEVLDIRNNSFSGFVPSALKRLNN---GFQY 241
Cdd:PLN00113 189 SLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNlqyLFLY 268

                 ..
gi 15225456  242 SN 243
Cdd:PLN00113 269 QN 270
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
423-687 5.99e-30

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: 120.32  E-value: 5.99e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDgSVAAIKCIAKSS---CKSDESEFLKGLKMLTLLKHENLARLRGFCCSkgRGECFLIYEFVPNG 499
Cdd:cd14159   1 IGEGGFGCVYQAVMRN-TEYAVKRLKEDSeldWSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQ--QGNYCLIYVYLPNG 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDVKDETgEVLEWATRVSIINGIARGIVYLHGENgnkPAIVHQNLSAEKILIDHWYNPSLADSGLHKlftddivF 579
Cdd:cd14159  78 SLEDRLHCQVSC-PCLSWSQRLHVLLGTARAIQYLHSDS---PSLIHGDVKSSNILLDAALNPKLGDFGLAR-------F 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 580 SKLKASAAM--------------GYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKI-----SHLMIL---------- 630
Cdd:cd14159 147 SRRPKQPGMsstlartqtvrgtlAYLPEEYVKTGTLSVEIDVYSFGVVLLELLTGRRAMevdscSPTKYLkdlvkeeeea 226
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225456 631 -------------QAVESG-RLNEDFMDPNLRKNFPEVeAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14159 227 qhtpttmthsaeaQAAQLAtSICQKHLDPQAGPCPPEL-GIEISQLACRCLHRRAKKRPPMTEVFQELERL 296
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
80-237 2.08e-28

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 121.88  E-value: 2.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   80 LTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPLLTDLYLNVNNLSGEIPPLIGNLDNLQVIQLCYNKLSGSIPTQ 159
Cdd:PLN00113 152 LSGEIPNDIGSFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVGQIPRELGQMKSLKWIYLGYNNLSGEIPYE 231
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456  160 FGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNLFGPVPVKLAGAPLLEVLDIRNNSFSGFVPSALKRLNN 237
Cdd:PLN00113 232 IGGLTSLNHLDLVYNNLTGPIPSSLGNLKNLQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNSLSGEIPELVIQLQN 309
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
423-687 2.41e-28

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: 114.98  E-value: 2.41e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAA--IKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgECfLIYEFVPNGN 500
Cdd:cd14160   1 IGEGEIFEVYRVRIGNRSYAVklFKQEKKMQWKKHWKRFLSELEVLLLFQHPNILELAAYFTETEK-FC-LVYPYMQNGT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDVKDETGEvLEWATRVSIINGIARGIVYLHgeNGNKPAIVHQNLSAEKILIDHWYNPSLADSGL-----HKLFTD 575
Cdd:cd14160  79 LFDRLQCHGVTKP-LSWHERINILIGIAKAIHYLH--NSQPCTVICGNISSANILLDDQMQPKLTDFALahfrpHLEDQS 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 576 DIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG---KSKISHLMILQAVESGRLNEDFMDPNLR---- 648
Cdd:cd14160 156 CTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGckvVLDDPKHLQLRDLLHELMEKRGLDSCLSfldl 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 649 --KNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14160 236 kfPPCPRNFSAKLFRLAGRCTATKAKLRPDMDEVLQRLEST 276
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
423-684 3.11e-28

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: 114.09  E-value: 3.11e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSV-AAIKCIAKSSCKSDESE-FLKGLKMLTLLKHENLARLRGFCcsKGRGECFLIYEFVPNGN 500
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGmVAIKCLHSSPNCIEERKaLLKEAEKMERARHSYVLPLLGVC--VERRSLGLVMEYMENGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFS 580
Cdd:cd13978  79 LKSLLEREIQD---VPWSLRFRIIHEIALGMNFLHNMD---PPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISAN 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 581 KLKASAAMG----YLAPEYITTG--RFTDKSDVYAFGMILLQILSGK----SKISHLMILQAVESGRlnedfmdpnlRKN 650
Cdd:cd13978 153 RRRGTENLGgtpiYMAPEAFDDFnkKPTSKSDVYSFAIVIWAVLTRKepfeNAINPLLIMQIVSKGD----------RPS 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 651 FPEVEAAQ-------LARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd13978 223 LDDIGRLKqienvqeLISLMIRCWDGNPDARPTFLECLDRL 263
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
417-682 1.01e-26

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 109.54  E-value: 1.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    417 FSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEF 495
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARdKKTGKLVAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDED--KLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    496 VPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTD 575
Cdd:smart00220  79 CEGGDLFDLLK---KRGRLSEDEAR-FYLRQILSALEYLHSKG-----IVHRDLKPENILLDEDGHVKLADFGLARQLDP 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456    576 DIVFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKS----KISHLMILQAVESGRLNEDFMDPNLRKnf 651
Cdd:smart00220 150 GEKLTTFVGTPE--YMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPpfpgDDQLLELFKKIGKPKPPFPPPEWDISP-- 225
                          250       260       270
                   ....*....|....*....|....*....|.
gi 15225456    652 pevEAAQLARlGLLCTHesSNQRPSMEDVIQ 682
Cdd:smart00220 226 ---EAKDLIR-KLLVKD--PEKRLTAEEALQ 250
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
420-688 2.21e-25

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: 106.70  E-value: 2.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKG---ILRD--GSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYE 494
Cdd:cd05038   9 IKQLGEGHFGSVELCrydPLGDntGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPGRRSLRLIME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLdvkDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFT 574
Cdd:cd05038  89 YLPSGSLRDYL---QRHRDQIDLKRLLLFASQICKGMEYLGSQR-----YIHRDLAARNILVESEDLVKISDFGLAKVLP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 --DDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESG---------RLNEdFM 643
Cdd:cd05038 161 edKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGiaqgqmivtRLLE-LL 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15225456 644 DPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLA 688
Cdd:cd05038 240 KSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
423-678 4.94e-24

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: 101.59  E-value: 4.94e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDEseFLKGLKMLTLLKHENLARLRGFCcskGRGE-CFLIYEFVPNGNL 501
Cdd:cd05034   3 LGAGQFGEVWMGVWNGTTKVAVKTLKPGTMSPEA--FLQEAQIMKKLRHDKLVQLYAVC---SDEEpIYIVTELMSKGSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSK 581
Cdd:cd05034  78 LDYL--RTGEGRALRLPQLIDMAAQIASGMAYLESRN-----YIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAR 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 LKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLM----ILQAVESGrlnedfmdpnLRKNFPEVEAA 657
Cdd:cd05034 151 EGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMtnreVLEQVERG----------YRMPKPPGCPD 220
                       250       260
                ....*....|....*....|.
gi 15225456 658 QLARLGLLCTHESSNQRPSME 678
Cdd:cd05034 221 ELYDIMLQCWKKEPEERPTFE 241
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
420-690 1.35e-23

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: 101.34  E-value: 1.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILR-DGSVA----AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIYE 494
Cdd:cd05057  12 GKVLGSGAFGTVYKGVWIpEGEKVkipvAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSS---QVQLITQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYldVKDETGEV-----LEWATRvsiingIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd05057  89 LMPLGCLLDY--VRNHRDNIgsqllLNWCVQ------IAKGMSYLE-EKR----LVHRDLAARNVLVKTPNHVKITDFGL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 570 HKLFtdDIVFSKLKASAAM---GYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESG-RLNEd 641
Cdd:cd05057 156 AKLL--DVDEKEYHAEGGKvpiKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKpyegIPAVEIPDLLEKGeRLPQ- 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15225456 642 fmdpnlrknfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05057 233 ----------PPICTIDVYMVLVKCWMIDAESRPTFKELANEFSKMARD 271
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
411-686 5.35e-23

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: 99.05  E-value: 5.35e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 411 ERATQSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIaKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcSKGRgECF 490
Cdd:cd05148   2 ERPREEFTLERKLGSGYFGEVWEGLWKNRVRVAIKIL-KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVC-SVGE-PVY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLH 570
Cdd:cd05148  79 IITELMEKGSLLAFL--RSPEGQVLPVASLIDMACQVAEGMAYLEEQN-----SIHRDLAARNILVGEDLVCKVADFGLA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLFTDDiVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSgKSKISHlmilqaveSGRLNE---DFMDPNL 647
Cdd:cd05148 152 RLIKED-VYLSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFT-YGQVPY--------PGMNNHevyDQITAGY 221
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15225456 648 RKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd05148 222 RMPCPAKCPQEIYKIMLECWAAEPEDRPSFKALREELDN 260
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
409-687 6.49e-23

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: 98.65  E-value: 6.49e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERatqsfSEI---NLLGKSNVSSVYKGIL-RDGSVAAIKCIAKSSCKSDEseFLKGLKMLTLLKHENLARLRGFCCSK 484
Cdd:cd05052   2 EIER-----TDItmkHKLGGGQYGEVYEGVWkKYNLTVAVKTLKEDTMEVEE--FLKEAAVMKEIKHPNLVQLLGVCTRE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 485 GrgECFLIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05052  75 P--PFYIITEFMPYGNLLDYL--RECNREELNAVVLLYMATQIASAMEYLEKKN-----FIHRDLAARNCLVGENHLVKV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 565 ADSGLHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQI----LSGKSKISHLMILQAVESGrlne 640
Cdd:cd05052 146 ADFGLSRLMTGDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIatygMSPYPGIDLSQVYELLEKG---- 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 641 dfmdpnLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05052 222 ------YRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
420-680 6.91e-23

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: 99.32  E-value: 6.91e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYK---GILRD--GSVAAIKCIAKSScKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYE 494
Cdd:cd14205   9 LQQLGKGNFGSVEMcryDPLQDntGEVVAVKKLQHST-EEHLRDFEREIEILKSLQHDNIVKYKGVCYSAGRRNLRLIME 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLDVKDET---GEVLEWATRvsiingIARGIVYLhgengNKPAIVHQNLSAEKILIDHWYNPSLADSGLHK 571
Cdd:cd14205  88 YLPYGSLRDYLQKHKERidhIKLLQYTSQ------ICKGMEYL-----GTKRYIHRDLATRNILVENENRVKIGDFGLTK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 572 LFTDDIVFSKLK--ASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQIL--SGKSKISHLMILQAVESGRLNE------- 640
Cdd:cd14205 157 VLPQDKEYYKVKepGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFtyIEKSKSPPAEFMRMIGNDKQGQmivfhli 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15225456 641 DFMDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDV 680
Cdd:cd14205 237 ELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDL 276
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
83-348 1.13e-22

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 101.16  E-value: 1.13e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  83 TIPPSIGLLTSLTGLYLHFNSLTGhIPKDISNLPLLTDLYLNVNNLSgEIPPLIGNLDNLQVIQLCYNKLSgSIPTQFGS 162
Cdd:COG4886 150 DLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTNLKELDLSNNQIT-DLPEPLGNLTNLEELDLSGNQLT-DLPEPLAN 226
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 163 LKKITVLALQYNQLSgAIPaSLGDIDTLTRLDLSFNNLFGpVPvKLAGAPLLEVLDIRNNSFSGFVPSALKRLNNGFQYS 242
Cdd:COG4886 227 LTNLETLDLSNNQLT-DLP-ELGNLTNLEELDLSNNQLTD-LP-PLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLL 302
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 243 NNHGLCGDGFTDLKACTGLNGPNPNRPDPTNPTNFTTVDVKPESADLQRSNCSNNNGGCSSKSLKSSPLGIVMGLIGSIL 322
Cdd:COG4886 303 LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTL 382
                       250       260
                ....*....|....*....|....*.
gi 15225456 323 AVAIFGGSTFTWYRRRKQKIGSSLDA 348
Cdd:COG4886 383 ALLLLTLLLLLLTTTAGVLLLTLALL 408
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
415-687 1.16e-22

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: 97.81  E-value: 1.16e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGILRDGSVAaIKCIAKSSCKSDEseFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYE 494
Cdd:cd05039   6 KDLKLGELIGKGEFGDVMLGDYRGQKVA-VKCLKDDSTAAQA--FLAEASVMTTLRHPNLVQLLGVVLEGN--GLYIVTE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLDVKDETgeVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFT 574
Cdd:cd05039  81 YMAKGSLVDYLRSRGRA--VITRKDQLGFALDVCEGMEYLESKK-----FVHRDLAARNVLVSEDNVAKVSDFGLAKEAS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIVFSKLkasaAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESG-RlnedfMDPnlrk 649
Cdd:cd05039 154 SNQDGGKL----PIKWTAPEALREKKFSTKSDVWSFGILLWEIYSfGRVpypRIPLKDVVPHVEKGyR-----MEA---- 220
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15225456 650 nfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05039 221 --PEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEHI 256
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
420-690 2.44e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 97.78  E-value: 2.44e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESE--FLKGLKMLTLLKHENLARLRGFccSKGRGECFLIYEFV 496
Cdd:COG0515  12 LRLLGRGGMGVVYLARdLRLGRPVALKVLRPELAADPEARerFRREARALARLNHPNIVRVYDV--GEEDGRPYLVMEYV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD 576
Cdd:COG0515  90 EGESLADLL----RRRGPLPPAEALRILAQLAEALAAAHAAG-----IVHRDIKPANILLTPDGRVKLIDFGIARALGGA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 IVfskLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---SKISHLMILQAVESGRLnedfmdPNLRKN 650
Cdd:COG0515 161 TL---TQTGTVVGtpgYMAPEQARGEPVDPRSDVYSLGVTLYELLTGRppfDGDSPAELLRAHLREPP------PPPSEL 231
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 651 FPEVeAAQLARLGLLCTHESSNQRP-SMEDVIQELNNLAAD 690
Cdd:COG0515 232 RPDL-PPALDAIVLRALAKDPEERYqSAAELAAALRAVLRS 271
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
422-684 2.54e-21

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: 93.92  E-value: 2.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGSVAAIKciaksSCKSD-----ESEFLKGLKMLTLLKHENLARLRGFCCSkgRGECFLIYEFV 496
Cdd:cd05085   3 LLGKGNFGEVYKGTLKDKTPVAVK-----TCKEDlpqelKIKFLSEARILKQYDHPNIVKLIGVCTQ--RQPIYIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL-DVKDE--TGEVLEWATRVsiingiARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF 573
Cdd:cd05085  76 PGGDFLSFLrKKKDElkTKQLVKFSLDA------AAGMAYLESKN-----CIHRDLAARNCLVGENNALKISDFGMSRQE 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 574 TDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVESgrlnedfMDPNLRKNFP 652
Cdd:cd05085 145 DDGVYSSSGLKQIPIKWTAPEALNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQAREQ-------VEKGYRMSAP 217
                       250       260       270
                ....*....|....*....|....*....|..
gi 15225456 653 EVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05085 218 QRCPEDIYKIMQRCWDYNPENRPKFSELQKEL 249
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
423-691 3.36e-21

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


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 93.66  E-value: 3.36e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAaIKCIAKSSCKSDeseFLKGLKMLTLLKHENLARLRGfCCSKGRGECfLIYEFVPNGNLL 502
Cdd:cd14058   1 VGRGSFGVVCKARWRNQIVA-VKIIESESEKKA---FEVEVRQLSRVDHPNIIKLYG-ACSNQKPVC-LVMEYAEGGSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDE-----TGEVLEWATRVsiingiARGIVYLHGEngnKP-AIVHQNLSAEKILIdhwYNPS----LADSGL--- 569
Cdd:cd14058  75 NVLHGKEPkpiytAAHAMSWALQC------AKGVAYLHSM---KPkALIHRDLKPPNLLL---TNGGtvlkICDFGTacd 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 570 -HKLFTDDivfsklKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHL-----MILQAVESGRlnedfm 643
Cdd:cd14058 143 iSTHMTNN------KGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEVITRRKPFDHIggpafRIMWAVHNGE------ 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 644 DPNLRKNFPEVeaaqLARLGLLCTHESSNQRPSMEDVIQELNNLAADY 691
Cdd:cd14058 209 RPPLIKNCPKP----IESLMTRCWSKDPEKRPSMKEIVKIMSHLMQFF 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
420-682 9.34e-21

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: 92.15  E-value: 9.34e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKS-DESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVP 497
Cdd:cd05117   5 GKVLGRGSFGVVRLAVHKkTGEEYAVKIIDKKKLKSeDEEMLRREIEILKRLDHPNIVKLYEVFEDDKN--LYLVMELCT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDvkdETGEVLEWATRVsIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPS---LADSGLHKLFT 574
Cdd:cd05117  83 GGELFDRIV---KKGSFSEREAAK-IMKQILSAVAYLH-SQG----IVHRDLKPENILLASKDPDSpikIIDFGLAKIFE 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIVFSKLKASAamGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKI---SHLMILQAVESGRLNedfMDPnlrKNF 651
Cdd:cd05117 154 EGEKLKTVCGTP--YYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFygeTEQELFEKILKGKYS---FDS---PEW 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 15225456 652 PEV--EAAQLARlGLLCTheSSNQRPSMEDVIQ 682
Cdd:cd05117 226 KNVseEAKDLIK-RLLVV--DPKKRLTAAEALN 255
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
422-687 1.52e-20

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: 91.96  E-value: 1.52e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGIL----RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFVP 497
Cdd:cd05063  12 VIGAGEFGEVFRGILkmpgRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEG-VVTKFK-PAMIITEYME 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLdvKDETGEVLEWATrVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD- 576
Cdd:cd05063  90 NGALDKYL--RDHDGEFSSYQL-VGMLRGIAAGMKYLSDMN-----YVHRDLAARNILVNSNLECKVSDFGLSRVLEDDp 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 -IVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVesgrlNEDFMDPNlrknf 651
Cdd:cd05063 162 eGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERpywdMSNHEVMKAI-----NDGFRLPA----- 231
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15225456 652 PEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05063 232 PMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLDKL 267
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
423-676 1.70e-20

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: 91.64  E-value: 1.70e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR--DGSV--AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcskgRGECF-LIYEFVP 497
Cdd:cd05060   3 LGHGNFGSVRKGVYLmkSGKEveVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVC----KGEPLmLVMELAP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDETG--EVLEWATRVsiingiARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFT 574
Cdd:cd05060  79 LGPLLKYLKKRREIPvsDLKELAHQV------AMGMAYLESKH-----FVHRDLAARNVLLVNRHQAKISDFGMSRaLGA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDivfSKLKASAA----MGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESGrlnedfmdpn 646
Cdd:cd05060 148 GS---DYYRATTAgrwpLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKpygeMKGPEVIAMLESG---------- 214
                       250       260       270
                ....*....|....*....|....*....|
gi 15225456 647 LRKNFPEVEAAQLARLGLLCTHESSNQRPS 676
Cdd:cd05060 215 ERLPRPEECPQEIYSIMLSCWKYRPEDRPT 244
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
423-684 2.91e-20

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: 90.58  E-value: 2.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR-DGSVAAIKciaksSCKSDESE-----FLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFV 496
Cdd:cd05041   3 IGRGNFGDVYRGVLKpDNTEVAVK-----TCRETLPPdlkrkFLQEARILKQYDHPNIVKLIGVCVQKQ--PIMIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDVKdetGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD 576
Cdd:cd05041  76 PGGSLLTFLRKK---GARLTVKQLLQMCLDAAAGMEYLESKN-----CIHRDLAARNCLVGENNVLKISDFGMSREEEDG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 I--VFSKLKaSAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMilqaveSGRLNEDFMDPNLRKNFPEV 654
Cdd:cd05041 148 EytVSDGLK-QIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGM------SNQQTREQIESGYRMPAPEL 220
                       250       260       270
                ....*....|....*....|....*....|
gi 15225456 655 EAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05041 221 CPEAVYRLMLQCWAYDPENRPSFSEIYNEL 250
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
409-679 3.91e-20

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


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 90.93  E-value: 3.91e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERatQSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSckSDESEFLKGLKMLTLLKHENLARLRGFCCskgRGE 488
Cdd:cd05068   4 EIDR--KSLKLLRKLGSGQFGEVWEGLWNNTTPVAVKTLKPGT--MDPEDFLREAQIMKKLRHPKLIQLYAVCT---LEE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 -CFLIYEFVPNGNLLQYLDVKdetGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADS 567
Cdd:cd05068  77 pIYIITELMKHGSLLEYLQGK---GRSLQLPQLIDMAAQVASGMAYLESQN-----YIHRDLAARNVLVGENNICKVADF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 568 GLHKLF-TDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GK---SKISHLMILQAVESG-RLned 641
Cdd:cd05068 149 GLARVIkVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTyGRipyPGMTNAEVLQQVERGyRM--- 225
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15225456 642 fmdPNLrKNFPEveaaQLARLGLLCTHESSNQRPSMED 679
Cdd:cd05068 226 ---PCP-PNCPP----QLYDIMLECWKADPMERPTFET 255
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
409-684 8.45e-20

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: 90.10  E-value: 8.45e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERatQSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIaKSSCKSDESeFLKGLKMLTLLKHENLARLrgFCCSKGRGE 488
Cdd:cd05072   3 EIPR--ESIKLVKKLGAGQFGEVWMGYYNNSTKVAVKTL-KPGTMSVQA-FLEEANLMKTLQHDKLVRL--YAVVTKEEP 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 CFLIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd05072  77 IYIITEYMAKGSLLDFL--KSDEGGKVLLPKLIDFSAQIAEGMAYIERKN-----YIHRDLRAANVLVSESLMCKIADFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 569 LHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSgKSKISHlmilqaveSGRLNEDFMDPNLR 648
Cdd:cd05072 150 LARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVT-YGKIPY--------PGMSNSDVMSALQR 220
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15225456 649 K-NFPEVE--AAQLARLGLLCTHESSNQRPSMeDVIQEL 684
Cdd:cd05072 221 GyRMPRMEncPDELYDIMKTCWKEKAEERPTF-DYLQSV 258
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
423-621 9.94e-20

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 89.37  E-value: 9.94e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAA--IKCIAKSSCkSDESefLKGLKMLTLLKHENLARLRGF--CCSKGRGEcFLIYEFVPN 498
Cdd:cd13979  11 LGSGGFGSVYKATYKGETVAVkiVRRRRKNRA-SRQS--FWAELNAARLRHENIVRVLAAetGTDFASLG-LIIMEYCGN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 GNLLQYLDvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLH-KLF-TDD 576
Cdd:cd13979  87 GTLQQLIY---EGSEPLPLAHRILISLDIARALRFCHSHG-----IVHLDVKPANILISEQGVCKLCDFGCSvKLGeGNE 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15225456 577 IVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd13979 159 VGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLTRE 203
STKc_IRAK2 cd14157
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; ...
431-620 1.06e-19

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 2; 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. IRAK2 plays a role in mediating NFkB activation by TLR3, TLR4, and TLR8. It is specifically targeted by the viral protein A52, which is important for virulence, to inhibit all IL-1/TLR pathways, indicating that IRAK2 has a predominant role in NFkB activation. It is redundant with IRAK1 in early signaling but is critical for late and sustained activation. The IRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271059 [Multi-domain]  Cd Length: 289  Bit Score: 89.90  E-value: 1.06e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 431 VYKGiLRDGSVAAIKCIAKSSC---KSDESEFLKGLKMLTLLKHENLARLRGFCcSKGRGECfLIYEFVPNGNLLQYLDV 507
Cdd:cd14157   9 IYKG-YRHGKQYVIKRLKETECespKSTERFFQTEVQICFRCCHPNILPLLGFC-VESDCHC-LIYPYMPNGSLQDRLQQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 508 KDETgEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTD---DIVFSK--- 581
Cdd:cd14157  86 QGGS-HPLPWEQRLSISLGLLKAVQHLHNFG-----ILHGNIKSSNVLLDGNLLPKLGHSGLRLCPVDkksVYTMMKtkv 159
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 15225456 582 LKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14157 160 LQISLA--YLPEDFVRHGQLTEKVDIFSCGVVLAEILTG 196
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
30-237 2.57e-19

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 90.76  E-value: 2.57e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  30 LLDIKSSLDPEKRFLTSWTPDADPCSSGSFDGVACDGNRRVANISLQGMGLTGTIPPSIGLLTSLTGLYLHFNsltghip 109
Cdd:COG4886  34 LLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGN------- 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 110 KDISNLPLLTDLYLNVNNLSgEIPPLIGNLDNLQVIQLCYNKLSgSIPTQFGSLKKITVLALQYNQLSGaIPASLGDIDT 189
Cdd:COG4886 107 EELSNLTNLESLDLSGNQLT-DLPEELANLTNLKELDLSNNQLT-DLPEPLGNLTNLKSLDLSNNQLTD-LPEELGNLTN 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 190 LTRLDLSFNNLfGPVPVKLAGAPLLEVLDIRNNSFSGFvPSALKRLNN 237
Cdd:COG4886 184 LKELDLSNNQI-TDLPEPLGNLTNLEELDLSGNQLTDL-PEPLANLTN 229
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
423-678 3.82e-19

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: 88.21  E-value: 3.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIaKSSCKSDESeFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIYEFVPNGNLL 502
Cdd:cd05071  17 LGQGCFGEVWMGTWNGTTRVAIKTL-KPGTMSPEA-FLQEAQVMKKLRHEKLVQLYAVVSEE---PIYIVTEYMSKGSLL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd05071  92 DFL--KGEMGKYLRLPQLVDMAAQIASGMAYVERMN-----YVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQ 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQiLSGKSKISHlmilqaveSGRLNEDFMDP---NLRKNFPEVEAAQL 659
Cdd:cd05071 165 GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTE-LTTKGRVPY--------PGMVNREVLDQverGYRMPCPPECPESL 235
                       250
                ....*....|....*....
gi 15225456 660 ARLGLLCTHESSNQRPSME 678
Cdd:cd05071 236 HDLMCQCWRKEPEERPTFE 254
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
409-678 4.98e-19

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


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 87.63  E-value: 4.98e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERATQSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSdeSEFLKGLKMLTLLKHENLARLRGFCCskgRGE 488
Cdd:cd05067   1 EWEVPRETLKLVERLGAGQFGEVWMGYYNGHTKVAIKSLKQGSMSP--DAFLAEANLMKQLQHQRLVRLYAVVT---QEP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 CFLIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd05067  76 IYIITEYMENGSLVDFL--KTPSGIKLTINKLLDMAAQIAEGMAFIEERN-----YIHRDLRAANILVSDTLSCKIADFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 569 LHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSgKSKISHlmilqaveSGRLNEDFMDpNLR 648
Cdd:cd05067 149 LARLIEDNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVT-HGRIPY--------PGMTNPEVIQ-NLE 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 649 KNF----PEVEAAQLARLGLLCTHESSNQRPSME 678
Cdd:cd05067 219 RGYrmprPDNCPEELYQLMRLCWKERPEDRPTFE 252
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
411-678 8.02e-19

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: 87.05  E-value: 8.02e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 411 ERATQSFSEINLLGKSNVSSVYKGILRDGSVAAIKCIaKSSCKSDESeFLKGLKMLTLLKHENLARLRGFCcskGRGECF 490
Cdd:cd05070   5 EIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAIKTL-KPGTMSPES-FLEEAQIMKKLKHDKLVQLYAVV---SEEPIY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLH 570
Cdd:cd05070  80 IVTEYMSKGSLLDFL--KDGEGRALKLPNLVDMAAQVAAGMAYIERMN-----YIHRDLRSANILVGNGLICKIADFGLA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSgKSKI-----SHLMILQAVESGrlnedfmdp 645
Cdd:cd05070 153 RLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVpypgmNNREVLEQVERG--------- 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 15225456 646 nLRKNFPEVEAAQLARLGLLCTHESSNQRPSME 678
Cdd:cd05070 223 -YRMPCPQDCPISLHELMIHCWKKDPEERPTFE 254
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
423-678 1.48e-18

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 85.74  E-value: 1.48e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIaKSSCKSDESeFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIYEFVPNGNLL 502
Cdd:cd14203   3 LGQGCFGEVWMGTWNGTTKVAIKTL-KPGTMSPEA-FLEEAQIMKKLRHDKLVQLYAVVSEE---PIYIVTEFMSKGSLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd14203  78 DFL--KDGEGKYLKLPQLVDMAAQIASGMAYIERMN-----YIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQ 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGmILLQILSGKSKI-----SHLMILQAVESGrlnedfmdpnLRKNFPEVEAA 657
Cdd:cd14203 151 GAKFPIKWTAPEAALYGRFTIKSDVWSFG-ILLTELVTKGRVpypgmNNREVLEQVERG----------YRMPCPPGCPE 219
                       250       260
                ....*....|....*....|.
gi 15225456 658 QLARLGLLCTHESSNQRPSME 678
Cdd:cd14203 220 SLHELMCQCWRKDPEERPTFE 240
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
420-684 4.85e-18

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: 84.56  E-value: 4.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDE--SEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFV 496
Cdd:cd14014   5 VRLLGRGGMGEVYRARdTLLGRPVAIKVLRPELAEDEEfrERFLREARALARLSHPNIVRVYDVGEDDGR--PYIVMEYV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDVKDEtgevLEWATRVSIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD 576
Cdd:cd14014  83 EGGSLADLLRERGP----LPPREALRILAQIADALAAAH-RAG----IVHRDIKPANILLTEDGRVKLTDFGIARALGDS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 ivfSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILqAVESGRLNEDFMDPN-LRKNFP 652
Cdd:cd14014 154 ---GLTQTGSVLGtpaYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPA-AVLAKHLQEAPPPPSpLNPDVP 229
                       250       260       270
                ....*....|....*....|....*....|...
gi 15225456 653 EveaaQLARLGLLCTHESSNQRP-SMEDVIQEL 684
Cdd:cd14014 230 P----ALDAIILRALAKDPEERPqSAAELLAAL 258
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
423-681 5.44e-18

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: 84.16  E-value: 5.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDEseFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFVPNGNLL 502
Cdd:cd05113  12 LGTGQFGVVKYGKWRGQYDVAIKMIKEGSMSEDE--FIEEAKVMMNLSHEKLVQLYG-VCTKQR-PIFIITEYMANGCLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd05113  88 NYLR---EMRKRFQTQQLLEMCKDVCEAMEYLESKQ-----FLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GK---SKISHLMILQAVESGRlnedfmdpnlRKNFPEVEAAQ 658
Cdd:cd05113 160 GSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSlGKmpyERFTNSETVEHVSQGL----------RLYRPHLASEK 229
                       250       260
                ....*....|....*....|...
gi 15225456 659 LARLGLLCTHESSNQRPSMEDVI 681
Cdd:cd05113 230 VYTIMYSCWHEKADERPTFKILL 252
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
421-686 6.21e-18

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 84.39  E-value: 6.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKG----ILRDGS---VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrGECFLIY 493
Cdd:cd05044   1 KFLGSGAFGEVFEGtakdILGDGSgetKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDN--DPQYIIL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQYL-DVKDETGE--VLEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHwYNPS-----LA 565
Cdd:cd05044  79 ELMEGGDLLSYLrAARPTAFTppLLTLKDLLSICVDVAKGCVYLE-----DMHFVHRDLAARNCLVSS-KDYRervvkIG 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 566 DSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVES-GRLN 639
Cdd:cd05044 153 DFGLARdIYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTlGQQpypARNNLEVLHFVRAgGRLD 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 640 EdfmdPNlrkNFPEveaaQLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd05044 233 Q----PD---NCPD----DLYELMLRCWSTDPEERPSFARILEQLQN 268
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
423-675 6.52e-18

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 84.04  E-value: 6.52e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCksDESEFLKGLKMLTLLKHENLARLRGFCCSkgRGECFLIYEFVPNGNLL 502
Cdd:cd05059  12 LGSGQFGVVHLGKWRGKIDVAIKMIKEGSM--SEDDFIEEAKVMMKLSHPKLVQLYGVCTK--QRPIFIVTEYMANGCLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDE---TGEVLEWATRVSiingiaRGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVF 579
Cdd:cd05059  88 NYLRERRGkfqTEQLLEMCKDVC------EAMEYLE-SNG----FIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 580 SKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVESgrlnedfMDPNLRKNFPEVEAAQ 658
Cdd:cd05059 157 SSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSeGKMPYERFSNSEVVEH-------ISQGYRLYRPHLAPTE 229
                       250
                ....*....|....*..
gi 15225456 659 LARLGLLCTHESSNQRP 675
Cdd:cd05059 230 VYTIMYSCWHEKPEERP 246
PLN03150 PLN03150
hypothetical protein; Provisional
30-185 7.28e-18

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 87.56  E-value: 7.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   30 LLDIKSSLDPEKRFltSWtpDADPC--SSGSFDGVACDGNRRVANISLQGMGLTGtippsiglltsltglylhfNSLTGH 107
Cdd:PLN03150 377 LQTLKSSLGLPLRF--GW--NGDPCvpQQHPWSGADCQFDSTKGKWFIDGLGLDN-------------------QGLRGF 433
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456  108 IPKDISNLPLLTDLYLNVNNLSGEIPPLIGNLDNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLG 185
Cdd:PLN03150 434 IPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSLSGRVPAALG 511
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
445-644 8.71e-18

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 83.56  E-value: 8.71e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 445 KCIAKSSCKSDESEFLkgLKMLTLLKHENLARLRGFCCSK-GRGECFLIY---EFVPNGNLLQYLDvkdeTGEVLEWATR 520
Cdd:cd14012  33 FKTSNGKKQIQLLEKE--LESLKKLRHPNLVSYLAFSIERrGRSDGWKVYlltEYAPGGSLSELLD----SVGSVPLDTA 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 521 VSIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHW---YNPSLADSGLHKLFTDDIVFSKLKASAAMGYLAPEYIT 597
Cdd:cd14012 107 RRWTLQLLEALEYLH-RNG----VVHKSLHAGNVLLDRDagtGIVKLTDYSLGKTLLDMCSRGSLDEFKQTYWLPPELAQ 181
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 15225456 598 TG-RFTDKSDVYAFGMILLQILSGKSKISHLMILQAV-ESGRLNEDFMD 644
Cdd:cd14012 182 GSkSPTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVlVSLDLSASLQD 230
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
423-618 1.47e-17

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: 82.92  E-value: 1.47e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD-GSVAAIKCIAKSScksDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGNL 501
Cdd:cd14065   1 LGKGFFGEVYKVTHREtGKVMVMKELKRFD---EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNK--LNFITEYVNGGTL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILI---DHWYNPSLADSGLHKLFTDDIV 578
Cdd:cd14065  76 EELLKSMDEQ---LPWSQRVSLAKDIASGMAYLHSKN-----IIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPDEKT 147
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 15225456 579 F--SKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQIL 618
Cdd:cd14065 148 KkpDRKKRLTVVGspyWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
417-678 1.92e-17

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: 82.75  E-value: 1.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRDGS--VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFccSKGRGECFLIYE 494
Cdd:cd14202   4 FSRKDLIGHGAFAVVFKGRHKEKHdlEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDF--QEIANSVYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLDVKdetGEVLEWATRVsIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDH----WYNPS-----LA 565
Cdd:cd14202  82 YCNGGDLADYLHTM---RTLSEDTIRL-FLQQIAGAMKMLHSK-----GIIHRDLKPQNILLSYsggrKSNPNnirikIA 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 566 DSGLHKLFTDDIVFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKishlmiLQAVESGRLNEDF-MD 644
Cdd:cd14202 153 DFGFARYLQNNMMAATLCGSPM--YMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAP------FQASSPQDLRLFYeKN 224
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15225456 645 PNLRKNFPEVEAAQLAR--LGLLctheSSNQRPSME 678
Cdd:cd14202 225 KSLSPNIPRETSSHLRQllLGLL----QRNQKDRMD 256
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
422-619 2.37e-17

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: 82.87  E-value: 2.37e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRdGSVAAIKCIAKSSCKSDESEflKGLKMLTLLKHENLArlrGFCCSKGRG-----ECFLIYEFV 496
Cdd:cd13998   2 VIGKGRFGEVWKASLK-NEPVAVKIFSSRDKQSWFRE--KEIYRTPMLKHENIL---QFIAADERDtalrtELWLVTAFH 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLHGE----NGNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd13998  76 PNGSL*DYL-----SLHTIDWVSLCRLALSVARGLAHLHSEipgcTQGKPAIAHRDLKSKNILVKNDGTCCIADFGLAVR 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 573 FTDDIVFSKLKASAAMG---YLAPEY----ITTGRFTD--KSDVYAFGMILLQILS 619
Cdd:cd13998 151 LSPSTGEEDNANNGQVGtkrYMAPEVlegaINLRDFESfkRVDIYAMGLVLWEMAS 206
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
441-680 2.45e-17

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: 83.45  E-value: 2.45e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 441 VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYL--------------- 505
Cdd:cd05096  48 LVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRLLGVCVDED--PLCMITEYMENGDLNQFLsshhlddkeengnda 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 506 DVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKA 584
Cdd:cd05096 126 VPPAHCLPAISYSSLLHVALQIASGMKYLSSLN-----FVHRDLATRNCLVGENLTIKIADFGMSRnLYAGDYYRIQGRA 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 585 SAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS--GKSKISHLMILQAVESGrlNEDFMDPNlRKNF---PEVEAAQL 659
Cdd:cd05096 201 VLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMlcKEQPYGELTDEQVIENA--GEFFRDQG-RQVYlfrPPPCPQGL 277
                       250       260
                ....*....|....*....|.
gi 15225456 660 ARLGLLCTHESSNQRPSMEDV 680
Cdd:cd05096 278 YELMLQCWSRDCRERPSFSDI 298
PLN03150 PLN03150
hypothetical protein; Provisional
123-258 3.38e-17

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 85.64  E-value: 3.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  123 LNVNN--LSGEIPPLIGNLDNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNL 200
Cdd:PLN03150 423 LGLDNqgLRGFIPNDISKLRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLNGNSL 502
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456  201 FGPVPVKLAGAPLlevldiRNNSFSgfvpsalkrlnngfqYSNNHGLCgdGFTDLKAC 258
Cdd:PLN03150 503 SGRVPAALGGRLL------HRASFN---------------FTDNAGLC--GIPGLRAC 537
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
420-687 4.08e-17

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 82.25  E-value: 4.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSV----YKGiLRD--GSVAAIKCIAKSSCKsDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIY 493
Cdd:cd05081   9 ISQLGKGNFGSVelcrYDP-LGDntGALVAVKQLQHSGPD-QQRDFQREIQILKALHSDFIVKYRGVSYGPGRRSLRLVM 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQYLdvkDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF 573
Cdd:cd05081  87 EYLPSGCLRDFL---QRHRARLDASRLLLYSSQICKGMEYLGSRR-----CVHRDLAARNILVESEAHVKIADFGLAKLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 574 TDD--IVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQIL-------SGKSKISHLM----ILQAVesGRLNE 640
Cdd:cd05081 159 PLDkdYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFtycdkscSPSAEFLRMMgcerDVPAL--CRLLE 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 641 dFMDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05081 237 -LLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLDML 282
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
422-687 5.75e-17

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: 81.29  E-value: 5.75e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGSVAaIKcIAKSSCKSDESEFLKGL----KMLTLLKHENLARLRGFCCSKGRgECfLIYEFVP 497
Cdd:cd14061   1 VIGVGGFGKVYRGIWRGEEVA-VK-AARQDPDEDISVTLENVrqeaRLFWMLRHPNIIALRGVCLQPPN-LC-LVMEYAR 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDETGEVL-EWATRvsiingIARGIVYLHgeNGNKPAIVHQNLSAEKILIDHWYNPS--------LADSG 568
Cdd:cd14061  77 GGALNRVLAGRKIPPHVLvDWAIQ------IARGMNYLH--NEAPVPIIHRDLKSSNILILEAIENEdlenktlkITDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 569 LHKLFTDDivfSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK---ISHLMILQAVESGRLNEDFmdP 645
Cdd:cd14061 149 LAREWHKT---TRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELLTGEVPykgIDGLAVAYGVAVNKLTLPI--P 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15225456 646 NlrkNFPEVEAAQLARlgllCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14061 224 S---TCPEPFAQLMKD----CWQPDPHDRPSFADILKQLENI 258
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
423-627 6.18e-17

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: 81.04  E-value: 6.18e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRdGSVAAIKCIAKS--SCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgRGECFLIYEFVPNGN 500
Cdd:cd14064   1 IGSGSFGKVYKGRCR-NKIVAIKRYRANtyCSKSDVDMFCREVSILCRLNHPCVIQFVGACLDD-PSQFAIVTQYVSGGS 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDvkdETGEVLEWATRVSIINGIARGIVYLHgeNGNKPaIVHQNLSAEKILIDHWYNPSLADSG----LHKLFTDD 576
Cdd:cd14064  79 LFSLLH---EQKRVIDLQSKLIIAVDVAKGMEYLH--NLTQP-IIHRDLNSHNILLYEDGHAVVADFGesrfLQSLDEDN 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15225456 577 IVfsklKASAAMGYLAPEYIT-TGRFTDKSDVYAFGMILLQILSGKSKISHL 627
Cdd:cd14064 153 MT----KQPGNLRWMAPEVFTqCTRYSIKADVFSYALCLWELLTGEIPFAHL 200
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
419-619 7.99e-17

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: 81.61  E-value: 7.99e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 419 EINLLGKSNVSSVYKGILRDGSV-AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskgRGE-CFLIYEFV 496
Cdd:cd05051  25 EANGLSDLTSDDFIGNDNKDEPVlVAVKMLRPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCT---RDEpLCMIVEYM 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL--------DVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd05051 102 ENGDLNQFLqkheaetqGASATNSKTLSYGTLLYMATQIASGMKYLESLN-----FVHRDLATRNCLVGPNYTIKIADFG 176
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 569 LHK-LFTDDivFSKLKASAAMG--YLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05051 177 MSRnLYSGD--YYRIEGRAVLPirWMAWESILLGKFTTKSDVWAFGVTLWEILT 228
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
409-636 1.04e-16

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 80.84  E-value: 1.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERATQSFSEinLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSdeSEFLKGLKMLTLLKHENLARLRGFCCskgRGE 488
Cdd:cd05073   7 EIPRESLKLEK--KLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSV--EAFLAEANVMKTLQHDKLVKLHAVVT---KEP 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 CFLIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd05073  80 IYIITEFMAKGSLLDFL--KSDEGSKQPLPKLIDFSAQIAEGMAFIEQRN-----YIHRDLRAANILVSASLVCKIADFG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15225456 569 LHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSK---ISHLMILQAVESG 636
Cdd:cd05073 153 LARVIEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTyGRIPypgMSNPEVIRALERG 224
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
463-680 1.20e-16

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 80.51  E-value: 1.20e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 463 LKMLTLLKHENLARLRGFCcsKGRGECFLIYEFVPNGNLLQYLDVKDETgevLEWATRVSIINGIARGIVYLHgengNKP 542
Cdd:cd13992  47 LNQLKELVHDNLNKFIGIC--INPPNIAVVTEYCTRGSLQDVLLNREIK---MDWMFKSSFIKDIVKGMNYLH----SSS 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 543 AIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAMGYL--APEYI----TTGRFTDKSDVYAFGMILLQ 616
Cdd:cd13992 118 IGYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKKLLwtAPELLrgslLEVRGTQKGDVYSFAIILYE 197
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 617 ILSGKSKISHLMILQAVESGRLNEDFM---DPNLRKNFPEVEAAQLARlglLCTHESSNQRPSMEDV 680
Cdd:cd13992 198 ILFRSDPFALEREVAIVEKVISGGNKPfrpELAVLLDEFPPRLVLLVK---QCWAENPEKRPSFKQI 261
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
431-687 1.32e-16

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 80.49  E-value: 1.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 431 VYKGILRDGS----VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFVPNGNLLQYLD 506
Cdd:cd05033  20 VCSGSLKLPGkkeiDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEG-VVTKSR-PVMIVTEYMENGSLDKFLR 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 507 VKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTD-DIVFSKLKAS 585
Cdd:cd05033  98 ENDGK---FTVTQLVGMLRGIASGMKYLSEMN-----YVHRDLAARNILVNSDLVCKVSDFGLSRRLEDsEATYTTKGGK 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 586 AAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESG-RLNEdfmdPnlrKNFPEVeaaqLA 660
Cdd:cd05033 170 IPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERpywdMSNQDVIKAVEDGyRLPP----P---MDCPSA----LY 238
                       250       260
                ....*....|....*....|....*..
gi 15225456 661 RLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05033 239 QLMLDCWQKDRNERPTFSQIVSTLDKM 265
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
417-682 1.60e-16

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: 80.21  E-value: 1.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESE---FLKGLKMLTLLKHENLARLRGFccSKGRGECFLI 492
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEVEtGKMRAIKQIVKRKVAGNDKNlqlFQREINILKSLEHPGIVRLIDW--YEDDQHIYLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLdvkDETGEVLEWATRvSIINGIARGIVYLHgengnKPAIVHQNLSAEKILI--DHWYNPSLADSGLH 570
Cdd:cd14098  80 MEYVEGGDLMDFI---MAWGAIPEQHAR-ELTKQILEAMAYTH-----SMGITHRDLKPENILItqDDPVIVKISDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLFTDDIVFSKLkaSAAMGYLAPEYITT------GRFTDKSDVYAFGMILLQILSGK---SKISHLMILQAVESGRLNEd 641
Cdd:cd14098 151 KVIHTGTFLVTF--CGTMAYLAPEILMSkeqnlqGGYSNLVDMWSVGCLVYVMLTGAlpfDGSSQLPVEKRIRKGRYTQ- 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15225456 642 fmDPNLrknfpEVEAAQLARLGLLCTHE-SSNQRPSMEDVIQ 682
Cdd:cd14098 228 --PPLV-----DFNISEEAIDFILRLLDvDPEKRMTAAQALD 262
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
417-684 1.60e-16

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: 80.41  E-value: 1.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLarLRGFCCSKGRGECFLIYEF 495
Cdd:cd13996   8 FEEIELLGSGGFGSVYKVRNKvDGVTYAIKKIRLTEKSSASEKVLREVKALAKLNHPNI--VRYYTAWVEEPPLYIQMEL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLD---VKDETGEVLEWatrvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILID-HWYNPSLADSGLHK 571
Cdd:cd13996  86 CEGGTLRDWIDrrnSSSKNDRKLAL----ELFKQILKGVSYIHSKG-----IVHRDLKPSNIFLDnDDLQVKIGDFGLAT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 572 LFTDDIVFSKL------KASAAM-------GYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISH-LMILQAVESGR 637
Cdd:cd13996 157 SIGNQKRELNNlnnnnnGNTSNNsvgigtpLYASPEQLDGENYNEKADIYSLGIILFEMLHPFKTAMErSTILTDLRNGI 236
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 638 LNEDFMDpnlrkNFPEvEAAQLARLgllcTHESSNQRPSMEDVIQEL 684
Cdd:cd13996 237 LPESFKA-----KHPK-EADLIQSL----LSKNPEERPSAEQLLRSL 273
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
431-678 1.92e-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: 79.72  E-value: 1.92e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 431 VYKGILRDGS--VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVPNGNLLQYLDVK 508
Cdd:cd14120   9 VFKGRHRKKPdlPVAIKCITKKNLSKSQNLLGKEIKILKELSHENVVAL--LDCQETSSSVYLVMEYCNGGDLADYLQAK 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 509 detGEVLEWATRVSIINgIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPS---------LADSGLHKLFTDDIVF 579
Cdd:cd14120  87 ---GTLSEDTIRVFLQQ-IAAAMKALHSK-----GIVHRDLKPQNILLSHNSGRKpspndirlkIADFGFARFLQDGMMA 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 580 SKLKASaAMgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKishlmiLQAVESGRLNEDFM-DPNLRKNFPEVEAAQ 658
Cdd:cd14120 158 ATLCGS-PM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKAP------FQAQTPQELKAFYEkNANLRPNIPSGTSPA 229
                       250       260
                ....*....|....*....|
gi 15225456 659 LARlgLLCTHESSNQRPSME 678
Cdd:cd14120 230 LKD--LLLGLLKRNPKDRID 247
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
439-684 2.23e-16

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


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 79.94  E-value: 2.23e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRGECF-LIYEFVPNGNLLQYLDvKDETG--EVL 515
Cdd:cd05080  33 GEMVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKG-CCSEQGGKSLqLIMEYVPLGSLRDYLP-KHSIGlaQLL 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 516 EWATRvsiingIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLK--ASAAMGYLAP 593
Cdd:cd05080 111 LFAQQ------ICEGMAYLHSQH-----YIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYYRVRedGDSPVFWYAP 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 594 EYITTGRFTDKSDVYAFGMILLQIL----SGKSKISHLMILQAVESGRLNE----DFMDPNLRKNFPEVEAAQLARLGLL 665
Cdd:cd05080 180 ECLKEYKFYYASDVWSFGVTLYELLthcdSSQSPPTKFLEMIGIAQGQMTVvrliELLERGERLPCPDKCPQEVYHLMKN 259
                       250
                ....*....|....*....
gi 15225456 666 CTHESSNQRPSMEDVIQEL 684
Cdd:cd05080 260 CWETEASFRPTFENLIPIL 278
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
423-684 2.45e-16

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: 79.73  E-value: 2.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGIL----RDGSV--AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcSKGRGECfLIYEFV 496
Cdd:cd05048  13 LGEGAFGKVYKGELlgpsSEESAisVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVC-TKEQPQC-MLFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL------------DVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05048  91 AHGDLHEFLvrhsphsdvgvsSDDDGTASSLDQSDFLHIAIQIAAGMEYLSSHH-----YVHRDLAARNCLVGDGLTVKI 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 565 ADSGLHKL-FTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GkskishlmiLQAVeSGRLNEDF 642
Cdd:cd05048 166 SDFGLSRDiYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSyG---------LQPY-YGYSNQEV 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15225456 643 MDpNLRKNF----PEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05048 236 IE-MIRSRQllpcPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRL 280
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
441-684 2.66e-16

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: 80.04  E-value: 2.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 441 VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKD-ETGEVLEWAT 519
Cdd:cd05095  48 LVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLAVCITDD--PLCMITEYMENGDLNQFLSRQQpEGQLALPSNA 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 520 R-VSIIN------GIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYL 591
Cdd:cd05095 126 LtVSYSDlrfmaaQIASGMKYLSSLN-----FVHRDLATRNCLVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIRWM 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 592 APEYITTGRFTDKSDVYAFGMILLQILS--GKSKISHLMILQAVESgrLNEDFMDPNLRKNFPE--VEAAQLARLGLLCT 667
Cdd:cd05095 201 SWESILLGKFTTASDVWAFGVTLWETLTfcREQPYSQLSDEQVIEN--TGEFFRDQGRQTYLPQpaLCPDSVYKLMLSCW 278
                       250
                ....*....|....*..
gi 15225456 668 HESSNQRPSMEDVIQEL 684
Cdd:cd05095 279 RRDTKDRPSFQEIHTLL 295
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
423-619 3.64e-16

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: 78.67  E-value: 3.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR-DGSVAAIKciaKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNL 501
Cdd:cd14155   1 IGSGFFSEVYKVRHRtSGQVMALK---MNTLSSNRANMLREVQLMNRLSHPNILRFMGVCVHQG--QLHALTEYINGGNL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKdetgEVLEWATRVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILI---DHWYNPSLADSGL-HKLFTDDI 577
Cdd:cd14155  76 EQLLDSN----EPLSWTVRVKLALDIARGLSYLHSK-----GIFHRDLTSKNCLIkrdENGYTAVVGDFGLaEKIPDYSD 146
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15225456 578 VFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd14155 147 GKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEIIA 188
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
421-687 4.59e-16

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


Pssm-ID: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 78.93  E-value: 4.59e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKG-ILRDGS--VAAIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCcsKGRGECFLIYEFV 496
Cdd:cd05047   1 DVIGEGNFGQVLKArIKKDGLrmDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC--EHRGYLYLAIEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLdvkdETGEVLEWATRVSIING----------------IARGIVYLhgengNKPAIVHQNLSAEKILIDHWY 560
Cdd:cd05047  79 PHGNLLDFL----RKSRVLETDPAFAIANStastlssqqllhfaadVARGMDYL-----SQKQFIHRDLAARNILVGENY 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 561 NPSLADSGLHKlfTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVEsgRLN 639
Cdd:cd05047 150 VAKIADFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYE--KLP 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 640 EDFmdpnlRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05047 226 QGY-----RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRM 268
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
423-678 5.46e-16

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 78.96  E-value: 5.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIaKSSCKSDESeFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIYEFVPNGNLL 502
Cdd:cd05069  20 LGQGCFGEVWMGTWNGTTKVAIKTL-KPGTMMPEA-FLQEAQIMKKLRHDKLVPLYAVVSEE---PIYIVTEFMGKGSLL 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd05069  95 DFL--KEGDGKYLKLPQLVDMAAQIADGMAYIERMN-----YIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQ 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSgKSKISHlmilqaveSGRLNEDFM---DPNLRKNFPEVEAAQL 659
Cdd:cd05069 168 GAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVT-KGRVPY--------PGMVNREVLeqvERGYRMPCPQGCPESL 238
                       250
                ....*....|....*....
gi 15225456 660 ARLGLLCTHESSNQRPSME 678
Cdd:cd05069 239 HELMKLCWKKDPDERPTFE 257
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
423-684 5.47e-16

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 78.43  E-value: 5.47e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNL 501
Cdd:cd05084   4 IGRGNFGEVFSGRLRaDNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQ--PIYIVMELVQGGDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKdetGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLfTDDIVFSk 581
Cdd:cd05084  82 LTFLRTE---GPRLKVKELIRMVENAAAGMEYLESKH-----CIHRDLAARNCLVTEKNVLKISDFGMSRE-EEDGVYA- 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 lkASAAM-----GYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLmilqaveSGRLNEDFMDPNLRKNFPEVE 655
Cdd:cd05084 152 --ATGGMkqipvKWTAPEALNYGRYSSESDVWSFGILLWETFSlGAVPYANL-------SNQQTREAVEQGVRLPCPENC 222
                       250       260
                ....*....|....*....|....*....
gi 15225456 656 AAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05084 223 PDEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
417-632 5.60e-16

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: 78.40  E-value: 5.60e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESeFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEF 495
Cdd:cd05122   2 FEILEKIGKGGFGVVYKARhKKTGQIVAIKKINLESKEKKES-ILNEIAILKKCKHPNIVKY--YGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTD 575
Cdd:cd05122  79 CSGGSLKDLLKNTNKT---LTEQQIAYVCKEVLKGLEYLHSHG-----IIHRDIKAANILLTSDGEVKLIDFGLSAQLSD 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 576 DIVFSKLkaSAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQA 632
Cdd:cd05122 151 GKTRNTF--VGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKA 205
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
437-687 6.79e-16

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: 78.37  E-value: 6.79e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAaIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFVPNGNLLQYLDVKDETGEVLE 516
Cdd:cd05066  31 REIPVA-IKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEG-VVTRSK-PVMIVTEYMENGSLDAFLRKHDGQFTVIQ 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 517 WatrVSIINGIARGIVYLhgengNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD--IVFSKLKASAAMGYLAPE 594
Cdd:cd05066 108 L---VGMLRGIASGMKYL-----SDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDpeAAYTTRGGKIPIRWTAPE 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 595 YITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESG-RLNEDFMDPnlrknfpeveaAQLARLGLLCTHE 669
Cdd:cd05066 180 AIAYRKFTSASDVWSYGIVMWEVMSYGERpyweMSNQDVIKAIEEGyRLPAPMDCP-----------AALHQLMLDCWQK 248
                       250
                ....*....|....*...
gi 15225456 670 SSNQRPSMEDVIQELNNL 687
Cdd:cd05066 249 DRNERPKFEQIVSILDKL 266
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
422-687 8.84e-16

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 77.99  E-value: 8.84e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGIL----RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcSKGRgECFLIYEFVP 497
Cdd:cd05065  11 VIGAGEFGEVCRGRLklpgKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVV-TKSR-PVMIITEFME 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDETGEVLEWatrVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD- 576
Cdd:cd05065  89 NGALDSFLRQNDGQFTVIQL---VGMLRGIAAGMKYLSEMN-----YVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDt 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 ---IVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVEsgrlnEDFMDPNlrk 649
Cdd:cd05065 161 sdpTYTSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERpywdMSNQDVINAIE-----QDYRLPP--- 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15225456 650 nfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05065 233 --PMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTLDKM 268
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
417-682 9.19e-16

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: 77.51  E-value: 9.19e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKS--SCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIY 493
Cdd:cd14007   2 FEIGKPLGKGKFGNVYLAReKKSGFIVALKVISKSqlQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKR--IYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQYLDVK---DEtgevlewATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLh 570
Cdd:cd14007  80 EYAPNGELYKELKKQkrfDE-------KEAAKYIYQLALALDYLHSKN-----IIHRDIKPENILLGSNGELKLADFGW- 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 klftdDIVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS---KISHLMILQAVESGRLNedfMD 644
Cdd:cd14007 147 -----SVHAPSNRRKTFCGtldYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGKPpfeSKSHQETYKRIQNVDIK---FP 218
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15225456 645 PNLRKnfpevEAAQLARlgLLCTHEsSNQRPSMEDVIQ 682
Cdd:cd14007 219 SSVSP-----EAKDLIS--KLLQKD-PSKRLSLEQVLN 248
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
408-687 1.05e-15

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: 77.78  E-value: 1.05e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 408 EEIERATQSFSEInlLGKSNVSSVYKGILrDGSVAAIKCiAKSSCKSDESEFLKGL----KMLTLLKHENLARLRGFCCs 483
Cdd:cd14145   1 LEIDFSELVLEEI--IGIGGFGKVYRAIW-IGDEVAVKA-ARHDPDEDISQTIENVrqeaKLFAMLKHPNIIALRGVCL- 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 484 KGRGECfLIYEFVPNGNLLQYLDVKDETGEVL-EWATRvsiingIARGIVYLHGENgnKPAIVHQNLSAEKILI------ 556
Cdd:cd14145  76 KEPNLC-LVMEFARGGPLNRVLSGKRIPPDILvNWAVQ------IARGMNYLHCEA--IVPVIHRDLKSSNILIlekven 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 557 DHWYNPSL--ADSGLHKLFTDDivfSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVE 634
Cdd:cd14145 147 GDLSNKILkiTDFGLAREWHRT---TKMSAAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLAVAY 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 15225456 635 SGRLNEdfmdpnLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14145 224 GVAMNK------LSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
421-626 1.24e-15

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: 78.17  E-value: 1.24e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILrDGSVAAIKCIAKSSCKSDESEflKGLKMLTLLKHENLARLRGFC---CSKGRGECFLIYEFVP 497
Cdd:cd14054   1 QLIGQGRYGTVWKGSL-DERPVAVKVFPARHRQNFQNE--KDIYELPLMEHSNILRFIGADerpTADGRMEYLLVLEYAP 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLHGE----NGNKPAIVHQNLSAEKILIDHWYNPSLADSGL---- 569
Cdd:cd14054  78 KGSLCSYL-----RENTLDWMSSCRMALSLTRGLAYLHTDlrrgDQYKPAIAHRDLNSRNVLVKADGSCVICDFGLamvl 152
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225456 570 --HKLFTDDIVFSKLKASAAMG---YLAPEYI-------TTGRFTDKSDVYAFGMILLQILSGKSKISH 626
Cdd:cd14054 153 rgSSLVRGRPGAAENASISEVGtlrYMAPEVLegavnlrDCESALKQVDVYALGLVLWEIAMRCSDLYP 221
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
414-690 1.59e-15

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 77.30  E-value: 1.59e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 414 TQSFSEINLLGKSNVSSVYKGI-LRDGSV----AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSkgrGE 488
Cdd:cd05111   6 ETELRKLKVLGSGVFGTVHKGIwIPEGDSikipVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPG---AS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 CFLIYEFVPNGNLLQYL-DVKDETGE--VLEWATRvsiingIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLA 565
Cdd:cd05111  83 LQLVTQLLPLGSLLDHVrQHRGSLGPqlLLNWCVQ------IAKGMYYLE-EHR----MVHRNLAARNVLLKSPSQVQVA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 566 DSGLHKL-FTDD--IVFSKLKASaaMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVesgrlnEDF 642
Cdd:cd05111 152 DFGVADLlYPDDkkYFYSEAKTP--IKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEV------PDL 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 643 MDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05111 224 LEKGERLAQPQICTIDVYMVMVKCWMIDENIRPTFKELANEFTRMARD 271
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
443-641 1.71e-15

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: 77.27  E-value: 1.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSS--CKSDESEFLKGLKMLTLLKHENLARLRGFCcskGRGECF-LIYEFVPNGNLLQYLDVKDETGEVlEWAT 519
Cdd:cd14026  26 AIKCLKLDSpvGDSERNCLLKEAEILHKARFSYILPILGIC---NEPEFLgIVTEYMTNGSLNELLHEKDIYPDV-AWPL 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 520 RVSIINGIARGIVYLHGENgnkPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAMG----YLAPEY 595
Cdd:cd14026 102 RLRILYEIALGVNYLHNMS---PPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSISQSRSSKSAPEGgtiiYMPPEE 178
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 596 ITTG---RFTDKSDVYAFGMILLQILSGK----SKISHLMILQAVESGR---LNED 641
Cdd:cd14026 179 YEPSqkrRASVKHDIYSYAIIMWEVLSRKipfeEVTNPLQIMYSVSQGHrpdTGED 234
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
464-680 2.63e-15

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: 76.38  E-value: 2.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 464 KMLTLLKHENLARLRGFCCSKGRGEcfLIYEFVPNGNLLQYLdvkdETGEVlEWATRVSIINGIARGIVYLHGENgnkpa 543
Cdd:cd14027  43 KMMNRLRHSRVVKLLGVILEEGKYS--LVMEYMEKGNLMHVL----KKVSV-PLSVKGRIILEIIEGMAYLHGKG----- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 544 IVHQNLSAEKILIDHWYNPSLADSGL------HKLFTDDI-VFSKLKASAA-----MGYLAPEYITT--GRFTDKSDVYA 609
Cdd:cd14027 111 VIHKDLKPENILVDNDFHIKIADLGLasfkmwSKLTKEEHnEQREVDGTAKknagtLYYMAPEHLNDvnAKPTEKSDVYS 190
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 610 FGMILLQILSGK----SKISHLMILQAVESG-RLNEDFMDPNLRKnfpevEAAQLARlglLCTHESSNQRPSMEDV 680
Cdd:cd14027 191 FAIVLWAIFANKepyeNAINEDQIIMCIKSGnRPDVDDITEYCPR-----EIIDLMK---LCWEANPEARPTFPGI 258
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
423-619 2.73e-15

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: 76.97  E-value: 2.73e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGIL-----RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRGECFLiYEFVP 497
Cdd:cd05090  13 LGECAFGKIYKGHLylpgmDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLG-VVTQEQPVCML-FEFMN 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYL-------DV---KDETGEV---LEWATRVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05090  91 QGDLHEFLimrsphsDVgcsSDEDGTVkssLDHGDFLHIAIQIAAGMEYLSSH-----FFVHKDLAARNILVGEQLHVKI 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 565 ADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05090 166 SDLGLSReIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFS 221
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
423-621 2.76e-15

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: 75.99  E-value: 2.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCiakssckSDESEflKGLKMLTLLKHENLARLRGFCCskgRGECF-LIYEFVPNGNL 501
Cdd:cd14059   1 LGSGAQGAVFLGKFRGEEVAVKKV-------RDEKE--TDIKHLRKLNHPNIIKFKGVCT---QAPCYcILMEYCPYGQL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKDETGEVL--EWATrvsiinGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIvf 579
Cdd:cd14059  69 YEVLRAGREITPSLlvDWSK------QIASGMNYLHLHK-----IIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKS-- 135
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15225456 580 SKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd14059 136 TKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLTGE 177
Pkinase pfam00069
Protein kinase domain;
417-682 2.85e-15

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 75.36  E-value: 2.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   417 FSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESE-FLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYE 494
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDtGKIVAIKKIKKEKIKKKKDKnILREIKILKKLNHPNIVRLYDAFEDKD--NLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   495 FVPNGNLLQYLDVKdetGEVLEWATRvSIINGIARGIvylhgENGNKPaivhqnlsaekilidhwynpsladsglhklft 574
Cdd:pfam00069  79 YVEGGSLFDLLSEK---GAFSEREAK-FIMKQILEGL-----ESGSSL-------------------------------- 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   575 DDIVFSKlkasaamGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESGRLNEDFMDPNLrKNFPEv 654
Cdd:pfam00069 118 TTFVGTP-------WYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELP-SNLSE- 188
                         250       260
                  ....*....|....*....|....*...
gi 15225456   655 EAAQLARlGLLCthESSNQRPSMEDVIQ 682
Cdd:pfam00069 189 EAKDLLK-KLLK--KDPSKRLTATQALQ 213
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
423-684 3.41e-15

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 76.14  E-value: 3.41e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKsdESEFLKGLKMLTLLKHENLARLRGFCCSkgRGECFLIYEFVPNGNLL 502
Cdd:cd05112  12 IGSGQFGLVHLGYWLNKDKVAIKTIREGAMS--EEDFIEEAEVMMKLSHPKLVQLYGVCLE--QAPICLVFEFMEHGCLS 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd05112  88 DYLRTQRGL---FSAETLLGMCLDVCEGMAYLEEAS-----VIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSST 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVESgrLNEDFmdpnlRKNFPEVEAAQLAR 661
Cdd:cd05112 160 GTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSeGKIPYENRSNSEVVED--INAGF-----RLYKPRLASTHVYE 232
                       250       260
                ....*....|....*....|...
gi 15225456 662 LGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05112 233 IMNHCWKERPEDRPSFSLLLRQL 255
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
443-687 3.49e-15

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 76.38  E-value: 3.49e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSC-KSDESEFLKGLKMLTLLKHENLARLRGFCcSKGRGecfLIYEFVPNGNLLQYLdvkdeTGEVLEWATRV 521
Cdd:cd14025  25 AIKCPPSLHVdDSERMELLEEAKKMEMAKFRHILPVYGIC-SEPVG---LVMEYMETGSLEKLL-----ASEPLPWELRF 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 522 SIINGIARGIVYLHGEngnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKL--FTDDIVFSKLKASAAMGYLAPEYI--T 597
Cdd:cd14025  96 RIIHETAVGMNFLHCM---KPPLLHLDLKPANILLDAHYHVKISDFGLAKWngLSHSHDLSRDGLRGTIAYLPPERFkeK 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 598 TGRFTDKSDVYAFGMILLQIL------SGKSKISHLMIlqAVESGRLNEDFMDPNLRKNfpevEAAQLARLGLLCTHESS 671
Cdd:cd14025 173 NRCPDTKHDVYSFAIVIWGILtqkkpfAGENNILHIMV--KVVKGHRPSLSPIPRQRPS----ECQQMICLMKRCWDQDP 246
                       250
                ....*....|....*.
gi 15225456 672 NQRPSMEDVIQELNNL 687
Cdd:cd14025 247 RKRPTFQDITSETENL 262
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
407-687 3.50e-15

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: 76.49  E-value: 3.50e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 407 LEEIERATQSFSEINLLGKSNVSSVYKGILR--DGSV--AAIKCI-AKSSCKSDESEFLKGLKMLTLLKHENLARLRGFC 481
Cdd:cd05074   1 LKDVLIQEQQFTLGRMLGKGEFGSVREAQLKseDGSFqkVAVKMLkADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 482 C---SKGRGEC-FLIYEFVPNGNLLQYLdVKDETGE---VLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKI 554
Cdd:cd05074  81 LrsrAKGRLPIpMVILPFMKHGDLHTFL-LMSRIGEepfTLPLQTLVRFMIDIASGMEYLSSKN-----FIHRDLAARNC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 555 LIDHWYNPSLADSGL-HKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKIShlmilqA 632
Cdd:cd05074 155 MLNENMTVCVADFGLsKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTrGQTPYA------G 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 633 VESGRLNEDFMDPNLRKNFPEVeAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05074 229 VENSEIYNYLIKGNRLKQPPDC-LEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
423-688 4.17e-15

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: 75.67  E-value: 4.17e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKsdESEFLKGLKMLTLLKHENLARLRGFCCSkgRGECFLIYEFVPNGNLL 502
Cdd:cd05114  12 LGSGLFGVVRLGKWRAQYKVAIKAIREGAMS--EEDFIEEAKVMMKLTHPKLVQLYGVCTQ--QKPIYIVTEFMENGCLL 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLdvKDETGeVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd05114  88 NYL--RQRRG-KLSRDMLLSMCQDVCEGMEYLERNN-----FIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSS 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GK---SKISHLMILQAVESGRlnedfmdpnlRKNFPEVEAAQ 658
Cdd:cd05114 160 GAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTeGKmpfESKSNYEVVEMVSRGH----------RLYRPKLASKS 229
                       250       260       270
                ....*....|....*....|....*....|
gi 15225456 659 LARLGLLCTHESSNQRPSMEDVIQELNNLA 688
Cdd:cd05114 230 VYEVMYSCWHEKPEGRPTFADLLRTITEIA 259
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
441-619 4.87e-15

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: 76.17  E-value: 4.87e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 441 VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrGECFLIYEFVPNGNLLQYLDVKdETGEVLEWATR 520
Cdd:cd05097  46 LVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSD--DPLCMITEYMENGDLNQFLSQR-EIESTFTHANN 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 521 ---VSIIN------GIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGY 590
Cdd:cd05097 123 ipsVSIANllymavQIASGMKYLASLN-----FVHRDLATRNCLVGNHYTIKIADFGMSRnLYSGDYYRIQGRAVLPIRW 197
                       170       180
                ....*....|....*....|....*....
gi 15225456 591 LAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05097 198 MAWESILLGKFTTASDVWAFGVTLWEMFT 226
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
424-687 7.03e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 74.61  E-value: 7.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 424 GKSNVSSVYKGI-LRDGSVAAIKCIAKSScksdeseflKGLKMLTLLKHENLARLRGfCCSKGRGECfLIYEFVPNGNLL 502
Cdd:cd14060   2 GGGSFGSVYRAIwVSQDKEVAVKKLLKIE---------KEAEILSVLSHRNIIQFYG-AILEAPNYG-IVTEYASYGSLF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKD----ETGEVLEWATRvsiingIARGIVYLHGEngnKP-AIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:cd14060  71 DYLNSNEseemDMDQIMTWATD------IAKGMHYLHME---APvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTT 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 578 VFSklkASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQ----AVESGRlnedfmdpnlRKNFPE 653
Cdd:cd14060 142 HMS---LVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQvawlVVEKNE----------RPTIPS 208
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 654 VEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14060 209 SCPRSFAELMRRCWEADVKERPSFKQIIGILESM 242
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
423-684 7.42e-15

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: 75.37  E-value: 7.42e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSV---AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgeCFLIYEFVPNG 499
Cdd:cd05115  12 LGSGNFGCVKKGVYKMRKKqidVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA---LMLVMEMASGG 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDVKDETGEVlewATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVF 579
Cdd:cd05115  89 PLNKFLSGKKDEITV---SNVVELMHQVSMGMKYLEEKN-----FVHRDLAARNVLLVNQHYAKISDFGLSKALGADDSY 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 580 SKLKASAA--MGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESgrlnedFMDPNLRKNFPEVEAA 657
Cdd:cd05115 161 YKARSAGKwpLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMS------FIEQGKRMDCPAECPP 234
                       250       260
                ....*....|....*....|....*..
gi 15225456 658 QLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05115 235 EMYALMSDCWIYKWEDRPNFLTVEQRM 261
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
434-619 7.63e-15

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 75.98  E-value: 7.63e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 434 GILRDGSV--AAIKCIaKSSCKSDESEFLKG-LKMLTLL-KHENLARLRGfCCSKGrGECFLIYEFVPNGNLLQYLDVKD 509
Cdd:cd05055  58 GLSKSDAVmkVAVKML-KPTAHSSEREALMSeLKIMSHLgNHENIVNLLG-ACTIG-GPILVITEYCCYGDLLNFLRRKR 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 510 ETgeVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAM 588
Cdd:cd05055 135 ES--FLTLEDLLSFSYQVAKGMAFLASKN-----CIHRDLAARNVLLTHGKIVKICDFGLARdIMNDSNYVVKGNARLPV 207
                       170       180       190
                ....*....|....*....|....*....|.
gi 15225456 589 GYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05055 208 KWMAPESIFNCVYTFESDVWSYGILLWEIFS 238
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
420-687 7.92e-15

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


Pssm-ID: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 75.02  E-value: 7.92e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILRdGSVAAIKCIaksscKSDESE--FLKGLKMLTLLKHENLARLRGFCCSKgRGECFLIYEFVP 497
Cdd:cd05082  11 LQTIGKGEFGDVMLGDYR-GNKVAVKCI-----KNDATAqaFLAEASVMTQLRHSNLVQLLGVIVEE-KGGLYIVTEYMA 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDETgeVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:cd05082  84 KGSLVDYLRSRGRS--VLGGDCLLKFSLDVCEAMEYLEGNN-----FVHRDLAARNVLVSEDNVAKVSDFGLTKEASSTQ 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 578 VFSKLKASaamgYLAPEYITTGRFTDKSDVYAFGMILLQILS-GK---SKISHLMILQAVESGRLnedfMD-PNlrkNFP 652
Cdd:cd05082 157 DTGKLPVK----WTAPEALREKKFSTKSDVWSFGILLWEIYSfGRvpyPRIPLKDVVPRVEKGYK----MDaPD---GCP 225
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15225456 653 EVEAAQLARlgllCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05082 226 PAVYDVMKN----CWHLDAAMRPSFLQLREQLEHI 256
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
448-685 1.05e-14

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: 74.96  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 448 AKSSCKSdESEFLKGLKMLTLLKHENLARLRGFCCSKgrgeCFLIYEFVPNGNLLQYLDVKDETGEVLEWATRVSIINGI 527
Cdd:cd14000  47 ATDAMKN-FRLLRQELTVLSHLHHPSIVYLLGIGIHP----LMLVLELAPLGSLDHLLQQDSRSFASLGRTLQQRIALQV 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 528 ARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPS-----LADSGLHKlftdDIVFSKLKASAAM-GYLAPEYITTGR- 600
Cdd:cd14000 122 ADGLRYLHSAM-----IIYRDLKSHNVLVWTLYPNSaiiikIADYGISR----QCCRMGAKGSEGTpGFRAPEIARGNVi 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 601 FTDKSDVYAFGMILLQILSGKSK-ISHLMILQAVE-SGRLNEDFMDPNLRKnFPEVEAaqlarLGLLCTHESSNQRPSME 678
Cdd:cd14000 193 YNEKVDVFSFGMLLYEILSGGAPmVGHLKFPNEFDiHGGLRPPLKQYECAP-WPEVEV-----LMKKCWKENPQQRPTAV 266

                ....*..
gi 15225456 679 DVIQELN 685
Cdd:cd14000 267 TVVSILN 273
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
422-684 1.43e-14

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: 74.25  E-value: 1.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGSVA--AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgECfLIYEFVPNG 499
Cdd:cd14148   1 IIGVGGFGKVYKGLWRGEEVAvkAARQDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPH-LC-LVMEYARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDVKDETGEVL-EWATRvsiingIARGIVYLHgeNGNKPAIVHQNLSAEKILI------DHWYNPSL--ADSGL- 569
Cdd:cd14148  79 ALNRALAGKKVPPHVLvNWAVQ------IARGMNYLH--NEAIVPIIHRDLKSSNILIlepienDDLSGKTLkiTDFGLa 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 570 ---HKLftddivfSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESGRLNEdfmdpn 646
Cdd:cd14148 151 rewHKT-------TKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNK------ 217
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15225456 647 LRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd14148 218 LTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRL 255
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
417-690 1.54e-14

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


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 75.10  E-value: 1.54e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGI-LRDGSVA----AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrgECFL 491
Cdd:cd05110   9 LKRVKVLGSGAFGTVYKGIwVPEGETVkipvAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCLSP---TIQL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 IYEFVPNGNLLQYL-DVKDETGE--VLEWATRvsiingIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd05110  86 VTQLMPHGCLLDYVhEHKDNIGSqlLLNWCVQ------IAKGMMYLEERR-----LVHRDLAARNVLVKSPNHVKITDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 569 LHKLFT-DDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVesgrlnEDFMDPNL 647
Cdd:cd05110 155 LARLLEgDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREI------PDLLEKGE 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15225456 648 RKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05110 229 RLPQPPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMARD 271
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
443-687 1.56e-14

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 74.83  E-value: 1.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGfCCSKGRGECFLIYEFVPNGNLLQYLDVKDE--TGEVLEWAT 519
Cdd:cd05054  41 AVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLLG-ACTKPGGPLMVIVEFCKFGNLSNYLRSKREefVPYRDKGAR 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 520 RVSIING--------------------IARGIVYLhgenGNKPAIvHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIV 578
Cdd:cd05054 120 DVEEEEDddelykepltledlicysfqVARGMEFL----ASRKCI-HRDLAARNILLSENNVVKICDFGLARdIYKDPDY 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 579 FSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMIlqavesgrlNEDF---MDPNLRKNFPEV 654
Cdd:cd05054 195 VRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASPYPGVQM---------DEEFcrrLKEGTRMRAPEY 265
                       250       260       270
                ....*....|....*....|....*....|...
gi 15225456 655 EAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05054 266 TTPEIYQIMLDCWHGEPKERPTFSELVEKLGDL 298
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
409-619 1.61e-14

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: 74.38  E-value: 1.61e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERATQSFSEInlLGKSNVSSVYKGILRDGSVAAIKcIAKSSCKSDES-----EFLKGLKMLTLLKHENLARLRGFCCS 483
Cdd:cd05056   2 EIQREDITLGRC--IGEGQFGDVYQGVYMSPENEKIA-VAVKTCKNCTSpsvreKFLQEAYIMRQFDHPHIVKLIGVITE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 484 KgrgECFLIYEFVPNGNLLQYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPS 563
Cdd:cd05056  79 N---PVWIVMELAPLGELRSYLQVNKYS---LDLASLILYAYQLSTALAYLESKR-----FVHRDIAARNVLVSSPDCVK 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 564 LADSGLHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05056 148 LGDFGLSRYMEDESYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILM 203
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
443-680 1.89e-14

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: 74.19  E-value: 1.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskgRGECFLIY-EFVPNGNLLQYLdvKDETGEvLEWATRV 521
Cdd:cd05064  37 AIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVIT---RGNTMMIVtEYMSNGALDSFL--RKHEGQ-LVAGQLM 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 522 SIINGIARGIVYLhGENGnkpaIVHQNLSAEKILIdhwyNPSLA--DSGLHKLFTDDI--VFSKLKASAAMGYLAPEYIT 597
Cdd:cd05064 111 GMLPGLASGMKYL-SEMG----YVHKGLAAHKVLV----NSDLVckISGFRRLQEDKSeaIYTTMSGKSPVLWAAPEAIQ 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 598 TGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESG-RLNEDFMDPNLrknfpeveaaqLARLGLLCTHESSN 672
Cdd:cd05064 182 YHHFSSASDVWSFGIVMWEVMSYGERpywdMSGQDVIKAVEDGfRLPAPRNCPNL-----------LHQLMLDCWQKERG 250

                ....*...
gi 15225456 673 QRPSMEDV 680
Cdd:cd05064 251 ERPRFSQI 258
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
431-619 2.48e-14

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: 73.90  E-value: 2.48e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 431 VYKGILRDGSVAaIKCIAKSSCKSDESEflKGLKMLTLLKHENLARlrgFCCSKGRG-----ECFLIYEFVPNGNLLQYL 505
Cdd:cd14053  11 VWKAQYLNRLVA-VKIFPLQEKQSWLTE--REIYSLPGMKHENILQ---FIGAEKHGesleaEYWLITEFHERGSLCDYL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 506 dvkdeTGEVLEWATRVSIINGIARGIVYLHGE-----NGNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFS 580
Cdd:cd14053  85 -----KGNVISWNELCKIAESMARGLAYLHEDipatnGGHKPSIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKSCG 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 581 KLKASaaMG---YLAPEyITTG--RFTDKS----DVYAFGMILLQILS 619
Cdd:cd14053 160 DTHGQ--VGtrrYMAPE-VLEGaiNFTRDAflriDMYAMGLVLWELLS 204
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
416-686 3.34e-14

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: 73.27  E-value: 3.34e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINLLGKSNVSSVY----KGILRDG--SVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcsKGRGEC 489
Cdd:cd05046   6 NLQEITTLGRGEFGEVFlakaKGIEEEGgeTLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLC--REAEPH 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 FLIYEFVPNGNLLQYLDV---KDETGEV--LEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05046  84 YMILEYTDLGDLKQFLRAtksKDEKLKPppLSTKQKVALCTQIALGMDHLS-----NARFVHRDLAARNCLVSSQREVKV 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 565 ADSGLHKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GK---SKISHLMILQAVESGRlne 640
Cdd:cd05046 159 SLLSLSKDVYNSEYYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTqGElpfYGLSDEEVLNRLQAGK--- 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15225456 641 dfmdpnLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd05046 236 ------LELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVSALGE 275
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
436-621 3.53e-14

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: 73.25  E-value: 3.53e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 436 LRDGSVAAIKCIAKSSCKSDESEFLKGLKMLT--------------LLKHENLARLRGFCCSkgRGECFLIYEFVPNGNL 501
Cdd:cd14077  23 IRTGEKCAIKIIPRASNAGLKKEREKRLEKEIsrdirtireaalssLLNHPHICRLRDFLRT--PNHYYMLFEYVDGGQL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDvkdETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDivfSK 581
Cdd:cd14077 101 LDYII---SHGKLKEKQAR-KFARQIASALDYLHRNS-----IVHRDLKIENILISKSGNIKIIDFGLSNLYDPR---RL 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 15225456 582 LKASAAMGYL-APEYITTGRFTD-KSDVYAFGMILLQILSGK 621
Cdd:cd14077 169 LRTFCGSLYFaAPELLQAQPYTGpEVDVWSFGVVLYVLVCGK 210
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
437-619 5.00e-14

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


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 73.04  E-value: 5.00e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEFVPNGNLLQYL---DVKDETGE 513
Cdd:cd05079  31 NTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEFLPSGSLKEYLprnKNKINLKQ 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 514 VLEWATRvsiingIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLK--ASAAMGYL 591
Cdd:cd05079 111 QLKYAVQ------ICKGMDYLGSRQ-----YVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKddLDSPVFWY 179
                       170       180
                ....*....|....*....|....*...
gi 15225456 592 APEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05079 180 APECLIQSKFYIASDVWSFGVTLYELLT 207
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
443-689 7.50e-14

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: 72.74  E-value: 7.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKDETG--------- 512
Cdd:cd05098  49 AVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDG--PLYVIVEYASKGNLREYLQARRPPGmeycynpsh 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 513 ---EVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAM 588
Cdd:cd05098 127 npeEQLSSKDLVSCAYQVARGMEYLASKK-----CIHRDLAARNVLVTEDNVMKIADFGLARdIHHIDYYKKTTNGRLPV 201
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 589 GYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVEsgrlnedFMDPNLRKNFPEVEAAQLARLGLLCT 667
Cdd:cd05098 202 KWMAPEALFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPGVPVEELFK-------LLKEGHRMDKPSNCTNELYMMMRDCW 274
                       250       260
                ....*....|....*....|..
gi 15225456 668 HESSNQRPSMEDVIQELNNLAA 689
Cdd:cd05098 275 HAVPSQRPTFKQLVEDLDRIVA 296
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
439-676 8.37e-14

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: 72.24  E-value: 8.37e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIAKSScKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGNLLQYL---DVKdetgevL 515
Cdd:cd14042  30 GNLVAIKKVNKKR-IDLTREVLKELKHMRDLQHDNLTRFIGACVDPPN--ICILTEYCPKGSLQDILeneDIK------L 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 516 EWATRVSIINGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAA-MGYLAPE 594
Cdd:cd14042 101 DWMFRYSLIHDIVKGMHYLH----DSEIKSHGNLKSSNCVVDSRFVLKITDFGLHSFRSGQEPPDDSHAYYAkLLWTAPE 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 595 YITTGRF----TDKSDVYAFGMILLQI--------LSGKSKISHLMILQAVESGrlnedfMDPNLRKNFPEVEAAQ-LAR 661
Cdd:cd14042 177 LLRDPNPpppgTQKGDVYSFGIILQEIatrqgpfyEEGPDLSPKEIIKKKVRNG------EKPPFRPSLDELECPDeVLS 250
                       250
                ....*....|....*
gi 15225456 662 LGLLCTHESSNQRPS 676
Cdd:cd14042 251 LMQRCWAEDPEERPD 265
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
439-684 8.78e-14

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 71.83  E-value: 8.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIaksSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgeCFLIYEFVPNGNLLQYLDVKDETGEVLEWA 518
Cdd:cd05083  29 GQKVAVKNI---KCDVTAQAFLEETAVMTKLQHKNLVRLLGVILHNG---LYIVMELMSKGNLVNFLRSRGRALVPVIQL 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 519 TRVSIinGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLkasaAMGYLAPEYITT 598
Cdd:cd05083 103 LQFSL--DVAEGMEYLESKK-----LVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDNSRL----PVKWTAPEALKN 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 599 GRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRLnedfMDPnlrknfPEVEAAQLARLGLLCTHESSNQR 674
Cdd:cd05083 172 KKFSSKSDVWSYGVLLWEVFSyGRApypKMSVKEVKEAVEKGYR----MEP------PEGCPPDVYSIMTSCWEAEPGKR 241
                       250
                ....*....|
gi 15225456 675 PSMEDVIQEL 684
Cdd:cd05083 242 PSFKKLREKL 251
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
423-621 8.89e-14

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: 71.55  E-value: 8.89e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGS--VAAIKCIAKSSCKSDESE-FLKGLKMLTLLKHENLARLRGFccSKGRGECFLIYEFVPNG 499
Cdd:cd14121   3 LGSGTYATVYKAYRKSGAreVVAVKCVSKSSLNKASTEnLLTEIELLKKLKHPHIVELKDF--QWDEEHIYLIMEYCSGG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDVKdetgEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSL--ADSGLHKLFTDDI 577
Cdd:cd14121  81 DLSRFIRSR----RTLPESTVRRFLQQLASALQFLREHN-----ISHMDLKPQNLLLSSRYNPVLklADFGFAQHLKPND 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15225456 578 VFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd14121 152 EAHSLRGSPL--YMAPEMILKKKYDARVDLWSVGVILYECLFGR 193
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
437-687 9.03e-14

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: 72.74  E-value: 9.03e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYL---------- 505
Cdd:cd05101  54 KEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDG--PLYVIVEYASKGNLREYLrarrppgmey 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 506 --DVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL- 582
Cdd:cd05101 132 syDINRVPEEQMTFKDLVSCTYQLARGMEYLASQK-----CIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTt 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVEsgrlnedFMDPNLRKNFPEVEAAQLAR 661
Cdd:cd05101 207 NGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPGIPVEELFK-------LLKEGHRMDKPANCTNELYM 279
                       250       260
                ....*....|....*....|....*.
gi 15225456 662 LGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05101 280 MMRDCWHAVPSQRPTFKQLVEDLDRI 305
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
440-689 9.20e-14

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


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 72.69  E-value: 9.20e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 440 SVAAIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYL------------D 506
Cdd:cd05099  45 VTVAVKMLKDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQEG--PLYVIVEYAAKGNLREFLrarrppgpdytfD 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 507 VKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKlFTDDIVFSKLKASA 586
Cdd:cd05099 123 ITKVPEEQLSFKDLVSCAYQVARGMEYLESRR-----CIHRDLAARNVLVTEDNVMKIADFGLAR-GVHDIDYYKKTSNG 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 587 AM--GYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSK---ISHLMILQAVESGRlnedfmdpnlRKNFPEVEAAQLA 660
Cdd:cd05099 197 RLpvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTlGGSPypgIPVEELFKLLREGH----------RMDKPSNCTHELY 266
                       250       260
                ....*....|....*....|....*....
gi 15225456 661 RLGLLCTHESSNQRPSMEDVIQELNNLAA 689
Cdd:cd05099 267 MLMRECWHAVPTQRPTFKQLVEALDKVLA 295
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
421-619 1.53e-13

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


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 71.95  E-value: 1.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRDGSV---AAIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCcsKGRGECFLIYEFV 496
Cdd:cd05088  13 DVIGEGNFGQVLKARIKKDGLrmdAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGAC--EHRGYLYLAIEYA 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLD------------VKDETGEVLEWATRVSIINGIARGIVYLhgengNKPAIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05088  91 PHGNLLDFLRksrvletdpafaIANSTASTLSSQQLLHFAADVARGMDYL-----SQKQFIHRDLAARNILVGENYVAKI 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 565 ADSGLHKlfTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05088 166 ADFGLSR--GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVS 218
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
423-690 1.77e-13

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: 71.19  E-value: 1.77e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGIL-RDGSV--AAIKCIAKSSCKSDESE-FLKGLKMLTLLKHENLARLRGFCCSKGRGECF----LIYE 494
Cdd:cd05075   8 LGEGEFGSVMEGQLnQDDSVlkVAVKTMKIAICTRSEMEdFLSEAVCMKEFDHPNVMRLIGVCLQNTESEGYpspvVILP 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLdVKDETGEV---LEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL-H 570
Cdd:cd05075  88 FMKHGDLHSFL-LYSRLGDCpvyLPTQMLVKFMTDIASGMEYLSSKN-----FIHRDLAARNCMLNENMNVCVADFGLsK 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKIShlmilqAVESGRLNEDFMDPNLRK 649
Cdd:cd05075 162 KIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATrGQTPYP------GVENSEIYDYLRQGNRLK 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 650 NFPEVEAAqLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05075 236 QPPDCLDG-LYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
423-621 1.80e-13

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: 71.10  E-value: 1.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKC---IAKSScKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEFVPNG 499
Cdd:cd13983   9 LGRGSFKTVYRAFDTEEGIEVAWNeikLRKLP-KAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIFITELMTSG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYL-DVKDETGEVLE-WATRvsiingIARGIVYLHGENgnkPAIVHQNLSAEKILIDhwynpslADSGLHKLftDDI 577
Cdd:cd13983  88 TLKQYLkRFKRLKLKVIKsWCRQ------ILEGLNYLHTRD---PPIIHRDLKCDNIFIN-------GNTGEVKI--GDL 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15225456 578 VFSKLK----ASAAMG---YLAPEyITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd13983 150 GLATLLrqsfAKSVIGtpeFMAPE-MYEEHYDEKVDIYAFGMCLLEMATGE 199
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
421-619 2.05e-13

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 70.97  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCK----SDESEFLKGLKMLTLLKHENLARLRGFCCSKgRGECFLIYEFV 496
Cdd:cd05058   1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRitdiEEVEQFLKEGIIMKDFSHPNVLSLLGICLPS-EGSPLVVLPYM 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL-------DVKDETGEVLEwatrvsiingIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd05058  80 KHGDLRNFIrsethnpTVKDLIGFGLQ----------VAKGMEYLASKK-----FVHRDLAARNCMLDESFTVKVADFGL 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15225456 570 HKLFTDDIVFS---KLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05058 145 ARDIYDKEYYSvhnHTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMT 197
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
423-686 2.18e-13

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: 70.96  E-value: 2.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR------DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFV 496
Cdd:cd05049  13 LGEGAFGKVFLGECYnlepeqDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEGD--PLLMVFEYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDVKD-----------ETGEvLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLA 565
Cdd:cd05049  91 EHGDLNKFLRSHGpdaaflasedsAPGE-LTLSQLLHIAVQIASGMVYLASQH-----FVHRDLATRNCLVGTNLVVKIG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 566 DSGLHK-LFTDDivFSKLKASAAMG--YLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRL 638
Cdd:cd05049 165 DFGMSRdIYSTD--YYRVGGHTMLPirWMPPESILYRKFTTESDVWSFGVVLWEIFTyGKQpwfQLSNTEVIECITQGRL 242
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 639 NEDfmdpnlrknfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd05049 243 LQR----------PRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQE 280
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
421-621 2.61e-13

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: 70.33  E-value: 2.61e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGI-LRDGSVAAIKCIaksSCKSDESEFLKGLKM----LTLLKHENLARLRGFccSKGRGECFLIYEF 495
Cdd:cd06627   6 DLIGRGAFGSVYKGLnLNTGEFVAIKQI---SLEKIPKSDLKSVMGeidlLKKLNHPNIVKYIGS--VKTKDSLYIILEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLDVKDETGEVLewatrVSI-INGIARGIVYLHGENgnkpaIVHQNLSAEKILIdhwynpslADSGLHKLfT 574
Cdd:cd06627  81 VENGSLASIIKKFGKFPESL-----VAVyIYQVLEGLAYLHEQG-----VIHRDIKGANILT--------TKDGLVKL-A 141
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 575 DDIVFSKLKASAAMG--------YLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd06627 142 DFGVATKLNEVEKDEnsvvgtpyWMAPEVIEMSGVTTASDIWSVGCTVIELLTGN 196
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
422-684 3.48e-13

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: 70.45  E-value: 3.48e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGSVA--AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNG 499
Cdd:cd14146   1 IIGVGGFGKVYRATWKGQEVAvkAARQDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEP--NLCLVMEFARGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDVKDETGE-----------VLEWATRvsiingIARGIVYLHgENGNKPaIVHQNLSAEKILI------DHWYNP 562
Cdd:cd14146  79 TLNRALAAANAAPGprrarripphiLVNWAVQ------IARGMLYLH-EEAVVP-ILHRDLKSSNILLlekiehDDICNK 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 563 SL--ADSGLHKLFTDDivfSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGK---SKISHLMILQAVESGR 637
Cdd:cd14146 151 TLkiTDFGLAREWHRT---TKMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEvpyRGIDGLAVAYGVAVNK 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 638 LNEDfmdpnlrknFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd14146 228 LTLP---------IPSTCPEPFAKLMKECWEQDPHIRPSFALILEQL 265
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
411-684 4.84e-13

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: 69.83  E-value: 4.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 411 ERATQSFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIaksscKSDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGEC 489
Cdd:cd14047   2 ERFRQDFKEIELIGSGGFGQVFKAKHRiDGKTYAIKRV-----KLNNEKAEREVKALAKLDHPNIVRY--NGCWDGFDYD 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 ----------------FLIYEFVPNGNLLQYldVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEK 553
Cdd:cd14047  75 petsssnssrsktkclFIQMEFCEKGTLESW--IEKRNGEKLDKVLALEIFEQITKGVEYIHSKK-----LIHRDLKPSN 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 554 ILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSgkskishlMILQAV 633
Cdd:cd14047 148 IFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLS--YMSPEQISSQDYGKEVDIYALGLILFELLH--------VCDSAF 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15225456 634 ESGRLNEDFMDPNLRKNFPEVEAAQLARLGLLCTHESSNqRPSMEDVIQEL 684
Cdd:cd14047 218 EKSKFWTDLRNGILPDIFDKRYKIEKTIIKKMLSKKPED-RPNASEILRTL 267
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
419-690 6.27e-13

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


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 69.67  E-value: 6.27e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 419 EINLLGKSNVSSVYKGI-LRDGS----VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIY 493
Cdd:cd05109  11 KVKVLGSGAFGTVYKGIwIPDGEnvkiPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTS---TVQLVT 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQYL-DVKDETG--EVLEWATRvsiingIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLH 570
Cdd:cd05109  88 QLMPYGCLLDYVrENKDRIGsqDLLNWCVQ------IAKGMSYLE-----EVRLVHRDLAARNVLVKSPNHVKITDFGLA 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLF-TDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMilqaveSGRLNEDFMDPNLRK 649
Cdd:cd05109 157 RLLdIDETEYHADGGKVPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGI------PAREIPDLLEKGERL 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 650 NFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05109 231 PQPPICTIDVYMIMVKCWMIDSECRPRFRELVDEFSRMARD 271
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
421-619 6.40e-13

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 70.03  E-value: 6.40e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILR-DGSV--AAIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCcsKGRGECFLIYEFV 496
Cdd:cd05089   8 DVIGEGNFGQVIKAMIKkDGLKmnAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGAC--ENRGYLYIAIEYA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDV------------KDETGEVLEWATRVSIINGIARGIVYLhgengNKPAIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05089  86 PYGNLLDFLRKsrvletdpafakEHGTASTLTSQQLLQFASDVAKGMQYL-----SEKQFIHRDLAARNVLVGENLVSKI 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 565 ADSGLHKlfTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05089 161 ADFGLSR--GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVS 213
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
459-690 9.43e-13

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: 69.07  E-value: 9.43e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 459 FLKGLKMLTLLKHENLARLRGFCcSKGRgECFLIYEFVPNGNLLQYLDVKDEtgeVLEWATRVSIINGIARGIVYLHGEN 538
Cdd:cd14154  37 FLKEVKVMRSLDHPNVLKFIGVL-YKDK-KLNLITEYIPGGTLKDVLKDMAR---PLPWAQRVRFAKDIASGMAYLHSMN 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 539 gnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLftddIVFSKLKASAAMG-----------------------YLAPEY 595
Cdd:cd14154 112 -----IIHRDLNSHNCLVREDKTVVVADFGLARL----IVEERLPSGNMSPsetlrhlkspdrkkrytvvgnpyWMAPEM 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 596 ITTGRFTDKSDVYAFGMILLQILsgkskishlmilqavesGRLNE--DFMDPNL---------RKNFPEVEAAQLARLGL 664
Cdd:cd14154 183 LNGRSYDEKVDIFSFGIVLCEII-----------------GRVEAdpDYLPRTKdfglnvdsfREKFCAGCPPPFFKLAF 245
                       250       260
                ....*....|....*....|....*.
gi 15225456 665 LCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd14154 246 LCCDLDPEKRPPFETLEEWLEALYLH 271
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
408-680 1.03e-12

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: 69.28  E-value: 1.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 408 EEIERATQSFSEinLLGKSNVSSVYKGIL------RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFC 481
Cdd:cd05091   1 KEINLSAVRFME--ELGEDRFGKVYKGHLfgtapgEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 482 CSKGrgECFLIYEFVPNGNLLQYLDVKDETGEV------------LEWATRVSIINGIARGIVYLHGENgnkpaIVHQNL 549
Cdd:cd05091  79 TKEQ--PMSMIFSYCSHGDLHEFLVMRSPHSDVgstdddktvkstLEPADFLHIVTQIAAGMEYLSSHH-----VVHKDL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 550 SAEKILIDHWYNPSLADSGLHK-LFTDDivFSKLKASAAMG--YLAPEYITTGRFTDKSDVYAFGMILLQILSGKskish 626
Cdd:cd05091 152 ATRNVLVFDKLNVKISDLGLFReVYAAD--YYKLMGNSLLPirWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYG----- 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 627 lmiLQAVeSGRLNEDFMDPNLRKNF---PEVEAAQLARLGLLCTHESSNQRPSMEDV 680
Cdd:cd05091 225 ---LQPY-CGYSNQDVIEMIRNRQVlpcPDDCPAWVYTLMLECWNEFPSRRPRFKDI 277
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
459-687 1.30e-12

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: 68.44  E-value: 1.30e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 459 FLKGLKMLTLLKHENLARLRGFCCSKGRGEcfLIYEFVPNGNLLQYLDVKDETgevLEWATRVSIINGIARGIVYLHGEN 538
Cdd:cd14221  37 FLKEVKVMRCLEHPNVLKFIGVLYKDKRLN--FITEYIKGGTLRGIIKSMDSH---YPWSQRVSFAKDIASGMAYLHSMN 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 539 gnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD-----IVFSKLKASAAMGY--------LAPEYITTGRFTDKS 605
Cdd:cd14221 112 -----IIHRDLNSHNCLVRENKSVVVADFGLARLMVDEktqpeGLRSLKKPDRKKRYtvvgnpywMAPEMINGRSYDEKV 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 606 DVYAFGMILLQILsGKSKISHLMILQAVESGRLNEDFMDPNLRKNFPeveaAQLARLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd14221 187 DVFSFGIVLCEII-GRVNADPDYLPRTMDFGLNVRGFLDRYCPPNCP----PSFFPIAVLCCDLDPEKRPSFSKLEHWLE 261

                ..
gi 15225456 686 NL 687
Cdd:cd14221 262 TL 263
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
417-678 1.33e-12

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: 68.50  E-value: 1.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRDGS--VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYE 494
Cdd:cd14201   8 YSRKDLVGHGAFAVVFKGRHRKKTdwEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVAL--YDVQEMPNSVFLVME 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLDVKdetGEVLEWATRVsIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLhKLFT 574
Cdd:cd14201  86 YCNGGDLADYLQAK---GTLSEDTIRV-FLQQIAAAMRILHSK-----GIIHRDLKPQNILLSYASRKKSSVSGI-RIKI 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIVFSKLKASAAMG--------YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKishlmiLQAVESGRLNEDF-MDP 645
Cdd:cd14201 156 ADFGFARYLQSNMMAatlcgspmYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPP------FQANSPQDLRMFYeKNK 229
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15225456 646 NLRKNFPEVEAAQLAR--LGLLctheSSNQRPSME 678
Cdd:cd14201 230 NLQPSIPRETSPYLADllLGLL----QRNQKDRMD 260
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
423-684 1.76e-12

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 68.14  E-value: 1.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD------GSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcSKGRgECFLIYEFV 496
Cdd:cd05032  14 LGQGSFGMVYEGLAKGvvkgepETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVV-STGQ-PTLVVMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDV---KDETGEVLEWATRVSIIN---GIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLh 570
Cdd:cd05032  92 AKGDLKSYLRSrrpEAENNPGLGPPTLQKFIQmaaEIADGMAYLAAKK-----FVHRDLAARNCMVAEDLTVKIGDFGM- 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 klfTDDIVFSKL--KASAAM---GYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESGrlneD 641
Cdd:cd05032 166 ---TRDIYETDYyrKGGKGLlpvRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQpyqgLSNEEVLKFVIDG----G 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15225456 642 FMDPnlrknfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05032 239 HLDL------PENCPDKLLELMRMCWQYNPKMRPTFLEIVSSL 275
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
423-685 1.80e-12

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: 67.89  E-value: 1.80e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR---DGSVAAIKCIAK---SSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskgRGECFLIYEFV 496
Cdd:cd05037   7 LGQGTFTNIYDGILRevgDGRVQEVEVLLKvldSDHRDISESFFETASLMSQISHKHLVKLYGVCV---ADENIMVQEYV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDvKDETGEVLEWatRVSIINGIARGIVYLHgENGnkpaIVHQNLSAEKILI----DHWYNP--SLADSGLH 570
Cdd:cd05037  84 RYGPLDKYLR-RMGNNVPLSW--KLQVAKQLASALHYLE-DKK----LIHGNVRGRNILLaregLDGYPPfiKLSDPGVP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KlftddIVFSKLKASAAMGYLAPEYI-----TTGRFTDKsdvYAFGMILLQILSGKSkishlMILQAVESGRLNEDFMDp 645
Cdd:cd05037 156 I-----TVLSREERVDRIPWIAPECLrnlqaNLTIAADK---WSFGTTLWEICSGGE-----EPLSALSSQEKLQFYED- 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15225456 646 nlRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd05037 222 --QHQLPAPDCAELAELIMQCWTYEPTKRPSFRAILRDLN 259
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
423-682 1.83e-12

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 68.11  E-value: 1.83e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKC--IAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGE-C-FLIYEFVPN 498
Cdd:cd14033   9 IGRGSFKTVYRGLDTETTVEVAWCelQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSWKSTVRGHkCiILVTELMTS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 GNLLQYLD-VKDETGEVLE-WAtrvsiiNGIARGIVYLHGENgnkPAIVHQNLSAEKILIDhwyNPS----LADSGLHKL 572
Cdd:cd14033  89 GTLKTYLKrFREMKLKLLQrWS------RQILKGLHFLHSRC---PPILHRDLKCDNIFIT---GPTgsvkIGDLGLATL 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 573 FTDDIVFSKLKASAamgYLAPEyITTGRFTDKSDVYAFGMILLQILSGKSKISHL----MILQAVESGrlnedfMDPNlr 648
Cdd:cd14033 157 KRASFAKSVIGTPE---FMAPE-MYEEKYDEAVDVYAFGMCILEMATSEYPYSECqnaaQIYRKVTSG------IKPD-- 224
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 649 kNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd14033 225 -SFYKVKVPELKEIIEGCIRTDKDERFTIQDLLE 257
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
423-684 2.33e-12

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: 68.07  E-value: 2.33e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD------GSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFV 496
Cdd:cd05061  14 LGQGSFGMVYEGNARDiikgeaETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLG-VVSKGQ-PTLVVMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL-----DVKDETG-------EVLEWATRvsiingIARGIVYLhgengNKPAIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05061  92 AHGDLKSYLrslrpEAENNPGrppptlqEMIQMAAE------IADGMAYL-----NAKKFVHRDLAARNCMVAHDFTVKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 565 ADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESGrln 639
Cdd:cd05061 161 GDFGMTRdIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQpyqgLSNEQVLKFVMDG--- 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 15225456 640 eDFMDPnlrknfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05061 238 -GYLDQ------PDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
407-690 2.49e-12

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 68.51  E-value: 2.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 407 LEEIEratqsFSEINLLGKSNVSSVYKGI-LRDGS----VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFC 481
Cdd:cd05108   4 LKETE-----FKKIKVLGSGAFGTVYKGLwIPEGEkvkiPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGIC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 482 CSKGrgeCFLIYEFVPNGNLLQYL-DVKDETGE--VLEWATRvsiingIARGIVYLHGENgnkpaIVHQNLSAEKILIDH 558
Cdd:cd05108  79 LTST---VQLITQLMPFGCLLDYVrEHKDNIGSqyLLNWCVQ------IAKGMNYLEDRR-----LVHRDLAARNVLVKT 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 559 WYNPSLADSGLHKLFT-DDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAV 633
Cdd:cd05108 145 PQHVKITDFGLAKLLGaEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKpydgIPASEISSIL 224
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 634 ESG-RLNEdfmdpnlrknfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05108 225 EKGeRLPQ-----------PPICTIDVYMIMVKCWMIDADSRPKFRELIIEFSKMARD 271
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
440-685 2.52e-12

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: 68.21  E-value: 2.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 440 SVAAIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGfCCSKGrGECFLIYEFVPNGNLLQYL------------D 506
Cdd:cd05053  44 VTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLG-ACTQD-GPLYVVVEYASKGNLREFLrarrppgeeaspD 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 507 VKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKlftdDIVFSKLKASA 586
Cdd:cd05053 122 DPRVPEEQLTQKDLVSFAYQVARGMEYLASKK-----CIHRDLAARNVLVTEDNVMKIADFGLAR----DIHHIDYYRKT 192
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 587 AMGYL-----APEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVesgrlneDFMDPNLRKNFPEVEAAQLA 660
Cdd:cd05053 193 TNGRLpvkwmAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELF-------KLLKEGHRMEKPQNCTQELY 265
                       250       260
                ....*....|....*....|....*
gi 15225456 661 RLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd05053 266 MLMRDCWHEVPSQRPTFKQLVEDLD 290
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
416-687 2.82e-12

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: 67.75  E-value: 2.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINL---LGKSNVSSVYKGILRdGSVAAIKCiAKSSCKSDESEFLKGLK----MLTLLKHENLARLRGFCCSKGrgE 488
Cdd:cd14147   1 SFQELRLeevIGIGGFGKVYRGSWR-GELVAVKA-ARQDPDEDISVTAESVRqearLFAMLAHPNIIALKAVCLEEP--N 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 CFLIYEFVPNGNLLQYLDVKDETGEVL-EWATRvsiingIARGIVYLHGENgnKPAIVHQNLSAEKILI------DHWYN 561
Cdd:cd14147  77 LCLVMEYAAGGPLSRALAGRRVPPHVLvNWAVQ------IARGMHYLHCEA--LVPVIHRDLKSNNILLlqpienDDMEH 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 562 PSL--ADSGL----HKLftddivfSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVES 635
Cdd:cd14147 149 KTLkiTDFGLarewHKT-------TQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYG 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15225456 636 GRLNEdfmdpnLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14147 222 VAVNK------LTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
423-686 3.32e-12

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: 67.30  E-value: 3.32e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAaiKCIAKSSCKSDES------EFLKGLKMLTLLKHENLARLRGFCcskgRGECF-LIYEF 495
Cdd:cd05116   3 LGSGNFGTVKKGYYQMKKVV--KTVAVKILKNEANdpalkdELLREANVMQQLDNPYIVRMIGIC----EAESWmLVMEM 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLDVKDETGE--VLEWATRVSIingiarGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF 573
Cdd:cd05116  77 AELGPLNKFLQKNRHVTEknITELVHQVSM------GMKYLEESN-----FVHRDLAARNVLLVTQHYAKISDFGLSKAL 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 574 TDDIVFSKLKASAA--MGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLM----ILQAVESGRlnedfmdpnl 647
Cdd:cd05116 146 RADENYYKAQTHGKwpVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMkgneVTQMIEKGE---------- 215
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15225456 648 RKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd05116 216 RMECPAGCPPEMYDLMKLCWTYDVDERPGFAAVELRLRN 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
417-654 3.55e-12

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: 67.24  E-value: 3.55e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSC-KSDESEFLKGLK-MLTLLKHENLARLrgFCCSKGRGECFLIY 493
Cdd:cd05581   3 FKFGKPLGEGSYSTVVLAKEKeTGKEYAIKVLDKRHIiKEKKVKYVTIEKeVLSRLAHPGIVKL--YYTFQDESKLYFVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQY------LDVKDE---TGEVLEwatrvsiingiarGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd05581  81 EYAPNGDLLEYirkygsLDEKCTrfyTAEIVL-------------ALEYLHSKG-----IIHRDLKPENILLDEDMHIKI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 565 ADSGLHKLFTDDIVFSKLKASAAMG----------------YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---SKIS 625
Cdd:cd05581 143 TDFGTAKVLGPDSSPESTKGDADSQiaynqaraasfvgtaeYVSPELLNEKPAGKSSDLWALGCIIYQMLTGKppfRGSN 222
                       250       260
                ....*....|....*....|....*....
gi 15225456 626 HLMILQAVESGrlnedfmDPNLRKNFPEV 654
Cdd:cd05581 223 EYLTFQKIVKL-------EYEFPENFPPD 244
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
443-687 3.95e-12

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 68.12  E-value: 3.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKDETG--------- 512
Cdd:cd05100  48 AVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDG--PLYVLVEYASKGNLREYLRARRPPGmdysfdtck 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 513 ---EVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAM 588
Cdd:cd05100 126 lpeEQLTFKDLVSCAYQVARGMEYLASQK-----CIHRDLAARNVLVTEDNVMKIADFGLARdVHNIDYYKKTTNGRLPV 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 589 GYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVEsgrlnedFMDPNLRKNFPEVEAAQLARLGLLCT 667
Cdd:cd05100 201 KWMAPEALFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPGIPVEELFK-------LLKEGHRMDKPANCTHELYMIMRECW 273
                       250       260
                ....*....|....*....|
gi 15225456 668 HESSNQRPSMEDVIQELNNL 687
Cdd:cd05100 274 HAVPSQRPTFKQLVEDLDRV 293
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
437-680 4.96e-12

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: 66.91  E-value: 4.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIaKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFVPNGNLLQYLDVKDETGEVLE 516
Cdd:cd05092  33 QDKMLVAVKAL-KEATESARQDFQREAELLTVLQHQHIVRFYG-VCTEGE-PLIMVFEYMRHGDLNRFLRSHGPDAKILD 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 517 WATRVS-----------IINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKA 584
Cdd:cd05092 110 GGEGQApgqltlgqmlqIASQIASGMVYLASLH-----FVHRDLATRNCLVGQGLVVKIGDFGMSRdIYSTDYYRVGGRT 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 585 SAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKISHLMILQAVESGRLNEDFMDPnlRKNFPEVEAAQLArlg 663
Cdd:cd05092 185 MLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTyGKQPWYQLSNTEAIECITQGRELERP--RTCPPEVYAIMQG--- 259
                       250
                ....*....|....*..
gi 15225456 664 llCTHESSNQRPSMEDV 680
Cdd:cd05092 260 --CWQREPQQRHSIKDI 274
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
412-620 5.11e-12

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: 66.94  E-value: 5.11e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 412 RATQSFSEInlLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESeFLKGLKMLTLLKHENLARLRGFccSKGRGECF 490
Cdd:cd14166   2 RETFIFMEV--LGSGAFSEVYLVKQRsTGKLYALKCIKKSPLSRDSS-LENEIAVLKRIKHENIVTLEDI--YESTTHYY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLqylDVKDETGEVLEW-ATRVsiINGIARGIVYLHgENGnkpaIVHQNLSAEKILidhWYNPS------ 563
Cdd:cd14166  77 LVMQLVSGGELF---DRILERGVYTEKdASRV--INQVLSAVKYLH-ENG----IVHRDLKPENLL---YLTPDenskim 143
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 564 LADSGLHKLFTDDIVFSklkASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14166 144 ITDFGLSKMEQNGIMST---ACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCG 197
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
421-633 7.25e-12

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: 66.27  E-value: 7.25e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESEFLKGL----KMLTLLKHENLARLRGfccSKGRGECFLIY-E 494
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDtGDFFAVKEVSLVDDDKKSRESVKQLeqeiALLSKLRHPNIVQYYG---TEREEDNLYIFlE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNG---NLLQYLDVKDEtgEVLEWATRvSIINGIArgivYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK 571
Cdd:cd06632  83 YVPGGsihKLLQRYGAFEE--PVIRLYTR-QILSGLA----YLHSRN-----TVHRDIKGANILVDTNGVVKLADFGMAK 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15225456 572 LFTDDIVFSKLKASAAmgYLAPEYITT--GRFTDKSDVYAFGMILLQILSGKSKISHLMILQAV 633
Cdd:cd06632 151 HVEAFSFAKSFKGSPY--WMAPEVIMQknSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAI 212
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
412-682 7.74e-12

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: 66.24  E-value: 7.74e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 412 RATQSFSEINLLGKSNVSSVYK--GILrDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLarLRGFCCSKGRGEC 489
Cdd:cd14046   3 RYLTDFEELQVLGKGAFGQVVKvrNKL-DGRYYAIKKIKLRSESKNNSRILREVMLLSRLNHQHV--VRYYQAWIERANL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 FLIYEFVPNGNLLQYLDVK--DETGEVleWatrvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADS 567
Cdd:cd14046  80 YIQMEYCEKSTLRDLIDSGlfQDTDRL--W----RLFRQILEGLAYIHSQG-----IIHRDLKPVNIFLDSNGNVKIGDF 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 568 GLHK-------LFTDDIVFSKLKASAAMG----------YLAPEYI--TTGRFTDKSDVYAFGMILLQIL----SGKSKI 624
Cdd:cd14046 149 GLATsnklnveLATQDINKSTSAALGSSGdltgnvgtalYVAPEVQsgTKSTYNEKVDMYSLGIIFFEMCypfsTGMERV 228
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 625 SHLMILqavesgRLNEDFMDPNLRKNFPEVEAAQLARLgllcTHESSNQRPSMEDVIQ 682
Cdd:cd14046 229 QILTAL------RSVSIEFPPDFDDNKHSKQAKLIRWL----LNHDPAKRPSAQELLK 276
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
417-682 8.26e-12

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: 65.90  E-value: 8.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKS-DESEFLKGLKMLTLLKHENLarLRGFCCSKGRGECFLIYE 494
Cdd:cd08529   2 FEILNKLGKGSFGVVYKVVRKvDGRVYALKQIDISRMSRkMREEAIDEARVLSKLNSPYV--IKYYDSFVDKGKLNIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFT 574
Cdd:cd08529  80 YAENGDLHSLI--KSQRGRPLPEDQIWKFFIQTLLGLSHLH-----SKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILS 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIVFsklkASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKishlmiLQAVESGRLNEDFMdpnlRKNF 651
Cdd:cd08529 153 DTTNF----AQTIVGtpyYLSPELCEDKPYNEKSDVWALGCVLYELCTGKHP------FEAQNQGALILKIV----RGKY 218
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 652 PEVEA---AQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd08529 219 PPISAsysQDLSQLIDSCLTKDYRQRPDTTELLR 252
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
443-620 8.96e-12

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: 65.74  E-value: 8.96e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVPNGNLlqyLDVKDETGEVLEWATRVS 522
Cdd:cd14185  29 AMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKL--FEVYETEKEIYLILEYVRGGDL---FDAIIESVKFTEHDAALM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 523 IINgIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPS----LADSGLHKLFTDDIvfskLKASAAMGYLAPEYITT 598
Cdd:cd14185 104 IID-LCEALVYIHSKH-----IVHRDLKPENLLVQHNPDKSttlkLADFGLAKYVTGPI----FTVCGTPTYVAPEILSE 173
                       170       180
                ....*....|....*....|..
gi 15225456 599 GRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14185 174 KGYGLEVDMWAAGVILYILLCG 195
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
443-687 1.11e-11

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: 66.54  E-value: 1.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLL-KHENLARLRGfCCSKGRGECFLIYEFVPNGNLLQYLDVKDE----------- 510
Cdd:cd05102  41 AVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLG-ACTKPNGPLMVIVEFCKYGNLSNFLRAKREgfspyrerspr 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 511 ---------------------TGEVLE------------------WATRVSIINGI------ARGIVYLHGENgnkpaIV 545
Cdd:cd05102 120 trsqvrsmveavradrrsrqgSDRVASftestsstnqprqevddlWQSPLTMEDLIcysfqvARGMEFLASRK-----CI 194
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 546 HQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSK 623
Cdd:cd05102 195 HRDLAARNILLSENNVVKICDFGLARdIYKDPDYVRKGSARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSlGASP 274
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 624 ISHLMIlqavesgrlNEDF---MDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05102 275 YPGVQI---------NEEFcqrLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPTFSDLVEILGDL 332
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
460-620 1.14e-11

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: 66.19  E-value: 1.14e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 460 LKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNgNLLQYLDvKDETGevLEWATRVSIINGIARGIVYLHGENg 539
Cdd:cd07833  48 LREVKVLRQLRHENIVNLKEAFRRKGR--LYLVFEYVER-TLLELLE-ASPGG--LPPDAVRSYIWQLLQAIAYCHSHN- 120
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 540 nkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFT-------DDIVfsklkasAAMGYLAPEYITTGRFTDKS-DVYAFG 611
Cdd:cd07833 121 ----IIHRDIKPENILVSESGVLKLCDFGFARALTarpasplTDYV-------ATRWYRAPELLVGDTNYGKPvDVWAIG 189

                ....*....
gi 15225456 612 MILLQILSG 620
Cdd:cd07833 190 CIMAELLDG 198
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
420-631 1.18e-11

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: 65.84  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLArlrGFCCSKGRGEC-FLIYEFVP 497
Cdd:cd06610   6 IEVIGSGATAVVYAAYcLPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVV---SYYTSFVVGDElWLVMPLLS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDETGeVLEWATRVSIINGIARGIVYLHgENGNkpaiVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:cd06610  83 GGSLLDIMKSSYPRG-GLDEAIIATVLKEVLKGLEYLH-SNGQ----IHRDVKAGNILLGEDGSVKIADFGVSASLATGG 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 578 VFSKLKASAAMG---YLAPEYITTGR-FTDKSDVYAFGMILLQILSGKSKISHL-------MILQ 631
Cdd:cd06610 157 DRTRKVRKTFVGtpcWMAPEVMEQVRgYDFKADIWSFGITAIELATGAAPYSKYppmkvlmLTLQ 221
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
440-687 1.21e-11

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: 66.14  E-value: 1.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 440 SVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKDETG------- 512
Cdd:cd05045  31 TTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDG--PLLLIVEYAKYGSLRSFLRESRKVGpsylgsd 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 513 -------------EVLEWATRVSIINGIARGIVYLhgengNKPAIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIV 578
Cdd:cd05045 109 gnrnssyldnpdeRALTMGDLISFAWQISRGMQYL-----AEMKLVHRDLAARNVLVAEGRKMKISDFGLSRdVYEEDSY 183
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 579 FSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKIShlmilqAVESGRLnEDFMDPNLRKNFPEVEAA 657
Cdd:cd05045 184 VKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYP------GIAPERL-FNLLKTGYRMERPENCSE 256
                       250       260       270
                ....*....|....*....|....*....|
gi 15225456 658 QLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05045 257 EMYNLMLTCWKQEPDKRPTFADISKELEKM 286
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
469-619 1.57e-11

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: 65.82  E-value: 1.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 469 LKHENLARlrgFCCSKGRG-----ECFLIYEFVPNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLH-------G 536
Cdd:cd14140  46 MKHENLLQ---FIAAEKRGsnlemELWLITAFHDKGSLTDYL-----KGNIVSWNELCHIAETMARGLSYLHedvprckG 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 537 EnGNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAM-GYLAPEYITTG-RFTDKS----DVYAF 610
Cdd:cd14140 118 E-GHKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGDTHGQVGTrRYMAPEVLEGAiNFQRDSflriDMYAM 196

                ....*....
gi 15225456 611 GMILLQILS 619
Cdd:cd14140 197 GLVLWELVS 205
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
421-618 1.97e-11

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: 65.37  E-value: 1.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRDGSVAAikciaKSSCKSDESEFLKGLKM--LTLLKHENLARLRGfCCSKGRGEC---FLIYEF 495
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGEKVAV-----KIFSSRDEDSWFRETEIyqTVMLRHENILGFIA-ADIKSTGSWtqlWLITEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLdvKDET---GEVLEWATrvSIINGIArgivYLHGE---NGNKPAIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd14056  75 HEHGSLYDYL--QRNTldtEEALRLAY--SAASGLA----HLHTEivgTQGKPAIAHRDLKSKNILVKRDGTCCIADLGL 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 570 HKLFTDDIVFSKLKASAAMG---YLAPEYITTGRFTD------KSDVYAFGMILLQIL 618
Cdd:cd14056 147 AVRYDSDTNTIDIPPNPRVGtkrYMAPEVLDDSINPKsfesfkMADIYSFGLVLWEIA 204
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
422-687 2.07e-11

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: 65.25  E-value: 2.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILR--DGSV--AAIKCIAKSSCKSDE-SEFLKGLKMLTLLKHENLARLRGFCCSKGRGECF----LI 492
Cdd:cd05035   6 ILGEGEFGSVMEAQLKqdDGSQlkVAVKTMKVDIHTYSEiEEFLSEAACMKDFDHPNVMRLIGVCFTASDLNKPpspmVI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLdVKDETGEV---LEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd05035  86 LPFMKHGDLHSYL-LYSRLGGLpekLPLQTLLKFMVDIAKGMEYLSNRN-----FIHRDLAARNCMLDENMTVCVADFGL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 570 -HKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKSKIShlmilqAVESGRLnEDFMDPNL 647
Cdd:cd05035 160 sRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATrGQTPYP------GVENHEI-YDYLRNGN 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 15225456 648 RKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05035 233 RLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENI 272
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
423-619 2.09e-11

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: 64.85  E-value: 2.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSscKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGNLL 502
Cdd:cd14156   1 IGSGFFSKVYKVTHGATGKVMVVKIYKN--DVDQHKIVREISLLQKLSHPNIVRYLGICVKDEK--LHPILEYVSGGCLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDETgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYN---PSLADSGLHKLFTDDIVF 579
Cdd:cd14156  77 ELLAREELP---LSWREKVELACDISRGMVYLHSKN-----IYHRDLNSKNCLIRVTPRgreAVVTDFGLAREVGEMPAN 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15225456 580 S---KLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd14156 149 DperKLSLVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILA 191
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
417-621 2.09e-11

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: 65.14  E-value: 2.09e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEF 495
Cdd:cd06621   3 IVELSSLGEGAGGSVTKCRLRNtKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQDSSIGIAMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQ-YLDVKDETGEVLEwatRV--SIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGlhkl 572
Cdd:cd06621  83 CEGGSLDSiYKKVKKKGGRIGE---KVlgKIAESVLKGLSYLHSRK-----IIHRDIKPSNILLTRKGQVKLCDFG---- 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 573 ftddiVFSKLKASAAMG------YLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd06621 151 -----VSGELVNSLAGTftgtsyYMAPERIQGGPYSITSDVWSLGLTLLEVAQNR 200
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
438-619 2.12e-11

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: 64.88  E-value: 2.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 438 DGSVAAIKCIAKSSCKSDESeFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKDETgevLEW 517
Cdd:cd14045  29 DGRTVAIKKIAKKSFTLSKR-IRKEVKQVRELDHPNLCKFIGGCIEVP--NVAIITEYCPKGSLNDVLLNEDIP---LNW 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 518 ATRVSIINGIARGIVYLHgenGNKpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIV--FSKLKASAAMGYLAPEY 595
Cdd:cd14045 103 GFRFSFATDIARGMAYLH---QHK--IYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSenASGYQQRLMQVYLPPEN 177
                       170       180
                ....*....|....*....|....*.
gi 15225456 596 ITTGRF--TDKSDVYAFGMILLQILS 619
Cdd:cd14045 178 HSNTDTepTQATDVYSYAIILLEIAT 203
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
423-688 3.33e-11

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 64.31  E-value: 3.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRdGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskgRGECFLIYEFVPNGNLL 502
Cdd:cd14151  16 IGSGSFGTVYKGKWH-GDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYST---KPQLAIVTQWCEGSSLY 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDETGEVLEWatrVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKL---FTDDIVF 579
Cdd:cd14151  92 HHLHIIETKFEMIKL---IDIARQTAQGMDYLHAK-----SIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQF 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 580 SKLkaSAAMGYLAPEYI---TTGRFTDKSDVYAFGMILLQILSGKSKISHL----MILQAVESGRLNEDFmdPNLRKNFP 652
Cdd:cd14151 164 EQL--SGSILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMTGQLPYSNInnrdQIIFMVGRGYLSPDL--SKVRSNCP 239
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 15225456 653 EveaaQLARLGLLCTHESSNQRPSMEDVIQELNNLA 688
Cdd:cd14151 240 K----AMKRLMAECLKKKRDERPLFPQILASIELLA 271
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
469-681 3.69e-11

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: 64.25  E-value: 3.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 469 LKHENLARLRGFCCSKGRGECFLIyEFVPNGNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHgENGnkpaIVHQN 548
Cdd:cd13994  54 LHHPNIVKVLDLCQDLHGKWCLVM-EYCPGGDLFTLI----EKADSLSLEEKDCFFKQILRGVAYLH-SHG----IAHRD 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 549 LSAEKILIDHWYNPSLADSGLHKLFTDD-----IVFSKLKASAAmgYLAPEYITTGRFTDKS-DVYAFGMILLQILSGK- 621
Cdd:cd13994 124 LKPENILLDEDGVLKLTDFGTAEVFGMPaekesPMSAGLCGSEP--YMAPEVFTSGSYDGRAvDVWSCGIVLFALFTGRf 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15225456 622 ----SKISHLMILQAVESGRLNEDFMDPNlrKNFPEVEAAQLARLGLlctHESSNQRPSMEDVI 681
Cdd:cd13994 202 pwrsAKKSDSAYKAYEKSGDFTNGPYEPI--ENLLPSECRRLIYRML---HPDPEKRITIDEAL 260
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
456-618 3.70e-11

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: 64.19  E-value: 3.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 456 ESEFLKGLKMLTLLKHENLARLRGFCCSKGRGEcfLIYEFVPNGNLLQYLDVKDEtgevLEWATRVSIINGIARGIVYLH 535
Cdd:cd14222  34 QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLN--LLTEFIEGGTLKDFLRADDP----FPWQQKVSFAKGIASGMAYLH 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 536 GEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVF----------------SKLKASAAMG---YLAPEYI 596
Cdd:cd14222 108 SM-----SIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKpppdkpttkkrtlrknDRKKRYTVVGnpyWMAPEML 182
                       170       180
                ....*....|....*....|..
gi 15225456 597 TTGRFTDKSDVYAFGMILLQIL 618
Cdd:cd14222 183 NGKSYDEKVDIFSFGIVLCEII 204
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
423-685 3.71e-11

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: 64.15  E-value: 3.71e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD---GSVAAIKCIAK---SSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIYEFV 496
Cdd:cd14208   7 LGKGSFTKIYRGLRTDeedDERCETEVLLKvmdPTHGNCQESFLEAASIMSQISHKHLVLLHGVCVGK---DSIMVQEFV 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDVKDETGEV-LEWatRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILI----DHWYNP--SLADSGL 569
Cdd:cd14208  84 CHGALDLYLKKQQQKGPVaISW--KLQVVKQLAYALNYLEDKQ-----LVHGNVSAKKVLLsregDKGSPPfiKLSDPGV 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 570 hklftDDIVFSKLKASAAMGYLAPEYITTGR-FTDKSDVYAFGMILLQILSGKSkishlMILQAVESGRLNEDFMDpnlR 648
Cdd:cd14208 157 -----SIKVLDEELLAERIPWVAPECLSDPQnLALEADKWGFGATLWEIFSGGH-----MPLSALDPSKKLQFYND---R 223
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15225456 649 KNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd14208 224 KQLPAPHWIELASLIQQCMSYNPLLRPSFRAIIRDLN 260
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
420-617 4.68e-11

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: 64.38  E-value: 4.68e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILRDGSVAaIKCIAKSSCKS--DESEFLKGLkmltLLKHENLArlrGFCCSK--GRGEC---FLI 492
Cdd:cd14142  10 VECIGKGRYGEVWRGQWQGESVA-VKIFSSRDEKSwfRETEIYNTV----LLRHENIL---GFIASDmtSRNSCtqlWLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLDVkdetgEVLEWATRVSIINGIARGIVYLHGE-NGN--KPAIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd14142  82 THYHENGSLYDYLQR-----TTLDHQEMLRLALSAASGLVHLHTEiFGTqgKPAIAHRDLKSKNILVKSNGQCCIADLGL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 570 ---HKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTD------KSDVYAFGMILLQI 617
Cdd:cd14142 157 avtHSQETNQLDVGNNPRVGTKRYMAPEVLDETINTDcfesykRVDIYAFGLVLWEV 213
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
423-639 4.92e-11

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: 63.40  E-value: 4.92e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESEFLKG-LKMLTLLKHENLARLRGfcCSKGRGECFLIYEFVPNGN 500
Cdd:cd14009   1 IGRGSFATVWKGRHKQtGEVVAIKEISRKKLNKKLQENLESeIAILKSIKHPNIVRLYD--VQKTEDFIYLVLEYCAGGD 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDVKdetGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILidhwynpsLADSGLH-KLFTDDIVF 579
Cdd:cd14009  79 LSQYIRKR---GRLPEAVAR-HFMQQLASGLKFLRSKN-----IIHRDLKPQNLL--------LSTSGDDpVLKIADFGF 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225456 580 SKLKASAAMG--------YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---SKISHLMILQAVESGRLN 639
Cdd:cd14009 142 ARSLQPASMAetlcgsplYMAPEILQFQKYDAKADLWSVGAILFEMLVGKppfRGSNHVQLLRNIERSDAV 212
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
443-621 6.15e-11

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: 63.36  E-value: 6.15e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESE-FL-KGLKMLTLLKHENLARLRGF--CCSKgrgeCFLIYEFVPNGNLLQYLDVKdetGEVLEWA 518
Cdd:cd14080  31 ACKIIDKKKAPKDFLEkFLpRELEILRKLRHPNIIQVYSIfeRGSK----VFIFMEYAEHGDLLEYIQKR---GALSESQ 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 519 TRVsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDD--IVFSK-LKASAAmgYLAPEy 595
Cdd:cd14080 104 ARI-WFRQLALAVQYLHSLD-----IAHRDLKCENILLDSNNNVKLSDFGFARLCPDDdgDVLSKtFCGSAA--YAAPE- 174
                       170       180
                ....*....|....*....|....*...
gi 15225456 596 ITTGRFTD--KSDVYAFGMILLQILSGK 621
Cdd:cd14080 175 ILQGIPYDpkKYDIWSLGVILYIMLCGS 202
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
423-675 7.10e-11

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


Pssm-ID: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 63.50  E-value: 7.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRdGSVAaIKCIAKSSCKSDESEFLKG-LKMLTLLKHENLARLRGFCCskgRGECFLIYEFVPNGNL 501
Cdd:cd14150   8 IGTGSFGTVFRGKWH-GDVA-VKILKVTEPTPEQLQAFKNeMQVLRKTRHVNILLFMGFMT---RPNFAIITQWCEGSSL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKDETGEVLEwatRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSK 581
Cdd:cd14150  83 YRHLHVTETRFDTMQ---LIDVARQTAQGMDYLHAKN-----IIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSQQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 L-KASAAMGYLAPEYI---TTGRFTDKSDVYAFGMILLQILSGKSKISHL----MILQAVESGRLNEDFmdPNLRKNFPE 653
Cdd:cd14150 155 VeQPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMSGTLPYSNInnrdQIIFMVGRGYLSPDL--SKLSSNCPK 232
                       250       260
                ....*....|....*....|..
gi 15225456 654 veaaQLARLGLLCTHESSNQRP 675
Cdd:cd14150 233 ----AMKRLLIDCLKFKREERP 250
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
423-621 7.88e-11

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: 63.08  E-value: 7.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGiLRDGSVA--AIKCIAKSScksdESEFLKGLKMLTLLKHENLarLRGFCCSKGRGECFLIYEFVPNGN 500
Cdd:cd14010   8 IGRGKHSVVYKG-RRKGTIEfvAIKCVDKSK----RPEVLNEVRLTHELKHPNV--LKFYEWYETSNHLWLVVEYCTGGD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYL--DVKDETGEVLEWATRvsiingIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI- 577
Cdd:cd14010  81 LETLLrqDGNLPESSVRKFGRD------LVRGLHYIH-----SKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEILk 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 578 -----------VFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd14010 150 elfgqfsdegnVNKVSKKQAKRGtpyYMAPELFQGGVHSFASDLWALGCVLYEMFTGK 207
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
443-687 8.61e-11

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 63.85  E-value: 8.61e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLLKHE-NLARLRGFCCSKGrGECFLIYEFVPNGNLLQYL---------------- 505
Cdd:cd05103  41 AVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLLGACTKPG-GPLMVIVEFCKFGNLSAYLrskrsefvpyktkgar 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 506 ----------------------------------------DVKDETGE-------VLEWATRVSIINGIARGIVYLHGEN 538
Cdd:cd05103 120 frqgkdyvgdisvdlkrrldsitssqssassgfveekslsDVEEEEAGqedlykdFLTLEDLICYSFQVAKGMEFLASRK 199
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 539 gnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQI 617
Cdd:cd05103 200 -----CIHRDLAARNILLSENNVVKICDFGLARdIYKDPDYVRKGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEI 274
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15225456 618 LS-GKSKISHLMIlqavesgrlNEDF---MDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd05103 275 FSlGASPYPGVKI---------DEEFcrrLKEGTRMRAPDYTTPEMYQTMLDCWHGEPSQRPTFSELVEHLGNL 339
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
449-681 1.13e-10

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 62.55  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 449 KSSCKSDESEFLKGLKMLTLLKHENLARL-RGFCCSKG-RGECFLIYEFVPNGNLLQYLDVKDETGEVL------EWATR 520
Cdd:cd13984  32 RKIFKAQEEKIRAVFDNLIQLDHPNIVKFhRYWTDVQEeKARVIFITEYMSSGSLKQFLKKTKKNHKTMnekswkRWCTQ 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 521 vsiingIARGIVYLHGENgnkPAIVHQNLSAEKILIDHwynpsladSGLHKL--FTDDIVFSKLKA----SAAMGYLAPE 594
Cdd:cd13984 112 ------ILSALSYLHSCD---PPIIHGNLTCDTIFIQH--------NGLIKIgsVAPDAIHNHVKTcreeHRNLHFFAPE 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 595 YITTGRFTDKSDVYAFGMILL-------QILSGKSKISHLMILQAVESgrlnedfMDPNLRKNFPEveaaqlarlglLCT 667
Cdd:cd13984 175 YGYLEDVTTAVDIYSFGMCALemaaleiQSNGEKVSANEEAIIRAIFS-------LEDPLQKDFIR-----------KCL 236
                       250
                ....*....|....
gi 15225456 668 HESSNQRPSMEDVI 681
Cdd:cd13984 237 SVAPQDRPSARDLL 250
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
437-688 1.38e-10

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: 62.72  E-value: 1.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIaKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCcskGRGE-CFLIYEFVPNGNLLQYLDV-------- 507
Cdd:cd05094  33 KDKMLVAVKTL-KDPTLAARKDFQREAELLTNLQHDHIVKFYGVC---GDGDpLIMVFEYMKHGDLNKFLRAhgpdamil 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 508 -----KDETGEvLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSK 581
Cdd:cd05094 109 vdgqpRQAKGE-LGLSQMLHIATQIASGMVYLASQH-----FVHRDLATRNCLVGANLLVKIGDFGMSRdVYSTDYYRVG 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 582 LKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRLNEDfmdpnlrknfPEVEAA 657
Cdd:cd05094 183 GHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTyGKQpwfQLSNTEVIECITQGRVLER----------PRVCPK 252
                       250       260       270
                ....*....|....*....|....*....|.
gi 15225456 658 QLARLGLLCTHESSNQRPSMEDVIQELNNLA 688
Cdd:cd05094 253 EVYDIMLGCWQREPQQRLNIKEIYKILHALG 283
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
441-687 1.77e-10

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 63.10  E-value: 1.77e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 441 VAAIKCIAKSSCKSDESEFLKGLKMLTLLKHE-NLARLRGFCCSKGrGECFLIYEFVPNGNLLQYL-------------- 505
Cdd:cd14207  39 VVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLLGACTKSG-GPLMVIVEYCKYGNLSNYLkskrdffvtnkdts 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 506 -------------------------------------------DVKDETGEVLEWATR-------VSIINGIARGIVYLH 535
Cdd:cd14207 118 lqeelikekkeaeptggkkkrlesvtssesfassgfqedkslsDVEEEEEDSGDFYKRpltmedlISYSFQVARGMEFLS 197
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 536 GENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMIL 614
Cdd:cd14207 198 SRK-----CIHRDLAARNILLSENNVVKICDFGLARdIYKNPDYVRKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLL 272
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 615 LQILS-GKSKISHLMIlqavesgrlNEDF---MDPNLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14207 273 WEIFSlGASPYPGVQI---------DEDFcskLKEGIRMRAPEFATSEIYQIMLDCWQGDPNERPRFSELVERLGDL 340
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
423-622 3.14e-10

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: 60.99  E-value: 3.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD-GSVAAIKCIAKSSC-KSDESEFLKGLK-MLTLLKHENLARLrgFCCSKGRGECFLIYEFVPNG 499
Cdd:cd05123   1 LGKGSFGKVLLVRKKDtGKLYAMKVLRKKEIiKRKEVEHTLNERnILERVNHPFIVKL--HYAFQTEEKLYLVLDYVPGG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDvkdETGEVLEWATRVsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVf 579
Cdd:cd05123  79 ELFSHLS---KEGRFPEERARF-YAAEIVLALEYLHSLG-----IIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGD- 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15225456 580 sklKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd05123 149 ---RTYTFCGtpeYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKP 191
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
415-682 3.38e-10

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: 61.13  E-value: 3.38e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGILRD-GSVAAIKCIaksSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGrGECFLIY 493
Cdd:cd06612   3 EVFDILEKLGEGSYGSVYKAIHKEtGQVVAIKVV---PVEEDLQEIIKEISILKQCDSPYIVKYYG-SYFKN-TDLWIVM 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLqylDVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF 573
Cdd:cd06612  78 EYCGAGSVS---DIMKITNKTLTEEEIAAILYQTLKGLEYLHSNK-----KIHRDIKAGNILLNEEGQAKLADFGVSGQL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 574 TDdivfSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVesgrlnedFMDPN---- 646
Cdd:cd06612 150 TD----TMAKRNTVIGtpfWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAI--------FMIPNkppp 217
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15225456 647 -LRKnfPEVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd06612 218 tLSD--PEKWSPEFNDFVKKCLVKDPEERPSAIQLLQ 252
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
423-686 3.43e-10

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: 61.59  E-value: 3.43e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVY----KGILRDG--SVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRgECFLIYEFV 496
Cdd:cd05062  14 LGQGSFGMVYegiaKGVVKDEpeTRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLG-VVSQGQ-PTLVIMELM 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL-----DVKDETGEVLEWATRVSIING-IARGIVYLhgeNGNKpaIVHQNLSAEKILIDHWYNPSLADSGLH 570
Cdd:cd05062  92 TRGDLKSYLrslrpEMENNPVQAPPSLKKMIQMAGeIADGMAYL---NANK--FVHRDLAARNCMVAEDFTVKIGDFGMT 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 K-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESGRLNEdfmDP 645
Cdd:cd05062 167 RdIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQpyqgMSNEQVLRFVMEGGLLD---KP 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 646 NlrkNFPEVeaaqLARLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd05062 244 D---NCPDM----LFELMRMCWQYNPKMRPSFLEIISSIKE 277
PHA02988 PHA02988
hypothetical protein; Provisional
401-684 3.72e-10

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 61.30  E-value: 3.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  401 ESFMFNLEEIERATQSFSEINLLGKSNVSSVYKGILRDGSVAaIKCIAKSS--CKSDESEFLKGLKMLTLLKHENLARLR 478
Cdd:PHA02988   6 RSYINDIKCIESDDIDKYTSVLIKENDQNSIYKGIFNNKEVI-IRTFKKFHkgHKVLIDITENEIKNLRRIDSNNILKIY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  479 GFCCSKGRGECF--LIYEFVPNGNLLQYLDVKDEtgevLEWATRVSIINGIARGIVYLHgENGNKPaivHQNLSAEKILI 556
Cdd:PHA02988  85 GFIIDIVDDLPRlsLILEYCTRGYLREVLDKEKD----LSFKTKLDMAIDCCKGLYNLY-KYTNKP---YKNLTSVSFLV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  557 DHWYNPSLADSGLHKLFTDdivfSKLKASAAMGYLAPEYITT--GRFTDKSDVYAFGMILLQILSGKSKISHL------- 627
Cdd:PHA02988 157 TENYKLKIICHGLEKILSS----PPFKNVNFMVYFSYKMLNDifSEYTIKDDIYSLGVVLWEIFTGKIPFENLttkeiyd 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456  628 MILQAVESGRLNEDfmDPNLRKNFpeVEAaqlarlgllCTHESSNQRPSMEDVIQEL 684
Cdd:PHA02988 233 LIINKNNSLKLPLD--CPLEIKCI--VEA---------CTSHDSIKRPNIKEILYNL 276
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
409-685 6.15e-10

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: 60.48  E-value: 6.15e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERAtqSFSEINLLGKSNVSSVYKGILRDGSV------AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCC 482
Cdd:cd05036   2 EVPRK--NLTLIRALGQGAFGEVYEGTVSGMPGdpsplqVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 483 SkgRGECFLIYEFVPNGNLLQYLDvkdetgEVLEWATRVSIIN---------GIARGIVYLHgENgnkpAIVHQNLSAEK 553
Cdd:cd05036  80 Q--RLPRFILLELMAGGDLKSFLR------ENRPRPEQPSSLTmldllqlaqDVAKGCRYLE-EN----HFIHRDIAARN 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 554 ILIDHwYNPS----LADSGLHKlftdDIVFSKL--KASAAM---GYLAPEYITTGRFTDKSDVYAFGMILLQILS----- 619
Cdd:cd05036 147 CLLTC-KGPGrvakIGDFGMAR----DIYRADYyrKGGKAMlpvKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSlgymp 221
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225456 620 --GKSKIShlmILQAVESG-RlnedfMDPNlrKNFPeveaAQLARLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd05036 222 ypGKSNQE---VMEFVTSGgR-----MDPP--KNCP----GPVYRIMTQCWQHIPEDRPNFSTILERLN 276
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
404-620 7.45e-10

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: 60.43  E-value: 7.45e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 404 MFNLEEIeRATQSFSEINLLGKSnvssvykgilRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFccS 483
Cdd:cd14167   4 IYDFREV-LGTGAFSEVVLAEEK----------RTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDI--Y 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 484 KGRGECFLIYEFVPNGNLlqyLDVKDETGEVLEW-ATRvsIINGIARGIVYLHgengnKPAIVHQNLSAEKIL---IDHW 559
Cdd:cd14167  71 ESGGHLYLIMQLVSGGEL---FDRIVEKGFYTERdASK--LIFQILDAVKYLH-----DMGIVHRDLKPENLLyysLDED 140
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225456 560 YNPSLADSGLHKLFTDDIVFSklKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14167 141 SKIMISDFGLSKIEGSGSVMS--TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG 199
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
423-684 7.81e-10

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: 60.10  E-value: 7.81e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRdGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGrgECFLIYEFVPNGNLL 502
Cdd:cd14062   1 IGSGSFGTVYKGRWH-GDVAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMG-YMTKP--QLAIVTQWCEGSSLY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDETGEVLewaTRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLftddivfsKL 582
Cdd:cd14062  77 KHLHVLETKFEML---QLIDIARQTAQGMDYLHAKN-----IIHRDLKSNNIFLHEDLTVKIGDFGLATV--------KT 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 KASAAMG---------YLAPEYI---TTGRFTDKSDVYAFGMILLQILSGKSKISHLM----ILQAVESGRLNEDFmdPN 646
Cdd:cd14062 141 RWSGSQQfeqptgsilWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLTGQLPYSHINnrdqILFMVGRGYLRPDL--SK 218
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 15225456 647 LRKNFPEveaaQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd14062 219 VRSDTPK----ALRRLMEDCIKFQRDERPLFPQILASL 252
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
417-627 9.96e-10

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: 60.07  E-value: 9.96e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGIL-RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEF 495
Cdd:cd06642   6 FTKLERIGKGSFGEVYKGIDnRTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTK--LWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLdvkdETGEvLEWATRVSIINGIARGIVYLHGENGnkpaiVHQNLSAEKILIDHWYNPSLADSGLHKLFTD 575
Cdd:cd06642  84 LGGGSALDLL----KPGP-LEETYIATILREILKGLDYLHSERK-----IHRDIKAANVLLSEQGDVKLADFGVAGQLTD 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 576 divfSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHL 627
Cdd:cd06642 154 ----TQIKRNTFVGtpfWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDL 204
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
422-681 9.98e-10

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: 59.86  E-value: 9.98e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGI-LRDGSVAAIK-----CIAKSSCKSDES--EFLKG-LKMLTLLKHENLARLRGFCCSKGRGECFLi 492
Cdd:cd06628   7 LIGSGSFGSVYLGMnASSGELMAVKqvelpSVSAENKDRKKSmlDALQReIALLRELQHENIVQYLGSSSDANHLNIFL- 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 yEFVPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd06628  86 -EYVPGGSVATLLN---NYGAFEESLVR-NFVRQILKGLNYLHNRG-----IIHRDIKGANILVDNKGGIKISDFGISKK 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 573 FTDDIVFSKLKAS-----AAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVesGRLNEdfmdpNL 647
Cdd:cd06628 156 LEANSLSTKNNGArpslqGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEMLTGTHPFPDCTQMQAI--FKIGE-----NA 228
                       250       260       270
                ....*....|....*....|....*....|....*
gi 15225456 648 RKNFPEvEAAQLARLGLLCTHE-SSNQRPSMEDVI 681
Cdd:cd06628 229 SPTIPS-NISSEARDFLEKTFEiDHNKRPTADELL 262
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
422-617 1.28e-09

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: 59.80  E-value: 1.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGSVAaIKcIAKSSCKSD---ESEFLKGLkmltLLKHENLArlrGFCCS--KGRG---ECFLIY 493
Cdd:cd14144   2 SVGKGRYGEVWKGKWRGEKVA-VK-IFFTTEEASwfrETEIYQTV----LMRHENIL---GFIAAdiKGTGswtQLYLIT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLHGE---NGNKPAIVHQNLSAEKILIDHWYNPSLADSGLH 570
Cdd:cd14144  73 DYHENGSLYDFL-----RGNTLDTQSMLKLAYSAACGLAHLHTEifgTQGKPAIAHRDIKSKNILVKKNGTCCIADLGLA 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 571 KLFTDDIVFSKLKASAAMG---YLAPEYI--TTGRFT----DKSDVYAFGMILLQI 617
Cdd:cd14144 148 VKFISETNEVDLPPNTRVGtkrYMAPEVLdeSLNRNHfdayKMADMYSFGLVLWEI 203
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
423-685 1.33e-09

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely expressed in many tissues. It 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 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. Despite this, the presumed pseudokinase (repeat 1) domain of Jak2 exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Inactivation of the repeat 1 domain increased Jak2 basal activity, suggesting that it modulates the kinase activity of the C-terminal catalytic (repeat 2) domain. The Jak2 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: 270663 [Multi-domain]  Cd Length: 262  Bit Score: 59.58  E-value: 1.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD----GSVAAIKCIAKSSCKSDES---EFLKGLKMLTLLKHENLARLRGFC-CSKgrgECFLIYE 494
Cdd:cd05078   7 LGQGTFTKIFKGIRREvgdyGQLHETEVLLKVLDKAHRNyseSFFEAASMMSQLSHKHLVLNYGVCvCGD---ENILVQE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLDVKDETGEVLeWATRVSiiNGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWY-----NP---SLAD 566
Cdd:cd05078  84 YVKFGSLDTYLKKNKNCINIL-WKLEVA--KQLAWAMHFLEEKT-----LVHGNVCAKNILLIREEdrktgNPpfiKLSD 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 567 SGLH-KLFTDDIVFSKLKasaamgYLAPEYITTGR-FTDKSDVYAFGMILLQILSGKSKIshlmiLQAVESGRLNEDFMD 644
Cdd:cd05078 156 PGISiTVLPKDILLERIP------WVPPECIENPKnLSLATDKWSFGTTLWEICSGGDKP-----LSALDSQRKLQFYED 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 645 pnlRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd05078 225 ---RHQLPAPKWTELANLINNCMDYEPDHRPSFRAIIRDLN 262
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
417-685 1.36e-09

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: 59.80  E-value: 1.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKH---ENLARLRGfCCSKGRgECFLI 492
Cdd:cd06917   3 YRRLELVGRGSYGAVYRGYhVKTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYG-SYLKGP-SLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLdvkdETGEVLEWATRVsIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd06917  81 MDYCEGGSIRTLM----RAGPIAERYIAV-IMREVLVALKFIH-----KDGIIHRDIKAANILVTNTGNVKLCDFGVAAS 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 573 FtddiVFSKLKASAAMG---YLAPEYITTGRFTD-KSDVYAFGMILLQILSGKSKISHLMILQAV------ESGRLNEDF 642
Cdd:cd06917 151 L----NQNSSKRSTFVGtpyWMAPEVITEGKYYDtKADIWSLGITTYEMATGNPPYSDVDALRAVmlipksKPPRLEGNG 226
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 15225456 643 MDPNLRK-------NFPE--VEAAQLARLGLLCTHeSSNQRPSMEDVIQELN 685
Cdd:cd06917 227 YSPLLKEfvaacldEEPKdrLSADELLKSKWIKQH-SKTPTSVLKELISRYN 277
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
437-620 1.64e-09

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: 59.31  E-value: 1.64e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGNLlqyLDVKDETGEVLE 516
Cdd:cd14083  26 ATGKLVAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSH--LYLVMELVTGGEL---FDRIVEKGSYTE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 517 W-ATRvsIINGIARGIVYLHgENGnkpaIVHQNLSAEKILidhWYNPSlADSglhKLFTDDIVFSKLKASAAM------- 588
Cdd:cd14083 101 KdASH--LIRQVLEAVDYLH-SLG----IVHRDLKPENLL---YYSPD-EDS---KIMISDFGLSKMEDSGVMstacgtp 166
                       170       180       190
                ....*....|....*....|....*....|..
gi 15225456 589 GYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14083 167 GYVAPEVLAQKPYGKAVDCWSIGVISYILLCG 198
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
404-620 1.89e-09

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: 59.68  E-value: 1.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 404 MFNLEEIeRATQSFSEINLLGKSNVSSVYkgilrdgsvaAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCS 483
Cdd:cd14168  11 IFEFKEV-LGTGAFSEVVLAEERATGKLF----------AVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYES 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 484 KgrGECFLIYEFVPNGNLlqyLDVKDETGEVLEwATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILidhWYNPS 563
Cdd:cd14168  80 P--NHLYLVMQLVSGGEL---FDRIVEKGFYTE-KDASTLIRQVLDAVYYLH-----RMGIVHRDLKPENLL---YFSQD 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225456 564 ------LADSGLHKLFTDDIVFSklKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14168 146 eeskimISDFGLSKMEGKGDVMS--TACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCG 206
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
420-620 1.92e-09

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: 59.37  E-value: 1.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILR--DGSVAAIKCIAKSSCKSDESE------FLKGLKMLTLLKHENLARLRGFCCSKGRgeCFL 491
Cdd:cd14096   6 INKIGEGAFSNVYKAVPLrnTGKPVAIKVVRKADLSSDNLKgssranILKEVQIMKRLSHPNIVKLLDFQESDEY--YYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 IYEFVPNGNL------LQYLDvkdetgevlEWATRvSIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHW-YNPS- 563
Cdd:cd14096  84 VLELADGGEIfhqivrLTYFS---------EDLSR-HVITQVASAVKYLH-EIG----VVHRDIKPENLLFEPIpFIPSi 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 564 -------------------------------LADSGLHKLFTDdivfSKLKAS-AAMGYLAPEYITTGRFTDKSDVYAFG 611
Cdd:cd14096 149 vklrkadddetkvdegefipgvggggigivkLADFGLSKQVWD----SNTKTPcGTVGYTAPEVVKDERYSKKVDMWALG 224

                ....*....
gi 15225456 612 MILLQILSG 620
Cdd:cd14096 225 CVLYTLLCG 233
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
422-639 2.82e-09

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: 58.52  E-value: 2.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESE-------FLKGLKMLTLL-KHENLARLRGFCcskgrgEC--- 489
Cdd:cd14093  10 ILGRGVSSTVRRCIEKEtGQEFAVKIIDITGEKSSENEaeelreaTRREIEILRQVsGHPNIIELHDVF------ESptf 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 -FLIYEFVPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd14093  84 iFLVFELCRKGELFDYLT---EVVTLSEKKTR-RIMRQLFEAVEFLHSLN-----IVHRDLKPENILLDDNLNVKISDFG 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 569 LHKLFTDDIVFSKLKASAamGYLAPEYITTGRFTD------KSDVYAFGMILLQILSGKSKISH---LMILQAVESGRLN 639
Cdd:cd14093 155 FATRLDEGEKLRELCGTP--GYLAPEVLKCSMYDNapgygkEVDMWACGVIMYTLLAGCPPFWHrkqMVMLRNIMEGKYE 232
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
423-682 2.96e-09

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: 58.37  E-value: 2.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrGECFLIYEFVPNGNL 501
Cdd:cd06623   9 LGQGSSGVVYKVRHKpTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKE--GEISIVLEYMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKDETGE-VLEWATRvsiinGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDdivfS 580
Cdd:cd06623  87 ADLLKKVGKIPEpVLAYIAR-----QILKGLDYLH----TKRHIIHRDIKPSNLLINSKGEVKIADFGISKVLEN----T 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 581 KLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---------SKISHLMILQAVESGRLNEDFMDPNLR 648
Cdd:cd06623 154 LDQCNTFVGtvtYMSPERIQGESYSYAADIWSLGLTLLECALGKfpflppgqpSFFELMQAICDGPPPSLPAEEFSPEFR 233
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 649 kNFPEveaaqlarlglLCTHESSNQRPSMEDVIQ 682
Cdd:cd06623 234 -DFIS-----------ACLQKDPKKRPSAAELLQ 255
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
423-681 3.40e-09

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: 58.58  E-value: 3.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSS--CKSDESEFLKGLKMLTLLKHENLARLRGFCCS--KGRGECFLIYEFVPN 498
Cdd:cd14031  18 LGRGAFKTVYKGLDTETWVEVAWCELQDRklTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESvlKGKKCIVLVTELMTS 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 GNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkPAIVHQNLSAEKILIDhwyNPS----LADSGLHKLFT 574
Cdd:cd14031  98 GTLKTYL----KRFKVMKPKVLRSWCRQILKGLQFLHTRT---PPIIHRDLKCDNIFIT---GPTgsvkIGDLGLATLMR 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIVFSKLKASAamgYLAPEyITTGRFTDKSDVYAFGMILLQILSGKSKISHL----MILQAVESGrlnedfMDPnlrKN 650
Cdd:cd14031 168 TSFAKSVIGTPE---FMAPE-MYEEHYDESVDVYAFGMCMLEMATSEYPYSECqnaaQIYRKVTSG------IKP---AS 234
                       250       260       270
                ....*....|....*....|....*....|.
gi 15225456 651 FPEVEAAQLARLGLLCTHESSNQRPSMEDVI 681
Cdd:cd14031 235 FNKVTDPEVKEIIEGCIRQNKSERLSIKDLL 265
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
415-621 3.92e-09

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: 58.13  E-value: 3.92e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSScksDESEFLKGLKMLTLLKHENLARLRGF---CCSKGrgECF 490
Cdd:cd06605   1 DDLEYLGELGEGNGGVVSKVRHRpSGQIMAVKVIRLEI---DEALQKQILRELDVLHKCNSPYIVGFygaFYSEG--DIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLDVKDETGE-VLEwatrvSIINGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd06605  76 ICMEYMDGGSLDKILKEVGRIPErILG-----KIAVAVVKGLIYLH----EKHKIIHRDVKPSNILVNSRGQVKLCDFGV 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15225456 570 HKLFTDDIVFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd06605 147 SGQLVDSLAKTFVGTRS---YMAPERISGGKYTVKSDIWSLGLSLVELATGR 195
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
437-688 3.96e-09

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: 58.51  E-value: 3.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIaKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKDETGEV-- 514
Cdd:cd05093  33 QDKILVAVKTL-KDASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGD--PLIMVFEYMKHGDLNKFLRAHGPDAVLma 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 515 -------LEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASA 586
Cdd:cd05093 110 egnrpaeLTQSQMLHIAQQIAAGMVYLASQH-----FVHRDLATRNCLVGENLLVKIGDFGMSRdVYSTDYYRVGGHTML 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 587 AMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESGRLNEDfmdpnlrknfPEVEAAQLARL 662
Cdd:cd05093 185 PIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTyGKQpwyQLSNNEVIECITQGRVLQR----------PRTCPKEVYDL 254
                       250       260
                ....*....|....*....|....*.
gi 15225456 663 GLLCTHESSNQRPSMEDVIQELNNLA 688
Cdd:cd05093 255 MLGCWQREPHMRLNIKEIHSLLQNLA 280
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
437-680 4.26e-09

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 58.30  E-value: 4.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRGECfLIYEFVPNGNLLQYL----------- 505
Cdd:cd05050  33 EPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLG-VCAVGKPMC-LLFEYMAYGDLNEFLrhrspraqcsl 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 506 -----DVKDETGEVLEWAT--RVSIINGIARGIVYLhGENgnkpAIVHQNLSAEKILIDHWYNPSLADSGL-HKLFTDDi 577
Cdd:cd05050 111 shstsSARKCGLNPLPLSCteQLCIAKQVAAGMAYL-SER----KFVHRDLATRNCLVGENMVVKIADFGLsRNIYSAD- 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 578 vFSKLKASAAMG--YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSK----ISHLMILQAVESGRLnedfmdpnlrKNF 651
Cdd:cd05050 185 -YYKASENDAIPirWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQpyygMAHEEVIYYVRDGNV----------LSC 253
                       250       260
                ....*....|....*....|....*....
gi 15225456 652 PEVEAAQLARLGLLCTHESSNQRPSMEDV 680
Cdd:cd05050 254 PDNCPLELYNLMRLCWSKLPSDRPSFASI 282
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
423-621 5.82e-09

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: 57.78  E-value: 5.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSS--CKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGE-CF-LIYEFVPN 498
Cdd:cd14032   9 LGRGSFKTVYKGLDTETWVEVAWCELQDRklTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAKGKrCIvLVTELMTS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 GNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkPAIVHQNLSAEKILIDhwyNPS----LADSGLHKLFT 574
Cdd:cd14032  89 GTLKTYL----KRFKVMKPKVLRSWCRQILKGLLFLHTRT---PPIIHRDLKCDNIFIT---GPTgsvkIGDLGLATLKR 158
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 575 DDIVFSKLKASAamgYLAPEyITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd14032 159 ASFAKSVIGTPE---FMAPE-MYEEHYDESVDVYAFGMCMLEMATSE 201
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
417-682 6.05e-09

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: 57.75  E-value: 6.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKsDESEFLKglKMLTLLKHENLARLRGFCCSKGRG-ECFLIYE 494
Cdd:cd06640   6 FTKLERIGKGSFGEVFKGIdNRTQQVVAIKIIDLEEAE-DEIEDIQ--QEITVLSQCDSPYVTKYYGSYLKGtKLWIIME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLdvkdETGEVLEWATrVSIINGIARGIVYLHGENGnkpaiVHQNLSAEKILIDHWYNPSLADSGLHKLFT 574
Cdd:cd06640  83 YLGGGSALDLL----RAGPFDEFQI-ATMLKEILKGLDYLHSEKK-----IHRDIKAANVLLSEQGDVKLADFGVAGQLT 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DdivfSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAV-ESGRLNEDFMDPNLRKN 650
Cdd:cd06640 153 D----TQIKRNTFVGtpfWMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLfLIPKNNPPTLVGDFSKP 228
                       250       260       270
                ....*....|....*....|....*....|..
gi 15225456 651 FPEVEAAqlarlgllCTHESSNQRPSMEDVIQ 682
Cdd:cd06640 229 FKEFIDA--------CLNKDPSFRPTAKELLK 252
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
422-687 6.40e-09

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: 57.69  E-value: 6.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKG-ILRDGSVAAIKCIAKSScKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRG---ECFLIYEFVP 497
Cdd:cd13986   7 LLGEGGFSFVYLVeDLSTGRLYALKKILCHS-KEDVKEAMREIENYRLFNHPNILRLLDSQIVKEAGgkkEVYLLLPYYK 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENGnkPAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDI 577
Cdd:cd13986  86 RGSLQDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPEL--VPYAHRDIKPGNVLLSEDDEPILMDLGSMNPARIEI 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 578 VFSK----LKASAA----MGYLAPEYIT--TGR-FTDKSDVYAFGMILLQILSGKSKIShlMILQ-------AVESGRLN 639
Cdd:cd13986 164 EGRRealaLQDWAAehctMPYRAPELFDvkSHCtIDEKTDIWSLGCTLYALMYGESPFE--RIFQkgdslalAVLSGNYS 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 640 edFMDPNlrkNFPEveaaQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd13986 242 --FPDNS---RYSE----ELHQLVKSMLVVNPAERPSIDDLLSRVHDL 280
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
422-619 7.38e-09

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: 57.77  E-value: 7.38e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGS-----VAAIK---CIAKSSCKSdESEFLKGLKmltlLKHENL-----ARLRGfccSKGRGE 488
Cdd:cd14055   2 LVGKGRFAEVWKAKLKQNAsgqyeTVAVKifpYEEYASWKN-EKDIFTDAS----LKHENIlqfltAEERG---VGLDRQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 489 CFLIYEFVPNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLHGE---NG-NKPAIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd14055  74 YWLITAYHENGSLQDYL-----TRHILSWEDLCKMAGSLARGLAHLHSDrtpCGrPKIPIAHRDLKSSNILVKNDGTCVL 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225456 565 ADSGLH-----KLFTDDivfskLKASAAMG---YLAPEYITTG-RFTD-----KSDVYAFGMILLQILS 619
Cdd:cd14055 149 ADFGLAlrldpSLSVDE-----LANSGQVGtarYMAPEALESRvNLEDlesfkQIDVYSMALVLWEMAS 212
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
421-682 9.05e-09

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: 57.06  E-value: 9.05e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSD--ESEFLK---GLKMLTLLKHENLARLRGFCCSKGRGECFLiyEF 495
Cdd:cd06631   7 NVLGKGAYGTVYCGLTSTGQLIAVKQVELDTSDKEkaEKEYEKlqeEVDLLKTLKHVNIVGYLGTCLEDNVVSIFM--EF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNG---NLLQYLDVKDETgeVLEWATRvsiinGIARGIVYLHGENgnkpaIVHQNLSAEKI---------LIDHWYNPS 563
Cdd:cd06631  85 VPGGsiaSILARFGALEEP--VFCRYTK-----QILEGVAYLHNNN-----VIHRDIKGNNImlmpngvikLIDFGCAKR 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 564 LADSGLHKLFTDdivfsKLKASAAMGY-LAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQA---VESGRln 639
Cdd:cd06631 153 LCINLSSGSQSQ-----LLKSMRGTPYwMAPEVINETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAifaIGSGR-- 225
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 15225456 640 eDFMdPNLRKNFPEvEAAQLARlglLCTHESSNQRPSMEDVIQ 682
Cdd:cd06631 226 -KPV-PRLPDKFSP-EARDFVH---ACLTRDQDERPSAEQLLK 262
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
423-617 9.75e-09

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: 57.36  E-value: 9.75e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAikciaKSSCKSDESEFLKGLKML--TLLKHENLArlrGFCCS--KGRG---ECFLIYEF 495
Cdd:cd14220   3 IGKGRYGEVWMGKWRGEKVAV-----KVFFTTEEASWFRETEIYqtVLMRHENIL---GFIAAdiKGTGswtQLYLITDY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLDVKdetgeVLEWATRVSIINGIARGIVYLHGE---NGNKPAIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd14220  75 HENGSLYDFLKCT-----TLDTRALLKLAYSAACGLCHLHTEiygTQGKPAIAHRDLKSKNILIKKNGTCCIADLGLAVK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 573 FTDDIVFSKLKASAAMG---YLAPEYITTGRFTDK------SDVYAFGMILLQI 617
Cdd:cd14220 150 FNSDTNEVDVPLNTRVGtkrYMAPEVLDESLNKNHfqayimADIYSFGLIIWEM 203
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
68-227 1.28e-08

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 55.95  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  68 RRVANISLQGMGLTgtippSIGLL---TSLTGLYLHFNSLTgHIPKdISNLPLLTDLYLNVNNLSgEIPPLiGNLDNLQV 144
Cdd:cd21340   2 KRITHLYLNDKNIT-----KIDNLslcKNLKVLYLYDNKIT-KIEN-LEFLTNLTHLYLQNNQIE-KIENL-ENLVNLKK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 145 IQLCYNKLS---GsiptqFGSLKKITVLALQYNQL-SGAI----PASLGDI-DTLTRLDLSFNNLFGPVPvkLAGAPLLE 215
Cdd:cd21340  73 LYLGGNRISvveG-----LENLTNLEELHIENQRLpPGEKltfdPRSLAALsNSLRVLNISGNNIDSLEP--LAPLRNLE 145
                       170
                ....*....|..
gi 15225456 216 VLDIRNNSFSGF 227
Cdd:cd21340 146 QLDASNNQISDL 157
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
469-619 1.41e-08

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: 56.59  E-value: 1.41e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 469 LKHENLARLRGfccSKGRG-----ECFLIYEFVPNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLHGE-----N 538
Cdd:cd14141  46 MKHENILQFIG---AEKRGtnldvDLWLITAFHEKGSLTDYL-----KANVVSWNELCHIAQTMARGLAYLHEDipglkD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 539 GNKPAIVHQNLSAEKILIDHWYNPSLADSGLHklftddivfSKLKASAAMG----------YLAPEYITTG-RFTDKS-- 605
Cdd:cd14141 118 GHKPAIAHRDIKSKNVLLKNNLTACIADFGLA---------LKFEAGKSAGdthgqvgtrrYMAPEVLEGAiNFQRDAfl 188
                       170
                ....*....|....*.
gi 15225456 606 --DVYAFGMILLQILS 619
Cdd:cd14141 189 riDMYAMGLVLWELAS 204
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
420-682 1.44e-08

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: 56.18  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESEFL-KGLKMLTLLKHENLARLRGfCCSKGRGeCFLIYEFVP 497
Cdd:cd14069   6 VQTLGEGAFGEVFLAVNRNtEEAVAVKFVDMKRAPGDCPENIkKEVCIQKMLSHKNVVRFYG-HRREGEF-QYLFLEYAS 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYL--DVKDETGEVLEWATRVsiingIArGIVYLHGeNGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTD 575
Cdd:cd14069  84 GGELFDKIepDVGMPEDVAQFYFQQL-----MA-GLKYLHS-CG----ITHRDIKPENLLLDENDNLKISDFGLATVFRY 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 576 D---IVFSKLKASaaMGYLAPEYITTGRF-TDKSDVYAFGMILLQILSGKskishLMILQAVESGRLNEDFMDPNLRKNF 651
Cdd:cd14069 153 KgkeRLLNKMCGT--LPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAGE-----LPWDQPSDSCQEYSDWKENKKTYLT 225
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 652 P--EVEAAQLARL-GLLctHESSNQRPSMEDVIQ 682
Cdd:cd14069 226 PwkKIDTAALSLLrKIL--TENPNKRITIEDIKK 257
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
443-619 1.62e-08

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: 56.20  E-value: 1.62e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDE--SEFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIYEFVPNGNLLQYLdvKDETGEVL----- 515
Cdd:cd05040  27 AVKCLKSDVLSQPNamDDFLKEVNAMHSLDHPNLIRLYGVVLSS---PLMMVTELAPLGSLLDRL--RKDQGHFListlc 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 516 EWATRvsiingIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF--TDDIVFSKLKASAAMGYLAP 593
Cdd:cd05040 102 DYAVQ------IANGMAYLESKR-----FIHRDLAARNILLASKDKVKIGDFGLMRALpqNEDHYVMQEHRKVPFAWCAP 170
                       170       180
                ....*....|....*....|....*.
gi 15225456 594 EYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd05040 171 ESLKTRKFSHASDVWMFGVTLWEMFT 196
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
439-622 2.35e-08

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: 55.96  E-value: 2.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIAKSSCKS-----DESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNLLQYLDVKDETGE 513
Cdd:cd14105  30 GLEYAAKFIKKRRSKAsrrgvSREDIEREVSILRQVLHPNIITLHDVFENKT--DVVLILELVAGGELFDFLAEKESLSE 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 514 vlEWATrvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNP----SLADSGLHKLFTDDIVFSKLKASAAmg 589
Cdd:cd14105 108 --EEAT--EFLKQILDGVNYLHTKN-----IAHFDLKPENIMLLDKNVPipriKLIDFGLAHKIEDGNEFKNIFGTPE-- 176
                       170       180       190
                ....*....|....*....|....*....|...
gi 15225456 590 YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd14105 177 FVAPEIVNYEPLGLEADMWSIGVITYILLSGAS 209
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
422-617 2.60e-08

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: 55.91  E-value: 2.60e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRDGSVAAIKCIAKSSCK-SDESEFLKGLkmltLLKHENLArlrGFCCS--KGRG---ECFLIYEF 495
Cdd:cd14143   2 SIGKGRFGEVWRGRWRGEDVAVKIFSSREERSwFREAEIYQTV----MLRHENIL---GFIAAdnKDNGtwtQLWLVSDY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 496 VPNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYLHGE---NGNKPAIVHQNLSAEKILIDHWYNPSLADSGL--- 569
Cdd:cd14143  75 HEHGSLFDYL-----NRYTVTVEGMIKLALSIASGLAHLHMEivgTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLavr 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 570 HKLFTDDIVFSKLKASAAMGYLAPEY----ITTGRFTD--KSDVYAFGMILLQI 617
Cdd:cd14143 150 HDSATDTIDIAPNHRVGTKRYMAPEVlddtINMKHFESfkRADIYALGLVFWEI 203
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
415-614 2.76e-08

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: 55.47  E-value: 2.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKsDESEFL---KGLKMLTLLKHENLARLrgFCCSKGRGECF 490
Cdd:cd14073   1 HRYELLETLGKGTYGKVKLAIERAtGREVAIKSIKKDKIE-DEQDMVrirREIEIMSSLNHPHIIRI--YEVFENKDKIV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLH 570
Cdd:cd14073  78 IVMEYASGGELYDYIS---ERRRLPEREAR-RIFRQIVSAVHYCH-----KNGVVHRDLKLENILLDQNGNAKIADFGLS 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15225456 571 KLFTDDIVFSKLKASAAmgYLAPEyITTGR--FTDKSDVYAFGMIL 614
Cdd:cd14073 149 NLYSKDKLLQTFCGSPL--YASPE-IVNGTpyQGPEVDCWSLGVLL 191
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
423-684 3.35e-08

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 55.19  E-value: 3.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYkgiLRDGSVAAIKCIAKSSCKSDESEF----LKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEFVPN 498
Cdd:cd13975   8 LGRGQYGVVY---ACDSWGGHFPCALKSVVPPDDKHWndlaLEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAVLLIM 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 GNLLQYLDVKDETGevLEWATRVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHK---LFTD 575
Cdd:cd13975  85 ERLHRDLYTGIKAG--LSLEERLQIALDVVEGIRFLHSQ-----GLVHRDIKLKNVLLDKKNRAKITDLGFCKpeaMMSG 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 576 DIVFSKLkasaamgYLAPEyITTGRFTDKSDVYAFGMILLQILSGKSKIShlmilQAVESGRlNEDFMDPNLRKNFPEVE 655
Cdd:cd13975 158 SIVGTPI-------HMAPE-LFSGKYDNSVDVYAFGILFWYLCAGHVKLP-----EAFEQCA-SKDHLWNNVRKGVRPER 223
                       250       260       270
                ....*....|....*....|....*....|...
gi 15225456 656 AAQLA----RLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd13975 224 LPVFDeecwNLMEACWSGDPSQRPLLGIVQPKL 256
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
417-617 3.50e-08

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: 55.51  E-value: 3.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYK--GILRDGSVAAIKCIAKSSCKSDES----EFLKGLKMLTLLKHENLARLrgFCCSKGRGECF 490
Cdd:cd14052   2 FANVELIGSGEFSQVYKvsERVPTGKVYAVKKLKPNYAGAKDRlrrlEEVSILRELTLDGHDNIVQL--IDSWEYHGHLY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLDVKDETGEVLEWatRV-SIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd14052  80 IQTELCENGSLDVFLSELGLLGRLDEF--RVwKILVELSLGLRFIHDHH-----FVHLDLKPANVLITFEGTLKIGDFGM 152
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 570 HKLFTDDivfSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQI 617
Cdd:cd14052 153 ATVWPLI---RGIEREGDREYIAPEILSEHMYDKPADIFSLGLILLEA 197
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
420-620 3.57e-08

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: 55.22  E-value: 3.57e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSV--YKGILrDGSVAAIKCIAKSSCK-SDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFV 496
Cdd:cd14072   5 LKTIGKGNFAKVklARHVL-TGREVAIKIIDKTQLNpSSLQKLFREVRIMKILNHPNIVKL--FEVIETEKTLYLVMEYA 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYLDVKdetGEVLEWATRVSIiNGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTdd 576
Cdd:cd14072  82 SGGEVFDYLVAH---GRMKEKEARAKF-RQIVSAVQYCHQKR-----IVHRDLKAENLLLDADMNIKIADFGFSNEFT-- 150
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 577 iVFSKLKA-SAAMGYLAPEyITTGRFTD--KSDVYAFGMILLQILSG 620
Cdd:cd14072 151 -PGNKLDTfCGSPPYAAPE-LFQGKKYDgpEVDVWSLGVILYTLVSG 195
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
423-681 4.47e-08

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: 55.06  E-value: 4.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSS--CKSDESEFLKGLKMLTLLKHENLARLRGF--CCSKGRGECFLIYEFVPN 498
Cdd:cd14030  33 IGRGSFKTVYKGLDTETTVEVAWCELQDRklSKSERQRFKEEAGMLKGLQHPNIVRFYDSweSTVKGKKCIVLVTELMTS 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 GNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkPAIVHQNLSAEKILIDhwyNPS----LADSGLHKLFT 574
Cdd:cd14030 113 GTLKTYL----KRFKVMKIKVLRSWCRQILKGLQFLHTRT---PPIIHRDLKCDNIFIT---GPTgsvkIGDLGLATLKR 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIvfsklkASAAMG---YLAPEYITTgRFTDKSDVYAFGMILLQILSGKSKISHL----MILQAVESGrlnedfMDPnl 647
Cdd:cd14030 183 ASF------AKSVIGtpeFMAPEMYEE-KYDESVDVYAFGMCMLEMATSEYPYSECqnaaQIYRRVTSG------VKP-- 247
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 648 rKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVI 681
Cdd:cd14030 248 -ASFDKVAIPEVKEIIEGCIRQNKDERYAIKDLL 280
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
463-682 4.50e-08

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: 55.09  E-value: 4.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 463 LKMLTLLKHENLARLRGfcCSKGRGECFL--IYEFVPNGNllqyldVKDET---GEVLEWATRvSIINGIARGIVYLHGE 537
Cdd:cd06651  60 IQLLKNLQHERIVQYYG--CLRDRAEKTLtiFMEYMPGGS------VKDQLkayGALTESVTR-KYTRQILEGMSYLHSN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 538 ngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKLFtDDIVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMIL 614
Cdd:cd06651 131 -----MIVHRDIKGANILRDSAGNVKLGDFGASKRL-QTICMSGTGIRSVTGtpyWMSPEVISGEGYGRKADVWSLGCTV 204
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 615 LQILSGKSKISHLMILQAVesGRLNEDFMDPNLRKNFPEveaaqLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd06651 205 VEMLTEKPPWAEYEAMAAI--FKIATQPTNPQLPSHISE-----HARDFLGCIFVEARHRPSAEELLR 265
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
423-687 4.65e-08

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 55.04  E-value: 4.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRdGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCskgRGECFLIYEFVPNGNLL 502
Cdd:cd14149  20 IGSGSFGTVYKGKWH-GDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMT---KDNLAIVTQWCEGSSLY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 503 QYLDVKDETGEVLEWatrVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKL 582
Cdd:cd14149  96 KHLHVQETKFQMFQL---IDIARQTAQGMDYLHAKN-----IIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQV 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 583 -KASAAMGYLAPEYI---TTGRFTDKSDVYAFGMILLQILSGKSKISHL----MILQAVESGRLNEDFmdPNLRKNFPEV 654
Cdd:cd14149 168 eQPTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMTGELPYSHInnrdQIIFMVGRGYASPDL--SKLYKNCPKA 245
                       250       260       270
                ....*....|....*....|....*....|...
gi 15225456 655 eaaqLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14149 246 ----MKRLVADCIKKVKEERPLFPQILSSIELL 274
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
421-690 4.97e-08

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 54.76  E-value: 4.97e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGILRDGSV----AAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfCCSKGRGECFLIYEFV 496
Cdd:cd05043  12 DLLQEGTFGRIFHGILRDEKGkeeeVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILH-VCIEDGEKPMVLYPYM 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLQYL----DVKDETGEVLEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHK- 571
Cdd:cd05043  91 NWGNLKLFLqqcrLSEANNPQALSTQQLVHMALQIACGMSYLH-----RRGVIHKDIAARNCVIDDELQVKITDNALSRd 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 572 LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILS-GKS---KISHLMILQAVESG-RLNEDFmdpn 646
Cdd:cd05043 166 LFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTlGQTpyvEIDPFEMAAYLKDGyRLAQPI---- 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15225456 647 lrkNFPEveaaQLARLGLLCTHESSNQRPSMEDVIQELNNLAAD 690
Cdd:cd05043 242 ---NCPD----ELFAVMACCWALDPEERPSFQQLVQCLTDFHAQ 278
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
400-633 5.12e-08

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


Pssm-ID: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 55.00  E-value: 5.12e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 400 FESFMFNLEEIERATQSFSEINLLGKSNVSSVYK-GILRDGSVAAIKCIAKSSCKSDESEFLKGLkMLTLLKHENLARLR 478
Cdd:cd06639   7 YNSSMLGLESLADPSDTWDIIETIGKGTYGKVYKvTNKKDGSLAAVKILDPISDVDEEIEAEYNI-LRSLPNHPNVVKFY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 479 GFCCSKGR---GECFLIYEFVPNGNLLQYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKIL 555
Cdd:cd06639  86 GMFYKADQyvgGQLWLVLELCNGGSVTELVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNR-----IIHRDVKGNNIL 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 556 IDHWYNPSLADSGLHKLFTDdivfSKLKASAAMG---YLAPEYITTGRFTDKS-----DVYAFGMILLQILSGKSKISHL 627
Cdd:cd06639 161 LTTEGGVKLVDFGVSAQLTS----ARLRRNTSVGtpfWMAPEVIACEQQYDYSydarcDVWSLGITAIELADGDPPLFDM 236

                ....*.
gi 15225456 628 MILQAV 633
Cdd:cd06639 237 HPVKAL 242
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
410-617 6.46e-08

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: 54.56  E-value: 6.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 410 IERATQSFSEInlLGKSNVSSVYKGILR--DGSV--AAIKCIAKSSCKSDE-SEFLKGLKMLTLLKHENLARLRGFCCSK 484
Cdd:cd14204   4 IDRNLLSLGKV--LGEGEFGSVMEGELQqpDGTNhkVAVKTMKLDNFSQREiEEFLSEAACMKDFNHPNVIRLLGVCLEV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 485 GRGEC---FLIYEFVPNGNLLQYL-DVKDETGEV-LEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHW 559
Cdd:cd14204  82 GSQRIpkpMVILPFMKYGDLHSFLlRSRLGSGPQhVPLQTLLKFMIDIALGMEYLSSRN-----FLHRDLAARNCMLRDD 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15225456 560 YNPSLADSGL-HKLFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQI 617
Cdd:cd14204 157 MTVCVADFGLsKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEI 215
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
456-614 7.35e-08

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: 54.21  E-value: 7.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 456 ESEFLKGLKmltllKHENLARLRGF---CCSKGRGECFLIYEFVPNGNLLQYLDVKDETG----EVLEwatrvsIINGIA 528
Cdd:cd14037  50 EIEIMKRLS-----GHKNIVGYIDSsanRSGNGVYEVLLLMEYCKGGGVIDLMNQRLQTGltesEILK------IFCDVC 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 529 RGIVYLHGEngnKPAIVHQNLSAEKILIDHWYNPSLADSG--------LHKLFTDDIVFSKLKASAAMGYLAPEYITTGR 600
Cdd:cd14037 119 EAVAAMHYL---KPPLIHRDLKVENVLISDSGNYKLCDFGsattkilpPQTKQGVTYVEEDIKKYTTLQYRAPEMIDLYR 195
                       170
                ....*....|....*..
gi 15225456 601 ---FTDKSDVYAFGMIL 614
Cdd:cd14037 196 gkpITEKSDIWALGCLL 212
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
417-627 8.23e-08

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: 54.35  E-value: 8.23e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSckSDE---SEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLI 492
Cdd:cd07861   2 YTKIEKIGEGTYGVVYKGRnKKTGQIVAMKKIRLES--EEEgvpSTAIREISLLKELQHPNIVCLEDVLMQENR--LYLV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVpNGNLLQYLDVKdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd07861  78 FEFL-SMDLKKYLDSL-PKGKYMDAELVKSYLYQILQGILFCHSRR-----VLHRDLKPQNLLIDNKGVIKLADFGLARA 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15225456 573 F-------TDDIVfsklkasaAMGYLAPEYITTG-RFTDKSDVYAFGMILLQILS------GKSKISHL 627
Cdd:cd07861 151 FgipvrvyTHEVV--------TLWYRAPEVLLGSpRYSTPVDIWSIGTIFAEMATkkplfhGDSEIDQL 211
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
429-628 9.54e-08

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: 54.11  E-value: 9.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 429 SSVYKGI-LRDGSVAAIKCIAKSscksDESE-----FLKGLKMLTLLKHENLARLRGFCCSKG----RGECFLIYEFVPN 498
Cdd:cd07840  13 GQVYKARnKKTGELVALKKIRME----NEKEgfpitAIREIKLLQKLDHPNVVRLKEIVTSKGsakyKGSIYMVFEYMDH 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 499 gnllqyldvkDETGEVLEWATRVSI--INGIAR----GIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd07840  89 ----------DLTGLLDNPEVKFTEsqIKCYMKqlleGLQYLHSNG-----ILHRDIKGSNILINNDGVLKLADFGLARP 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 573 FTDDIVFSKLKASAAMGYLAPEyITTG--RFTDKSDVYAFGMILLQILSGK------------SKISHLM 628
Cdd:cd07840 154 YTKENNADYTNRVITLWYRPPE-LLLGatRYGPEVDMWSVGCILAELFTGKpifqgkteleqlEKIFELC 222
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
415-684 1.03e-07

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: 53.98  E-value: 1.03e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKgILR--DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLI 492
Cdd:cd06620   5 QDLETLKDLGAGNGGSVSK-VLHipTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNIIICM 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 yEFVPNGNLLQYLDVKDE-TGEVLEwatrvSIINGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNPSLADSGLHK 571
Cdd:cd06620  84 -EYMDCGSLDKILKKKGPfPEEVLG-----KIAVAVLEGLTYLY----NVHRIIHRDIKPSNILVNSKGQIKLCDFGVSG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 572 LFTDDIVFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGMILLQILSGK--------------SKISHLMILQAVesgr 637
Cdd:cd06620 154 ELINSIADTFVGTST---YMSPERIQGGKYSVKSDVWSLGLSIIELALGEfpfagsnddddgynGPMGILDLLQRI---- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 15225456 638 LNEDfmDPNLRKN--FPEVeaaqLARLGLLCTHESSNQRPSmedvIQEL 684
Cdd:cd06620 227 VNEP--PPRLPKDriFPKD----LRDFVDRCLLKDPRERPS----PQLL 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
417-621 1.22e-07

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: 53.55  E-value: 1.22e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKgILR--DGSVAAIKCIAKSSCKSDESE-FLKGLKMLTLLKHENLARLR-GFCcsKGRGECfLI 492
Cdd:cd08530   2 FKVLKKLGKGSYGSVYK-VKRlsDNQVYALKEVNLGSLSQKEREdSVNEIRLLASVNHPNIIRYKeAFL--DGNRLC-IV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd08530  78 MEYAPFGDLSKLISKRKKKRRLFPEDDIWRIFIQMLRGLKALHDQK-----ILHRDLKSANILLSAGDLVKIGDLGISKV 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 15225456 573 FTDDIvfsklkASAAMG---YLAPEyITTGR-FTDKSDVYAFGMILLQILSGK 621
Cdd:cd08530 153 LKKNL------AKTQIGtplYAAPE-VWKGRpYDYKSDIWSLGCLLYEMATFR 198
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
443-620 1.26e-07

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: 53.74  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGNLlqyLDVKDETGEVLEW-ATRV 521
Cdd:cd14169  32 ALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPTH--LYLAMELVTGGEL---FDRIIERGSYTEKdASQL 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 522 siINGIARGIVYLHgengnKPAIVHQNLSAEKILidhwYNPSLADSglhKLFTDDIVFSKLKASAAM-------GYLAPE 594
Cdd:cd14169 107 --IGQVLQAVKYLH-----QLGIVHRDLKPENLL----YATPFEDS---KIMISDFGLSKIEAQGMLstacgtpGYVAPE 172
                       170       180
                ....*....|....*....|....*.
gi 15225456 595 YITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14169 173 LLEQKPYGKAVDVWAIGVISYILLCG 198
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
422-633 1.52e-07

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: 53.15  E-value: 1.52e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSD---------------ESEFLKGLKmltllkHENLARLRGFccskG 485
Cdd:cd06629   8 LIGKGTYGRVYLAMnATTGEMLAVKQVELPKTSSDradsrqktvvdalksEIDTLKDLD------HPNIVQYLGF----E 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 486 RGECFL-IY-EFVPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPS 563
Cdd:cd06629  78 ETEDYFsIFlEYVPGGSIGSCLR---KYGKFEEDLVR-FFTRQILDGLAYLHSKG-----ILHRDLKADNILVDLEGICK 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 564 LADSGLHKLfTDDIvFSKLKASAAMG---YLAPEYITTGR--FTDKSDVYAFGMILLQILSGKSKISHLMILQAV 633
Cdd:cd06629 149 ISDFGISKK-SDDI-YGNNGATSMQGsvfWMAPEVIHSQGqgYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAM 221
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
469-682 1.96e-07

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: 52.93  E-value: 1.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 469 LKHENLARLRGFCCSKGRGECFLIYEFVPNGNLLQYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENGNKPAIVHQN 548
Cdd:cd08217  56 LKHPNIVRYYDRIVDRANTTLYIVMEYCEGGDLAQLIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRSVGGGKILHRD 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 549 LSAEKILIDHWYNPSLADSGLHKLFTDDIVFsklkASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK---S 622
Cdd:cd08217 136 LKPANIFLDSDNNVKLGDFGLARVLSHDSSF----AKTYVGtpyYMSPELLNEQSYDEKSDIWSLGCLIYELCALHppfQ 211
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 623 KISHLMILQAVESGRLNedfmdpnlrkNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd08217 212 AANQLELAKKIKEGKFP----------RIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQ 261
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
449-681 2.55e-07

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 52.62  E-value: 2.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 449 KSSCKSDESEFLKGLKMLTLLKHENLARLRGFC--CSKGRGECFLIYEFVPNGNLLQYLDVKDETGEVL------EWATR 520
Cdd:cd14035  32 KKAFKAHEDKIKTMFENLTLVDHPNIVKFHKYWldVKDNHARVVFITEYVSSGSLKQFLKKTKKNHKTMnarawkRWCTQ 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 521 vsiingIARGIVYLHGengNKPAIVHQNLSAEKILIDHwyNPSLA-DSGLHKLFT----DDIVFSKLKAS----AAMGYL 591
Cdd:cd14035 112 ------ILSALSYLHS---CEPPIIHGNLTSDTIFIQH--NGLIKiGSVWHRLFVnvlpEGGVRGPLRQEreelRNLHFF 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 592 APEYittGRFTDKS--DVYAFGMILLQIL------SGKSKISHLMILQAVESgrlnedFMDPNLRKnfpeveaaqlarLG 663
Cdd:cd14035 181 PPEY---GSCEDGTavDIFSFGMCALEMAvleiqaNGDTRVSEEAIARARHS------LEDPNMRE------------FI 239
                       250
                ....*....|....*...
gi 15225456 664 LLCTHESSNQRPSMEDVI 681
Cdd:cd14035 240 LSCLRHNPCKRPTAHDLL 257
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
423-680 3.26e-07

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: 52.26  E-value: 3.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGSVAAIKCIAKSSCKsDESEFL---KGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVPNG 499
Cdd:cd14161  11 LGKGTYGRVKKARDSSGRLVAIKSIRKDRIK-DEQDLLhirREIEIMSSLNHPHIISV--YEVFENSSKIVIVMEYASRG 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLdvkDETGEVLEWATRvSIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVF 579
Cdd:cd14161  88 DLYDYI---SERQRLSELEAR-HFFRQIVSAVHYCH-ANG----IVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 580 SKLKASAAmgYLAPEyITTGR--FTDKSDVYAFGMILLQILSGKSKI---SHLMILQAVESGrlneDFMDPNlrknfPEV 654
Cdd:cd14161 159 QTYCGSPL--YASPE-IVNGRpyIGPEVDSWSLGVLLYILVHGTMPFdghDYKILVKQISSG----AYREPT-----KPS 226
                       250       260
                ....*....|....*....|....*.
gi 15225456 655 EAAQLARLGLLCTHEssnQRPSMEDV 680
Cdd:cd14161 227 DACGLIRWLLMVNPE---RRATLEDV 249
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
420-617 3.79e-07

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: 52.36  E-value: 3.79e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILRDGSVAAikciaKSSCKSDESEFLKGLKML--TLLKHENLArlrGFCCS--KGRG---ECFLI 492
Cdd:cd14219  10 VKQIGKGRYGEVWMGKWRGEKVAV-----KVFFTTEEASWFRETEIYqtVLMRHENIL---GFIAAdiKGTGswtQLYLI 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLDVKdetgeVLEWATRVSIINGIARGIVYLHGE---NGNKPAIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd14219  82 TDYHENGSLYDYLKST-----TLDTKAMLKLAYSSVSGLCHLHTEifsTQGKPAIAHRDLKSKNILVKKNGTCCIADLGL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 570 HKLFTDDIVFSKLKASAAMG---YLAPEYI--TTGRFTDKS----DVYAFGMILLQI 617
Cdd:cd14219 157 AVKFISDTNEVDIPPNTRVGtkrYMPPEVLdeSLNRNHFQSyimaDMYSFGLILWEV 213
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
422-686 4.34e-07

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: 51.88  E-value: 4.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILRdGSVAAIKCIAKSScksdESEFLKG-LKMLTLLKHENLARLrgfcCSKGRGECFLIYEFVPNGN 500
Cdd:cd14068   1 LLGDGGFGSVYRAVYR-GEDVAVKIFNKHT----SFRLLRQeLVVLSHLHHPSLVAL----LAAGTAPRMLVMELAPKGS 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDvKDETGEVLEWATRVSIinGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPS-----LADSGLHKLFTD 575
Cdd:cd14068  72 LDALLQ-QDNASLTRTLQHRIAL--HVADGLRYLH-----SAMIIYRDLKPHNVLLFTLYPNCaiiakIADYGIAQYCCR 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 576 DIVFSklkASAAMGYLAPEyITTGR--FTDKSDVYAFGMILLQILSGKSKISH-LMILQAVESGRLNEDFMDPNLRKN-- 650
Cdd:cd14068 144 MGIKT---SEGTPGFRAPE-VARGNviYNQQADVYSFGLLLYDILTCGERIVEgLKFPNEFDELAIQGKLPDPVKEYGca 219
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 15225456 651 -FPEVEAaqlarLGLLCTHESSNQRPSMEDVIQELNN 686
Cdd:cd14068 220 pWPGVEA-----LIKDCLKENPQCRPTSAQVFDILNS 251
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
493-684 4.36e-07

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: 52.72  E-value: 4.36e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK- 571
Cdd:cd05105 214 YKGSNDSEVKNLL--SDDGSEGLTTLDLLSFTYQVARGMEFLASKN-----CVHRDLAARNVLLAQGKIVKICDFGLARd 286
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 572 LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESGRLNEDFmdpnlRKNF 651
Cdd:cd05105 287 IMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPGMIVDSTFYNKIKSGY-----RMAK 361
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15225456 652 PEVEAAQLARLGLLCTHESSNQRPS---MEDVIQEL 684
Cdd:cd05105 362 PDHATQEVYDIMVKCWNSEPEKRPSflhLSDIVESL 397
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
420-626 4.71e-07

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: 51.94  E-value: 4.71e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESE------FLKGLKMLTLLKHENLARL--------RGFCCsk 484
Cdd:cd13990   5 LNLLGKGGFSEVYKAFdLVEQRYVACKIHQLNKDWSEEKKqnyikhALREYEIHKSLDHPRIVKLydvfeidtDSFCT-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 485 grgecflIYEFVPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLhgeNGNKPAIVHQNLSAEKILIDHWY---N 561
Cdd:cd13990  83 -------VLEYCDGNDLDFYLK---QHKSIPEREAR-SIIMQVVSALKYL---NEIKPPIIHYDLKPGNILLHSGNvsgE 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 562 PSLADSGLHKLFTDDIVFS---KLKASAAmG---YLAPEYITTG----RFTDKSDVYAFGMILLQILSGKSKISH 626
Cdd:cd13990 149 IKITDFGLSKIMDDESYNSdgmELTSQGA-GtywYLPPECFVVGktppKISSKVDVWSVGVIFYQMLYGRKPFGH 222
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
415-627 5.09e-07

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: 51.86  E-value: 5.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGfccskgrgeCFL-- 491
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIdKRTNQVVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYG---------SFLkg 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 -----IYEFVPNGNLLQYLdvkdETGEVLEWATRVsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLAD 566
Cdd:cd06609  72 sklwiIMEYCGGGSVLDLL----KPGPLDETYIAF-ILREVLLGLEYLHSEG-----KIHRDIKAANILLSEEGDVKLAD 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15225456 567 SGLhklfTDDIVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHL 627
Cdd:cd06609 142 FGV----SGQLTSTMSKRNTFVGtpfWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDL 201
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
415-621 6.97e-07

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: 51.01  E-value: 6.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSD--ESEFLKGLKMLTLLKHENLARLRGFCcsKGRGECFL 491
Cdd:cd14186   1 EDFKVLNLLGKGSFACVYRARsLHTGLEVAIKMIDKKAMQKAgmVQRVRNEVEIHCQLKHPSILELYNYF--EDSNYVYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 IYEFVPNGNLLQYLdvKDETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL-- 569
Cdd:cd14186  79 VLEMCHNGEMSRYL--KNRKKPFTEDEAR-HFMHQIVTGMLYLHSHG-----ILHRDLTLSNLLLTRNMNIKIADFGLat 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 570 ------HKLFTddivfsklkASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd14186 151 qlkmphEKHFT---------MCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLLVGR 199
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
464-683 7.34e-07

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: 51.27  E-value: 7.34e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 464 KMLTLLKHENLAR-LRGFCCSKGrgeCFLIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkp 542
Cdd:cd08220  51 KVLSMLHHPNIIEyYESFLEDKA---LMIVMEYAPGGTLFEYI--QQRKGSLLSEEEILHFFVQILLALHHVHSKQ---- 121
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 543 aIVHQNLSAEKILID-HWYNPSLADSGLHKlftddIVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQIL 618
Cdd:cd08220 122 -ILHRDLKTQNILLNkKRTVVKIGDFGISK-----ILSSKSKAYTVVGtpcYISPELCEGKPYNQKSDIWALGCVLYELA 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 619 SGKskishlmilQAVESGRLNEDFMDPnLRKNF---PEVEAAQLARLGLLCTHESSNQRPSMEDVIQE 683
Cdd:cd08220 196 SLK---------RAFEAANLPALVLKI-MRGTFapiSDRYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
422-682 7.51e-07

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: 51.28  E-value: 7.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGilRD---GSVAAIKCIakSSCKSDESE-------FLKGLKMLTLLKHENLARLRGFCCSKGRGECFL 491
Cdd:cd06630   7 LLGTGAFSSCYQA--RDvktGTLMAVKQV--SFCRNSSSEqeevveaIREEIRMMARLNHPNIVRMLGATQHKSHFNIFV 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 iyEFVPNGNLLQYLDvkdETGEVLEwATRVSIINGIARGIVYLHgENgnkpAIVHQNLSAEKILIDHW-YNPSLADSGLH 570
Cdd:cd06630  83 --EWMAGGSVASLLS---KYGAFSE-NVIINYTLQILRGLAYLH-DN----QIIHRDLKGANLLVDSTgQRLRIADFGAA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 571 KLFTDDIVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGK-----SKIS-HLMILQAVESGrlned 641
Cdd:cd06630 152 ARLASKGTGAGEFQGQLLGtiaFMAPEVLRGEQYGRSCDVWSVGCVIIEMATAKppwnaEKISnHLALIFKIASA----- 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 15225456 642 fMDPnlrKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd06630 227 -TTP---PPIPEHLSPGLRDVTLRCLELQPEDRPPARELLK 263
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
443-686 1.25e-06

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: 50.86  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 443 AIKCIAKSSCKSDESEFLKGL----KMLTLLKHENLARLRGFCCSKGRGECfLIYEFVpNGNLLQYLDVKDETGE-VLEW 517
Cdd:cd14001  32 AVKKINSKCDKGQRSLYQERLkeeaKILKSLNHPNIVGFRAFTKSEDGSLC-LAMEYG-GKSLNDLIEERYEAGLgPFPA 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 518 ATRVSIINGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNP-SLADSGLHKLFTDDI-VFSKLKASaamgYL---- 591
Cdd:cd14001 110 ATILKVALSIARALEYLH----NEKKILHGDIKSGNVLIKGDFESvKLCDFGVSLPLTENLeVDSDPKAQ----YVgtep 181
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 592 --APEYITTGR-FTDKSDVYAFGMILLQILSgkSKISHLmilqavESGRLNEDFMDPNLRKNFPEVEAAqLARLGLL--- 665
Cdd:cd14001 182 wkAKEALEEGGvITDKADIFAYGLVLWEMMT--LSVPHL------NLLDIEDDDEDESFDEDEEDEEAY-YGTLGTRpal 252
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 15225456 666 ------------------CTHESSNQRPSMEDVIQELNN 686
Cdd:cd14001 253 nlgelddsyqkvielfyaCTQEDPKDRPSAAHIVEALEA 291
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
421-621 1.49e-06

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 50.91  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  421 NLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESEF-------------LKGLKMLTLLKHENLARLRGFCCSKGr 486
Cdd:PTZ00024  15 AHLGEGTYGKVEKAYdTLTGKIVAIKKVKIIEISNDVTKDrqlvgmcgihfttLRELKIMNEIKHENIMGLVDVYVEGD- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  487 gecfliyeFVpngNLLqyLDVKD-ETGEVLEWATRVS------IINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHW 559
Cdd:PTZ00024  94 --------FI---NLV--MDIMAsDLKKVVDRKIRLTesqvkcILLQILNGLNVLH-----KWYFMHRDLSPANIFINSK 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456  560 YNPSLADSGLHKLFTDDIVF---SKLKASA----------AMGYLAPEYIT-TGRFTDKSDVYAFGMILLQILSGK 621
Cdd:PTZ00024 156 GICKIADFGLARRYGYPPYSdtlSKDETMQrreemtskvvTLWYRAPELLMgAEKYHFAVDMWSVGCIFAELLTGK 231
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
437-622 1.72e-06

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: 49.92  E-value: 1.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIAKSSCKSDESEFLKgLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVPNGNLLQylDVKDETGEVLE 516
Cdd:cd14190  27 RTGLKLAAKVINKQNSKDKEMVLLE-IQVMNQLNHRNLIQL--YEAIETPNEIVLFMEYVEGGELFE--RIVDEDYHLTE 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 517 WATRVsIINGIARGIVYLHgengnKPAIVHQNLSAEKILI--DHWYNPSLADSGLHKLFTDDivfSKLKAS-AAMGYLAP 593
Cdd:cd14190 102 VDAMV-FVRQICEGIQFMH-----QMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPR---EKLKVNfGTPEFLSP 172
                       170       180
                ....*....|....*....|....*....
gi 15225456 594 EYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd14190 173 EVVNYDQVSFPTDMWSMGVITYMLLSGLS 201
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
423-622 1.79e-06

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: 49.92  E-value: 1.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGI-LRDGSVAAIKCIaKSSCKSDESEFLKGLKMLTLLKHENLARL-RGFCCSKgrgECFLIYEFVPNGN 500
Cdd:cd14103   1 LGRGKFGTVYRCVeKATGKELAAKFI-KCRKAKDREDVRNEIEIMNQLRHPRLLQLyDAFETPR---EMVLVMEYVAGGE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQylDVKDETGEVLEWATrVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIdhwYNPS-----LADSGLHKLFTD 575
Cdd:cd14103  77 LFE--RVVDDDFELTERDC-ILFMRQICEGVQYMHKQG-----ILHLDLKPENILC---VSRTgnqikIIDFGLARKYDP 145
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15225456 576 DivfSKLKASAamG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd14103 146 D---KKLKVLF--GtpeFVAPEVVNYEPISYATDMWSVGVICYVLLSGLS 190
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
409-628 1.82e-06

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: 49.70  E-value: 1.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 409 EIERAtqsfseinlLGKSNVSSVYKGILR-DGSVAAIKCIAKSscKSDESEFLK---GLKMLTLLKHENLARLRGFCCSK 484
Cdd:cd14071   3 DIERT---------IGKGNFAVVKLARHRiTKTEVAIKIIDKS--QLDEENLKKiyrEVQIMKMLNHPHIIKLYQVMETK 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 485 GRgeCFLIYEFVPNGNLLQYLDvkdETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSL 564
Cdd:cd14071  72 DM--LYLVTEYASNGEIFDYLA---QHGRMSEKEAR-KKFWQILSAVEYCHKRH-----IVHRDLKAENLLLDANMNIKI 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 565 ADSGLHKLFTDDIVFSKLKASAAmgYLAPEYITTGRFTD-KSDVYAFGMIL--------------LQ-----ILSGKSKI 624
Cdd:cd14071 141 ADFGFSNFFKPGELLKTWCGSPP--YAAPEVFEGKEYEGpQLDIWSLGVVLyvlvcgalpfdgstLQtlrdrVLSGRFRI 218

                ....
gi 15225456 625 SHLM 628
Cdd:cd14071 219 PFFM 222
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
423-620 1.82e-06

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: 49.82  E-value: 1.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDeSEFLKGLK----MLTLLKHENLARLRGFCcsKGRGECFLIYEFVP 497
Cdd:cd14070  10 LGEGSFAKVREGLhAVTGEKVAIKVIDKKKAKKD-SYVTKNLRregrIQQMIRHPNITQLLDIL--ETENSYYLVMELCP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDVKDEtgevLEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHKLF---- 573
Cdd:cd14070  87 GGNLMHRIYDKKR----LEEREARRYIRQLVSAVEHLH-----RAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAgilg 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 574 -TDDivFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14070 158 ySDP--FSTQCGSPA--YAAPELLARKKYGPKVDVWSIGVNMYAMLTG 201
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
416-621 1.98e-06

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: 49.96  E-value: 1.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYE 494
Cdd:cd07870   1 SYLNLEKLGEGSYATVYKGISRiNGQLVALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKE--TLTFVFE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVpNGNLLQYLdvKDETGEVLEWATRVSIINgIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKlfT 574
Cdd:cd07870  79 YM-HTDLAQYM--IQHPGGLHPYNVRLFMFQ-LLRGLAYIHGQH-----ILHRDLKPQNLLISYLGELKLADFGLAR--A 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15225456 575 DDIVFSKLKASAAMGYLAPEYITTGRfTDKS---DVYAFGMILLQILSGK 621
Cdd:cd07870 148 KSIPSQTYSSEVVTLWYRPPDVLLGA-TDYSsalDIWGAGCIFIEMLQGQ 196
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
477-614 2.16e-06

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: 50.25  E-value: 2.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 477 LRGFCCSKGRGECFL--IYEFVPNGNLLQYLDVKDETGevlewATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKI 554
Cdd:cd13977  96 LKGERCFDPRSACYLwfVMEFCDGGDMNEYLLSRRPDR-----QTNTSFMLQLSSALAFLH-----RNQIVHRDLKPDNI 165
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225456 555 LIDHWY-NPSL--ADSGLHKLFT-------DDIVFSKLKASAAMG---YLAPEyITTGRFTDKSDVYAFGMIL 614
Cdd:cd13977 166 LISHKRgEPILkvADFGLSKVCSgsglnpeEPANVNKHFLSSACGsdfYMAPE-VWEGHYTAKADIFALGIII 237
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
420-682 2.52e-06

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: 49.73  E-value: 2.52e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGILRD-GSVAAIKCIakssCKSDESEFLKGL-----KMLTLLKHENLARLRGFCCSKGRgeCFLIY 493
Cdd:cd07846   6 LGLVGEGSYGMVMKCRHKEtGQIVAIKKF----LESEDDKMVKKIamreiKMLKQLRHENLVNLIEVFRRKKR--WYLVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVpNGNLLQYLDvKDETGevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIdhwynpslADSGLHKLF 573
Cdd:cd07846  80 EFV-DHTVLDDLE-KYPNG--LDESRVRKYLFQILRGIDFCHSHN-----IIHRDIKPENILV--------SQSGVVKLC 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 574 tdDIVFSKLKAS---------AAMGYLAPEYITTG-RFTDKSDVYAFGMILLQILSGK---------SKISHLMILQAVE 634
Cdd:cd07846 143 --DFGFARTLAApgevytdyvATRWYRAPELLVGDtKYGKAVDVWAVGCLVTEMLTGEplfpgdsdiDQLYHIIKCLGNL 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225456 635 SGRLNEDFM-DP--------------NLRKNFPEVEAAqLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd07846 221 IPRHQELFQkNPlfagvrlpevkevePLERRYPKLSGV-VIDLAKKCLHIDPDKRPSCSELLH 282
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
458-622 4.71e-06

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: 48.80  E-value: 4.71e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 458 EFLKGLKMLTLLKHENLARLRGFccSKGRGECFLIYEFVPNGNLLQYLDVKDETGEvlEWATRvsIINGIARGIVYLHGE 537
Cdd:cd14196  54 EIEREVSILRQVLHPNIITLHDV--YENRTDVVLILELVSGGELFDFLAQKESLSE--EEATS--FIKQILDGVNYLHTK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 538 NgnkpaIVHQNLSAEKILIDHWYNP----SLADSGLHKLFTDDIVFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGMI 613
Cdd:cd14196 128 K-----IAHFDLKPENIMLLDKNIPiphiKLIDFGLAHEIEDGVEFKNIFGTPE--FVAPEIVNYEPLGLEADMWSIGVI 200

                ....*....
gi 15225456 614 LLQILSGKS 622
Cdd:cd14196 201 TYILLSGAS 209
LRR_8 pfam13855
Leucine rich repeat;
141-200 5.55e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 44.05  E-value: 5.55e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456   141 NLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQLSGAIPASLGDIDTLTRLDLSFNNL 200
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
416-627 5.99e-06

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: 48.65  E-value: 5.99e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIA-KSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIY 493
Cdd:cd07860   1 NFQKVEKIGEGTYGVVYKARnKLTGEVVALKKIRlDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENK--LYLVF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVpNGNLLQYLDVKDETGevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF 573
Cdd:cd07860  79 EFL-HQDLKKFMDASALTG--IPLPLIKSYLFQLLQGLAFCHSHR-----VLHRDLKPQNLLINTEGAIKLADFGLARAF 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 574 -------TDDIVfsklkasaAMGYLAPEYITTGRF-TDKSDVYAFGMILLQILS------GKSKISHL 627
Cdd:cd07860 151 gvpvrtyTHEVV--------TLWYRAPEILLGCKYySTAVDIWSLGCIFAEMVTrralfpGDSEIDQL 210
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
457-686 7.36e-06

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: 48.42  E-value: 7.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 457 SEFLKGLKMLTLLKHENLARLRGFCCSKgrgECFLIyEFVPNGNLLQYLDVKDETGEVLEWATRVS--IINGIARGIVYL 534
Cdd:cd14067  55 SEFRQEASMLHSLQHPCIVYLIGISIHP---LCFAL-ELAPLGSLNTVLEENHKGSSFMPLGHMLTfkIAYQIAAGLAYL 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 535 HGENgnkpaIVHQNLSAEKILIdhW-------YNPSLADSGLHKLFTDDIVfskLKASAAMGYLAPEYITTGRFTDKSDV 607
Cdd:cd14067 131 HKKN-----IIFCDLKSDNILV--WsldvqehINIKLSDYGISRQSFHEGA---LGVEGTPGYQAPEIRPRIVYDEKVDM 200
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 608 YAFGMILLQILSG-KSKISH--LMILQAVESGrlnedfmdpnLRKNFPEVEAAQLARLGLL---CTHESSNQRPSMEDVI 681
Cdd:cd14067 201 FSYGMVLYELLSGqRPSLGHhqLQIAKKLSKG----------IRPVLGQPEEVQFFRLQALmmeCWDTKPEKRPLACSVV 270

                ....*
gi 15225456 682 QELNN 686
Cdd:cd14067 271 EQMKD 275
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
463-633 8.95e-06

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: 47.71  E-value: 8.95e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 463 LKMLTLLKHENLARLRGfCCSKGRGECFLIY-EFVPNGNllqyldVKDET---GEVLEWATRvSIINGIARGIVYLHGEn 538
Cdd:cd06653  55 IQLLKNLRHDRIVQYYG-CLRDPEEKKLSIFvEYMPGGS------VKDQLkayGALTENVTR-RYTRQILQGVSYLHSN- 125
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 539 gnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKLFtDDIVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILL 615
Cdd:cd06653 126 ----MIVHRDIKGANILRDSAGNVKLGDFGASKRI-QTICMSGTGIKSVTGtpyWMSPEVISGEGYGRKADVWSVACTVV 200
                       170
                ....*....|....*...
gi 15225456 616 QILSGKSKISHLMILQAV 633
Cdd:cd06653 201 EMLTEKPPWAEYEAMAAI 218
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
466-617 9.28e-06

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 47.82  E-value: 9.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 466 LTLLKHENLARLRGFCC--SKGRGECFLIYEFVPNGNLLQYLDVKDETGEVLEWATRVSIINGIARGIVYLHGENgnkPA 543
Cdd:cd14034  64 LIQLEHLNIVKFHKYWAdvKENRARVIFITEYMSSGSLKQFLKKTKKNHKTMNEKAWKRWCTQILSALSYLHSCD---PP 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 544 IVHQNLSAEKILIDHwynpsladSGLHKL--FTDDIVFSKLKA----SAAMGYLAPEYITTGRFTDKSDVYAFGMILLQI 617
Cdd:cd14034 141 IIHGNLTCDTIFIQH--------NGLIKIgsVAPDTINNHVKTcreeQKNLHFFAPEYGEVANVTTAVDIYSFGMCALEM 212
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
469-619 9.29e-06

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: 47.79  E-value: 9.29e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 469 LKHENLARLRGFCCSKGRGEcfLIYEFVPNG---NLLQYLDVKdetgevLEWATRVSIINGIARGIVYLHgengnKPAIV 545
Cdd:cd14043  53 LRHENVNLFLGLFVDCGILA--IVSEHCSRGsleDLLRNDDMK------LDWMFKSSLLLDLIKGMRYLH-----HRGIV 119
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 546 HQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAMGYLAPEYI----TTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd14043 120 HGRLKSRNCVVDGRFVLKITDYGYNEILEAQNLPLPEPAPEELLWTAPELLrdprLERRGTFPGDVFSFAIIMQEVIV 197
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
416-624 9.82e-06

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: 47.71  E-value: 9.82e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINLLGKSNVSSVYKGI-LRDGSVAAIKciaKSSCKSDES--EFLKGLK-MLTLLKHENLARLRG--FCCSKGRGEC 489
Cdd:cd13985   1 RYQVTKQLGEGGFSYVYLAHdVNTGRRYALK---RMYFNDEEQlrVAIKEIEiMKRLCGHPNIVQYYDsaILSSEGRKEV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 FLIYEFVPnGNLLQYLDVKDETG----EVLEwatrvsIINGIARGIVYLHGEngnKPAIVHQNLSAEKILIDHWYNPSLA 565
Cdd:cd13985  78 LLLMEYCP-GSLVDILEKSPPSPlseeEVLR------IFYQICQAVGHLHSQ---SPPIIHRDIKIENILFSNTGRFKLC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 566 DSG----LHKLFTD----DIVFSKLKASAAMGYLAPEYI---TTGRFTDKSDVYAFGMIL---------------LQILS 619
Cdd:cd13985 148 DFGsattEHYPLERaeevNIIEEEIQKNTTPMYRAPEMIdlySKKPIGEKADIWALGCLLyklcffklpfdesskLAIVA 227

                ....*
gi 15225456 620 GKSKI 624
Cdd:cd13985 228 GKYSI 232
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
382-621 1.28e-05

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 47.90  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  382 PLGRGQSSNNNSALSQEVFESFMFNLEEIERatqsfseINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFL 460
Cdd:PLN00034  48 PPPSSSSSSSSSSSASGSAPSAAKSLSELER-------VNRIGSGAGGTVYKVIHRpTGRLYALKVIYGNHEDTVRRQIC 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  461 KGLKMLTLLKHENLARLRGFccSKGRGECFLIYEFVPNGNLlQYLDVKDEtgEVLEWATRvSIINGIArgivYLHgengn 540
Cdd:PLN00034 121 REIEILRDVNHPNVVKCHDM--FDHNGEIQVLLEFMDGGSL-EGTHIADE--QFLADVAR-QILSGIA----YLH----- 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  541 KPAIVHQNLSAEKILIDHWYNPSLADSGLHKLF--TDDIVFSKLKASAamgYLAPEYITT----GRFTDKS-DVYAFGMI 613
Cdd:PLN00034 186 RRHIVHRDIKPSNLLINSAKNVKIADFGVSRILaqTMDPCNSSVGTIA---YMSPERINTdlnhGAYDGYAgDIWSLGVS 262

                 ....*...
gi 15225456  614 LLQILSGK 621
Cdd:PLN00034 263 ILEFYLGR 270
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
422-620 1.34e-05

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: 47.59  E-value: 1.34e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILR-DGSVAAIKCIAKSSC-KSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEFVPNG 499
Cdd:cd05590   2 VLGKGSFGKVMLARLKeSGRLYAVKVLKKDVIlQDDDVECTMTEKRILSLARNHPFLTQLYCCFQTPDRLFFVMEFVNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDVKDETGEVLEWATRVSIINGIargiVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKlftdDIVF 579
Cdd:cd05590  82 DLMFHIQKSRRFDEARARFYAAEITSAL----MFLHDK-----GIIYRDLKLDNVLLDHEGHCKLADFGMCK----EGIF 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 15225456 580 SKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd05590 149 NGKTTSTFCGtpdYIAPEILQEMLYGPSVDWWAMGVLLYEMLCG 192
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
423-649 1.52e-05

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: 47.31  E-value: 1.52e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDeseF----LKGLKMLTLLKHENLARL------RGFCCSKGRGECFL 491
Cdd:cd07866  16 LGEGTFGEVYKARqIKTGRVVALKKILMHNEKDG---FpitaLREIKILKKLKHPNVVPLidmaveRPDKSKRKRGSVYM 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 IYEFVP---NGnLLQYLDVKdetgevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd07866  93 VTPYMDhdlSG-LLENPSVK------LTESQIKCYMLQLLEGINYLHENH-----ILHRDIKAANILIDNQGILKIADFG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 569 LHKLFTDDIvfSKLKASAAMG------------YLAPEYITTGR-FTDKSDVYAFGMILLQ------ILSGKSKISHL-M 628
Cdd:cd07866 161 LARPYDGPP--PNPKGGGGGGtrkytnlvvtrwYRPPELLLGERrYTTAVDIWGIGCVFAEmftrrpILQGKSDIDQLhL 238
                       250       260
                ....*....|....*....|.
gi 15225456 629 ILQAVesGRLNEDFMdPNLRK 649
Cdd:cd07866 239 IFKLC--GTPTEETW-PGWRS 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
415-620 1.66e-05

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: 47.02  E-value: 1.66e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEiNLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKG-LKMLTLLKHENLARLRGFCCSKGRgeCFLI 492
Cdd:cd14082   4 QIFPD-EVLGSGQFGIVYGGKHRkTGRDVAIKVIDKLRFPTKQESQLRNeVAILQQLSHPGVVNLECMFETPER--VFVV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVpNGNLLQYLdVKDETGEVLEWATRVsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILI---DHWYNPSLADSGL 569
Cdd:cd14082  81 MEKL-HGDMLEMI-LSSEKGRLPERITKF-LVTQILVALRYLHSKN-----IVHCDLKPENVLLasaEPFPQVKLCDFGF 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 570 -----HKLFTDDIVfsklkasAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14082 153 ariigEKSFRRSVV-------GTPAYLAPEVLRNKGYNRSLDMWSVGVIIYVSLSG 201
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
422-622 1.67e-05

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: 47.25  E-value: 1.67e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILR-DGSVAAIKCIAKSSC-KSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGECFLIYEFVPNG 499
Cdd:cd05620   2 VLGKGSFGKVLLAELKgKGEYFAVKALKKDVVlIDDDVECTMVEKRVLALAWENPFLTHLYCTFQTKEHLFFVMEFLNGG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYldVKDETGEVLEWATRVSiiNGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKlftdDIVF 579
Cdd:cd05620  82 DLMFH--IQDKGRFDLYRATFYA--AEIVCGLQFLHSK-----GIIYRDLKLDNVMLDRDGHIKIADFGMCK----ENVF 148
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15225456 580 SKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd05620 149 GDNRASTFCGtpdYIAPEILQGLKYTFSVDWWSFGVLLYEMLIGQS 194
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
469-620 1.86e-05

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: 46.93  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 469 LKHENLARLRGFCCSKGRGECFLiyEFVPNGNLLQYLDvkdETGEVLE----WATRvsiinGIARGIVYLHGENgnkpaI 544
Cdd:cd13995  53 FRHENIAELYGALLWEETVHLFM--EAGEGGSVLEKLE---SCGPMREfeiiWVTK-----HVLKGLDFLHSKN-----I 117
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 545 VHQNLSAEKILIDHwYNPSLADSGLHKLFTDDIVFSKLKASAAMgYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd13995 118 IHHDIKPSNIVFMS-TKAVLVDFGLSVQMTEDVYVPKDLRGTEI-YMSPEVILCRGHNTKADIYSLGATIIHMQTG 191
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
463-621 2.04e-05

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: 46.88  E-value: 2.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 463 LKMLTLLKHENLARLRGFCCS---KGRGECFLIYEFVpNGNLLQYLDVKDETGEVLEwaTRVSIINGIARGIVYLHGEng 539
Cdd:cd07863  53 LKRLEAFDHPNIVRLMDVCATsrtDRETKVTLVFEHV-DQDLRTYLDKVPPPGLPAE--TIKDLMRQFLRGLDFLHAN-- 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 540 nkpAIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASaaMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd07863 128 ---CIVHRDLKPENILVTSGGQVKLADFGLARIYSCQMALTPVVVT--LWYRAPEVLLQSTYATPVDMWSVGCIFAEMFR 202

                ..
gi 15225456 620 GK 621
Cdd:cd07863 203 RK 204
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
422-620 2.48e-05

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: 46.57  E-value: 2.48e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGiLRDGSVAaIKCIAKSSCKSDESEFLKG-LKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGN 500
Cdd:cd14063   7 VIGKGRFGRVHRG-RWHGDVA-IKLLNIDYLNEEQLEAFKEeVAAYKNTRHDNLVLFMGACMDPPH--LAIVTSLCKGRT 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDvkdETGEVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHwYNPSLADSGL---HKLFTDDI 577
Cdd:cd14063  83 LYSLIH---ERKEKFDFNKTVQIAQQICQGMGYLHAKG-----IIHKDLKSKNIFLEN-GRVVITDFGLfslSGLLQPGR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 578 VFSKLKASAA-MGYLAPEYITTGR----------FTDKSDVYAFGMILLQILSG 620
Cdd:cd14063 154 REDTLVIPNGwLCYLAPEIIRALSpdldfeeslpFTKASDVYAFGTVWYELLAG 207
LRRNT_2 pfam08263
Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence ...
28-65 2.74e-05

Leucine rich repeat N-terminal domain; Leucine Rich Repeats pfam00560 are short sequence motifs present in a number of proteins with diverse functions and cellular locations. Leucine Rich Repeats are often flanked by cysteine rich domains. This domain is often found at the N-terminus of tandem leucine rich repeats.


Pssm-ID: 462411 [Multi-domain]  Cd Length: 41  Bit Score: 41.51  E-value: 2.74e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 15225456    28 DILLDIKSSLDPEKRFLTSWT-PDADPCssgSFDGVACD 65
Cdd:pfam08263   6 QALLAFKSSLNDPPGALSSWNsSSSDPC---SWTGVTCD 41
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
417-621 2.92e-05

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: 46.37  E-value: 2.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESEFLKGLKML-TLLKHENLARLRG-FccsKGRGECFLIY 493
Cdd:cd07830   1 YKVIKQLGDGTFGSVYLARNKEtGELVAIKKMKKKFYSWEECMNLREVKSLrKLNEHPNIVKLKEvF---RENDELYFVF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVpNGNLLQYldVKDETGEVLEWATRVSIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-- 571
Cdd:cd07830  78 EYM-EGNLYQL--MKDRKGKPFSESVIRSIIYQILQGLAHIH-KHG----FFHRDLKPENLLVSGPEVVKIADFGLARei 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 572 ----LFTDDIvfsklkasAAMGYLAPEYITtgRFTDKS---DVYAFGMILLQILSGK 621
Cdd:cd07830 150 rsrpPYTDYV--------STRWYRAPEILL--RSTSYSspvDIWALGCIMAELYTLR 196
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
459-684 2.94e-05

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; 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 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 Tyk2 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: 270661 [Multi-domain]  Cd Length: 273  Bit Score: 46.44  E-value: 2.94e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 459 FLKGLKMLTLLKHENLARLRGFCCskgRG-ECFLIYEFVPNGNLLQYLDvKDETGEVLEWatRVSIINGIARGIVYLHGE 537
Cdd:cd05076  62 FFETASLMSQVSHTHLVFVHGVCV---RGsENIMVEEFVEHGPLDVWLR-KEKGHVPMAW--KFVVARQLASALSYLENK 135
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 538 NgnkpaIVHQNLSAEKILI-----DHWYNP--SLADSGLHklFTddiVFSKLKASAAMGYLAPEYITTG-RFTDKSDVYA 609
Cdd:cd05076 136 N-----LVHGNVCAKNILLarlglEEGTSPfiKLSDPGVG--LG---VLSREERVERIPWIAPECVPGGnSLSTAADKWG 205
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 610 FGMILLQI-LSGKSKISHlmilqavESGRLNEDFMDPNLRknFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQEL 684
Cdd:cd05076 206 FGATLLEIcFNGEAPLQS-------RTPSEKERFYQRQHR--LPEPSCPELATLISQCLTYEPTQRPSFRTILRDL 272
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
418-622 2.98e-05

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: 46.06  E-value: 2.98e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 418 SEINLLGKSNVSSVYKGILRDGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVP 497
Cdd:cd14193   7 NKEEILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQLNHANLIQL--YDAFESRNDIVLVMEYVD 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQylDVKDETGEVLEWATrVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILI--DHWYNPSLADSGLHKLFTD 575
Cdd:cd14193  85 GGELFD--RIIDENYNLTELDT-ILFIKQICEGIQYMH-----QMYILHLDLKPENILCvsREANQVKIIDFGLARRYKP 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 576 DivfSKLKAS-AAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd14193 157 R---EKLRVNfGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSGLS 201
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
490-618 3.73e-05

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: 46.03  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 FLIYEFVPNGNLLQYLDVK----DETgeVLEWATRVSIINGIARGIVYLHGENGNkpaiVHQNLSAEKILIDHWYNPSLA 565
Cdd:cd14044  79 FGVIEYCERGSLRDVLNDKisypDGT--FMDWEFKISVMYDIAKGMSYLHSSKTE----VHGRLKSTNCVVDSRMVVKIT 152
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15225456 566 DSGLHklftddivfSKLKASAAMgYLAPEYITTGRFTDKSDVYAFGMILLQIL 618
Cdd:cd14044 153 DFGCN---------SILPPSKDL-WTAPEHLRQAGTSQKGDVYSYGIIAQEII 195
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
527-682 4.33e-05

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: 45.78  E-value: 4.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHgengNKPAIVHQNLSAEKILID---HWY-----------NPSLADSGLHKLFTDDIVFSKLKasaaMGYLA 592
Cdd:cd14011 123 ISEALSFLH----NDVKLVHGNICPESVVINsngEWKlagfdfcisseQATDQFPYFREYDPNLPPLAQPN----LNYLA 194
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 593 PEYITTGRFTDKSDVYAFGMILLQILSgKSKIshlmILQAVESG-----RLNE-DFMDPNLRKNFPEvEAAQLARLGLlc 666
Cdd:cd14011 195 PEYILSKTCDPASDMFSLGVLIYAIYN-KGKP----LFDCVNNLlsykkNSNQlRQLSLSLLEKVPE-ELRDHVKTLL-- 266
                       170
                ....*....|....*.
gi 15225456 667 tHESSNQRPSMEDVIQ 682
Cdd:cd14011 267 -NVTPEVRPDAEQLSK 281
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
423-685 4.54e-05

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: 45.70  E-value: 4.54e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD---------GSVAAIKCIAK---SSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECF 490
Cdd:cd05077   7 LGRGTRTQIYAGILNYkdddedegySYEKEIKVILKvldPSHRDISLAFFETASMMRQVSHKHIVLLYGVCVRDV--ENI 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLDVKDEtgeVLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKIL-----IDHWYNP--S 563
Cdd:cd05077  85 MVEEFVEFGPLDLFMHRKSD---VLTTPWKFKVAKQLASALSYLEDKD-----LVHGNVCTKNILlaregIDGECGPfiK 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 564 LADSGLhklftDDIVFSKLKASAAMGYLAPEYITTGR-FTDKSDVYAFGMILLQI-LSGKSKISHLMILQavesgrlNED 641
Cdd:cd05077 157 LSDPGI-----PITVLSRQECVERIPWIAPECVEDSKnLSIAADKWSFGTTLWEIcYNGEIPLKDKTLAE-------KER 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15225456 642 FMDPNLRKNFPEVEaaQLARLGLLCTHESSNQRPSMEDVIQELN 685
Cdd:cd05077 225 FYEGQCMLVTPSCK--ELADLMTHCMNYDPNQRPFFRAIMRDIN 266
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
527-687 4.78e-05

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: 46.16  E-value: 4.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKS 605
Cdd:cd05107 248 VANGMEFLASKN-----CVHRDLAARNVLICEGKLVKICDFGLARdIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLS 322
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 606 DVYAFGMILLQILS-GKSKISHLmilqavesgRLNEDFMDP---NLRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVI 681
Cdd:cd05107 323 DVWSFGILLWEIFTlGGTPYPEL---------PMNEQFYNAikrGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLV 393

                ....*.
gi 15225456 682 QELNNL 687
Cdd:cd05107 394 HLVGDL 399
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
463-621 4.92e-05

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: 45.79  E-value: 4.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 463 LKMLTLLKHENLARLRGFCC---SKGRGECFLIYEFVpNGNLLQYLDVKDETGEVLEwaTRVSIINGIARGIVYLHGENg 539
Cdd:cd07862  55 LRHLETFEHPNVVRLFDVCTvsrTDRETKLTLVFEHV-DQDLTTYLDKVPEPGVPTE--TIKDMMFQLLRGLDFLHSHR- 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 540 nkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASaaMGYLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd07862 131 ----VVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVT--LWYRAPEVLLQSSYATPVDLWSVGCIFAEMFR 204

                ..
gi 15225456 620 GK 621
Cdd:cd07862 205 RK 206
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
439-620 5.26e-05

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: 45.55  E-value: 5.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIAKSSCKSDESefLKGLK-----MLTLLKHENLARLrgFCCSKGRGECFLIYEFVPNGN---LLQYLDVKDE 510
Cdd:cd05611  21 GDYFAIKVLKKSDMIAKNQ--VTNVKaeraiMMIQGESPYVAKL--YYSFQSKDYLYLVMEYLNGGDcasLIKTLGGLPE 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 511 tgevlEWATRVsiINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLftDDIVFSKLKASAAMGY 590
Cdd:cd05611  97 -----DWAKQY--IAEVVLGVEDLHQRG-----IIHRDIKPENLLIDQTGHLKLTDFGLSRN--GLEKRHNKKFVGTPDY 162
                       170       180       190
                ....*....|....*....|....*....|
gi 15225456 591 LAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd05611 163 LAPETILGVGDDKMSDWWSLGCVIFEFLFG 192
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
438-682 5.99e-05

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: 45.19  E-value: 5.99e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 438 DGSVAAIKCIAKSSCKSDE-SEFLKGLKMLTLLKHENLARLR-GFccsKGRGECFLIYEFVPNGNLLQYLD----VKDET 511
Cdd:cd08218  24 DGKQYVIKEINISKMSPKErEESRKEVAVLSKMKHPNIVQYQeSF---EENGNLYIVMDYCDGGDLYKRINaqrgVLFPE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 512 GEVLEWATRVSIingiarGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFsklkASAAMG-- 589
Cdd:cd08218 101 DQILDWFVQLCL------ALKHVHDRK-----ILHRDIKSQNIFLTKDGIIKLGDFGIARVLNSTVEL----ARTCIGtp 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 590 -YLAPEYITTGRFTDKSDVYAFGMILLQILSGKskishlmilQAVESGRLnEDFMDPNLRKNFPEVE---AAQLARLGLL 665
Cdd:cd08218 166 yYLSPEICENKPYNNKSDIWALGCVLYEMCTLK---------HAFEAGNM-KNLVLKIIRGSYPPVPsrySYDLRSLVSQ 235
                       250
                ....*....|....*..
gi 15225456 666 CTHESSNQRPSMEDVIQ 682
Cdd:cd08218 236 LFKRNPRDRPSINSILE 252
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
423-620 6.23e-05

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: 45.24  E-value: 6.23e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRDGS-VAAIKCIAKSSCKSD--ESEFLKGLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNG 499
Cdd:cd14117  14 LGKGKFGNVYLAREKQSKfIVALKVLFKSQIEKEgvEHQLRREIEIQSHLRHPNILRLYNYFHDRKR--IYLILEYAPRG 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 500 NLLQYLDvKDETGEVLEWATrvsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG--LHKlftddI 577
Cdd:cd14117  92 ELYKELQ-KHGRFDEQRTAT---FMEELADALHYCHEKK-----VIHRDIKPENLLMGYKGELKIADFGwsVHA-----P 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15225456 578 VFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14117 158 SLRRRTMCGTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELLVG 200
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
412-682 6.49e-05

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: 45.44  E-value: 6.49e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 412 RATQSFSEINLLGKSNVSSVYKGilRD---GSVAAIKCIAKSscKSDESEFLKGLKMLTLL---KHENLARLRGFCCSKG 485
Cdd:cd07845   4 RSVTEFEKLNRIGEGTYGIVYRA--RDttsGEIVALKKVRMD--NERDGIPISSLREITLLlnlRHPNIVELKEVVVGKH 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 486 RGECFLIYEFVPN--GNLLQYLDVKDETGEVlewatrVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPS 563
Cdd:cd07845  80 LDSIFLVMEYCEQdlASLLDNMPTPFSESQV------KCLMLQLLRGLQYLHEN-----FIIHRDLKVSNLLLTDKGCLK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 564 LADSGLHKLFtDDIVFSKLKASAAMGYLAPEYITTGRFTDKS-DVYAFGMILLQILS------GKSKISHL-MILQAVes 635
Cdd:cd07845 149 IADFGLARTY-GLPAKPMTPKVVTLWYRAPELLLGCTTYTTAiDMWAVGCILAELLAhkpllpGKSEIEQLdLIIQLL-- 225
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 636 GRLNE----DFMD------------P--NLRKNFPEVEAAQLARLGLLCTHESSnQRPSMEDVIQ 682
Cdd:cd07845 226 GTPNEsiwpGFSDlplvgkftlpkqPynNLKHKFPWLSEAGLRLLNFLLMYDPK-KRATAEEALE 289
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
492-620 7.55e-05

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 45.02  E-value: 7.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 IYEFVPNGNLLQYLDVKDE-----------TG-EVLEW---------ATRVSIINGIARGIVYLHgengnKPAIVHQNLS 550
Cdd:cd14088  52 ILKMVKHPNILQLVDVFETrkeyfiflelaTGrEVFDWildqgyyseRDTSNVIRQVLEAVAYLH-----SLKIVHRNLK 126
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 551 AEKILidhWYNpSLADSglhKLFTDDIVFSKLKAS------AAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14088 127 LENLV---YYN-RLKNS---KIVISDFHLAKLENGlikepcGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLSG 195
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
530-622 8.27e-05

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: 45.35  E-value: 8.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 530 GIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLH-KLFTDDIVFSKLkasAAMGYLAPEYITTGRFTDKSDVY 608
Cdd:cd05632 116 GLEDLHREN-----TVYRDLKPENILLDDYGHIRISDLGLAvKIPEGESIRGRV---GTVGYMAPEVLNNQRYTLSPDYW 187
                        90
                ....*....|....
gi 15225456 609 AFGMILLQILSGKS 622
Cdd:cd05632 188 GLGCLIYEMIEGQS 201
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
417-621 8.86e-05

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: 44.56  E-value: 8.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKG-LKMLTLLKHENLARLrgFCCSKGRGECFLIYE 494
Cdd:cd08225   2 YEIIKKIGEGSFGKIYLAKAKsDSEHCVIKEIDLTKMPVKEKEASKKeVILLAKMKHPNIVTF--FASFQENGRLFIVME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQYLD----VKDETGEVLEWATRVSIingiarGIVYLHGENgnkpaIVHQNLSAEKILID-HWYNPSLADSGL 569
Cdd:cd08225  80 YCDGGDLMKRINrqrgVLFSEDQILSWFVQISL------GLKHIHDRK-----ILHRDIKSQNIFLSkNGMVAKLGDFGI 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 15225456 570 HKLFTDDIVFSKLKASAAMgYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd08225 149 ARQLNDSMELAYTCVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELCTLK 199
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
527-682 1.02e-04

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: 45.28  E-value: 1.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKS 605
Cdd:cd05104 223 VAKGMEFLASKN-----CIHRDLAARNILLTHGRITKICDFGLARdIRNDSNYVVKGNARLPVKWMAPESIFECVYTFES 297
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 606 DVYAFGMILLQILSGKSKISHLMILQAVESGRLNEDFmdpnlRKNFPEVEAAQLARLGLLCTHESSNQRPSMEDVIQ 682
Cdd:cd05104 298 DVWSYGILLWEIFSLGSSPYPGMPVDSKFYKMIKEGY-----RMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQ 369
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
416-622 1.09e-04

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: 44.57  E-value: 1.09e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKsDESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYE 494
Cdd:cd14192   5 AVCPHEVLGGGRFGQVHKCTeLSTGLTLAAKIIKVKGAK-EREEVKNEINIMNQLNHVNLIQL--YDAFESKTNLTLIME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVPNGNLLQylDVKDETGEVLEWATrVSIINGIARGIVYLHgengnKPAIVHQNLSAEKIL-IDHWYNP-SLADSGLHKL 572
Cdd:cd14192  82 YVDGGELFD--RITDESYQLTELDA-ILFTRQICEGVHYLH-----QHYILHLDLKPENILcVNSTGNQiKIIDFGLARR 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15225456 573 FTDDivfSKLKAS-AAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd14192 154 YKPR---EKLKVNfGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSGLS 201
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
72-237 1.20e-04

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 44.92  E-value: 1.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  72 NISLQGMGLTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPLLTDLYLNVNNLSGEIPPLIGNLDNLQVIQLCYNK 151
Cdd:COG4886   6 LSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLL 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 152 LSGsiPTQFGSLKKITVLALQYNQlsgaipaSLGDIDTLTRLDLSFNNLfGPVPVKLAGAPLLEVLDIRNNSFSgFVPSA 231
Cdd:COG4886  86 LLG--LTDLGDLTNLTELDLSGNE-------ELSNLTNLESLDLSGNQL-TDLPEELANLTNLKELDLSNNQLT-DLPEP 154

                ....*.
gi 15225456 232 LKRLNN 237
Cdd:COG4886 155 LGNLTN 160
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
527-622 1.22e-04

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: 44.44  E-value: 1.22e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDivfSKLKASAAM-GYLAPEYITTGRFTDKS 605
Cdd:cd05577 104 IICGLEHLHNRF-----IVYRDLKPENILLDDHGHVRISDLGLAVEFKGG---KKIKGRVGThGYMAPEVLQKEVAYDFS 175
                        90
                ....*....|....*...
gi 15225456 606 -DVYAFGMILLQILSGKS 622
Cdd:cd05577 176 vDWFALGCMLYEMIAGRS 193
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
527-622 1.29e-04

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: 44.63  E-value: 1.29e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDivfSKLKAS-AAMGYLAPEYITTGRFTDKS 605
Cdd:cd05630 111 ICCGLEDLHRER-----IVYRDLKPENILLDDHGHIRISDLGLAVHVPEG---QTIKGRvGTVGYMAPEVVKNERYTFSP 182
                        90
                ....*....|....*..
gi 15225456 606 DVYAFGMILLQILSGKS 622
Cdd:cd05630 183 DWWALGCLLYEMIAGQS 199
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
415-621 1.33e-04

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: 44.62  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKgrgECF-LI 492
Cdd:cd07871   5 ETYVKLDKLGEGTYATVFKGRSKlTENLVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTE---RCLtLV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNgNLLQYLDvkdETGEVLEWATRVSIINGIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLH-- 570
Cdd:cd07871  82 FEYLDS-DLKQYLD---NCGNLMSMHNVKIFMFQLLRGLSYCH-----KRKILHRDLKPQNLLINEKGELKLADFGLAra 152
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 571 -----KLFTDDIVfsklkasaAMGYLAPEYIT-TGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd07871 153 ksvptKTYSNEVV--------TLWYRPPDVLLgSTEYSTPIDMWGVGCILYEMATGR 201
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
439-622 1.60e-04

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: 44.24  E-value: 1.60e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIAKSSCKSD-----ESEFLKGLKMLTLLKHENLARLRGfcCSKGRGECFLIYEFVPNGNLLQYLDVKDETGE 513
Cdd:cd14194  30 GLQYAAKFIKKRRTKSSrrgvsREDIEREVSILKEIQHPNVITLHE--VYENKTDVILILELVAGGELFDFLAEKESLTE 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 514 vlEWATRvsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNP----SLADSGL-HKL-FTDDivFSKLKASAA 587
Cdd:cd14194 108 --EEATE--FLKQILNGVYYLHSLQ-----IAHFDLKPENIMLLDRNVPkpriKIIDFGLaHKIdFGNE--FKNIFGTPE 176
                       170       180       190
                ....*....|....*....|....*....|....*
gi 15225456 588 mgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd14194 177 --FVAPEIVNYEPLGLEADMWSIGVITYILLSGAS 209
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
437-621 1.69e-04

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: 43.88  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 437 RDGSVAAIKCIAKSSCKSDESEFLKG-LKMLTLLKHENLARLRGfcCSKGRGECFLIYEFVPNGNllqyldVKDE---TG 512
Cdd:cd06625  26 RELAVKQVEIDPINTEASKEVKALECeIQLLKNLQHERIVQYYG--CLQDEKSLSIFMEYMPGGS------VKDEikaYG 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 513 EVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTddiVFSKLKASAAMG-- 589
Cdd:cd06625  98 ALTENVTR-KYTRQILEGLAYLHSNM-----IVHRDIKGANILRDSNGNVKLGDFGASKrLQT---ICSSTGMKSVTGtp 168
                       170       180       190
                ....*....|....*....|....*....|...
gi 15225456 590 -YLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd06625 169 yWMSPEVINGEGYGRKADIWSVGCTVVEMLTTK 201
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
490-620 2.07e-04

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: 43.80  E-value: 2.07e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 490 FLIYEFVPNGNLLQYLDVKDETGEVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKI------------LID 557
Cdd:cd14038  74 LLAMEYCQGGDLRKYLNQFENCCGLREGAIL-TLLSDISSALRYLHENR-----IIHRDLKPENIvlqqgeqrlihkIID 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15225456 558 HWYNPSLADSGLHKLFTddivfsklkasAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14038 148 LGYAKELDQGSLCTSFV-----------GTLQYLAPELLEQQKYTVTVDYWSFGTLAFECITG 199
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
417-621 2.13e-04

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: 43.40  E-value: 2.13e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDES--EFLKGLKMLTLLKHENLARLR-GFCcskGRGECFLI 492
Cdd:cd05578   2 FQILRVIGKGSFGKVCIVQKKDtKKMFAMKYMNKQKCIEKDSvrNVLNELEILQELEHPFLVNLWySFQ---DEEDMYMV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLDVKdetGEVLEWATRVsIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKL 572
Cdd:cd05578  79 VDLLLGGDLRYHLQQK---VKFSEETVKF-YICEIVLALDYLHSKN-----IIHRDIKPDNILLDEQGHVHITDFNIATK 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 15225456 573 FTDD-IVFSKlkaSAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd05578 150 LTDGtLATST---SGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEMLRGK 196
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
491-622 2.26e-04

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: 43.84  E-value: 2.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLDVKDETGEvlewaTRVSIING-IARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd05613  82 LILDYINGGELFTHLSQRERFTE-----NEVQIYIGeIVLALEHLH-----KLGIIYRDIKLENILLDSSGHVVLTDFGL 151
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 570 HKLFTDDIVFSKLKASAAMGYLAPEYITTGRFT-DKS-DVYAFGMILLQILSGKS 622
Cdd:cd05613 152 SKEFLLDENERAYSFCGTIEYMAPEIVRGGDSGhDKAvDWWSLGVLMYELLTGAS 206
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
431-627 2.58e-04

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: 43.43  E-value: 2.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 431 VYKGI-LRDGSVAAIKCIAKSSckSDE---SEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVpNGNLLQYLD 506
Cdd:cd07835  15 VYKARdKLTGEIVALKKIRLET--EDEgvpSTAIREISLLKELNHPNIVRL--LDVVHSENKLYLVFEFL-DLDLKKYMD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 507 VKDETGevLEWATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLF-------TDDIVf 579
Cdd:cd07835  90 SSPLTG--LDPPLIKSYLYQLLQGIAFCHSHR-----VLHRDLKPQNLLIDTEGALKLADFGLARAFgvpvrtyTHEVV- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15225456 580 sklkasaAMGYLAPEYITTGRFTDKS-DVYAFGMILLQ------ILSGKSKISHL 627
Cdd:cd07835 162 -------TLWYRAPEILLGSKHYSTPvDIWSVGCIFAEmvtrrpLFPGDSEIDQL 209
LRR_8 pfam13855
Leucine rich repeat;
116-176 2.91e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.43  E-value: 2.91e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225456   116 PLLTDLYLNVNNLSGEIPPLIGNLDNLQVIQLCYNKLSGSIPTQFGSLKKITVLALQYNQL 176
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
411-624 3.48e-04

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: 43.12  E-value: 3.48e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 411 ERATQSFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLtllkHE-NLARLRGFCCS-KGRG 487
Cdd:cd06650   1 ELKDDDFEKISELGAGNGGVVFKVSHKpSGLVMARKLIHLEIKPAIRNQIIRELQVL----HEcNSPYIVGFYGAfYSDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 488 ECFLIYEFVPNGNLLQYLDvkdETGEVLEWAT-RVSIinGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNPSLAD 566
Cdd:cd06650  77 EISICMEHMDGGSLDQVLK---KAGRIPEQILgKVSI--AVIKGLTYLR----EKHKIMHRDVKPSNILVNSRGEIKLCD 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15225456 567 SGLHKLFTDDIVFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKI 624
Cdd:cd06650 148 FGVSGQLIDSMANSFVGTRS---YMSPERLQGTHYSVQSDIWSMGLSLVEMAVGRYPI 202
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
445-620 3.55e-04

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: 42.91  E-value: 3.55e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 445 KCIAKSSCKSDeseflkgLKMLTLLKHENLARLRGFCCSKGRgeCFLIYEFVPNGNLLQYLDVKDETGEvlEWATRVsiI 524
Cdd:cd14087  37 KCRGREVCESE-------LNVLRRVRHTNIIQLIEVFETKER--VYMVMELATGGELFDRIIAKGSFTE--RDATRV--L 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 525 NGIARGIVYLHGengnkPAIVHQNLSAEKILidhWYNPSlADSGLhkLFTDDIVFSKLKAS---------AAMGYLAPEY 595
Cdd:cd14087 104 QMVLDGVKYLHG-----LGITHRDLKPENLL---YYHPG-PDSKI--MITDFGLASTRKKGpnclmkttcGTPEYIAPEI 172
                       170       180
                ....*....|....*....|....*
gi 15225456 596 ITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14087 173 LLRKPYTQSVDMWAVGVIAYILLSG 197
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
482-622 3.56e-04

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: 43.45  E-value: 3.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 482 CSKGRGECFLIYEFVPNGNLLQYLDvkdETGEVLEwATRVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYN 561
Cdd:cd05616  69 CFQTMDRLYFVMEYVNGGDLMYHIQ---QVGRFKE-PHAVFYAAEIAIGLFFLQSK-----GIIYRDLKLDNVMLDSEGH 139
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15225456 562 PSLADSGLHKLFTDDIVFSKLKASAAmGYLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd05616 140 IKIADFGMCKENIWDGVTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQA 199
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
416-620 3.77e-04

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: 43.14  E-value: 3.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 416 SFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYE 494
Cdd:cd07869   6 SYEKLEKLGEGSYATVYKGKSKvNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKE--TLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 495 FVpNGNLLQYLDvkDETGEVLEWATRVSIINgIARGIVYLHgengnKPAIVHQNLSAEKILIDHWYNPSLADSGLHK--- 571
Cdd:cd07869  84 YV-HTDLCQYMD--KHPGGLHPENVKLFLFQ-LLRGLSYIH-----QRYILHRDLKPQNLLISDTGELKLADFGLARaks 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 572 ----LFTDDIVfsklkasaAMGYLAPEYIT-TGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd07869 155 vpshTYSNEVV--------TLWYRPPDVLLgSTEYSTCLDMWGVGCIFVEMIQG 200
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
424-680 4.31e-04

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: 42.57  E-value: 4.31e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 424 GKSNVSSVYKGIlrdgSVA--AIKCIAKSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGrgECFLIYEFVPNGNL 501
Cdd:cd05042   9 GKVLLGEIYSGT----SVAqvVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAI--PYLLVMEFCDLGDL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 502 LQYLDVKDETgEVLEWATRV--SIINGIARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGL-HKLFTDDIV 578
Cdd:cd05042  83 KAYLRSEREH-ERGDSDTRTlqRMACEVAAGLAHLHKLN-----FVHSDLALRNCLLTSDLTVKIGDYGLaHSRYKEDYI 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 579 FSKLKASAAMGYLAPEYITT--GRF-----TDKSDVYAFGMILLQILS-GKSKISHLMILQAVESGRLNEDFMDPNLRKN 650
Cdd:cd05042 157 ETDDKLWFPLRWTAPELVTEfhDRLlvvdqTKYSNIWSLGVTLWELFEnGAQPYSNLSDLDVLAQVVREQDTKLPKPQLE 236
                       250       260       270
                ....*....|....*....|....*....|....
gi 15225456 651 FPEV----EAAQLARLgllctheSSNQRPSMEDV 680
Cdd:cd05042 237 LPYSdrwyEVLQFCWL-------SPEQRPAAEDV 263
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
411-624 4.67e-04

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: 43.11  E-value: 4.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 411 ERATQSFSEINLLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSDESEFLKGLKMLtllkHE-NLARLRGFCCS-KGRG 487
Cdd:cd06649   1 ELKDDDFERISELGAGNGGVVTKVQHKpSGLIMARKLIHLEIKPAIRNQIIRELQVL----HEcNSPYIVGFYGAfYSDG 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 488 ECFLIYEFVPNGNLLQYLDVKDETGEvlEWATRVSIinGIARGIVYLHgengNKPAIVHQNLSAEKILIDHWYNPSLADS 567
Cdd:cd06649  77 EISICMEHMDGGSLDQVLKEAKRIPE--EILGKVSI--AVLRGLAYLR----EKHQIMHRDVKPSNILVNSRGEIKLCDF 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 568 GLHKLFTDDIVFSKLKASAamgYLAPEYITTGRFTDKSDVYAFGMILLQILSGKSKI 624
Cdd:cd06649 149 GVSGQLIDSMANSFVGTRS---YMSPERLQGTHYSVQSDIWSMGLSLVELAIGRYPI 202
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
420-626 6.94e-04

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: 42.35  E-value: 6.94e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESE------FLKGLKMLTLLKHENLARLRGFCCSKGRGECfLI 492
Cdd:cd14040  11 LHLLGRGGFSEVYKAFdLYEQRYAAVKIHQLNKSWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYFSLDTDTFC-TV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLhgeNGNKPAIVHQNLSAEKILI---DHWYNPSLADSGL 569
Cdd:cd14040  90 LEYCEGNDLDFYL----KQHKLMSEKEARSIVMQIVNALRYL---NEIKPPIIHYDLKPGNILLvdgTACGEIKITDFGL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 570 HKLFTDD---IVFSKLKASAA--MGYLAPEYITTGR----FTDKSDVYAFGMILLQILSGKSKISH 626
Cdd:cd14040 163 SKIMDDDsygVDGMDLTSQGAgtYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCLYGRKPFGH 228
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
422-622 7.42e-04

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: 42.22  E-value: 7.42e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 422 LLGKSNVSSVYKGILR-DGSVAAIKCIAKSSCKSD---ESEFLKGLKMLTLLKHENLARLrgFCCSKGRGECFLIYEFVP 497
Cdd:cd05619  12 MLGKGSFGKVFLAELKgTNQFFAIKALKKDVVLMDddvECTMVEKRVLSLAWEHPFLTHL--FCTFQTKENLFFVMEYLN 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGLHKlftdDI 577
Cdd:cd05619  90 GGDLMFHI----QSCHKFDLPRATFYAAEIICGLQFLHSK-----GIVYRDLKLDNILLDKDGHIKIADFGMCK----EN 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15225456 578 VFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd05619 157 MLGDAKTSTFCGtpdYIAPEILLGQKYNTSVDWWSFGVLLYEMLIGQS 204
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
527-622 7.64e-04

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: 41.96  E-value: 7.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLH-KLFTDDIVFSKLkasAAMGYLAPEYITTGRFTDKS 605
Cdd:cd05605 111 ITCGLEHLHSER-----IVYRDLKPENILLDDHGHVRISDLGLAvEIPEGETIRGRV---GTVGYMAPEVVKNERYTFSP 182
                        90
                ....*....|....*..
gi 15225456 606 DVYAFGMILLQILSGKS 622
Cdd:cd05605 183 DWWGLGCLIYEMIEGQA 199
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
439-620 8.69e-04

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: 41.82  E-value: 8.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 439 GSVAAIKCIAKSScksdesefLKGLKMLTLLKHEN--LARLRG------FCCSKGRGECFLIYEFVPNGN---LLQYLDV 507
Cdd:cd05579  18 GDLYAIKVIKKRD--------MIRKNQVDSVLAERniLSQAQNpfvvklYYSFQGKKNLYLVMEYLPGGDlysLLENVGA 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 508 KDEtgevlEWAtRVsIINGIARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGL--------------HKLF 573
Cdd:cd05579  90 LDE-----DVA-RI-YIAEIVLALEYLH-SHG----IIHRDLKPDNILIDANGHLKLTDFGLskvglvrrqiklsiQKKS 157
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15225456 574 TDDIVFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd05579 158 NGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVG 204
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
421-687 9.27e-04

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: 41.53  E-value: 9.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 421 NLLGKSNVSSVYKGilRDGSVAAIKCIaksSCKSDESEFLKGLKMLTL----LKHENLARLRGFCCSKGRgecFLIYEFV 496
Cdd:cd14153   6 ELIGKGRFGQVYHG--RWHGEVAIRLI---DIERDNEEQLKAFKREVMayrqTRHENVVLFMGACMSPPH---LAIITSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 497 PNGNLLqYLDVKDETgEVLEWATRVSIINGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWyNPSLADSGLhklFTDD 576
Cdd:cd14153  78 CKGRTL-YSVVRDAK-VVLDVNKTRQIAQEIVKGMGYLHAK-----GILHKDLKSKNVFYDNG-KVVITDFGL---FTIS 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 577 IVFS------KLK-ASAAMGYLAPEYITTGR---------FTDKSDVYAFGMILLQILSG----KSKISHLMILQaVESG 636
Cdd:cd14153 147 GVLQagrredKLRiQSGWLCHLAPEIIRQLSpeteedklpFSKHSDVFAFGTIWYELHARewpfKTQPAEAIIWQ-VGSG 225
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 15225456 637 rlnedfMDPNLRKnfpEVEAAQLARLGLLCTHESSNQRPSMEDVIQELNNL 687
Cdd:cd14153 226 ------MKPNLSQ---IGMGKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
491-620 9.78e-04

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: 41.83  E-value: 9.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 491 LIYEFVPNGNLLQYLDvKDETGEVLEWATRVSIINGIARGIVYLHgENgnkpAIVHQNLSAEKILidhwynpsLADSG-- 568
Cdd:cd14039  73 LAMEYCSGGDLRKLLN-KPENCCGLKESQVLSLLSDIGSGIQYLH-EN----KIIHRDLKPENIV--------LQEINgk 138
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15225456 569 -LHKL----FTDDIVFSKLKAS--AAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14039 139 iVHKIidlgYAKDLDQGSLCTSfvGTLQYLAPELFENKSYTVTVDYWSFGTMVFECIAG 197
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
420-626 1.20e-03

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: 41.58  E-value: 1.20e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 420 INLLGKSNVSSVYKGI-LRDGSVAAIKCIAKSSCKSDESE------FLKGLKMLTLLKHENLARLRGFCCSKGRGECfLI 492
Cdd:cd14041  11 LHLLGRGGFSEVYKAFdLTEQRYVAVKIHQLNKNWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYFSLDTDSFC-TV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 493 YEFVPNGNLLQYLdvkdETGEVLEWATRVSIINGIARGIVYLhgeNGNKPAIVHQNLSAEKILIDHWY---NPSLADSGL 569
Cdd:cd14041  90 LEYCEGNDLDFYL----KQHKLMSEKEARSIIMQIVNALKYL---NEIKPPIIHYDLKPGNILLVNGTacgEIKITDFGL 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 570 HKLFTDDIVFS------KLKASAAMGYLAPEYITTGR----FTDKSDVYAFGMILLQILSGKSKISH 626
Cdd:cd14041 163 SKIMDDDSYNSvdgmelTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFYQCLYGRKPFGH 229
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
423-620 1.23e-03

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: 41.25  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGI-LRDGSVAAIKCIA-KSSCKSDESEFLKGLKMLTLLKHENLARLRGFCCSKGRGecFLIYEFVPNGN 500
Cdd:cd14086   9 LGKGAFSVVRRCVqKSTGQEFAAKIINtKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFH--YLVFDLVTGGE 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 501 LLQYLDVKDETGEvlewATRVSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILI---DHWYNPSLADSGLhKLFTDDI 577
Cdd:cd14086  87 LFEDIVAREFYSE----ADASHCIQQILESVNHCHQNG-----IVHRDLKPENLLLaskSKGAAVKLADFGL-AIEVQGD 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 15225456 578 VFSKLKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSG 620
Cdd:cd14086 157 QQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVG 199
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
458-622 1.61e-03

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: 41.14  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 458 EFLKGLKMLTLLKHENLARLRGFCcsKGRGECFLIYEFVPNGNLLQYLDVKDETGEvlEWATRvsIINGIARGIVYLHGE 537
Cdd:cd14195  54 EIEREVNILREIQHPNIITLHDIF--ENKTDVVLILELVSGGELFDFLAEKESLTE--EEATQ--FLKQILDGVHYLHSK 127
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 538 NgnkpaIVHQNLSAEKILIDHWYNPS----LADSGL-HKLFTDDiVFSKLKASAAmgYLAPEYITTGRFTDKSDVYAFGM 612
Cdd:cd14195 128 R-----IAHFDLKPENIMLLDKNVPNprikLIDFGIaHKIEAGN-EFKNIFGTPE--FVAPEIVNYEPLGLEADMWSIGV 199
                       170
                ....*....|
gi 15225456 613 ILLQILSGKS 622
Cdd:cd14195 200 ITYILLSGAS 209
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
423-622 1.78e-03

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: 41.22  E-value: 1.78e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 423 LGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSD---ESEFLKGlKMLTL-LKHENLARLrgFCCSKGRGECFLIYEFVP 497
Cdd:cd05592   3 LGKGSFGKVMLAELKGtNQYFAIKALKKDVVLEDddvECTMIER-RVLALaSQHPFLTHL--FCTFQTESHLFFVMEYLN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 498 NGNLLQYLDvkdETGEVLEWATR---VSIINGIArgivYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFt 574
Cdd:cd05592  80 GGDLMFHIQ---QSGRFDEDRARfygAEIICGLQ----FLH-SRG----IIYRDLKLDNVLLDREGHIKIADFGMCKEN- 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 15225456 575 ddiVFSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILSGKS 622
Cdd:cd05592 147 ---IYGENKASTFCGtpdYIAPEILKGQKYNQSVDWWSFGVLLYEMLIGQS 194
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
488-682 1.80e-03

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: 40.79  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 488 ECFLIYEFVPNGNLLqylDVKDETGEVLEWATRVSIinGIARGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADS 567
Cdd:cd06658  93 ELWVVMEFLEGGALT---DIVTHTRMNEEQIATVCL--SVLRALSYLHNQ-----GVIHRDIKSDSILLTSDGRIKLSDF 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 568 GLHKLFTDDIvfSKLKASAAMGY-LAPEYITTGRFTDKSDVYAFGMILLQILSGKSKISHLMILQAVESGRlneDFMDPN 646
Cdd:cd06658 163 GFCAQVSKEV--PKRKSLVGTPYwMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIR---DNLPPR 237
                       170       180       190
                ....*....|....*....|....*....|....*.
gi 15225456 647 LrKNFPEVEAAQLARLGLLCTHESSnQRPSMEDVIQ 682
Cdd:cd06658 238 V-KDSHKVSSVLRGFLDLMLVREPS-QRATAQELLQ 271
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
482-621 1.83e-03

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: 41.14  E-value: 1.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 482 CSKGRGECFLIYEFVPNGNLLQYLDV--KDETGEVLEWATRVSIingiarGIVYLHgengnKPAIVHQNLSAEKILIDHW 559
Cdd:cd05615  79 CFQTVDRLYFVMEYVNGGDLMYHIQQvgKFKEPQAVFYAAEISV------GLFFLH-----KKGIIYRDLKLDNVMLDSE 147
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15225456 560 YNPSLADSGLHKLFTDDIVFSKlKASAAMGYLAPEYITTGRFTDKSDVYAFGMILLQILSGK 621
Cdd:cd05615 148 GHIKIADFGMCKEHMVEGVTTR-TFCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQ 208
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
415-617 2.26e-03

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: 40.37  E-value: 2.26e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 415 QSFSEINLLGKSNVSSVYKGILR-DGSVAAIKciakSSCKSDESEFLKGLKMLTLLKHENLARLRgfCCSK------GRG 487
Cdd:cd14050   1 QCFTILSKLGEGSFGEVFKVRSReDGKLYAVK----RSRSRFRGEKDRKRKLEEVERHEKLGEHP--NCVRfikaweEKG 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 488 ECFLIYEFVpNGNLLQYLDVKDETGEVLEWATRVSIIngiaRGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADS 567
Cdd:cd14050  75 ILYIQTELC-DTSLQQYCEETHSLPESEVWNILLDLL----KGLKHLHDHG-----LIHLDIKPANIFLSKDGVCKLGDF 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 568 GL-HKLFTDDIvfsklkASAAMG---YLAPEYITtGRFTDKSDVYAFGMILLQI 617
Cdd:cd14050 145 GLvVELDKEDI------HDAQEGdprYMAPELLQ-GSFTKAADIFSLGITILEL 191
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
449-681 2.53e-03

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: 40.11  E-value: 2.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 449 KSSCKSDESEFLKGLKMLTLLKHENL-ARLRGFCcskgRGECFLI-YEFVPNGNLlqYLDVKDETGEVLEWATRVSIING 526
Cdd:cd08221  36 SRLSEKERRDALNEIDILSLLNHDNIiTYYNHFL----DGESLFIeMEYCNGGNL--HDKIAQQKNQLFPEEVVLWYLYQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHgENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKlftddivfsKLKASAAMG--------YLAPEYITT 598
Cdd:cd08221 110 IVSAVSHIH-KAG----ILHRDIKTLNIFLTKADLVKLGDFGISK---------VLDSESSMAesivgtpyYMSPELVQG 175
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 599 GRFTDKSDVYAFGMILLQILSGKSkishlmILQAVESGRLNEDFMDPNlRKNFPEVEAAQLARLGLLCTHESSNQRPSME 678
Cdd:cd08221 176 VKYNFKSDIWAVGCVLYELLTLKR------TFDATNPLRLAVKIVQGE-YEDIDEQYSEEIIQLVHDCLHQDPEDRPTAE 248

                ...
gi 15225456 679 DVI 681
Cdd:cd08221 249 ELL 251
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
527-629 2.63e-03

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: 40.60  E-value: 2.63e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 527 IARGIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHK-LFTDDIVFSKLKASAAMGYLAPEYITTGRFTDKS 605
Cdd:cd05106 221 VAQGMDFLASKN-----CIHRDVAARNVLLTDGRVAKICDFGLARdIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQS 295
                        90       100
                ....*....|....*....|....*
gi 15225456 606 DVYAFGMILLQILS-GKSKISHLMI 629
Cdd:cd05106 296 DVWSYGILLWEIFSlGKSPYPGILV 320
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
494-621 3.25e-03

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: 40.00  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 494 EFVPNGNLLQylDVKDETGeVLEWATRvSIINGIARGIVYLHGENgnkpaIVHQNLSAEKILI--DHWYNPSLADSGLHK 571
Cdd:cd13987  71 EYAPYGDLFS--IIPPQVG-LPEERVK-RCAAQLASALDFMHSKN-----LVHRDIKPENVLLfdKDCRRVKLCDFGLTR 141
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15225456 572 lftddIVFSKLKA-SAAMGYLAPEYITTGR---FT-DKS-DVYAFGMILLQILSGK 621
Cdd:cd13987 142 -----RVGSTVKRvSGTIPYTAPEVCEAKKnegFVvDPSiDVWAFGVLLFCCLTGN 192
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
530-622 3.54e-03

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: 39.73  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 530 GIVYLHGENgnkpaIVHQNLSAEKILIDHWYNPSLADSGLHklfTDdivFSKLKASAAMG---YLAPEYITTGRFTDKS- 605
Cdd:cd05606 110 GLEHMHNRF-----IVYRDLKPANILLDEHGHVRISDLGLA---CD---FSKKKPHASVGthgYMAPEVLQKGVAYDSSa 178
                        90
                ....*....|....*..
gi 15225456 606 DVYAFGMILLQILSGKS 622
Cdd:cd05606 179 DWFSLGCMLYKLLKGHS 195
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
521-651 3.72e-03

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: 40.05  E-value: 3.72e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 521 VSIINGIArgivYLHGENGnkpaIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDDIVFSKLKASAAmgYLAPEYITTGR 600
Cdd:cd06618 121 VSIVKALH----YLKEKHG----VIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAA--YMAPERIDPPD 190
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15225456 601 FTD---KSDVYAFGMILLQILSGKSKISHLMILQAVESGRLNEDFMDPNLRKNF 651
Cdd:cd06618 191 NPKydiRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPSLPPNEGF 244
PLN03150 PLN03150
hypothetical protein; Provisional
80-117 4.66e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.18  E-value: 4.66e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15225456   80 LTGTIPPSIGLLTSLTGLYLHFNSLTGHIPKDISNLPL 117
Cdd:PLN03150 478 FNGSIPESLGQLTSLRILNLNGNSLSGRVPAALGGRLL 515
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
417-622 4.83e-03

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 39.66  E-value: 4.83e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 417 FSEINLLGKSNVSSVYKGILRD-GSVAAIKCIAKSSCKSDESEFLKGLK--MLTLLKHENLARL--RGFCCSKGRGECFL 491
Cdd:cd05633   7 FSVHRIIGRGGFGEVYGCRKADtGKMYAMKCLDKKRIKMKQGETLALNEriMLSLVSTGDCPFIvcMTYAFHTPDKLCFI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 492 IyEFVPNGNLLQYLDVKD--ETGEVLEWATRVSIingiarGIVYLHGEngnkpAIVHQNLSAEKILIDHWYNPSLADSGL 569
Cdd:cd05633  87 L-DLMNGGDLHYHLSQHGvfSEKEMRFYATEIIL------GLEHMHNR-----FVVYRDLKPANILLDEHGHVRISDLGL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15225456 570 HklftddIVFSKLKASAAMG---YLAPEYITTGRFTDKS-DVYAFGMILLQILSGKS 622
Cdd:cd05633 155 A------CDFSKKKPHASVGthgYMAPEVLQKGTAYDSSaDWFSLGCMLFKLLRGHS 205
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
92-200 5.33e-03

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 39.77  E-value: 5.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456  92 TSLTGLYLHFNSLTGH----IPKDISNLPLLTDLYLNVNNLSGE----IPPLIGNLDNLQVIQLCYNKLSG----SIPTQ 159
Cdd:COG5238 264 TTVETLYLSGNQIGAEgaiaLAKALQGNTTLTSLDLSVNRIGDEgaiaLAEGLQGNKTLHTLNLAYNGIGAqgaiALAKA 343
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 15225456 160 FGSLKKITVLALQYNQLSG----AIPASLGDIDTLTRLDLSFNNL 200
Cdd:COG5238 344 LQENTTLHSLDLSDNQIGDegaiALAKYLEGNTTLRELNLGKNNI 388
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
456-568 6.36e-03

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: 37.42  E-value: 6.36e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 456 ESEFLKglkMLTLLKHE-NLARLRGFCcsKGRGECFLIYEFVPNGNLLQYLdvkdeTGEVLEWATRVSIINGIARGIVYL 534
Cdd:cd13968  38 ESEMDI---LRRLKGLElNIPKVLVTE--DVDGPNILLMELVKGGTLIAYT-----QEEELDEKDVESIMYQLAECMRLL 107
                        90       100       110
                ....*....|....*....|....*....|....
gi 15225456 535 HGENgnkpaIVHQNLSAEKILIDHWYNPSLADSG 568
Cdd:cd13968 108 HSFH-----LIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
464-621 6.53e-03

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: 38.96  E-value: 6.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 464 KMLTLLKHENLARLR-GFCCskGRGECFLIYEFVPNGNLLQYLdvKDETGEVLEWATRVSIINGIARGIVYLHGENgnkp 542
Cdd:cd08223  51 KLLSKLKHPNIVSYKeSFEG--EDGFLYIVMGFCEGGDLYTRL--KEQKGVLLEERQVVEWFVQIAMALQYMHERN---- 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15225456 543 aIVHQNLSAEKILIDHWYNPSLADSGLHKLFTDdivfSKLKASAAMG---YLAPEYITTGRFTDKSDVYAFGMILLQILS 619
Cdd:cd08223 123 -ILHRDLKTQNIFLTKSNIIKVGDLGIARVLES----SSDMATTLIGtpyYMSPELFSNKPYNHKSDVWALGCCVYEMAT 197

                ..
gi 15225456 620 GK 621
Cdd:cd08223 198 LK 199
 
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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