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Conserved domains on  [gi|71980965|ref|NP_001021908|]
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Tyrosine-protein kinase receptor cam-1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
568-832 1.75e-125

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: 379.19  E-value: 1.75e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGD--GKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGiTEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd00192  79 EGGDLLDFLRKSRPVFPSPEPS-TLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:cd00192 158 DDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELY 237
                       250       260
                ....*....|....*....|....*
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd00192 238 ELMLSCWQLDPEDRPTFSELVERLE 262
CRD_TK_ROR_like cd07459
Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) ...
177-309 2.47e-44

Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


:

Pssm-ID: 143568  Cd Length: 135  Bit Score: 156.40  E-value: 2.47e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 177 GDCVQYRGEACRQYLSNKFVMMTNESREEmyDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVC-ESDSNNQIV 255
Cdd:cd07459   1 GYCQPYRGSVCAKYLGNKSVYVTSKQTQE--DIEEQLSAAFTVISTSSDVSPKCQQYALPSLCYYAFPLCdEGSSTPKPR 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 256 SICKHDCDVIQNDECPSELALAAQHELVGdtPKALFPLCSRLSST-----SNCIPVMST 309
Cdd:cd07459  79 RICRDECELLENDLCKKEYAIAKRHPLIG--HQLLLPDCSSLPSPgspesSNCIRLGIP 135
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
326-405 3.84e-32

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


:

Pssm-ID: 214527  Cd Length: 83  Bit Score: 119.80  E-value: 3.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    326 HWCYVNSGTQYEGTVAQTSSGKQCAPWIDSTS--RDFNVHRFPELMNSKNYCRNPGGKKSRPWCYSKPMGQE-EYCDVPQ 402
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPhlHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRwEYCDIPQ 80

                   ...
gi 71980965    403 CPS 405
Cdd:smart00130  81 CEE 83
I-set pfam07679
Immunoglobulin I-set domain;
13-101 1.12e-16

Immunoglobulin I-set domain;


:

Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    13 RLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAAS 92
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                  ....*....
gi 71980965    93 VNTTSVLRV 101
Cdd:pfam07679  82 AEASAELTV 90
 
Name Accession Description Interval E-value
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
568-832 1.75e-125

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: 379.19  E-value: 1.75e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGD--GKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGiTEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd00192  79 EGGDLLDFLRKSRPVFPSPEPS-TLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:cd00192 158 DDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELY 237
                       250       260
                ....*....|....*....|....*
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd00192 238 ELMLSCWQLDPEDRPTFSELVERLE 262
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
564-831 5.16e-122

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: 369.96  E-value: 5.16e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    564 LSVREKIGEGQFGVVHSGIYTSGLFaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    644 FEYMVHGDLHELLKvrvppaDHDMGGITeaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:smart00221  80 MEYMPGGDLLDYLR------KNRPKELS--LSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    724 TSYGSDYYKMLHRsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCP 803
Cdd:smart00221 152 DLYDDDYYKVKGG-KLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCP 230
                          250       260
                   ....*....|....*....|....*...
gi 71980965    804 TNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:smart00221 231 PELYKLMLQCWAEDPEDRPTFSELVEIL 258
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
568-831 3.17e-109

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 336.39  E-value: 3.17e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   568 EKIGEGQFGVVHSGIYTSGLFAPEpMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEGENTK-IKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   648 VHGDLHELLKVRVPPadhdmggITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:pfam07714  84 PGGDLLDFLRKHKRK-------LTLK--DLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:pfam07714 155 DDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLEDGYRLPQPENCPDELY 234
                         250       260
                  ....*....|....*....|....
gi 71980965   808 SLMVECWHENIERRPTFSEIRSRL 831
Cdd:pfam07714 235 DLMKQCWAYDPEDRPTFSELVEDL 258
CRD_TK_ROR_like cd07459
Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) ...
177-309 2.47e-44

Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143568  Cd Length: 135  Bit Score: 156.40  E-value: 2.47e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 177 GDCVQYRGEACRQYLSNKFVMMTNESREEmyDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVC-ESDSNNQIV 255
Cdd:cd07459   1 GYCQPYRGSVCAKYLGNKSVYVTSKQTQE--DIEEQLSAAFTVISTSSDVSPKCQQYALPSLCYYAFPLCdEGSSTPKPR 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 256 SICKHDCDVIQNDECPSELALAAQHELVGdtPKALFPLCSRLSST-----SNCIPVMST 309
Cdd:cd07459  79 RICRDECELLENDLCKKEYAIAKRHPLIG--HQLLLPDCSSLPSPgspesSNCIRLGIP 135
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
326-405 3.84e-32

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 119.80  E-value: 3.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    326 HWCYVNSGTQYEGTVAQTSSGKQCAPWIDSTS--RDFNVHRFPELMNSKNYCRNPGGKKSRPWCYSKPMGQE-EYCDVPQ 402
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPhlHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRwEYCDIPQ 80

                   ...
gi 71980965    403 CPS 405
Cdd:smart00130  81 CEE 83
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
325-404 1.85e-31

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 117.86  E-value: 1.85e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 325 THWCYVNSGTQYEGTVAQTSSGKQCAPWIDST--SRDFNVHRFPELMNSKNYCRNPGGKKSRPWCY-SKPMGQEEYCDVP 401
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLphQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYtTDPNVRWEYCDIP 80

                ...
gi 71980965 402 QCP 404
Cdd:cd00108  81 RCE 83
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
566-808 2.93e-25

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 109.06  E-value: 2.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSgiytsglfAPEPMAVAVK--KCRHDATNAERAQLEQEIRAVATFDHP-NVIKLIGVCYMDNSLLA 642
Cdd:COG0515   4 ILRKLGEGSFGEVYL--------ARDRKLVALKvlAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRVPPADHDmggiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVG-DTRTIKIADFGL 721
Cdd:COG0515  76 VMEYVDGGSLEDLLKKIGRKGPLS-------ESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRTSYGSDYYKMLHRSWMPV----RWMSKEAIEQ---GRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVaNRH 794
Cdd:COG0515 149 AKLLPDPGSTSSIPALPSTSvgtpGYMAPEVLLGlslAYASSSSDIWSLGITLYEL-LTGLPPFEGEKNSSATSQT-LKI 226
                       250
                ....*....|....
gi 71980965 795 LLECPHNCPTNIYS 808
Cdd:COG0515 227 ILELPTPSLASPLS 240
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
328-403 7.09e-19

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 81.58  E-value: 7.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   328 CYVNSGTQYEGTVAQTSSGKQCAPWiDSTS----RDFNVHRFPELMNSKNYCRNPGGkKSRPWCYSK-PMGQEEYCDVPQ 402
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAW-DSQTphrhSKYTPENFPAKGLGENYCRNPDG-DERPWCYTTdPRVRWEYCDIPR 78

                  .
gi 71980965   403 C 403
Cdd:pfam00051  79 C 79
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
606-827 9.42e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 83.91  E-value: 9.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  606 NAER--AQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLH----ELLKVRVPPADHDMGgiteanaeFLY 679
Cdd:PTZ00267 104 NDERqaAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNkqikQRLKEHLPFQEYEVG--------LLF 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  680 IatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR-----------TSY-GSDYYkmlhrswmpvrwMSKE 747
Cdd:PTZ00267 176 Y--QIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKqysdsvsldvaSSFcGTPYY------------LAPE 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  748 AIEQGRFSEASDVWSFGVTLWEIWSFGRqPYEGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:PTZ00267 242 LWERKRYSKKADMWSLGVILYELLTLHR-PFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQL 320
I-set pfam07679
Immunoglobulin I-set domain;
13-101 1.12e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    13 RLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAAS 92
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                  ....*....
gi 71980965    93 VNTTSVLRV 101
Cdd:pfam07679  82 AEASAELTV 90
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
29-98 2.68e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 68.51  E-value: 2.68e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  29 VRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSV 98
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19-101 7.48e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 7.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965     19 RNATKSSGDEVRFKCEALGTPPLKFIWLKNNG-PVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTS 97
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 71980965     98 VLRV 101
Cdd:smart00410  82 TLTV 85
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
595-782 3.80e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 66.74  E-value: 3.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  595 VAVKKCRHD-ATNAE-RAQLEQEIRAVATFDHPNVIKLI------GVCYMdnsllaVFEYmVHG-DLHELLKVR--VPPA 663
Cdd:NF033483  35 VAVKVLRPDlARDPEfVARFRREAQSAASLSHPNIVSVYdvgedgGIPYI------VMEY-VDGrTLKDYIREHgpLSPE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  664 dhdmggitEAnaefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR----TSY-------GSDYYk 732
Cdd:NF033483 108 --------EA----VEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARalssTTMtqtnsvlGTVHY- 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 71980965  733 mlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:NF033483 175 -----------LSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFDGDS 212
 
Name Accession Description Interval E-value
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
568-832 1.75e-125

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: 379.19  E-value: 1.75e-125
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd00192   1 KKLGEGAFGEVYKGKLKGGD--GKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGiTEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd00192  79 EGGDLLDFLRKSRPVFPSPEPS-TLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYD 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:cd00192 158 DDYYRKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELY 237
                       250       260
                ....*....|....*....|....*
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd00192 238 ELMLSCWQLDPEDRPTFSELVERLE 262
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
564-831 5.16e-122

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: 369.96  E-value: 5.16e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    564 LSVREKIGEGQFGVVHSGIYTSGLFaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLKGKGD-GKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIV 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    644 FEYMVHGDLHELLKvrvppaDHDMGGITeaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:smart00221  80 MEYMPGGDLLDYLR------KNRPKELS--LSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    724 TSYGSDYYKMLHRsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCP 803
Cdd:smart00221 152 DLYDDDYYKVKGG-KLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCP 230
                          250       260
                   ....*....|....*....|....*...
gi 71980965    804 TNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:smart00221 231 PELYKLMLQCWAEDPEDRPTFSELVEIL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
568-831 1.02e-120

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 366.47  E-value: 1.02e-120
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    568 EKIGEGQFGVVHSGIYTSGLFAPEpMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:smart00219   5 KKLGEGAFGEVYKGKLKGKGGKKK-VEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYM 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    648 VHGDLHELLKVRVPPadhdmggITeaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:smart00219  84 EGGDLLSYLRKNRPK-------LS--LSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYD 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    728 SDYYKMLHRsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:smart00219 155 DDYYRKRGG-KLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELY 233
                          250       260
                   ....*....|....*....|....
gi 71980965    808 SLMVECWHENIERRPTFSEIRSRL 831
Cdd:smart00219 234 DLMLQCWAEDPEDRPTFSELVEIL 257
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
558-834 2.51e-114

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: 350.91  E-value: 2.51e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSG--IYTSGlfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCY 635
Cdd:cd05048   1 EIPLSAVRFLEELGEGAFGKVYKGelLGPSS--EESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCT 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDLHELLKVRVPpadHDMGGITEANA---------EFLYIATQIALGMEYLASMSFVHRDLATRNC 706
Cdd:cd05048  79 KEQPQCMLFEYMAHGDLHEFLVRHSP---HSDVGVSSDDDgtassldqsDFLHIAIQIAAGMEYLSSHHYVHRDLAARNC 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 707 LVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQV 786
Cdd:cd05048 156 LVGDGLTVKISDFGLSRDIYSSDYYRVQSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEV 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 787 IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05048 236 IEMIRSRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLRTW 283
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
568-831 3.17e-109

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 336.39  E-value: 3.17e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   568 EKIGEGQFGVVHSGIYTSGLFAPEpMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:pfam07714   5 EKLGEGAFGEVYKGTLKGEGENTK-IKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYM 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   648 VHGDLHELLKVRVPPadhdmggITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:pfam07714  84 PGGDLLDFLRKHKRK-------LTLK--DLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDIYD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:pfam07714 155 DDYYRKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLEDGYRLPQPENCPDELY 234
                         250       260
                  ....*....|....*....|....
gi 71980965   808 SLMVECWHENIERRPTFSEIRSRL 831
Cdd:pfam07714 235 DLMKQCWAYDPEDRPTFSELVEDL 258
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
558-833 1.30e-99

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: 312.73  E-value: 1.30e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVH------SGIYTSGLF-----APEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPN 626
Cdd:cd05051   1 EFPREKLEFVEKLGEGQFGEVHlceangLSDLTSDDFigndnKDEPVLVAVKMLRPDASKNAREDFLKEVKIMSQLKDPN 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 627 VIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVP--PADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATR 704
Cdd:cd05051  81 IVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHEAetQGASATNSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLATR 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 705 NCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGR-QPYEGASN 783
Cdd:cd05051 161 NCLVGPNYTIKIADFGMSRNLYSGDYYRIEGRAVLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKeQPYEHLTD 240
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 784 QQVIE----LVAN---RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05051 241 EQVIEnageFFRDdgmEVYLSRPPNCPKEIYELMLECWRRDEEDRPTFREIHLFLQR 297
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
558-834 1.14e-89

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: 286.14  E-value: 1.14e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGiytsGLFAPEP----MAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGV 633
Cdd:cd05091   2 EINLSAVRFMEELGEDRFGKVYKG----HLFGTAPgeqtQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSLLAVFEYMVHGDLHELLKVRVPPADhdMGGI--------TEANAEFLYIATQIALGMEYLASMSFVHRDLATRN 705
Cdd:cd05091  78 VTKEQPMSMIFSYCSHGDLHEFLVMRSPHSD--VGSTdddktvksTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRN 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 706 CLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQ 785
Cdd:cd05091 156 VLVFDKLNVKISDLGLFREVYAADYYKLMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQD 235
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71980965 786 VIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05091 236 VIEMIRNRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRLRTW 284
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
558-832 5.15e-85

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: 273.57  E-value: 5.15e-85
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd05049   1 HIKRDTIVLKRELGEGAFGKVFLGECYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVRVPPA------DHDMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDT 711
Cdd:cd05049  81 DPLLMVFEYMEHGDLNKFLRSHGPDAaflaseDSAPGELTLS--QLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTN 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 712 RTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVA 791
Cdd:cd05049 159 LVVKIGDFGMSRDIYSTDYYRVGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECIT 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 792 NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05049 239 QGRLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRLQ 279
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
558-833 2.74e-84

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: 271.52  E-value: 2.74e-84
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd05032   2 ELPREKITLIRELGQGSFGMVYEGLAKGVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTG 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05032  82 QPTLVVMELMAKGDLKSYLRSRRPEAENNPGLGPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIG 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLE 797
Cdd:cd05032 162 DFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGHLD 241
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71980965 798 CPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05032 242 LPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLKD 277
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
558-834 1.65e-83

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: 269.96  E-value: 1.65e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSG-IYTSGLfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05090   1 ELPLSAVRFMEELGECAFGKIYKGhLYLPGM--DHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTQ 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRVPPAD----HDMGGITEA---NAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVG 709
Cdd:cd05090  79 EQPVCMLFEFMNQGDLHEFLIMRSPHSDvgcsSDEDGTVKSsldHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 710 DTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIEL 789
Cdd:cd05090 159 EQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEM 238
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 71980965 790 VANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05090 239 VRKRQLLPCSEDCPPRMYSLMTECWQEIPSRRPRFKDIHARLRSW 283
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
558-831 1.91e-80

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: 261.83  E-value: 1.91e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVH----SGI-----YTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVI 628
Cdd:cd05097   1 EFPRQQLRLKEKLGEGQFGEVHlceaEGLaeflgEGAPEFDGQPVLVAVKMLRADVTKTARNDFLKEIKIMSRLKNPNII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 629 KLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadHDMGGITEAN-------AEFLYIATQIALGMEYLASMSFVHRDL 701
Cdd:cd05097  81 RLLGVCVSDDPLCMITEYMENGDLNQFLSQR-----EIESTFTHANnipsvsiANLLYMAVQIASGMKYLASLNFVHRDL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 702 ATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGR-QPYEG 780
Cdd:cd05097 156 ATRNCLVGNHYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFTLCKeQPYSL 235
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 781 ASNQQVIELVAN------RHL-LECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05097 236 LSDEQVIENTGEffrnqgRQIyLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFL 293
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
570-832 1.01e-79

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: 259.76  E-value: 1.01e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGiYTSGLFAPEPMA-VAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd05050  13 IGQGAFGRVFQA-RAPGLLPYEPFTmVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFEYMA 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKVRVPPADHDMGGITEANA------------EFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05050  92 YGDLNEFLRHRSPRAQCSLSHSTSSARkcglnplplsctEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKI 171
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05050 172 ADFGLSRNIYSADYYKASENDAIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEEVIYYVRDGNVL 251
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05050 252 SCPDNCPLELYNLMRLCWSKLPSDRPSFASINRILQ 287
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
564-833 1.66e-79

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: 259.54  E-value: 1.66e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVH----SGI--YTSGLFAPE-----PMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIG 632
Cdd:cd05095   7 LTFKEKLGEGQFGEVHlceaEGMekFMDKDFALEvsenqPVLVAVKMLRADANKNARNDFLKEIKIMSRLKDPNIIRLLA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDM--GGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGD 710
Cdd:cd05095  87 VCITDDPLCMITEYMENGDLNQFLSRQQPEGQLALpsNALTVSYSDLRFMAAQIASGMKYLSSLNFVHRDLATRNCLVGK 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 711 TRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGR-QPYEGASNQQVIEL 789
Cdd:cd05095 167 NYTIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLTFCReQPYSQLSDEQVIEN 246
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 71980965 790 VAN-------RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05095 247 TGEffrdqgrQTYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLLQE 297
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
558-833 6.25e-76

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: 249.23  E-value: 6.25e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd05036   2 EVPRKNLTLIRALGQGAFGEVYEGTVSGMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVCFQR 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVRVPPADHD----MGgiteanaEFLYIATQIALGMEYLASMSFVHRDLATRNCLV---GD 710
Cdd:cd05036  82 LPRFILLELMAGGDLKSFLRENRPRPEQPssltML-------DLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLtckGP 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 711 TRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELV 790
Cdd:cd05036 155 GRVAKIGDFGMARDIYRADYYRKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFV 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 791 ANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05036 235 TSGGRMDPPKNCPGPVYRIMTQCWQHIPEDRPNFSTILERLNY 277
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
562-833 2.78e-75

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: 248.31  E-value: 2.78e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVH-----------SGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKL 630
Cdd:cd05096   5 GHLLFKEKLGEGQFGEVHlcevvnpqdlpTLQFPFNVRKGRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPNIIRL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 631 IGVCYMDNSLLAVFEYMVHGDLHELLKVRV---------PPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDL 701
Cdd:cd05096  85 LGVCVDEDPLCMITEYMENGDLNQFLSSHHlddkeengnDAVPPAHCLPAISYSSLLHVALQIASGMKYLSSLNFVHRDL 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 702 ATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGR-QPYEG 780
Cdd:cd05096 165 ATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLCKeQPYGE 244
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 781 ASNQQVIELVAN-------RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05096 245 LTDEQVIENAGEffrdqgrQVYLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFLTE 304
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
557-831 7.14e-75

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: 246.18  E-value: 7.14e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSglFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCyM 636
Cdd:cd05056   1 YEIQREDITLGRCIGEGQFGDVYQGVYMS--PENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVI-T 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05056  78 ENPVWIVMELAPLGELRSYLQVNKYSLDL---------ASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05056 149 GDFGLSRYMEDESYYKA-SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERL 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05056 228 PMPPNCPPTLYSLMTKCWAYDPSKRPRFTELKAQL 262
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
570-832 7.66e-74

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: 243.09  E-value: 7.66e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGL-FAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd05044   3 LGSGAFGEVFEGTAKDILgDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKVRVPPAdhdMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLV----GDTRTIKIADFGLMRT 724
Cdd:cd05044  83 GGDLLSYLRAARPTA---FTPPLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVsskdYRERVVKIGDFGLARD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 725 SYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPT 804
Cdd:cd05044 160 IYKNDYYRKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPD 239
                       250       260
                ....*....|....*....|....*...
gi 71980965 805 NIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05044 240 DLYELMLRCWSTDPEERPSFARILEQLQ 267
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
569-833 3.49e-73

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: 241.79  E-value: 3.49e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRhDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd05092  12 ELGEGAFGKVFLAECHNLLPEQDKMLVAVKALK-EATESARQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMR 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKVRVPPADHDMGGITEANAEF-----LYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd05092  91 HGDLNRFLRSHGPDAKILDGGEGQAPGQLtlgqmLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSR 170
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCP 803
Cdd:cd05092 171 DIYSTDYYRVGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQGRELERPRTCP 250
                       250       260       270
                ....*....|....*....|....*....|
gi 71980965 804 TNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05092 251 PEVYAIMQGCWQREPQQRHSIKDIHSRLQA 280
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
556-827 5.79e-73

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: 241.94  E-value: 5.79e-73
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 556 VFEITPSQLSVREKIGEGQFG-VVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGV 633
Cdd:cd05053   6 EWELPRDRLTLGKPLGEGAFGqVVKAEAVGLDNKPNEVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSLLAVFEYMVHGDLHELLKVRVPP---ADHDMGGITEANAEFLYI---ATQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd05053  86 CTQDGPLYVVVEYASKGNLREFLRARRPPgeeASPDDPRVPEEQLTQKDLvsfAYQVARGMEYLASKKCIHRDLAARNVL 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 708 VGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVI 787
Cdd:cd05053 166 VTEDNVMKIADFGLARDIHHIDYYRKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 245
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 788 ELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05053 246 KLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQL 285
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
568-831 7.10e-72

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: 237.63  E-value: 7.10e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDnSLLAVFEYM 647
Cdd:cd05060   1 KELGHGNFGSVRKGVYLMK--SGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGE-PLMLVMELA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMggiteanaefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR-TSY 726
Cdd:cd05060  78 PLGPLLKYLKKRREIPVSDL----------KELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRaLGA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 727 GSDYYKM-LHRSWmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTN 805
Cdd:cd05060 148 GSDYYRAtTAGRW-PLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQE 226
                       250       260
                ....*....|....*....|....*.
gi 71980965 806 IYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05060 227 IYSIMLSCWKYRPEDRPTFSELESTF 252
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
568-832 2.30e-71

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: 235.80  E-value: 2.30e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05041   1 EKIGRGNFGDVYRGVLK-----PDNTEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKvrvppadhdmggiTEANA----EFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd05041  76 PGGSLLTFLR-------------KKGARltvkQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCP 803
Cdd:cd05041 143 EEEDGEYTVSDGLKQIPIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCP 222
                       250       260
                ....*....|....*....|....*....
gi 71980965 804 TNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05041 223 EAVYRLMLQCWAYDPENRPSFSEIYNELQ 251
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
557-832 3.51e-70

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: 234.09  E-value: 3.51e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05061   1 WEVSREKITLLRELGQGSFGMVYEGNARDIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05061  81 GQPTLVVMELMAHGDLKSYLRSLRPEAENNPGRPPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKI 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05061 161 GDFGMTRDIYETDYYRKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYL 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05061 241 DQPDNCPERVTDLMRMCWQFNPKMRPTFLEIVNLLK 276
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
559-831 5.76e-70

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: 232.34  E-value: 5.76e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTSglfapePMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd05059   1 IDPSELTFLKELGSGQFGVVHLGKWRG------KIDVAIKMIKEGSMSED--DFIEEAKVMMKLSHPKLVQLYGVCTKQR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvrvppadhDMGGItEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05059  73 PIFIVTEYMANGCLLNYLR--------ERRGK-FQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRTSYgSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLEC 798
Cdd:cd05059 144 FGLARYVL-DDEYTSSVGTKFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYR 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 71980965 799 PHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05059 223 PHLAPTEVYTIMYSCWHEKPEERPTFKILLSQL 255
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
558-833 5.85e-70

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: 232.24  E-value: 5.85e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYtsglfapEPMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd05039   2 AINKKDLKLGELIGKGEFGDVMLGDY-------RGQKVAVKCLKDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLEG 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05039  73 NGLYIVTEYMAKGSLVDYLRSR--------GRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVS 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGLMR-TSYGSDYYKMlhrswmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05039 145 DFGLAKeASSNQDGGKL------PIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRM 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05039 219 EAPEGCPPEVYKVMKNCWELDPAKRPTFKQLREKLEH 255
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
568-831 2.36e-68

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: 227.55  E-value: 2.36e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfapepmAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05034   1 KKLGAGQFGEVWMGVWNGTT------KVAVKTLKPGTMSPE--AFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtSYG 727
Cdd:cd05034  73 SKGSLLDYLR--------TGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLAR-LIE 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:cd05034 144 DDEYTAREGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELY 223
                       250       260
                ....*....|....*....|....
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05034 224 DIMLQCWKKEPEERPTFEYLQSFL 247
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
570-831 1.77e-67

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 225.11  E-value: 1.77e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepmaVAVKKCRHDATNAERAQ-LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd13999   1 IGSGSFGEVYKGKWRGTD-------VAIKKLKVEDDNDELLKeFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMP 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKVRVPPadhdmggITEANAefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGS 728
Cdd:cd13999  74 GGSLYDLLHKKKIP-------LSWSLR--LKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNST 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 729 DYYKMLHRSWmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHL-LECPHNCPTNIY 807
Cdd:cd13999 145 TEKMTGVVGT--PRWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAAAVVQKGLrPPIPPDCPPELS 221
                       250       260
                ....*....|....*....|....
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd13999 222 KLIKRCWNEDPEKRPSFSEIVKRL 245
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
559-832 1.94e-66

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: 223.02  E-value: 1.94e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTsgLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd05033   1 IDASYVTIEKVIGGGEFGEVCSGSLK--LPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKSR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKVrvppadHDMGGITEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05033  79 PVMIVTEYMENGSLDKFLRE------NDGKFTVTQLVGMLR---GIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRTSYGSD--YYKMLHRSwmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05033 150 FGLSRRLEDSEatYTTKGGKI--PIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRL 227
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05033 228 PPPMDCPSALYQLMLDCWQKDRNERPTFSQIVSTLD 263
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
557-827 3.37e-66

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: 224.07  E-value: 3.37e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFG-VVHSGIYTSGLFAPE-PMAVAVKKCRHDATNAERAQLEQEIRAVATFD-HPNVIKLIGV 633
Cdd:cd05099   7 WEFPRDRLVLGKPLGEGCFGqVVRAEAYGIDKSRPDqTVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNIINLLGV 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYI------ATQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd05099  87 CTQEGPLYVIVEYAAKGNLREFLRARRPPGPDYTFDITKVPEEQLSFkdlvscAYQVARGMEYLESRRCIHRDLAARNVL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 708 VGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVI 787
Cdd:cd05099 167 VTEDNVMKIADFGLARGVHDIDYYKKTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGIPVEELF 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 788 ELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05099 247 KLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQL 286
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
568-831 5.57e-66

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: 221.45  E-value: 5.57e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfAPEPMAVAVKKCRHDATNAERAQLE--QEIRAVATFDHPNVIKLIGVCyMDNSLLAVFE 645
Cdd:cd05040   1 EKLGDGSFGVVRRGEWTTP--SGKVIQVAVKCLKSDVLSQPNAMDDflKEVNAMHSLDHPNLIRLYGVV-LSSPLMMVTE 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLkvrvppadHDMGGITEANAEFLYiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT- 724
Cdd:cd05040  78 LAPLGSLLDRL--------RKDQGHFLISTLCDY-AVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRAl 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 725 SYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELV-ANRHLLECPHNCP 803
Cdd:cd05040 149 PQNEDHYVMQEHRKVPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIdKEGERLERPDDCP 228
                       250       260
                ....*....|....*....|....*...
gi 71980965 804 TNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05040 229 QDIYNVMLQCWAHKPADRPTFVALRDFL 256
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
557-832 8.36e-66

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: 221.14  E-value: 8.36e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAE----RAQLEQEIRavatfdHPNVIKLIG 632
Cdd:cd05052   1 WEIERTDITMKHKLGGGQYGEVYEGVWKK-----YNLTVAVKTLKEDTMEVEeflkEAAVMKEIK------HPNLVQLLG 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDLHELLKVRVPpadHDMGGITeanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:cd05052  70 VCTREPPFYIITEFMPYGNLLDYLRECNR---EELNAVV-----LLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENH 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 713 TIKIADFGLMRTSYGsDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVAN 792
Cdd:cd05052 142 LVKVADFGLSRLMTG-DTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEK 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 793 RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05052 221 GYRMERPEGCPPKVYELMRACWQWNPSDRPSFAEIHQALE 260
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
558-834 8.39e-66

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: 221.13  E-value: 8.39e-66
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTSglfapePMAVAVKKCRHDATNAE----RAQLEQEIRavatfdHPNVIKLIGV 633
Cdd:cd05068   4 EIDRKSLKLLRKLGSGQFGEVWEGLWNN------TTPVAVKTLKPGTMDPEdflrEAQIMKKLR------HPKLIQLYAV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSLLAVFEYMVHGDLHELLkvrvppadHDMGGITEAnAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd05068  72 CTLEEPIYIITELMKHGSLLEYL--------QGKGRSLQL-PQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNI 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANR 793
Cdd:cd05068 143 CKVADFGLARVIKVEDEYEAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERG 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05068 223 YRMPCPPNCPPQLYDIMLECWKADPMERPTFETLQWKLEDF 263
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
566-841 1.55e-65

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: 221.45  E-value: 1.55e-65
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRhDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd05093   9 LKRELGEGAFGKVFLAECYNLCPEQDKILVAVKTLK-DASDNARKDFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRVPPA--DHDMGGITE-ANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd05093  88 YMKHGDLNKFLRAHGPDAvlMAEGNRPAElTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMS 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 723 RTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNC 802
Cdd:cd05093 168 RDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRVLQRPRTC 247
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 803 PTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASPAH 841
Cdd:cd05093 248 PKEVYDLMLGCWQREPHMRLNIKEIHSLLQNLAKASPVY 286
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
566-839 7.89e-64

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: 216.80  E-value: 7.89e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRhDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd05094   9 LKRELGEGAFGKVFLAECYNLSPTKDKMLVAVKTLK-DPTLAARKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFE 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRVPPADHDMGGIT-EANAEF-----LYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd05094  88 YMKHGDLNKFLRAHGPDAMILVDGQPrQAKGELglsqmLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDF 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECP 799
Cdd:cd05094 168 GMSRDVYSTDYYRVGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQGRVLERP 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 800 HNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASP 839
Cdd:cd05094 248 RVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHALGKATP 287
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
570-831 2.30e-63

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: 215.02  E-value: 2.30e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH----SGIYTSGLFAPepmaVAVKKCRHdaTNAERAQLE--QEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd05046  13 LGRGEFGEVFlakaKGIEEEGGETL----VLVKALQK--TKDENLQSEfrRELDMFRKLSHKNVVRLLGLCREAEPHYMI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVRvPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd05046  87 LEYTDLGDLKQFLRAT-KSKDEKLKPPPLSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSK 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKmLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHL-LECPHNC 802
Cdd:cd05046 166 DVYNSEYYK-LRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGKLeLPVPEGC 244
                       250       260
                ....*....|....*....|....*....
gi 71980965 803 PTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05046 245 PSRLYKLMTRCWAVNPKDRPSFSELVSAL 273
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
569-827 9.52e-63

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: 213.40  E-value: 9.52e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSGLFAPEPMaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD--NSLLAVFEY 646
Cdd:cd05038  11 QLGEGHFGSVELCRYDPLGDNTGEQ-VAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCESPgrRSLRLIMEY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT-S 725
Cdd:cd05038  90 LPSGSLRDYLQRHRDQIDL---------KRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVlP 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASN--------------QQVIELVA 791
Cdd:cd05038 161 EDKEYYYVKEPGESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGDPSQSPPALflrmigiaqgqmivTRLLELLK 240
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71980965 792 NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05038 241 SGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDL 276
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
570-832 1.05e-62

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: 213.16  E-value: 1.05e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGlfAPEPMAVAVKKCRhdATNAERAQLEQEIRAVAT---FDHPNVIKLIGVCYMDNSL------ 640
Cdd:cd05035   7 LGEGEFGSVMEAQLKQD--DGSQLKVAVKTMK--VDIHTYSEIEEFLSEAACmkdFDHPNVMRLIGVCFTASDLnkppsp 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHGDLHE-LLKVRvppadhdmggiTEANAEFLYIAT------QIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd05035  83 MVILPFMKHGDLHSyLLYSR-----------LGGLPEKLPLQTllkfmvDIAKGMEYLSNRNFIHRDLAARNCMLDENMT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANR 793
Cdd:cd05035 152 VCVADFGLSRKIYSGDYYRQGRISKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNG 231
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05035 232 NRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLE 270
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
559-831 1.43e-62

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: 212.12  E-value: 1.43e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTsglfapEPMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd05112   1 IDPSELTFVQEIGSGQFGLVHLGYWL------NKDKVAIKTIREGAMSEE--DFIEEAEVMMKLSHPKLVQLYGVCLEQA 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05112  73 PICLVFEFMEHGCLSDYLRTQ--------RGLFSAET-LLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRTSYgSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLEC 798
Cdd:cd05112 144 FGMTRFVL-DDQYTSSTGTKFPVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYK 222
                       250       260       270
                ....*....|....*....|....*....|...
gi 71980965 799 PHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05112 223 PRLASTHVYEIMNHCWKERPEDRPSFSLLLRQL 255
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
568-832 1.80e-62

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: 211.71  E-value: 1.80e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05084   2 ERIGRGNFGEVFSGRLRA-----DNTPVAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRvppadhdmgGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd05084  77 QGGDFLTFLRTE---------GPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEED 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:cd05084 148 GVYAATGGMKQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVY 227
                       250       260
                ....*....|....*....|....*
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05084 228 RLMEQCWEYDPRKRPSFSTVHQDLQ 252
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
557-833 1.24e-61

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: 209.60  E-value: 1.24e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSGLfapePMAVAVKKcRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05148   1 WERPREEFTLERKLGSGYFGEVWEGLWKNRV----RVAIKILK-SDDLLKQQ--DFQKEVQALKRLRHKHLISLFAVCSV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05148  74 GEPVYIITELMEKGSLLAFLR--------SPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05148 146 ADFGLARLIKEDVY--LSSDKKIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRM 223
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05148 224 PCPAKCPQEIYKIMLECWAAEPEDRPSFKALREELDN 260
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
557-832 2.38e-61

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: 209.50  E-value: 2.38e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIyTSGLFAPEPMA-VAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCY 635
Cdd:cd05062   1 WEVAREKITMSRELGQGSFGMVYEGI-AKGVVKDEPETrVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVS 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd05062  80 QGQPTLVIMELMTRGDLKSYLRSLRPEMENNPVQAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHL 795
Cdd:cd05062 160 IGDFGMTRDIYETDYYRKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGL 239
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 796 LECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05062 240 LDKPDNCPDMLFELMRMCWQYNPKMRPSFLEIISSIK 276
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
568-833 3.32e-60

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: 205.79  E-value: 3.32e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSL-LAVFEY 646
Cdd:cd05058   1 EVIGKGHFGCVYHGTLIDS--DGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSpLVVLPY 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELlkVRVP---PADHDMGGIteanaeflyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd05058  79 MKHGDLRNF--IRSEthnPTVKDLIGF----------GLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLAR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKML--HRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQV-IELVANRHLLEcPH 800
Cdd:cd05058 147 DIYDKEYYSVHnhTGAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDItVYLLQGRRLLQ-PE 225
                       250       260       270
                ....*....|....*....|....*....|...
gi 71980965 801 NCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05058 226 YCPDPLYEVMLSCWHPKPEMRPTFSELVSRISQ 258
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
568-833 3.34e-60

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: 205.24  E-value: 3.34e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTsglfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05085   2 ELLGKGNFGEVYKGTLK------DKTPVAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADhdmggiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd05085  76 PGGDFLSFLRKKKDELK---------TKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSwMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIY 807
Cdd:cd05085 147 GVYSSSGLKQ-IPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIY 225
                       250       260
                ....*....|....*....|....*.
gi 71980965 808 SLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05085 226 KIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
563-832 6.68e-60

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: 205.97  E-value: 6.68e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd05045   1 NLVLGKTLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKV--RVPPADHDMGGITEANAEF------------LYIATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd05045  81 IVEYAKYGSLRSFLREsrKVGPSYLGSDGNRNSSYLDnpderaltmgdlISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 GDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIE 788
Cdd:cd05045 161 AEGRKMKISDFGLSRDVYEEDSYVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLFN 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71980965 789 LVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05045 241 LLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELE 284
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
563-839 1.60e-59

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: 204.47  E-value: 1.60e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSGLFApepMAVAVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDN--- 638
Cdd:cd05075   1 KLALGKTLGEGEFGSVMEGQLNQDDSV---LKVAVKTMKiAICTRSEMEDFLSEAVCMKEFDHPNVMRLIGVCLQNTese 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 ---SLLAVFEYMVHGDLHE-LLKVRVppADHDMGGITEANAEFLyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd05075  78 gypSPVVILPFMKHGDLHSfLLYSRL--GDCPVYLPTQMLVKFM---TDIASGMEYLSSKNFIHRDLAARNCMLNENMNV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRH 794
Cdd:cd05075 153 CVADFGLSKKIYNGDYYRQGRISKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGN 232
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 71980965 795 LLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASP 839
Cdd:cd05075 233 RLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDLP 277
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
564-839 3.25e-59

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: 203.63  E-value: 3.25e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHSGiytsGLFAPE--PMAVAVKKCRHDatNAERAQLEQ---EIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd14204   9 LSLGKVLGEGEFGSVMEG----ELQQPDgtNHKVAVKTMKLD--NFSQREIEEflsEAACMKDFNHPNVIRLLGVCLEVG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SL-----LAVFEYMVHGDLHE-LLKVRvppadHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:cd14204  83 SQripkpMVILPFMKYGDLHSfLLRSR-----LGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDM 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 713 TIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVAN 792
Cdd:cd14204 158 TVCVADFGLSKKIYSGDYYRQGRIAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLH 237
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 71980965 793 RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASP 839
Cdd:cd14204 238 GHRLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESLP 284
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
557-827 6.89e-59

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: 204.48  E-value: 6.89e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFG--VVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGV 633
Cdd:cd05100   7 WELSRTRLTLGKPLGEGCFGqvVMAEAIGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNIINLLGA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSLLAVFEYMVHGDLHELLKVRVPPA---DHDMGGITEANAEF---LYIATQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd05100  87 CTQDGPLYVLVEYASKGNLREYLRARRPPGmdySFDTCKLPEEQLTFkdlVSCAYQVARGMEYLASQKCIHRDLAARNVL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 708 VGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVI 787
Cdd:cd05100 167 VTEDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELF 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 788 ELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05100 247 KLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQL 286
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
557-827 1.46e-58

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: 202.94  E-value: 1.46e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFG--VVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGV 633
Cdd:cd05101  19 WEFPRDKLTLGKPLGEGCFGqvVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGA 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSLLAVFEYMVHGDLHELLKVRVPPA---DHDMGGITEANAEFLYIAT---QIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd05101  99 CTQDGPLYVIVEYASKGNLREYLRARRPPGmeySYDINRVPEEQMTFKDLVSctyQLARGMEYLASQKCIHRDLAARNVL 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 708 VGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVI 787
Cdd:cd05101 179 VTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELF 258
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 788 ELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05101 259 KLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQL 298
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
562-832 3.62e-58

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: 199.71  E-value: 3.62e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCrhDATnaERAQLEqEIRAVATFDHPNVIKLIGVCyMDNSLL 641
Cdd:cd05083   6 QKLTLGEIIGEGEFGAVLQGEYMG-----QKVAVKNIKC--DVT--AQAFLE-ETAVMTKLQHKNLVRLLGVI-LHNGLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVR----VPPAdhdmggiteanaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05083  75 IVMELMSKGNLVNFLRSRgralVPVI------------QLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKIS 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGLMRTSYgsdyyKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLE 797
Cdd:cd05083 143 DFGLAKVGS-----MGVDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRME 217
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71980965 798 CPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05083 218 PPEGCPPDVYSIMTSCWEAEPGKRPSFKKLREKLE 252
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
562-827 1.05e-57

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: 199.56  E-value: 1.05e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYTsglfaPE----PMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCyMD 637
Cdd:cd05057   7 TELEKGKVLGSGAFGTVYKGVWI-----PEgekvKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGIC-LS 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKvrvppaDHDmggiTEANAE-FLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05057  81 SQVQLITQLMPLGCLLDYVR------NHR----DNIGSQlLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRT-SYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHL 795
Cdd:cd05057 151 TDFGLAKLlDVDEKEYHA-EGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGER 229
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 796 LECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05057 230 LPQPPICTIDVYMVLVKCWMIDAESRPTFKEL 261
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
557-827 3.17e-57

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: 199.08  E-value: 3.17e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGiYTSGLFAPEP---MAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIG 632
Cdd:cd05098   8 WELPRDRLVLGKPLGEGCFGQVVLA-EAIGLDKDKPnrvTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNIINLLG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYI------ATQIALGMEYLASMSFVHRDLATRNC 706
Cdd:cd05098  87 ACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPSHNPEEQLSSkdlvscAYQVARGMEYLASKKCIHRDLAARNV 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 707 LVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQV 786
Cdd:cd05098 167 LVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEEL 246
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 787 IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05098 247 FKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQL 287
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
558-832 6.32e-56

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: 194.04  E-value: 6.32e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIY-TSGlfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05063   1 EIHPSHITKQKVIGAGEFGEVFRGILkMPG---RKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKvrvppaDHDmGGITeaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05063  78 FKPAMIITEYMENGALDKYLR------DHD-GEFS--SYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKV 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRT-------SYGSDYYKMlhrswmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIEL 789
Cdd:cd05063 149 SDFGLSRVleddpegTYTTSGGKI------PIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKA 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 790 VANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05063 223 INDGFRLPAPMDCPSAVYQLMLQCWQQDRARRPRFVDIVNLLD 265
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
559-832 1.26e-55

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: 193.98  E-value: 1.26e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTS--GLFapepMAVAVKKCRHDATNAerAQLEQEIRAVA---TFDHPNVIKLIGV 633
Cdd:cd05074   6 IQEQQFTLGRMLGKGEFGSVREAQLKSedGSF----QKVAVKMLKADIFSS--SDIEEFLREAAcmkEFDHPNVIKLIGV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNSL------LAVFEYMVHGDLHE-LLKVRVPPADhdmggITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNC 706
Cdd:cd05074  80 SLRSRAKgrlpipMVILPFMKHGDLHTfLLMSRIGEEP-----FTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNC 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 707 LVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQV 786
Cdd:cd05074 155 MLNENMTVCVADFGLSKKIYSGDYYRQGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEI 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 787 IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05074 235 YNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLE 280
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
559-827 3.00e-55

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: 192.00  E-value: 3.00e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTSglfapePMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd05114   1 INPSELTFMKELGSGLFGVVRLGKWRA------QYKVAIKAIREGAMSEE--DFIEEAKVMMKLTHPKLVQLYGVCTQQK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKVRVPPADHDMggiteanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05114  73 PIYIVTEFMENGCLLNYLRQRRGKLSRDM---------LLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRTSYgSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLEC 798
Cdd:cd05114 144 FGMTRYVL-DDQYTSSSGAKFPVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYR 222
                       250       260
                ....*....|....*....|....*....
gi 71980965 799 PHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05114 223 PKLASKSVYEVMYSCWHEKPEGRPTFADL 251
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
559-831 3.63e-54

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: 189.31  E-value: 3.63e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTsgLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd05066   1 IDASCIKIEKVIGAGEFGEVCSGRLK--LPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSK 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvrvppaDHDmGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05066  79 PVMIVTEYMENGSLDAFLR------KHD-GQFTVI--QLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSD 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRT-------SYGSDYYKMlhrswmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVA 791
Cdd:cd05066 150 FGLSRVleddpeaAYTTRGGKI------PIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIE 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 792 NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05066 224 EGYRLPAPMDCPAALHQLMLDCWQKDRNERPKFEQIVSIL 263
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
563-832 1.01e-53

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: 187.50  E-value: 1.01e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapepMAVAVKKCRHDATnaerAQ-LEQEIRAVATFDHPNVIKLIGVCYMDN-SL 640
Cdd:cd05082   7 ELKLLQTIGKGEFGDVMLGDYRG-------NKVAVKCIKNDAT----AQaFLAEASVMTQLRHSNLVQLLGVIVEEKgGL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd05082  76 YIVTEYMAKGSLVDYLRSR--------GRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMR-TSYGSDYYKMlhrswmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECP 799
Cdd:cd05082 148 LTKeASSTQDTGKL------PVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAP 221
                       250       260       270
                ....*....|....*....|....*....|...
gi 71980965 800 HNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05082 222 DGCPPAVYDVMKNCWHLDAAMRPSFLQLREQLE 254
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
559-832 1.34e-52

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: 184.31  E-value: 1.34e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGIYTSglfapePMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd05113   1 IDPKDLTFLKELGTGQFGVVKYGKWRG------QYDVAIKMIKEGSMSED--EFIEEAKVMMNLSHEKLVQLYGVCTKQR 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvrvppadhdMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05113  73 PIFIITEYMANGCLLNYLR---------EMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRTSYGSDYYKMLHrSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLEC 798
Cdd:cd05113 144 FGLSRYVLDDEYTSSVG-SKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYR 222
                       250       260       270
                ....*....|....*....|....*....|....
gi 71980965 799 PHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05113 223 PHLASEKVYTIMYSCWHEKADERPTFKILLSNIL 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
569-834 2.51e-52

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: 183.63  E-value: 2.51e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSGLFAPepmAVAVKKCRHDATN-AERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLaVFEYM 647
Cdd:cd05116   2 ELGSGNFGTVKKGYYQMKKVVK---TVAVKILKNEANDpALKDELLREANVMQQLDNPYIVRMIGICEAESWML-VMEMA 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDmggITEanaeflyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtSYG 727
Cdd:cd05116  78 ELGPLNKFLQKNRHVTEKN---ITE-------LVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSK-ALR 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SD--YYK-MLHRSWmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPT 804
Cdd:cd05116 147 ADenYYKaQTHGKW-PVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPP 225
                       250       260       270
                ....*....|....*....|....*....|
gi 71980965 805 NIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05116 226 EMYDLMKLCWTYDVDERPGFAAVELRLRNY 255
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
559-831 1.43e-51

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: 181.99  E-value: 1.43e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHSGiytsGLFAP--EPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05065   1 IDVSCVKIEEVIGAGEFGEVCRG----RLKLPgkREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRvppaDHDMGGIteanaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05065  77 SRPVMIITEFMENGALDSFLRQN----DGQFTVI-----QLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMR----TSYGSDYYKMLHRSwMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVAN 792
Cdd:cd05065 148 SDFGLSRfledDTSDPTYTSSLGGK-IPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQ 226
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 793 RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05065 227 DYRLPPPMDCPTALHQLMLDCWQKDRNLRPKFGQIVNTL 265
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
558-831 4.43e-51

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: 180.50  E-value: 4.43e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTsgLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd05064   1 ELDNKSIKIERILGTGRFGELCRGCLK--LPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRG 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKvrvppaDHDmGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05064  79 NTMMIVTEYMSNGALDSFLR------KHE-GQLVAG--QLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKIS 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFG-LMRTSYGSDYYKMLHRSwmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05064 150 GFRrLQEDKSEAIYTTMSGKS--PVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRL 227
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05064 228 PAPRNCPNLLHQLMLDCWQKERGERPRFSQIHSIL 262
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
569-837 4.81e-51

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: 180.53  E-value: 4.81e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTsglFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNsLLAVFEYMV 648
Cdd:cd05115  11 ELGSGNFGCVKKGVYK---MRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEA-LMLVMEMAS 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKvrvppADHDMggITEAN-AEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtSYG 727
Cdd:cd05115  87 GGPLNKFLS-----GKKDE--ITVSNvVELMH---QVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSK-ALG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SD--YYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTN 805
Cdd:cd05115 156 ADdsYYKARSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPE 235
                       250       260       270
                ....*....|....*....|....*....|....
gi 71980965 806 IYSLMVECWHENIERRPTFSEIRSRLQS--WSLA 837
Cdd:cd05115 236 MYALMSDCWIYKWEDRPNFLTVEQRMRTyyYSIA 269
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
570-831 5.93e-51

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: 180.24  E-value: 5.93e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFG-VVHSGIYTSGLfapePMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05047   3 IGEGNFGqVLKARIKKDGL----RMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGYLYLAIEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELL-KVRVPPADHDMG-----GITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd05047  79 PHGNLLDFLrKSRVLETDPAFAianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRtsyGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHN 801
Cdd:cd05047 159 SR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLN 235
                       250       260       270
                ....*....|....*....|....*....|
gi 71980965 802 CPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05047 236 CDDEVYDLMRQCWREKPYERPSFAQILVSL 265
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
557-837 6.05e-51

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: 180.08  E-value: 6.05e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSGlfapepMAVAVKKCRhDATNAERAQLeQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05067   2 WEVPRETLKLVERLGAGQFGEVWMGYYNGH------TKVAIKSLK-QGSMSPDAFL-AEANLMKQLQHQRLVRLYAVVTQ 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DnSLLAVFEYMVHGDLHELLKVrvpPADHDMggiteANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05067  74 E-PIYIITEYMENGSLVDFLKT---PSGIKL-----TINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKI 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05067 145 ADFGLARLIEDNEYTAR-EGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRM 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLA 837
Cdd:cd05067 224 PRPDNCPEELYQLMRLCWKERPEDRPTFEYLRSVLEDFFTA 264
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
566-827 6.10e-51

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 179.65  E-value: 6.10e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    566 VREKIGEGQFGVVHSGIYT-SGLFapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:smart00220   3 ILEKLGEGSFGKVYLARDKkTGKL------VAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVM 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    645 EYMVHGDLHELLKvrvppadhDMGGITEANAefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL--- 721
Cdd:smart00220  77 EYCEGGDLFDLLK--------KRGRLSEDEA--RFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLarq 146
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    722 -----MRTSY-GSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVI-ELVANRH 794
Cdd:smart00220 147 ldpgeKLTTFvGTPEY------------MAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELfKKIGKPK 213
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 71980965    795 --LLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:smart00220 214 ppFPPPEWDISPEAKDLIRKLLVKDPEKRLTAEEA 248
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
570-831 5.87e-49

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 172.45  E-value: 5.87e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd00180   1 LGKGSFGKVYKARDKE-----TGKKVAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKVRvppadhdMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSD 729
Cdd:cd00180  76 GSLKDLLKEN-------KGPLSEE--EALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 730 YYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIwsfgrqpyegasnqqvielvanrhllecphncpTNIYSL 809
Cdd:cd00180 147 SLLKTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDL 193
                       250       260
                ....*....|....*....|..
gi 71980965 810 MVECWHENIERRPTFSEIRSRL 831
Cdd:cd00180 194 IRRMLQYDPKKRPSAKELLEHL 215
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
547-833 1.11e-48

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: 174.98  E-value: 1.11e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 547 EPIDDNSYkvFEITPSQLSVREK-------------IGEGQFG-VVHSGIYtsGLFAPEP-MAVAVKKCRHDATNAERAQ 611
Cdd:cd05055   9 ESINGNEY--VYIDPTQLPYDLKwefprnnlsfgktLGAGAFGkVVEATAY--GLSKSDAvMKVAVKMLKPTAHSSEREA 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 612 LEQEIRAVATF-DHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadhdmggiTEANAEF---LYIATQIALG 687
Cdd:cd05055  85 LMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYCCYGDLLNFLRRK-----------RESFLTLedlLSFSYQVAKG 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 688 MEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTL 767
Cdd:cd05055 154 MAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILL 233
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 768 WEIWSFGRQPYEGAS-NQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05055 234 WEIFSLGSNPYPGMPvDSKFYKLIKEGYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQIVQLIGK 300
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
563-832 1.66e-48

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: 173.66  E-value: 1.66e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYtsglfapEPM------AVAVKKCRHdATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd14205   5 HLKFLQQLGKGNFGSVEMCRY-------DPLqdntgeVVAVKKLQH-STEEHLRDFEREIEILKSLQHDNIVKYKGVCYS 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 --DNSLLAVFEYMVHGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd14205  77 agRRNLRLIMEYLPYGSLRDYLQKHKERIDH---------IKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGLMRT-SYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWS-----------FGRQPYEGAS 782
Cdd:cd14205 148 KIGDFGLTKVlPQDKEYYKVKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTyieksksppaeFMRMIGNDKQ 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 783 NQQV----IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14205 228 GQMIvfhlIELLKNNGRLPRPDGCPDEIYMIMTECWNNNVNQRPSFRDLALRVD 281
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
557-838 4.65e-48

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: 172.15  E-value: 4.65e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSGlfapepMAVAVKKCRhDATNAERAQLEqEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05072   2 WEIPRESIKLVKKLGAGQFGEVWMGYYNNS------TKVAVKTLK-PGTMSVQAFLE-EANLMKTLQHDKLVRLYAVVTK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKvrvppadHDMGGITEAnAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05072  74 EEPIYIITEYMAKGSLLDFLK-------SDEGGKVLL-PKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKI 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTsYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05072 146 ADFGLARV-IEDNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRM 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLAS 838
Cdd:cd05072 225 PRMENCPDELYDIMKTCWKEKAEERPTFDYLQSVLDDFYTAT 266
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
559-832 2.05e-47

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: 170.32  E-value: 2.05e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREK--IGEGQFGVVHSGIYTSGLFAPEPmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05043   1 IAVSRERVTLSdlLQEGTFGRIFHGILRDEKGKEEE--VLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIE 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSL-LAVFEYMVHGDLHELL-KVRVPPADhdmGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd05043  79 DGEKpMVLYPYMNWGNLKLFLqQCRLSEAN---NPQALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQV 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRH 794
Cdd:cd05043 156 KITDNALSRDLFPMDYHCLGDNENRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGY 235
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 71980965 795 LLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05043 236 RLAQPINCPDELFAVMACCWALDPEERPSFQQLVQCLT 273
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
570-841 2.31e-47

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: 170.95  E-value: 2.31e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFG-VVHSGIYTSGLfapePMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05089  10 IGEGNFGqVIKAMIKKDGL----KMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGACENRGYLYIAIEYA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELL-KVRVPPAD------HDMGGiTEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd05089  86 PYGNLLDFLrKSRVLETDpafakeHGTAS-TLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFG 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRtsyGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPH 800
Cdd:cd05089 165 LSR---GEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRMEKPR 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 801 NCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLASPAH 841
Cdd:cd05089 242 NCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKAY 282
Pkinase pfam00069
Protein kinase domain;
568-827 5.06e-47

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 168.56  E-value: 5.06e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   568 EKIGEGQFGVVHSGI-YTSGLFapepmaVAVKKCRHD-ATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:pfam00069   5 EKLGSGSFGTVYKAKhRDTGKI------VAIKKIKKEkIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   646 YMVHGDLHELLKVRvppadhdmGGITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR-T 724
Cdd:pfam00069  79 YVEGGSLFDLLSEK--------GAFSEREAKF--IMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFGLARqL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   725 SYGSDYYKMLHRSWmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVANR--HLLECPHNC 802
Cdd:pfam00069 149 NSGSSLTTFVGTPW----YMAPEVLGGNPYGPKVDVWSLGCILYELL-TGKPPFPGINGNEIYELIIDQpyAFPELPSNL 223
                         250       260
                  ....*....|....*....|....*
gi 71980965   803 PTNIYSLMVECWHENIERRPTFSEI 827
Cdd:pfam00069 224 SEEAKDLLKKLLKKDPSKRLTATEA 248
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
569-832 1.32e-45

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: 164.32  E-value: 1.32e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSGlfapepMAVAVKKCRhDATNAERAQLEqEIRAVATFDHPNVIKLIGVCyMDNSLLAVFEYMV 648
Cdd:cd14203   2 KLGQGCFGEVWMGTWNGT------TKVAIKTLK-PGTMSPEAFLE-EAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTsYGS 728
Cdd:cd14203  73 KGSLLDFLK--------DGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARL-IED 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 729 DYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTNIYS 808
Cdd:cd14203 144 NEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHE 223
                       250       260
                ....*....|....*....|....
gi 71980965 809 LMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14203 224 LMCQCWRKDPEERPTFEYLQSFLE 247
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
570-833 1.69e-45

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: 164.10  E-value: 1.69e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepmaVAVKKCRHDATN---AERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14061   2 IGVGGFGKVYRGIWRGEE-------VAVKAARQDPDEdisVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELL-KVRVPPAdhdmggiteanaEFLYIATQIALGMEYL---ASMSFVHRDLATRNCLVGDT--------RTI 714
Cdd:cd14061  75 ARGGALNRVLaGRKIPPH------------VLVDWAIQIARGMNYLhneAPVPIIHRDLKSSNILILEAienedlenKTL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGLMRtsygsdyyKMLHRSWMPV----RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14061 143 KITDFGLAR--------EWHKTTRMSAagtyAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGV 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71980965 791 A-NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14061 214 AvNKLTLPIPSTCPEPFAQLMKDCWQPDPHDRPSFADILKQLEN 257
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
557-831 2.64e-45

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: 164.97  E-value: 2.64e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHS----GIYTSglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLI 631
Cdd:cd05054   2 WEFPRDRLKLGKPLGRGAFGKVIQasafGIDKS----ATCRTVAVKMLKEGATASEHKALMTELKILIHIgHHLNVVNLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 GVCYMDNS-LLAVFEYMVHGDLHELLKVR----VPPADHDMGGITEANAEFLYI------------ATQIALGMEYLASM 694
Cdd:cd05054  78 GACTKPGGpLMVIVEFCKFGNLSNYLRSKreefVPYRDKGARDVEEEEDDDELYkepltledlicySFQVARGMEFLASR 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 695 SFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFG 774
Cdd:cd05054 158 KCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLG 237
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965 775 RQPYEGAsnqQVIELVANR----HLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05054 238 ASPYPGV---QMDEEFCRRlkegTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKL 295
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
561-829 1.37e-44

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: 162.43  E-value: 1.37e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 561 PSQLSVREKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQLEQEIR----AVATFDHPNVIKLIGVCyM 636
Cdd:cd05111   6 ETELRKLKVLGSGVFGTVHKGIWI-----PEGDSIKIPVAIKVIQDRSGRQSFQAVTdhmlAIGSLDHAYIVRLLGIC-P 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRVPPADHDMggiteanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05111  80 GASLQLVTQLLPLGSLLDHVRQHRGSLGPQL---------LLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05111 151 ADFGVADLLYPDDKKYFYSEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERL 230
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71980965 797 ECPHNCPTNIYSLMVECW--HENIerRPTFSEIRS 829
Cdd:cd05111 231 AQPQICTIDVYMVMVKCWmiDENI--RPTFKELAN 263
CRD_TK_ROR_like cd07459
Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) ...
177-309 2.47e-44

Cysteine-rich domain of tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143568  Cd Length: 135  Bit Score: 156.40  E-value: 2.47e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 177 GDCVQYRGEACRQYLSNKFVMMTNESREEmyDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVC-ESDSNNQIV 255
Cdd:cd07459   1 GYCQPYRGSVCAKYLGNKSVYVTSKQTQE--DIEEQLSAAFTVISTSSDVSPKCQQYALPSLCYYAFPLCdEGSSTPKPR 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 256 SICKHDCDVIQNDECPSELALAAQHELVGdtPKALFPLCSRLSST-----SNCIPVMST 309
Cdd:cd07459  79 RICRDECELLENDLCKKEYAIAKRHPLIG--HQLLLPDCSSLPSPgspesSNCIRLGIP 135
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
562-827 3.06e-44

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: 162.09  E-value: 3.06e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFG-VVHSGIYTSGLfapePMAVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGVCYMDNS 639
Cdd:cd05088   7 NDIKFQDVIGEGNFGqVLKARIKKDGL----RMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELL-KVRVPPADHDMG-----GITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd05088  83 LYLAIEYAPHGNLLDFLrKSRVLETDPAFAianstASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRtsyGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANR 793
Cdd:cd05088 163 AKIADFGLSR---GQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQG 239
                       250       260       270
                ....*....|....*....|....*....|....
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05088 240 YRLEKPLNCDDEVYDLMRQCWREKPYERPSFAQI 273
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
564-833 3.12e-44

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: 161.61  E-value: 3.12e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHSGIYTSGLFAPEPMaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM--DNSLL 641
Cdd:cd05080   6 LKKIRDLGEGHFGKVSLYCYDPTNDGTGEM-VAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgGKSLQ 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLkvrvppADHDMGgiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd05080  85 LIMEYVPLGSLRDYL------PKHSIG-----LAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGL 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MR-TSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGR-------------QPYEGASNQ-QV 786
Cdd:cd05080 154 AKaVPEGHEYYRVREDGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCDssqspptkflemiGIAQGQMTVvRL 233
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 71980965 787 IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05080 234 IELLERGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKT 280
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
556-838 5.24e-44

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: 160.62  E-value: 5.24e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 556 VFEITPSQLSVREKIGEGQFGVVHSGIYTSGlfapepMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCy 635
Cdd:cd05070   3 VWEIPRESLQLIKRLGNGQFGEVWMGTWNGN------TKVAIKTLKPGTMSPE--SFLEEAQIMKKLKHDKLVQLYAVV- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd05070  74 SEEPIYIVTEYMSKGSLLDFLK--------DGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHL 795
Cdd:cd05070 146 IADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYR 224
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 796 LECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLAS 838
Cdd:cd05070 225 MPCPQDCPISLHELMIHCWKKDPEERPTFEYLQGFLEDYFTAT 267
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
570-831 7.59e-44

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: 160.19  E-value: 7.59e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglfAPE----PMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCyMDNSLLAVFE 645
Cdd:cd05109  15 LGSGAFGTVYKGIW-----IPDgenvKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGIC-LTSTVQLVTQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKvrvppADHDMGGiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR-- 723
Cdd:cd05109  89 LMPYGCLLDYVR-----ENKDRIG----SQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARll 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 ----TSYGSDYYKMlhrswmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECP 799
Cdd:cd05109 160 dideTEYHADGGKV------PIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQP 233
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 800 HNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05109 234 PICTIDVYMIMVKCWMIDSECRPRFRELVDEF 265
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
562-850 1.54e-42

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: 157.54  E-value: 1.54e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYT-SGLFAPEPMAVAVKkcrhDATNAERAQLE--QEIRAVATFDHPNVIKLIGVCyMDN 638
Cdd:cd05110   7 TELKRVKVLGSGAFGTVYKGIWVpEGETVKIPVAIKIL----NETTGPKANVEfmDEALIMASMDHPHLVRLLGVC-LSP 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELlkvrVPPADHDMGgiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05110  82 TIQLVTQLMPHGCLLDY----VHEHKDNIG-----SQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITD 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLEC 798
Cdd:cd05110 153 FGLARLLEGDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQ 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 799 PHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSlASPAHSILQQHNNR 850
Cdd:cd05110 233 PPICTIDVYMVMVKCWMIDADSRPKFKELAAEFSRMA-RDPQRYLVIQGDDR 283
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
557-834 1.53e-41

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: 153.69  E-value: 1.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSglfapePMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCyM 636
Cdd:cd05071   4 WEIPRESLRLEVKLGQGCFGEVWMGTWNG------TTRVAIKTLKPGTMSPE--AFLQEAQVMKKLRHEKLVQLYAVV-S 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLK------VRVPpadhdmggiteanaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGD 710
Cdd:cd05071  75 EEPIYIVTEYMSKGSLLDFLKgemgkyLRLP--------------QLVDMAAQIASGMAYVERMNYVHRDLRAANILVGE 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 711 TRTIKIADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELV 790
Cdd:cd05071 141 NLVCKVADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQV 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71980965 791 ANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05071 220 ERGYRMPCPPECPESLHDLMCQCWRKEPEERPTFEYLQAFLEDY 263
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
563-833 2.81e-41

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: 152.49  E-value: 2.81e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSGLfapepmaVAVKKCRHD-----ATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd14147   4 ELRLEEVIGIGGFGKVYRGSWRGEL-------VAVKAARQDpdediSVTAE--SVRQEARLFAMLAHPNIIALKAVCLEE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLK-VRVPPadHDMggiteanaefLYIATQIALGMEYLASMSFV---HRDLATRNCL-----V 708
Cdd:cd14147  75 PNLCLVMEYAAGGPLSRALAgRRVPP--HVL----------VNWAVQIARGMHYLHCEALVpviHRDLKSNNILllqpiE 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 GDT---RTIKIADFGLMRtsygsDYYKMLHRSWMPV-RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ 784
Cdd:cd14147 143 NDDmehKTLKITDFGLAR-----EWHKTTQMSAAGTyAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCL 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 71980965 785 QVIELVA-NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14147 217 AVAYGVAvNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEA 266
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
568-833 3.53e-41

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


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 152.41  E-value: 3.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14206   3 QEIGNGWFGKVILGEIFSDY---TPAQVVVKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETIPFLLIMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd14206  80 QLGDLKRYLRAQRKADGMTPDLPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHNNYK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQ--GRF-----SEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVA-NRHL---- 795
Cdd:cd14206 160 EDYYLTPDRLWIPLRWVAPELLDElhGNLivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVVrEQQMklak 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 796 --LECPHNcpTNIYSLMVECWHENiERRPTFSEIRSRLQS 833
Cdd:cd14206 240 prLKLPYA--DYWYEIMQSCWLPP-SQRPSVEELHLQLSY 276
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
568-831 5.53e-41

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: 151.59  E-value: 5.53e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05042   1 QEIGNGWFGKVLLGEIYSGT---SVAQVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAIPYLLVMEFC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGITeanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd05042  78 DLGDLKAYLRSEREHERGDSDTRT-----LQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSRYK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIE--QGRF-----SEASDVWSFGVTLWEIWSFGRQPYEGASNQQVI-ELVANRHL---- 795
Cdd:cd05042 153 EDYIETDDKLWFPLRWTAPELVTefHDRLlvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLaQVVREQDTklpk 232
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 71980965 796 --LECPHNcpTNIYSLMVECWHENiERRPTFSEIRSRL 831
Cdd:cd05042 233 pqLELPYS--DRWYEVLQFCWLSP-EQRPAAEDVHLLL 267
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
570-827 9.50e-41

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: 152.48  E-value: 9.50e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGiytsgLFAPE----PMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCyMDNSLLAVFE 645
Cdd:cd05108  15 LGSGAFGTVYKG-----LWIPEgekvKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGIC-LTSTVQLITQ 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRvppaDHDMGGiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd05108  89 LMPFGCLLDYVREH----KDNIGS-----QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLL 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPHNCPTN 805
Cdd:cd05108 160 GAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTID 239
                       250       260
                ....*....|....*....|..
gi 71980965 806 IYSLMVECWHENIERRPTFSEI 827
Cdd:cd05108 240 VYMIMVKCWMIDADSRPKFREL 261
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
557-838 1.66e-40

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: 150.61  E-value: 1.66e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSglfapePMAVAVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCyM 636
Cdd:cd05069   7 WEIPRESLRLDVKLGQGCFGEVWMGTWNG------TTKVAIKTLKPGTMMPE--AFLQEAQIMKKLRHDKLVPLYAVV-S 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05069  78 EEPIYIVTEFMGKGSLLDFLK--------EGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKI 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05069 150 ADFGLARLIEDNEYTAR-QGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRM 228
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSLAS 838
Cdd:cd05069 229 PCPQGCPESLHELMKLCWKKDPDERPTFEYIQSFLEDYFTAT 270
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
570-832 4.00e-40

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: 149.66  E-value: 4.00e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglfapEPMA------VAVKKCRHDATNAERaQLEQEIRAVATFDHPNVIKLIGVCYMDN--SLL 641
Cdd:cd05081  12 LGKGNFGSVELCRY-------DPLGdntgalVAVKQLQHSGPDQQR-DFQREIQILKALHSDFIVKYRGVSYGPGrrSLR 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLkvrvPPADHDMGGITeanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd05081  84 LVMEYLPSGCLRDFL----QRHRARLDASR-----LLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRT-SYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSF---GRQPYE------GASNQQ-----V 786
Cdd:cd05081 155 AKLlPLDKDYYVVREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYcdkSCSPSAeflrmmGCERDVpalcrL 234
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 787 IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05081 235 LELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRPSFSALGPQLD 280
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
558-833 4.57e-40

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: 149.04  E-value: 4.57e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTSglfapepMAVAVKKCRHDATNAERAQLE---QEIRAVATFDHPNVIKLIGVC 634
Cdd:cd14145   2 EIDFSELVLEEIIGIGGFGKVYRAIWIG-------DEVAVKAARHDPDEDISQTIEnvrQEAKLFAMLKHPNIIALRGVC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 635 YMDNSLLAVFEYMVHGDLHELLK-VRVPPAdhdmggiteanaEFLYIATQIALGMEYL---ASMSFVHRDLATRNCLV-- 708
Cdd:cd14145  75 LKEPNLCLVMEFARGGPLNRVLSgKRIPPD------------ILVNWAVQIARGMNYLhceAIVPVIHRDLKSSNILIle 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 ----GD--TRTIKIADFGLMRtsygsDYYKMLHRSWM-PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGA 781
Cdd:cd14145 143 kvenGDlsNKILKITDFGLAR-----EWHRTTKMSAAgTYAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGI 216
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 782 SNQQVIELVA-NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14145 217 DGLAVAYGVAmNKLSLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTA 269
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
557-831 6.24e-40

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: 150.92  E-value: 6.24e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFG-VVHS---GIYTSglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHP-NVIKLI 631
Cdd:cd14207   2 WEFARERLKLGKSLGRGAFGkVVQAsafGIKKS----PTCRVVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 GVCYMDNS-LLAVFEYMVHGDLHELLKVR----VPPADHDMGG---------------------IT-------------- 671
Cdd:cd14207  78 GACTKSGGpLMVIVEYCKYGNLSNYLKSKrdffVTNKDTSLQEelikekkeaeptggkkkrlesVTssesfassgfqedk 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 672 ---------EANAEF----------LYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYK 732
Cdd:cd14207 158 slsdveeeeEDSGDFykrpltmedlISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYV 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 733 MLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGAsnqQVIELVANR----HLLECPHNCPTNIYS 808
Cdd:cd14207 238 RKGDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGV---QIDEDFCSKlkegIRMRAPEFATSEIYQ 314
                       330       340
                ....*....|....*....|...
gi 71980965 809 LMVECWHENIERRPTFSEIRSRL 831
Cdd:cd14207 315 IMLDCWQGDPNERPRFSELVERL 337
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
570-833 7.95e-40

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: 148.21  E-value: 7.95e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapepMAVAVKKCRHD-----ATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd14148   2 IGVGGFGKVYKGLWRG-------EEVAVKAARQDpdediAVTAE--NVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVM 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLK-VRVPPadHDMggiteanaefLYIATQIALGMEYLASMSFV---HRDLATRNCLVGD--------TR 712
Cdd:cd14148  73 EYARGGALNRALAgKKVPP--HVL----------VNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILEpienddlsGK 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 713 TIKIADFGLMRtsygsDYYKMLHRSWMPV-RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVA 791
Cdd:cd14148 141 TLKITDFGLAR-----EWHKTTKMSAAGTyAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVAYGVA 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 792 -NRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14148 215 mNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLED 257
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
557-834 1.19e-39

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: 147.87  E-value: 1.19e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTsglfapEPMAVAVKKCRHDATNAErAQLEqEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05073   6 WEIPRESLKLEKKLGAGQFGEVWMATYN------KHTKVAVKTMKPGSMSVE-AFLA-EANVMKTLQHDKLVKLHAVVTK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DnSLLAVFEYMVHGDLHELLKvrvppADHdmgGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05073  78 E-PIYIITEFMAKGSLLDFLK-----SDE---GSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLL 796
Cdd:cd05073 149 ADFGLARVIEDNEYTAR-EGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRM 227
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSW 834
Cdd:cd05073 228 PRPENCPEELYNIMMRCWKNRPEERPTFEYIQSVLDDF 265
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
547-832 1.42e-39

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: 150.77  E-value: 1.42e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 547 EPIDDNSYKVfeITPSQLSVREK-------------IGEGQFG-VVHSGIYTSGLfAPEPMAVAVKKCRHDATNAERAQL 612
Cdd:cd05106  12 EAAEGNNYTF--IDPTQLPYNEKwefprdnlqfgktLGAGAFGkVVEATAFGLGK-EDNVLRVAVKMLKASAHTDEREAL 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 613 EQEIRAVATF-DHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVR-------------VPPADHDMGGITEANA--- 675
Cdd:cd05106  89 MSELKILSHLgQHKNIVNLLGACTHGGPVLVITEYCCYGDLLNFLRKKaetflnfvmalpeISETSSDYKNITLEKKyir 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 676 --------------------------------------------EFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDT 711
Cdd:cd05106 169 sdsgfssqgsdtyvemrpvsssssqssdskdeedtedswpldldDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDG 248
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 712 RTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEG-ASNQQVIELV 790
Cdd:cd05106 249 RVAKICDFGLARDIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGiLVNSKFYKMV 328
                       330       340       350       360
                ....*....|....*....|....*....|....*....|..
gi 71980965 791 ANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05106 329 KRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFSQISQLIQ 370
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
570-831 1.46e-39

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: 146.49  E-value: 1.46e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepmaVAVKKCRHdatnaeraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd14059   1 LGSGAQGAVFLGKFRGEE-------VAVKKVRD--------EKETDIKHLRKLNHPNIIKFKGVCTQAPCYCILMEYCPY 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKVR--VPPAdhdmggiteanaefLYI--ATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtS 725
Cdd:cd14059  66 GQLYEVLRAGreITPS--------------LLVdwSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSK-E 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSwmPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHL-LECPHNCPT 804
Cdd:cd14059 131 LSEKSTKMSFAG--TVAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIWGVGSNSLqLPVPSTCPD 207
                       250       260
                ....*....|....*....|....*..
gi 71980965 805 NIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd14059 208 GFKLLMKQCWNSKPRNRPSFRQILMHL 234
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
570-833 1.67e-38

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: 144.41  E-value: 1.67e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglfapEPMAVAVKKCRHDATNAERAQLE---QEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14146   2 IGVGGFGKVYRATW-------KGQEVAVKAARQDPDEDIKATAEsvrQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKVrVPPADHDMGGITEANAEFLYIATQIALGMEYLASMSFV---HRDLATRNCLVGD--------TRTIK 715
Cdd:cd14146  75 ARGGTLNRALAA-ANAAPGPRRARRIPPHILVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEkiehddicNKTLK 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRtsygsDYYKMLHRSWMPV-RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVA-NR 793
Cdd:cd14146 154 ITDFGLAR-----EWHRTTKMSAAGTyAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAYGVAvNK 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14146 228 LTLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTA 267
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
557-827 2.71e-38

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: 146.28  E-value: 2.71e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFG-VVHSGIYtsGLFAPEPM-AVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGV 633
Cdd:cd05102   2 WEFPRDRLRLGKVLGHGAFGkVVEASAF--GIDKSSSCeTVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 CYMDNS-LLAVFEYMVHGDLHELLKV----------RVPPADHDMGGITEA----------------------------- 673
Cdd:cd05102  80 CTKPNGpLMVIVEFCKYGNLSNFLRAkregfspyreRSPRTRSQVRSMVEAvradrrsrqgsdrvasftestsstnqprq 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 674 NAEFLYIAT-----------QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVR 742
Cdd:cd05102 160 EVDDLWQSPltmedlicysfQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVRKGSARLPLK 239
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 743 WMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGAS-NQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERR 821
Cdd:cd05102 240 WMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKER 319

                ....*.
gi 71980965 822 PTFSEI 827
Cdd:cd05102 320 PTFSDL 325
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
570-827 6.64e-38

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: 143.53  E-value: 6.64e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTsglfaPEP----MAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD--NSLLAV 643
Cdd:cd05079  12 LGEGHFGKVELCRYD-----PEGdntgEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLI 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLkvrvpPADHDMGGITEanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd05079  87 MEFLPSGSLKEYL-----PRNKNKINLKQ----QLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTK 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 T-SYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYE---------GASNQQ-----VIE 788
Cdd:cd05079 158 AiETDKEYYTVKDDLDSPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCDSESSpmtlflkmiGPTHGQmtvtrLVR 237
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 789 LVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05079 238 VLEEGKRLPRPPNCPEEVYQLMRKCWEFQPSKRTTFQNL 276
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
544-832 1.15e-37

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: 145.43  E-value: 1.15e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 544 PSQEPIDDNsykvFEITPSQLSVREKIGEGQFG-VVHSGIYtsGLF-APEPMAVAVKKCRHDATNAERAQLEQEIRAVAT 621
Cdd:cd05104  21 PTQLPYDHK----WEFPRDRLRFGKTLGAGAFGkVVEATAY--GLAkADSAMTVAVKMLKPSAHSTEREALMSELKVLSY 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 622 F-DHPNVIKLIGVCYMDNSLLAVFEYMVHGDL-------------------------HELLKVRVPPADH-----DM--- 667
Cdd:cd05104  95 LgNHINIVNLLGACTVGGPTLVITEYCCYGDLlnflrrkrdsficpkfedlaeaalyRNLLHQREMACDSlneymDMkps 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 668 -----------------GGITEANAE---------------FLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd05104 175 vsyvvptkadkrrgvrsGSYVDQDVTseileedelaldtedLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITK 254
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGAS-NQQVIELVANRH 794
Cdd:cd05104 255 ICDFGLARDIRNDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPvDSKFYKMIKEGY 334
                       330       340       350
                ....*....|....*....|....*....|....*...
gi 71980965 795 LLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd05104 335 RMDSPEFAPSEMYDIMRSCWDADPLKRPTFKQIVQLIE 372
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
557-831 3.12e-37

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: 143.20  E-value: 3.12e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHS----GIYTSGlfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHP-NVIKLI 631
Cdd:cd05103   2 WEFPRDRLKLGKPLGRGAFGQVIEadafGIDKTA----TCRTVAVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 GVCYMDNS-LLAVFEYM-------------------------------VHGDLHELLKVRVPPADHDMGGIT-------- 671
Cdd:cd05103  78 GACTKPGGpLMVIVEFCkfgnlsaylrskrsefvpyktkgarfrqgkdYVGDISVDLKRRLDSITSSQSSASsgfveeks 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 672 -------EANAEFLY-----------IATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKM 733
Cdd:cd05103 158 lsdveeeEAGQEDLYkdfltledlicYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVR 237
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 734 LHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGAS-NQQVIELVANRHLLECPHNCPTNIYSLMVE 812
Cdd:cd05103 238 KGDARLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKiDEEFCRRLKEGTRMRAPDYTTPEMYQTMLD 317
                       330
                ....*....|....*....
gi 71980965 813 CWHENIERRPTFSEIRSRL 831
Cdd:cd05103 318 CWHGEPSQRPTFSELVEHL 336
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
570-827 4.46e-37

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: 139.88  E-value: 4.46e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapepMAVAVKKCRHDAtnaERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd14058   1 VGRGSFGVVCKARWRN-------QIVAVKIIESES---EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEG 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKVRVPPADHdmggiTEANAefLYIATQIALGMEYLASMS---FVHRDLATRNCLVGDTRT-IKIADFGL---- 721
Cdd:cd14058  71 GSLYNVLHGKEPKPIY-----TAAHA--MSWALQCAKGVAYLHSMKpkaLIHRDLKPPNLLLTNGGTvLKICDFGTacdi 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 ---MRTSYGSdyykmlhrswmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYE--GASNQQVIELVANRHLL 796
Cdd:cd14058 144 sthMTNNKGS------------AAWMAPEVFEGSKYSEKCDVFSWGIILWEVIT-RRKPFDhiGGPAFRIMWAVHNGERP 210
                       250       260       270
                ....*....|....*....|....*....|.
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd14058 211 PLIKNCPKPIESLMTRCWSKDPEKRPSMKEI 241
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
568-827 8.13e-37

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


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 139.74  E-value: 8.13e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLFAPEpmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05087   3 KEIGHGWFGKVFLGEVNSGLSSTQ---VVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEVTPYLLVMEFC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKvrvppADHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG 727
Cdd:cd05087  80 PLGDLKGYLR-----SCRAAESMAPDPLTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLSHCKYK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPVRWMSKEAIEQ--GRF-----SEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHLLECPH 800
Cdd:cd05087 155 EDYFVTADQLWVPLRWIAPELVDEvhGNLlvvdqTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTVREQQLKLPK 234
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 801 -----NCPTNIYSLMVECWHENiERRPTFSEI 827
Cdd:cd05087 235 pqlklSLAERWYEVMQFCWLQP-EQRPTAEEV 265
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
544-833 1.80e-36

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: 142.47  E-value: 1.80e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 544 PSQEPIDDNsykvFEITPSQLSVREKIGEGQFGVVHSGIyTSGLFAPEP-MAVAVKKCRHDATNAERAQLEQEIRAVATF 622
Cdd:cd05105  23 PMQLPYDSR----WEFPRDGLVLGRILGSGAFGKVVEGT-AYGLSRSQPvMKVAVKMLKPTARSSEKQALMSELKIMTHL 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 623 D-HPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELL----------KVRVPPADHDMGGITEANA---------------- 675
Cdd:cd05105  98 GpHLNIVNLLGACTKSGPIYIITEYCFYGDLVNYLhknrdnflsrHPEKPKKDLDIFGINPADEstrsyvilsfenkgdy 177
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 676 ------------------------------------------------------------EFLYIATQIALGMEYLASMS 695
Cdd:cd05105 178 mdmkqadttqyvpmleikeaskysdiqrsnydrpasykgsndsevknllsddgseglttlDLLSFTYQVARGMEFLASKN 257
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 696 FVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGR 775
Cdd:cd05105 258 CVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGG 337
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 776 QPYEGA-SNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd05105 338 TPYPGMiVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVES 396
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
544-827 1.11e-35

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: 140.15  E-value: 1.11e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 544 PSQEPIDDNsykvFEITPSQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFD 623
Cdd:cd05107  23 PMQLPYDSA----WEMPRDNLVLGRTLGSGAFGRVVEATAHGLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLG 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 624 -HPNVIKLIGVCYMDNSLLAVFEYMVHGDL----------------------HELLKVRVPPADH--------------- 665
Cdd:cd05107  99 pHLNIVNLLGACTKGGPIYIITEYCRYGDLvdylhrnkhtflqyyldknrddGSLISGGSTPLSQrkshvslgsesdggy 178
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 666 ---------------DMGG------ITEANAEFLY------------------------------IATQIALGMEYLASM 694
Cdd:cd05107 179 mdmskdesadyvpmqDMKGtvkyadIESSNYESPYdqylpsapertrrdtlinespalsymdlvgFSYQVANGMEFLASK 258
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 695 SFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFG 774
Cdd:cd05107 259 NCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLG 338
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 775 RQPY-EGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05107 339 GTPYpELPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQL 392
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
568-784 1.51e-34

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 132.64  E-value: 1.51e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYT-SGLFapepmaVAVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd06606   6 ELLGKGSFGSVYLALNLdTGEL------MAVKEVElSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKvrvppadhDMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd06606  80 YVPGGSLASLLK--------KFGKLPEPVVRKY--TRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 726 YGSDYYKMLHrsWM---PvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ 784
Cdd:cd06606 150 AEIATGEGTK--SLrgtP-YWMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNP 207
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
570-831 1.80e-34

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


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 132.58  E-value: 1.80e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepMAVAVKkCRHDATN--AERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd13978   1 LGSGGFGTVSKARHVSWF-----GMVAIK-CLHSSPNciEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYM 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGiteanaeflYIATQIALGMEYLASMS--FVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd13978  75 ENGSLKSLLEREIQDVPWSLRF---------RIIHEIALGMNFLHNMDppLLHHDLKPENILLDNHFHVKISDFGLSKLG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSdyYKMLHRSWMP-----VRWMSKEAIE--QGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVI---ELVANRHL 795
Cdd:cd13978 146 MKS--ISANRRRGTEnlggtPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLImqiVSKGDRPS 222
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 796 LE-----CPHNCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd13978 223 LDdigrlKQIENVQELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
566-833 3.21e-34

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: 131.94  E-value: 3.21e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTS-GLFapepmaVAVKKCRHDATNAE--RAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd14014   4 LVRLLGRGGMGEVYRARDTLlGRP------VAIKVLRPELAEDEefRERFLREARALARLSHPNIVRVYDVGEDDGRPYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRvppadhdmGGITEanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd14014  78 VMEYVEGGSLADLLRER--------GPLPP--REALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIA 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 723 R-----------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV- 790
Cdd:cd14014 148 RalgdsgltqtgSVLGTPAY------------MAPEQARGGPVDPRSDIYSLGVVLYELLT-GRPPFDGDSPAAVLAKHl 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 791 --ANRHLLECPHNCPTNIYSLMVECWHENIERRP-TFSEIRSRLQS 833
Cdd:cd14014 215 qeAPPPPSPLNPDVPPALDAIILRALAKDPEERPqSAAELLAALRA 260
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
571-833 5.34e-33

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: 127.77  E-value: 5.34e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 571 GEGQFGVVHSGIYTsglfaPEPMAVAVKKCRhdatnaeraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHG 650
Cdd:cd14060   2 GGGSFGSVYRAIWV-----SQDKEVAVKKLL---------KIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYG 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 651 DLHELLKVRvPPADHDMggiteanAEFLYIATQIALGMEYL---ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtsYG 727
Cdd:cd14060  68 SLFDYLNSN-ESEEMDM-------DQIMTWATDIAKGMHYLhmeAPVKVIHRDLKSRNVVIAADGVLKICDFGASR--FH 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 728 SDYYKMLHRSWMPvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfgRQ-PYEGASNQQVIELVANRH-LLECPHNCPTN 805
Cdd:cd14060 138 SHTTHMSLVGTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLT--REvPFKGLEGLQVAWLVVEKNeRPTIPSSCPRS 213
                       250       260
                ....*....|....*....|....*...
gi 71980965 806 IYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14060 214 FAELMRRCWEADVKERPSFKQIIGILES 241
KR smart00130
Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like ...
326-405 3.84e-32

Kringle domain; Named after a Danish pastry. Found in several serine proteases and in ROR-like receptors. Can occur in up to 38 copies (in apolipoprotein(a)). Plasminogen-like kringles possess affinity for free lysine and lysine- containing peptides.


Pssm-ID: 214527  Cd Length: 83  Bit Score: 119.80  E-value: 3.84e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    326 HWCYVNSGTQYEGTVAQTSSGKQCAPWIDSTS--RDFNVHRFPELMNSKNYCRNPGGKKSRPWCYSKPMGQE-EYCDVPQ 402
Cdd:smart00130   1 RECYAGNGESYRGTVSVTKSGKPCQRWDSQTPhlHRFTPESFPDLGLEENYCRNPDGDSEGPWCYTTDPNVRwEYCDIPQ 80

                   ...
gi 71980965    403 CPS 405
Cdd:smart00130  81 CEE 83
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
565-823 9.34e-32

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: 124.62  E-value: 9.34e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 565 SVREKIGEGQFGVVHSGIYTSGLFApepmaVAVKKCRHDaTNAERAQLEQEIRAVATFDHPNVIKLIGvCYM-DNSLLAV 643
Cdd:cd05122   3 EILEKIGKGGFGVVYKARHKKTGQI-----VAIKKINLE-SKEKKESILNEIAILKKCKHPNIVKYYG-SYLkKDELWIV 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVRvppadhdMGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-- 721
Cdd:cd05122  76 MEFCSGGSLKDLLKNT-------NKTLTEQQIA--YVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLsa 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 ------MRTS-YGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVANRH 794
Cdd:cd05122 147 qlsdgkTRNTfVGTPY------------WMAPEVIQGKPYGFKADIWSLGITAIEM-AEGKPPYSELPPMKALFLIATNG 213
                       250       260       270
                ....*....|....*....|....*....|.
gi 71980965 795 L--LECPHNCPTNIYSLMVECWHENIERRPT 823
Cdd:cd05122 214 PpgLRNPKKWSKEFKDFLKKCLQKDPEKRPT 244
KR cd00108
Kringle domain; Kringle domains are believed to play a role in binding mediators, such as ...
325-404 1.85e-31

Kringle domain; Kringle domains are believed to play a role in binding mediators, such as peptides, other proteins, membranes, or phospholipids. They are autonomous structural domains, found in a varying number of copies, in blood clotting and fibrinolytic proteins, some serine proteases and plasma proteins. Plasminogen-like kringles possess affinity for free lysine and lysine-containing peptides.


Pssm-ID: 238056  Cd Length: 83  Bit Score: 117.86  E-value: 1.85e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 325 THWCYVNSGTQYEGTVAQTSSGKQCAPWIDST--SRDFNVHRFPELMNSKNYCRNPGGKKSRPWCY-SKPMGQEEYCDVP 401
Cdd:cd00108   1 TRDCYWGNGESYRGTVSTTKSGKPCQRWNSQLphQHKFNPERFPEGLLEENYCRNPDGDPEGPWCYtTDPNVRWEYCDIP 80

                ...
gi 71980965 402 QCP 404
Cdd:cd00108  81 RCE 83
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
568-831 8.91e-31

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


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 122.28  E-value: 8.91e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFG-VVHSGIYTSGLFApepmAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd05086   3 QEIGNGWFGkVLLGEIYTGTSVA----RVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAIPYLLVFEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLhellKVRVPPADHDMGGITEAnAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSY 726
Cdd:cd05086  79 CDLGDL----KTYLANQQEKLRGDSQI-MLLQRMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIGFSRY 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 727 GSDYYKMLHRSWMPVRWMSKEAIE--QGRF-----SEASDVWSFGVTLWEIWSFGRQPYEGASNQQVI-ELVANRHL--- 795
Cdd:cd05086 154 KEDYIETDDKKYAPLRWTAPELVTsfQDGLlaaeqTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLnHVIKERQVklf 233
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 796 ---LECPHNcpTNIYSLMVECWHENiERRPTFSEIRSRL 831
Cdd:cd05086 234 kphLEQPYS--DRWYEVLQFCWLSP-EKRPTAEEVHRLL 269
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
568-829 1.64e-29

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 118.00  E-value: 1.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTsglfaPEPMAVAVKK-CRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14003   6 KTLGEGSFGKVKLARHK-----LTGEKVAIKIiDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKVRvppadhdmGGITEANAEFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL----- 721
Cdd:cd14003  81 ASGGELFDYIVNN--------GRLSEDEARRFFQ--QLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLsnefr 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 ----MRTSYGSDYYkmlhrswmpvrwMSKEAIE-QGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVANRHlL 796
Cdd:cd14003 151 ggslLKTFCGTPAY------------AAPEVLLgRKYDGPKADVWSLGVILYAM-LTGYLPFDDDNDSKLFRKILKGK-Y 216
                       250       260       270
                ....*....|....*....|....*....|...
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14003 217 PIPSHLSPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
570-836 1.80e-29

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: 118.38  E-value: 1.80e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFG----VVHSgiyTSGlfapepmAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14154   1 LGKGFFGqaikVTHR---ETG-------EVMVMKELIRFDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITE 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT- 724
Cdd:cd14154  71 YIPGGTLKDVLKDMARPLPW---------AQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLi 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 725 ------SYGSDYYKMLHRSWMPVR-----------WMSKEAIEQGRFSEASDVWSFGVTLWEIwsFGRQPYEGASNQQVI 787
Cdd:cd14154 142 veerlpSGNMSPSETLRHLKSPDRkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEI--IGRVEADPDYLPRTK 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 788 ELVANRHLLE---CPhNCPTNIYSLMVECWHENIERRPTFSEIRSRLQSWSL 836
Cdd:cd14154 220 DFGLNVDSFRekfCA-GCPPPFFKLAFLCCDLDPEKRPPFETLEEWLEALYL 270
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
562-827 1.43e-28

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: 115.92  E-value: 1.43e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYtsglfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06610   1 DDYELIEVIGSGATAVVYAAYC-----LPKKEKVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRVPPadhdmGGITEAnaeflYIAT---QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd06610  76 LVMPLLSGGSLLDIMKSSYPR-----GGLDEA-----IIATvlkEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIAD 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGL--MRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGR-FSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVANRHL 795
Cdd:cd06610 146 FGVsaSLATGGDRTRKVRKTFVGTPCWMAPEVMEQVRgYDFKADIWSFGITAIEL-ATGAAPYSKYPPMKVLMLTLQNDP 224
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 796 LECPHNCPTNIYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd06610 225 PSLETGADYKKYSksfrkMISLCLQKDPSKRPTAEEL 261
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
610-830 1.86e-28

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: 115.29  E-value: 1.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 610 AQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDL-HELLKVRVPpadhdmggiTEANAEFLYiatQIALGM 688
Cdd:cd14027  36 EALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLmHVLKKVSVP---------LSVKGRIIL---EIIEGM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 689 EYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVR-----------WMSKEAIE--QGRFS 755
Cdd:cd14027 104 AYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLTKEEHNEQREVDgtakknagtlyYMAPEHLNdvNAKPT 183
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 756 EASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV---ANR-HLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSR 830
Cdd:cd14027 184 EKSDVYSFAIVLWAIFA-NKEPYENAINEDQIIMCiksGNRpDVDDITEYCPREIIDLMKLCWEANPEARPTFPGIEEK 261
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
570-827 2.30e-28

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: 114.63  E-value: 2.30e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfAPEPMAVavkKC--RHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14009   1 IGRGSFATVWKGRHKQ---TGEVVAI---KEisRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRvppadhdmGGITEANAefLYIATQIALGMEYLASMSFVHRDLATRNCLV---GDTRTIKIADFGLMR- 723
Cdd:cd14009  75 AGGDLSQYIRKR--------GRLPEAVA--RHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARs 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 --------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQV---IELVAN 792
Cdd:cd14009 145 lqpasmaeTLCGSPLY------------MAPEILQFQKYDAKADLWSVGAILFEM-LVGKPPFRGSNHVQLlrnIERSDA 211
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 793 RHLLECPHN----CPTNIYSLMvecwHENIERRPTFSEI 827
Cdd:cd14009 212 VIPFPIAAQlspdCKDLLRRLL----RRDPAERISFEEF 246
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
614-833 3.53e-28

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: 114.67  E-value: 3.53e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYiATQIALGMEYLAS 693
Cdd:cd14221  39 KEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLRGIIK--------SMDSHYPWSQRVSF-AKDIASGMAYLHS 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 694 MSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG-SDYYKMLHRSWMPVR-----------WMSKEAIEQGRFSEASDVW 761
Cdd:cd14221 110 MNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDeKTQPEGLRSLKKPDRkkrytvvgnpyWMAPEMINGRSYDEKVDVF 189
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 762 SFGVTLWEIwsFGRQPYEGASNQQVIELVAN-RHLLE--CPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14221 190 SFGIVLCEI--IGRVNADPDYLPRTMDFGLNvRGFLDryCPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLET 262
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
562-823 4.38e-28

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 114.23  E-value: 4.38e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYtsglfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06623   1 SDLERVKVLGQGSSGVVYKVRH-----KPTGKIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRvppadhdmGGITEanaEFL-YIATQIALGMEYLASMS-FVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd06623  76 IVLEYMDGGSLADLLKKV--------GKIPE---PVLaYIARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GLMRTSYGSDYYKMlhrSWM-PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVanRHLL-E 797
Cdd:cd06623 145 GISKVLENTLDQCN---TFVgTVTYMSPERIQGESYSYAADIWSLGLTLLEC-ALGKFPFLPPGQPSFFELM--QAICdG 218
                       250       260       270
                ....*....|....*....|....*....|.
gi 71980965 798 CPHNCPTNIYSLMVE-----CWHENIERRPT 823
Cdd:cd06623 219 PPPSLPAEEFSPEFRdfisaCLQKDPKKRPS 249
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
608-831 5.29e-28

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: 113.74  E-value: 5.29e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 608 ERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppaDHDmggITEANAEFLYIATQIALG 687
Cdd:cd14065  31 EQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLEELLK------SMD---EQLPWSQRVSLAKDIASG 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 688 MEYLASMSFVHRDLATRNCLV---GDTRTIKIADFGLMR----------------TSYGSDYykmlhrswmpvrWMSKEA 748
Cdd:cd14065 102 MAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLARempdektkkpdrkkrlTVVGSPY------------WMAPEM 169
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 749 IEQGRFSEASDVWSFGVTLWEIwsFGRQPYE----------GASNQQVIELVanrhllecPHNCPTNIYSLMVECWHENI 818
Cdd:cd14065 170 LRGESYDEKVDVFSFGIVLCEI--IGRVPADpdylprtmdfGLDVRAFRTLY--------VPDCPPSFLPLAIRCCQLDP 239
                       250
                ....*....|...
gi 71980965 819 ERRPTFSEIRSRL 831
Cdd:cd14065 240 EKRPSFVELEHHL 252
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
568-823 5.67e-28

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: 113.47  E-value: 5.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGLFapepmaVAVKKC-RHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd06627   6 DLIGRGAFGSVYKGLnLNTGEF------VAIKQIsLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKvrvppadhDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG----L 721
Cdd:cd06627  80 YVENGSLASIIK--------KFGKFPESLVAV-YIY-QVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGvatkL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRTS------YGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY-EGASNQQVIELVANRH 794
Cdd:cd06627 150 NEVEkdensvVGTPY------------WMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYyDLQPMAALFRIVQDDH 216
                       250       260       270
                ....*....|....*....|....*....|.
gi 71980965 795 --LlecPHNCPTNIYSLMVECWHENIERRPT 823
Cdd:cd06627 217 ppL---PENISPELRDFLLQCFQKDPTLRPS 244
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
570-832 9.27e-28

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: 112.87  E-value: 9.27e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglFAPepmaVAVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNslLAVFEYMV 648
Cdd:cd14062   1 IGSGSFGTVYKGRW----HGD----VAVKKLNvTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQ--LAIVTQWC 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDlhELLK-VRVPPADHDMGGITEanaeflyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL--MRTS 725
Cdd:cd14062  71 EGS--SLYKhLHVLETKFEMLQLID-------IARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLatVKTR 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 Y-GSDYYKMLHRSwmpVRWMSKEAI---EQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHLL----- 796
Cdd:cd14062 142 WsGSQQFEQPTGS---ILWMAPEVIrmqDENPYSFQSDVYAFGIVLYELLT-GQLPYSHINNRDQILFMVGRGYLrpdls 217
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14062 218 KVRSDTPKALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
570-832 1.01e-27

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: 113.52  E-value: 1.01e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepmAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd14066   1 IGSGGFGTVYKGVLENGT------VVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLESDEKLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKVRVPPADHDMggiteanAEFLYIATQIALGMEYLASMSF---VHRDLATRNCLVGDTRTIKIADFGLMRTSY 726
Cdd:cd14066  75 GSLEDRLHCHKGSPPLPW-------PQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIP 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 727 GSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQP-YEGASNQQVIELV----------ANRHL 795
Cdd:cd14066 148 PSESVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAvDENRENASRKDLVewveskgkeeLEDIL 226
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71980965 796 LECPHNCPT-------NIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14066 227 DKRLVDDDGveeeeveALLRLALLCTRSDPSLRPSMKEVVQMLE 270
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
568-827 1.25e-27

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 112.56  E-value: 1.25e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVH--SGIYTSGLfapepmaVAVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd08215   6 RVIGKGSFGSAYlvRRKSDGKL-------YVLKEIDlSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRVPPADHdmggITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR- 723
Cdd:cd08215  79 EYADGGDLAQKIKKQKKKGQP----FPEE--QILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKv 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 ---------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASnqqVIELVANrh 794
Cdd:cd08215 153 lesttdlakTVVGTPYY------------LSPELCENKPYNYKSDIWALGCVLYELCTL-KHPFEANN---LPALVYK-- 214
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 71980965 795 LLECPHNCPTNIYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd08215 215 IVKGQYPPIPSQYSselrdLVNSMLQKDPEKRPSANEI 252
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
569-833 1.73e-27

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: 113.36  E-value: 1.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGiYTSGLfapepmAVAVKKCR---HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14158  22 KLGEGGFGVVFKG-YINDK------NVAVKKLAamvDISTEDLTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLCLVYT 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELL--KVRVPPADHDMGgiteanaefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd14158  95 YMPNGSLLDRLacLNDTPPLSWHMR---------CKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKMLHRSWMPVRWMSKEAIeQGRFSEASDVWSFGVTLWEIWS------FGRQPY-------EGASNQQVIELV 790
Cdd:cd14158 166 ASEKFSQTIMTERIVGTTAYMAPEAL-RGEITPKSDIFSFGVVLLEIITglppvdENRDPQllldikeEIEDEEKTIEDY 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 791 ANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14158 245 VDKKMGDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQE 287
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
570-832 7.39e-26

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: 107.62  E-value: 7.39e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepmaVAVKKCRHDA--TNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA-VFEY 646
Cdd:cd14064   1 IGSGSFGKVYKGRCRNKI-------VAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPSQFAiVTQY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLASMS--FVHRDLATRNCLVGDTRTIKIADFGLMRt 724
Cdd:cd14064  74 VSGGSLFSLLHEQKRVIDL---------QSKLIIAVDVAKGMEYLHNLTqpIIHRDLNSHNILLYEDGHAVVADFGESR- 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 725 sygsdYYKMLHRSWMP-----VRWMSKEAIEQ-GRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHLL-E 797
Cdd:cd14064 144 -----FLQSLDEDNMTkqpgnLRWMAPEVFTQcTRYSIKADVFSYALCLWELLT-GEIPFAHLKPAAAAADMAYHHIRpP 217
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71980965 798 CPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14064 218 IGYSIPKPISSLLMRGWNAEPESRPSFVEIVALLE 252
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
563-831 7.46e-26

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: 107.82  E-value: 7.46e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapepmAVAVKKCRHDATNAEraQLEQEIRAVATFD---HPNVIKLIGVCYMDNS 639
Cdd:cd14063   1 ELEIKEVIGKGRFGRVHRGRWHG--------DVAIKLLNIDYLNEE--QLEAFKEEVAAYKntrHDNLVLFMGACMDPPH 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELlkVRVPPADHDMggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIkIADF 719
Cdd:cd14063  71 LAIVTSLCKGRTLYSL--IHERKEKFDF-------NKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDF 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GLMRTS-----YGSDYYKMLHRSWMP------VRWMS--KEAIEQGRFSEASDVWSFGVTLWEI----WSFGRQPYEGAS 782
Cdd:cd14063 141 GLFSLSgllqpGRREDTLVIPNGWLCylapeiIRALSpdLDFEESLPFTKASDVYAFGTVWYELlagrWPFKEQPAESII 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 71980965 783 NQQVIELVANRHLLEcphnCPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd14063 221 WQVGCGKKQSLSQLD----IGREVKDILMQCWAYDPEKRPTFSDLLRML 265
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
568-790 1.33e-25

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: 106.79  E-value: 1.33e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAERA---------------QLEQEIRAVATFDHPNVIKLIG 632
Cdd:cd05117   6 KVLGRGSFGVV-------------------RLAVHKKTGEEYAvkiidkkklksedeeMLRREIEILKRLDHPNIVKLYE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDLHELLkvrvppadHDMGGITEANAefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:cd05117  67 VFEDDKNLYLVMELCTGGELFDRI--------VKKGSFSEREA--AKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD 136
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 713 ---TIKIADFGL---------MRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEG 780
Cdd:cd05117 137 pdsPIKIIDFGLakifeegekLKTVCGTPYY------------VAPEVLKGKGYGKKCDIWSLGVILYILLC-GYPPFYG 203
                       250
                ....*....|
gi 71980965 781 ASNQQVIELV 790
Cdd:cd05117 204 ETEQELFEKI 213
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
615-836 1.47e-25

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: 107.34  E-value: 1.47e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGIT-EANAEFlyiATQIALGMEYLAS 693
Cdd:cd14222  40 EVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLKDFLR--------ADDPFPwQQKVSF---AKGIASGMAYLHS 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 694 MSFVHRDLATRNCLVGDTRTIKIADFGLMR----------TSYGSDYYKMLHRSWMPVR--------WMSKEAIEQGRFS 755
Cdd:cd14222 109 MSIIHRDLNSHNCLIKLDKTVVVADFGLSRliveekkkppPDKPTTKKRTLRKNDRKKRytvvgnpyWMAPEMLNGKSYD 188
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 756 EASDVWSFGVTLWEIwsFGRQPYEGASNQQVIELVANRHLLE---CPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14222 189 EKVDIFSFGIVLCEI--IGQVYADPDCLPRTLDFGLNVRLFWekfVPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFE 266

                ....
gi 71980965 833 SWSL 836
Cdd:cd14222 267 ALSL 270
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
570-828 2.55e-25

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


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 106.10  E-value: 2.55e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSG--IYTSGLFApepMAVAVKKCRHDATNAERAQLEQE------IRAVA---TFDHPNVIKLIGVcyMD- 637
Cdd:cd14008   1 LGRGSFGKVKLAldTETGQLYA---IKIFNKSRLRKRREGKNDRGKIKnalddvRREIAimkKLDHPNIVRLYEV--IDd 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 ---NSLLAVFEYMVHGDLHELlkvrvpPADHDMGGITEANAefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd14008  76 pesDKLYLVLEYCEGGPVMEL------DSGDRVPPLPEETA--RKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTV 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFG----------LMRTSYGSDYYkmlhrswmpvrwMSKEA--IEQGRFS-EASDVWSFGVTLWeIWSFGRQPYEGA 781
Cdd:cd14008 148 KISDFGvsemfedgndTLQKTAGTPAF------------LAPELcdGDSKTYSgKAADIWALGVTLY-CLVFGRLPFNGD 214
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 782 SNQQVIELVANRHL-LECPHNCPTNIYSLMVECWHENIERRPTFSEIR 828
Cdd:cd14008 215 NILELYEAIQNQNDeFPIPPELSPELKDLLRRMLEKDPEKRITLKEIK 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
566-808 2.93e-25

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 109.06  E-value: 2.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSgiytsglfAPEPMAVAVK--KCRHDATNAERAQLEQEIRAVATFDHP-NVIKLIGVCYMDNSLLA 642
Cdd:COG0515   4 ILRKLGEGSFGEVYL--------ARDRKLVALKvlAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRVPPADHDmggiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVG-DTRTIKIADFGL 721
Cdd:COG0515  76 VMEYVDGGSLEDLLKKIGRKGPLS-------ESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGL 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRTSYGSDYYKMLHRSWMPV----RWMSKEAIEQ---GRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVaNRH 794
Cdd:COG0515 149 AKLLPDPGSTSSIPALPSTSvgtpGYMAPEVLLGlslAYASSSSDIWSLGITLYEL-LTGLPPFEGEKNSSATSQT-LKI 226
                       250
                ....*....|....
gi 71980965 795 LLECPHNCPTNIYS 808
Cdd:COG0515 227 ILELPTPSLASPLS 240
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
557-832 4.18e-25

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


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 105.91  E-value: 4.18e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGIYTSGlfapepmaVAVKKCRHDATNAERAQ-LEQEIRAVATFDHPNVIKLIGvcY 635
Cdd:cd14151   3 WEIPDGQITVGQRIGSGSFGTVYKGKWHGD--------VAVKMLNVTAPTPQQLQaFKNEVGVLRKTRHVNILLFMG--Y 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGD--LHELlkvRVPPADHDMggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd14151  73 STKPQLAIVTQWCEGSslYHHL---HIIETKFEM-------IKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLT 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRTS---YGSDYYKMLHRSwmpVRWMSKEAI---EQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ-QV 786
Cdd:cd14151 143 VKIGDFGLATVKsrwSGSHQFEQLSGS---ILWMAPEVIrmqDKNPYSFQSDVYAFGIVLYELMT-GQLPYSNINNRdQI 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 71980965 787 IELVANRH----LLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14151 219 IFMVGRGYlspdLSKVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIE 268
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
568-724 1.39e-24

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 104.49  E-value: 1.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVV------HSGIYtsglfapepmaVAVKKCRHDATN------AERaqleqEIRAVATFDHPNVIKLIGVCY 635
Cdd:cd07829   5 EKLGEGTYGVVykakdkKTGEI-----------VALKKIRLDNEEegipstALR-----EISLLKELKHPNIVKLLDVIH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHgDLHELLKVRVPPadhdmggITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd07829  69 TENKLYLVFEYCDQ-DLKKYLDKRPGP-------LPPN--LIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLK 138

                ....*....
gi 71980965 716 IADFGLMRT 724
Cdd:cd07829 139 LADFGLARA 147
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
562-770 5.92e-24

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: 102.32  E-value: 5.92e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIY-TSGLfapepmAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGvCYMDNSL 640
Cdd:cd06609   1 ELFTLLERIGKGSFGEVYKGIDkRTNQ------VVAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYG-SFLKGSK 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LA-VFEYMVHGDLHELLKvrvppadhdMGGITEAnaeflYIAT---QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd06609  74 LWiIMEYCGGGSVLDLLK---------PGPLDET-----YIAFilrEVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKL 139
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 717 ADFGL----------MRTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06609 140 ADFGVsgqltstmskRNTFVGTPF------------WMAPEVIKQSGYDEKADIWSLGITAIEL 191
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
555-826 1.34e-23

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: 100.80  E-value: 1.34e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 555 KVFEITpsqlsvrEKIGEGQFGVVHSGIYTSGLFApepmaVAVKKCRHDATNAEraqLEQEIRAVATFDHPNVIKLIGVC 634
Cdd:cd06612   3 EVFDIL-------EKLGEGSYGSVYKAIHKETGQV-----VAIKVVPVEEDLQE---IIKEISILKQCDSPYIVKYYGSY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 635 YMDNSLLAVFEYMVHGDLHELLKVRvppadhdmgGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd06612  68 FKNTDLWIVMEYCGAGSVSDIMKIT---------NKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQA 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGL----------MRTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQ 784
Cdd:cd06612 139 KLADFGVsgqltdtmakRNTVIGTPF------------WMAPEVIQEIGYNNKADIWSLGITAIEM-AEGKPPYSDIHPM 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 71980965 785 QVIELVANR--HLLECPHNCPTNIYSLMVECWHENIERRPTFSE 826
Cdd:cd06612 206 RAIFMIPNKppPTLSDPEKWSPEFNDFVKKCLVKDPEERPSAIQ 249
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
570-827 5.02e-23

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: 99.40  E-value: 5.02e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI--YTSGLFA-PEPMAVAVKKCRHDATnaerAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd06632   8 LGSGSFGSVYEGFngDTGDFFAvKEVSLVDDDKKSRESV----KQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLkvrvppadHDMGGITEanaEFLYIAT-QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd06632  84 VPGGSIHKLL--------QRYGAFEE---PVIRLYTrQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSwmpVRWMSKEAIEQ--GRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHLL-ECPHNC 802
Cdd:cd06632 153 EAFSFAKSFKGS---PYWMAPEVIMQknSGYGLAVDIWSLGCTVLEMAT-GKPPWSQYEGVAAIFKIGNSGELpPIPDHL 228
                       250       260
                ....*....|....*....|....*
gi 71980965 803 PTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06632 229 SPDAKDFIRLCLQRDPEDRPTASQL 253
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
563-832 1.18e-22

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: 98.55  E-value: 1.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSGlfapepmaVAVKKCRHDATNAERAQ-LEQEIRAVATFDHPNVIKLIGvcYMDNSLL 641
Cdd:cd14150   1 EVSMLKRIGTGSFGTVFRGKWHGD--------VAVKILKVTEPTPEQLQaFKNEMQVLRKTRHVNILLFMG--FMTRPNF 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGD-LHELLkvRVPPADHDMggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd14150  71 AIITQWCEGSsLYRHL--HVTETRFDT-------MQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTSYGSDYYKMLHRSWMPVRWMSKEAI---EQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ-QVIELVANRHLL 796
Cdd:cd14150 142 LATVKTRWSGSQQVEQPSGSILWMAPEVIrmqDTNPYSFQSDVYAYGVVLYELMS-GTLPYSNINNRdQIIFMVGRGYLS 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 797 ----ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14150 221 pdlsKLSSNCPKAMKRLLIDCLKFKREERPLFPQILVSIE 260
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
585-832 1.68e-22

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: 97.55  E-value: 1.68e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 585 SGLFApepmavAVKKCRHDAT-----------NAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLH 653
Cdd:cd14155   3 SGFFS------EVYKVRHRTSgqvmalkmntlSSNRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 654 ELLKVRVPpadhdmggitEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLV---GDTRTIKIADFGLMRT--SYGS 728
Cdd:cd14155  77 QLLDSNEP----------LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKipDYSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 729 dyykmlHRSWMPV----RWMSKEAIEQGRFSEASDVWSFGVTLWEIwsFGRQP----YEGASNQQVIELVANRHLleCPh 800
Cdd:cd14155 147 ------GKEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGIILCEI--IARIQadpdYLPRTEDFGLDYDAFQHM--VG- 215
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 801 NCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14155 216 DCPPDFLQLAFNCCNMDPKSRPSFHDIVKTLE 247
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
564-770 1.73e-22

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 97.67  E-value: 1.73e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERaqLEQEIRAVATFDHPNVIKLIGvCYMDNSLL-A 642
Cdd:cd06614   2 YKNLEKIGEGASGEVYKATDRA-----TGKEVAIKKMRLRKQNKEL--IINEILIMKECKHPNIVDYYD-SYLVGDELwV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLkvrvppaDHDMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL- 721
Cdd:cd06614  74 VMEYMDGGSLTDII-------TQNPVRMNES--QIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFa 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 722 --------MRTSY-GSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06614 145 aqltkeksKRNSVvGTPY------------WMAPEVIKRKDYGPKVDIWSLGIMCIEM 190
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
569-792 2.29e-22

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: 97.16  E-value: 2.29e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIY-TSGlfapepMAVAVK---KcRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd14007   7 PLGKGKFGNVYLAREkKSG------FIVALKvisK-SQLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYLIL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKvRVPPadhdmggITEANAeFLYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL--- 721
Cdd:cd14007  80 EYAPNGELYKELK-KQKR-------FDEKEA-AKYIY-QLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWsvh 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 722 ----MRTSY-GS-DYykmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVAN 792
Cdd:cd14007 150 apsnRRKTFcGTlDY-------------LPPEMVEGKEYDYKVDIWSLGVLCYELL-VGKPPFESKSHQETYKRIQN 212
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
570-833 3.11e-22

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: 97.68  E-value: 3.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIY-------------TSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYm 636
Cdd:cd14000   2 LGDGGFGSVYRASYkgepvavkifnkhTSSNFANVPADTMLRHLRATDAMKNFRLLRQELTVLSHLHHPSIVYLLGIGI- 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 dNSLLAVFEYMVHGDLHELLKvrvppaDHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLV-----GDT 711
Cdd:cd14000  81 -HPLMLVLELAPLGSLDHLLQ------QDSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSA 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 712 RTIKIADFGLMR--------TSYGSDYYkmlhrswmpvrwMSKEAIEQGR-FSEASDVWSFGVTLWEIWSFGRQPYEGAS 782
Cdd:cd14000 154 IIIKIADYGISRqccrmgakGSEGTPGF------------RAPEIARGNViYNEKVDVFSFGMLLYEILSGGAPMVGHLK 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 783 NQQVIELVANRHLLECPHNC--PTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14000 222 FPNEFDIHGGLRPPLKQYECapWPEVEVLMKKCWKENPQQRPTAVTVVSILNS 274
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
568-826 5.90e-22

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


Pssm-ID: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 96.30  E-value: 5.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapepMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGV--CYMDNSL-LAVF 644
Cdd:cd13979   9 EPLGSGGFGSVYKATYKG-------ETVAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAetGTDFASLgLIIM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRVPPAdhdmggiteANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG---L 721
Cdd:cd13979  82 EYCGNGTLQQLIYEGSEPL---------PLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsvK 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRTSYGSDyykmLHRSWM--PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGaSNQQVI-ELVANRHLLEC 798
Cdd:cd13979 153 LGEGNEVG----TPRSHIggTYTYRAPELLKGERVTPKADIYSFGITLWQM-LTRELPYAG-LRQHVLyAVVAKDLRPDL 226
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 799 PHNCPT----NIYSLMVECWHENIERRPTFSE 826
Cdd:cd13979 227 SGLEDSefgqRLRSLISRCWSAQPAERPNADE 258
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
595-833 8.17e-22

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: 96.08  E-value: 8.17e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCRHDATNAERaQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHE-LLKVRVPpadhdmggiteA 673
Cdd:cd14045  33 VAIKKIAKKSFTLSK-RIRKEVKQVRELDHPNLCKFIGGCIEVPNVAIITEYCPKGSLNDvLLNEDIP-----------L 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 674 NAEFLY-IATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR------TSYGSDYYKMLHRSWMPVRWMSK 746
Cdd:cd14045 101 NWGFRFsFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTyrkedgSENASGYQQRLMQVYLPPENHSN 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 747 EAIEQgrfSEASDVWSFGVTLWEIWSFGR------QPYEGASNQQVIELVANRHLLECPhnCPTNIYSLMVECWHENIER 820
Cdd:cd14045 181 TDTEP---TQATDVYSYAIILLEIATRNDpvpeddYSLDEAWCPPLPELISGKTENSCP--CPADYVELIRRCRKNNPAQ 255
                       250
                ....*....|...
gi 71980965 821 RPTFSEIRSRLQS 833
Cdd:cd14045 256 RPTFEQIKKTLHK 268
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
566-808 8.67e-22

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 95.78  E-value: 8.67e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSG--IYTSGLFApepMAVAVKKCRHDAtnaERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd14002   5 VLELIGEGSFGKVYKGrrKYTGQVVA---LKFIPKRGKSEK---ELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYmVHGDLHELLKvrvppadhDMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd14002  79 TEY-AQGELFQILE--------DDGTLPEE--EVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 T-SYGSdyykMLHRS--WMPVrWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYegaSNQQVIELVanRHLLECPH 800
Cdd:cd14002 148 AmSCNT----LVLTSikGTPL-YMAPELVQEQPYDHTADLWSLGCILYELF-VGQPPF---YTNSIYQLV--QMIVKDPV 216

                ....*...
gi 71980965 801 NCPTNIYS 808
Cdd:cd14002 217 KWPSNMSP 224
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
608-831 9.66e-22

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: 95.92  E-value: 9.66e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 608 ERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppaDHDMGGIteanaeFLY-IATQIAL 686
Cdd:cd13992  39 EKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCTRGSLQDVLLNR----EIKMDWM------FKSsFIKDIVK 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 687 GMEYLASMSF-VHRDLATRNCLVGDTRTIKIADFGLMR---------TSYGSDYYKMLhrsWMPVRwMSKEAIEQGRFSE 756
Cdd:cd13992 109 GMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNlleeqtnhqLDEDAQHKKLL---WTAPE-LLRGSLLEVRGTQ 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 757 ASDVWSFGVTLWEIwsFGRQ-PYEGASNQQVIELVANR---------HLLECPhnCPTNIYSLMVECWHENIERRPTFSE 826
Cdd:cd13992 185 KGDVYSFAIILYEI--LFRSdPFALEREVAIVEKVISGgnkpfrpelAVLLDE--FPPRLVLLVKQCWAENPEKRPSFKQ 260

                ....*
gi 71980965 827 IRSRL 831
Cdd:cd13992 261 IKKTL 265
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
568-836 1.80e-21

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: 94.79  E-value: 1.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCrhDATNAERAQLEQ---EIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd08529   6 NKLGKGSFGVVYKVVRKV-----DGRVYALKQI--DISRMSRKMREEaidEARVLSKLNSPYVIKYYDSFVDKGKLNIVM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRvppadhdMGG-ITEANAEFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG--- 720
Cdd:cd08529  79 EYAENGDLHSLIKSQ-------RGRpLPEDQIWKFFI--QTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGvak 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 -------LMRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIELVANR 793
Cdd:cd08529 150 ilsdttnFAQTIVGTPYY------------LSPELCEDKPYNEKSDVWALGCVLYELCTG-KHPFEAQNQGALILKIVRG 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEIrsrLQSWSL 836
Cdd:cd08529 217 KYPPISASYSQDLSQLIDSCLTKDYRQRPDTTEL---LRNPSL 256
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
551-832 2.79e-21

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: 95.10  E-value: 2.79e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 551 DNSYkVFEITPSQLSVREKIGEGQFGVVHSGIYTSGlfapepmaVAVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIK 629
Cdd:cd14149   2 DSSY-YWEIEASEVMLSTRIGSGSFGTVYKGKWHGD--------VAVKILKvVDPTPEQFQAFRNEVAVLRKTRHVNILL 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 630 LIGvcYMDNSLLAVFEYMVHGD-LHELLKVRvpPADHDMggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd14149  73 FMG--YMTKDNLAIVTQWCEGSsLYKHLHVQ--ETKFQM-------FQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFL 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 GDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAI---EQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ- 784
Cdd:cd14149 142 HEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSILWMAPEVIrmqDNNPFSFQSDVYSYGIVLYELMT-GELPYSHINNRd 220
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 785 QVIELV----ANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14149 221 QIIFMVgrgyASPDLSKLYKNCPKAMKRLVADCIKKVKEERPLFPQILSSIE 272
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
566-770 6.78e-21

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


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 93.07  E-value: 6.78e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYT-SGLFapepmaVAVKKCRHDATNAERAQleQEIRAV----ATFDHPNVIKLIGVCY--MDN 638
Cdd:cd05118   3 VLRKIGEGAFGTVWLARDKvTGEK------VAIKKIKNDFRHPKAAL--REIKLLkhlnDVEGHPNIVKLLDVFEhrGGN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMvHGDLHELLKVRVPPADHDMggiteanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLV-GDTRTIKIA 717
Cdd:cd05118  75 HLCLVFELM-GMNLYELIKDYPRGLPLDL---------IKSYLYQLLQALDFLHSNGIIHRDLKPENILInLELGQLKLA 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 718 DFGLMRTSYGSDYYKMLHRSWmpvrWMSKEAI-EQGRFSEASDVWSFGVTLWEI 770
Cdd:cd05118 145 DFGLARSFTSPPYTPYVATRW----YRAPEVLlGAKPYGSSIDIWSLGCILAEL 194
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
570-829 8.23e-21

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


Pssm-ID: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 92.71  E-value: 8.23e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLfapepMAVAVK-----KCRHDAtNAErAQLEQEIRAVATFDHPNVIKLIGVCYMDNS--LLA 642
Cdd:cd14119   1 LGEGSYGKVKEVLDTETL-----CRRAVKilkkrKLRRIP-NGE-ANVKREIQILRRLNHRNVIKLVDVLYNEEKqkLYM 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYmVHGDLHELLKV----RVPpadhdmggITEANAEFlyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd14119  74 VMEY-CVGGLQEMLDSapdkRLP--------IWQAHGYF----VQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISD 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FG------------LMRTSYGSDYYKmlhrswmpvrwmSKE-AIEQGRFSE-ASDVWSFGVTLWEIWSfGRQPYEGasnQ 784
Cdd:cd14119 141 FGvaealdlfaeddTCTTSQGSPAFQ------------PPEiANGQDSFSGfKVDIWSAGVTLYNMTT-GKYPFEG---D 204
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*..
gi 71980965 785 QVIELVAN--RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14119 205 NIYKLFENigKGEYTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQIRQ 251
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
624-831 2.43e-20

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: 91.39  E-value: 2.43e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 624 HPNVIKLIGVCYMDNSLLaVFEYMVHGDLHELLkvrvppadHDMGGITEAnAEFLYIATQIALGMEYLASMSFVHRDLAT 703
Cdd:cd05037  61 HKHLVKLYGVCVADENIM-VQEYVRYGPLDKYL--------RRMGNNVPL-SWKLQVAKQLASALHYLEDKKLIHGNVRG 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 704 RNCLV------GDTRTIKIADFGLmRTSYGSDYYKMLHRSWMPVRWMSkeaIEQGRFSEASDVWSFGVTLWEIWSFGRQP 777
Cdd:cd05037 131 RNILLaregldGYPPFIKLSDPGV-PITVLSREERVDRIPWIAPECLR---NLQANLTIAADKWSFGTTLWEICSGGEEP 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 778 YEGASNQQVIELVANRHLLECPhNCPtNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd05037 207 LSALSSQEKLQFYEDQHQLPAP-DCA-ELAELIMQCWTYEPTKRPSFRAILRDL 258
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
570-827 2.68e-20

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: 91.83  E-value: 2.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTsglFAPEPMAVavKKCRHDATNAERAQ--------LEQEIRAVATFDHPNVIKLIGvCYMDNSLL 641
Cdd:cd06628   8 IGSGSFGSVYLGMNA---SSGELMAV--KQVELPSVSAENKDrkksmldaLQREIALLRELQHENIVQYLG-SSSDANHL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVF-EYMVHGDLHELLkvrvppadhDMGGITEANAEFLYIaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd06628  82 NIFlEYVPGGSVATLL---------NNYGAFEESLVRNFV-RQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 ------LMRTSYGSDYYK-MLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANR 793
Cdd:cd06628 152 iskkleANSLSTKNNGARpSLQGS---VFWMAPEVVKQTSYTRKADIWSLGCLVVEMLT-GTHPFPDCTQMQAIFKIGEN 227
                       250       260       270
                ....*....|....*....|....*....|....
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06628 228 ASPTIPSNISSEARDFLEKTFEIDHNKRPTADEL 261
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
568-769 3.48e-20

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 91.86  E-value: 3.48e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYT-SGlfapepMAVAVKKCRhdatNAERAQLE--------QEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd07841   6 KKLGEGTYAVVYKARDKeTG------RIVAIKKIK----LGERKEAKdginftalREIKLLQELKHPNIIGLLDVFGHKS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMvHGDLHELLK---VRVPPADhdmggiTEAnaeflyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd07841  76 NINLVFEFM-ETDLEKVIKdksIVLTPAD------IKS------YMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLK 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 716 IADFGLMRtSYGSDYYKMLHRswmpV--RWM-SKEAIEQGR-FSEASDVWSFGVTLWE 769
Cdd:cd07841 143 LADFGLAR-SFGSPNRKMTHQ----VvtRWYrAPELLFGARhYGVGVDMWSVGCIFAE 195
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
614-832 3.86e-20

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: 91.04  E-value: 3.86e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppADHDMGGITEANAEflyIATQIALGMEYLAS 693
Cdd:cd14156  37 REISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLEELL------AREELPLSWREKVE---LACDISRGMVYLHS 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 694 MSFVHRDLATRNCLVGDT---RTIKIADFGLMRtSYGSDYYKMLHRSWMPVR---WMSKEAIEQGRFSEASDVWSFGVTL 767
Cdd:cd14156 108 KNIYHRDLNSKNCLIRVTprgREAVVTDFGLAR-EVGEMPANDPERKLSLVGsafWMAPEMLRGEPYDRKVDVFSFGIVL 186
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 768 WEIwsFGRQPyegaSNQQV--------IELVANRHLleCPhNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14156 187 CEI--LARIP----ADPEVlprtgdfgLDVQAFKEM--VP-GCPEPFLDLAASCCRMDAFKRPSFAELLDELE 250
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
570-824 4.22e-20

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: 91.52  E-value: 4.22e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglfAPEPMAVAVKkCRHDAT---NAERAQL--EQEIRAVATFDHpnVIKLIGVCYMDNSLLAVF 644
Cdd:cd14026   5 LSRGAFGTVSRARH-----ADWRVTVAIK-CLKLDSpvgDSERNCLlkEAEILHKARFSY--ILPILGICNEPEFLGIVT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELL--KVRVPPAdhdmggiteANAEFLYIATQIALGMEYLASMS--FVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd14026  77 EYMTNGSLNELLheKDIYPDV---------AWPLRLRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRtsygsdyYKMLH----RSWMP------VRWMSKEAIEQGRFSEAS---DVWSFGVTLWEIWSfGRQPYEGASNQ-QV 786
Cdd:cd14026 148 LSK-------WRQLSisqsRSSKSapeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLS-RKIPFEEVTNPlQI 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 71980965 787 IELVANRHLLEC-----PHNCPTN--IYSLMVECWHENIERRPTF 824
Cdd:cd14026 220 MYSVSQGHRPDTgedslPVDIPHRatLINLIESGWAQNPDERPSF 264
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
566-777 4.60e-20

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


Pssm-ID: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 92.20  E-value: 4.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRH---DATNAERAqLeQEIRAVATFDHPNVIKLIGVCYMD----- 637
Cdd:cd07834   4 LLKPIGSGAYGVVCSAYDKR-----TGRKVAIKKISNvfdDLIDAKRI-L-REIKILRHLKHENIIGLLDILRPPspeef 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMvHGDLHELLKVRVPpadhdmggITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd07834  77 NDVYIVTELM-ETDLHKVIKSPQP--------LTDDHIQyFLY---QILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKI 144
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 717 ADFGLMRTSYGSDYYKMLhRSWMPVRW--------MSKeaieqgRFSEASDVWSFGVTLWEIwsFGRQP 777
Cdd:cd07834 145 CDFGLARGVDPDEDKGFL-TEYVVTRWyrapelllSSK------KYTKAIDIWSVGCIFAEL--LTRKP 204
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
563-764 7.04e-20

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


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 90.85  E-value: 7.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKC----RHD--ATNAERaqleqEIRAVATF-DHPNVIKLIGVCY 635
Cdd:cd07832   1 RYKILGRIGEGAHGIVFKAKDRE-----TGETVALKKValrkLEGgiPNQALR-----EIKALQACqGHPYVVKLRDVFP 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHgDLHELLKVRVPPadhdmggITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd07832  71 HGTGFVLVFEYMLS-SLSEVLRDEERP-------LTEAQVK--RYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLK 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71980965 716 IADFGLMRTSYGSDYYKMLHRswMPVRW-MSKEAIEQGR-FSEASDVWSFG 764
Cdd:cd07832 141 IADFGLARLFSEEDPRLYSHQ--VATRWyRAPELLYGSRkYDEGVDLWAVG 189
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
562-834 1.38e-19

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


Pssm-ID: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 90.02  E-value: 1.38e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGiYTSGLFAPEPMAVAVKK--------CRHDATNAERA-------------QLEQEIRAVA 620
Cdd:cd14199   2 NQYKLKDEIGKGSYGVVKLA-YNEDDNTYYAMKVLSKKklmrqagfPRRPPPRGARAapegctqprgpieRVYQEIAILK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 621 TFDHPNVIKLIGVC--YMDNSLLAVFEYMVHGDLHELlkvrvpPADHDMGgitEANAEFLYiaTQIALGMEYLASMSFVH 698
Cdd:cd14199  81 KLDHPNVVKLVEVLddPSEDHLYMVFELVKQGPVMEV------PTLKPLS---EDQARFYF--QDLIKGIEYLHYQKIIH 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 699 RDLATRNCLVGDTRTIKIADFGLMRTSYGSDyyKMLHRSWMPVRWMSKEAIEQGR--FS-EASDVWSFGVTLWeIWSFGR 775
Cdd:cd14199 150 RDVKPSNLLVGEDGHIKIADFGVSNEFEGSD--ALLTNTVGTPAFMAPETLSETRkiFSgKALDVWAMGVTLY-CFVFGQ 226
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 776 QPYegaSNQQVIELVA--NRHLLECP--HNCPTNIYSLMVECWHENIERRPTFSEIrsRLQSW 834
Cdd:cd14199 227 CPF---MDERILSLHSkiKTQPLEFPdqPDISDDLKDLLFRMLDKNPESRISVPEI--KLHPW 284
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
570-829 2.16e-19

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: 88.90  E-value: 2.16e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHsgIYTSGLFAPEpMAVAVKKCRHDATNA------ERAQLEQEIraVATFDHPNVIKLIGVCY-MDNSLLA 642
Cdd:cd13994   1 IGKGATSVVR--IVTKKNPRSG-VLYAVKEYRRRDDESkrkdyvKRLTSEYII--SSKLHHPNIVKVLDLCQdLHGKWCL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELL-KVRVPPADhdmggitEANAEFLyiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd13994  76 VMEYCPGGDLFTLIeKADSLSLE-------EKDCFFK----QILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGT 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 mrtsygSDYYKMLHRSWMPVR--------WMSKEAIEQGRFS-EASDVWSFGVTLWEIWsFGRQP-------------YE 779
Cdd:cd13994 145 ------AEVFGMPAEKESPMSaglcgsepYMAPEVFTSGSYDgRAVDVWSCGIVLFALF-TGRFPwrsakksdsaykaYE 217
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 71980965 780 GASNQQVIELVANRHLLecPHNCPTNIYSLMvecwHENIERRPTFSEIRS 829
Cdd:cd13994 218 KSGDFTNGPYEPIENLL--PSECRRLIYRML----HPDPEKRITIDEALN 261
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
570-821 2.33e-19

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: 88.34  E-value: 2.33e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH--SGIYTSGLFApepM-----AVAVKKCRHDATNAERAQLEQeiravatFDHPNVIKLigVCYM--DNSL 640
Cdd:cd05123   1 LGKGSFGKVLlvRKKDTGKLYA---MkvlrkKEIIKRKEVEHTLNERNILER-------VNHPFIVKL--HYAFqtEEKL 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd05123  69 YLVLDYVPGGELFSHLS--------KEGRFPEERARF-YAA-EIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFG 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTSYGSDyykmlHRSWMPV---RWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVANRHlLE 797
Cdd:cd05123 139 LAKELSSDG-----DRTYTFCgtpEYLAPEVLLGKGYGKAVDWWSLGVLLYEML-TGKPPFYAENRKEIYEKILKSP-LK 211
                       250       260
                ....*....|....*....|....
gi 71980965 798 CPHNCPTNIYSLMVECWHENIERR 821
Cdd:cd05123 212 FPEYVSPEAKSLISGLLQKDPTKR 235
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
562-827 2.82e-19

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: 88.56  E-value: 2.82e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVhsgiyTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06605   1 DDLEYLGELGEGNGGVV-----SKVRHRPSGQIMAVKVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDIS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKvrvppadhDMGGITEanaEFL-YIATQIALGMEYLAS-MSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd06605  76 ICMEYMDGGSLDKILK--------EVGRIPE---RILgKIAVAVVKGLIYLHEkHKIIHRDVKPSNILVNSRGQVKLCDF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 G--------LMRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYegaSNQQVIELVA 791
Cdd:cd06605 145 GvsgqlvdsLAKTFVGTRSY------------MAPERISGGKYTVKSDIWSLGLSLVEL-ATGRFPY---PPPNAKPSMM 208
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 792 NRHLLEC-----PHNCPTNIYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd06605 209 IFELLSYivdepPPLLPSGKFSpdfqdFVSQCLQKDPTERPSYKEL 254
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
570-777 3.32e-19

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


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 88.87  E-value: 3.32e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI-YTSGLFapepmaVAVKKCRhdatnaerAQLEQE------IRAVA------TFDHPNVIKLIGVCY- 635
Cdd:cd07838   7 IGEGAYGTVYKARdLQDGRF------VALKKVR--------VPLSEEgiplstIREIAllkqleSFEHPNVVRLLDVCHg 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 --MDN--SLLAVFEYmVHGDLHELLKvRVPPAdhdmgGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDT 711
Cdd:cd07838  73 prTDRelKLTLVFEH-VDQDLATYLD-KCPKP-----GLPPETIKDL--MRQLLRGLDFLHSHRIVHRDLKPQNILVTSD 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 712 RTIKIADFGLMRTsYGsdyYKMLHRSWMPVRWM-SKEAIEQGRFSEASDVWSFGVTLWEIwsFGRQP 777
Cdd:cd07838 144 GQVKLADFGLARI-YS---FEMALTSVVVTLWYrAPEVLLQSSYATPVDMWSVGCIFAEL--FNRRP 204
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
586-829 4.76e-19

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 88.19  E-value: 4.76e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 586 GLFAPEPMAVAVKKCRHDATNAERAQleQEIRAVATFDHPNVIKLIGVcyMD----NSLLAVFEYMVHGDLhellkVRVP 661
Cdd:cd14118  37 GFFRRPPPRRKPGALGKPLDPLDRVY--REIAILKKLDHPNVVKLVEV--LDdpneDNLYMVFELVDKGAV-----MEVP 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 662 PADhdmgGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDyyKMLHRSWMPV 741
Cdd:cd14118 108 TDN----PLSEETARSYF--RDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDD--ALLSSTAGTP 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 742 RWMSKEAIEQGR--FS-EASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELVANRHlLECPHNCPTN--IYSLMVECWHE 816
Cdd:cd14118 180 AFMAPEALSESRkkFSgKALDIWAMGVTLY-CFVFGRCPFEDDHILGLHEKIKTDP-VVFPDDPVVSeqLKDLILRMLDK 257
                       250
                ....*....|...
gi 71980965 817 NIERRPTFSEIRS 829
Cdd:cd14118 258 NPSERITLPEIKE 270
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
570-790 5.24e-19

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: 87.94  E-value: 5.24e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd14664   1 IGRGGAGTVYKGVM------PNGTLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPN 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKVRVPPADHdMGGITEANaeflyIATQIALGMEYL---ASMSFVHRDLATRNCLVGDTRTIKIADFGL----- 721
Cdd:cd14664  75 GSLGELLHSRPESQPP-LDWETRQR-----IALGSARGLAYLhhdCSPLIIHRDVKSNNILLDEEFEAHVADFGLaklmd 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 722 ---------MRTSYGsdyykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14664 149 dkdshvmssVAGSYG---------------YIAPEYAYTGKVSEKSDVYSYGVVLLELIT-GKRPFDEAFLDDGVDIV 210
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
568-829 5.45e-19

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: 87.70  E-value: 5.45e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfapepMAVAVKKCRHDATNAER--AQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14161   9 ETLGKGTYGRVKKARDSSG------RLVAIKSIRKDRIKDEQdlLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVME 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRVPPADhdmggiTEANAEFlyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd14161  83 YASRGDLYDYISERQRLSE------LEARHFF----RQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLY 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSwmPVrWMSKEaIEQGRFSEASDV--WSFGVTLWeIWSFGRQPYEGASNQQVIELVANRHLLECPH--- 800
Cdd:cd14161 153 NQDKFLQTYCGS--PL-YASPE-IVNGRPYIGPEVdsWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGAYREPTKpsd 227
                       250       260
                ....*....|....*....|....*....
gi 71980965 801 NCPTNIYSLMVecwheNIERRPTFSEIRS 829
Cdd:cd14161 228 ACGLIRWLLMV-----NPERRATLEDVAS 251
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
563-826 6.15e-19

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: 87.76  E-value: 6.15e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd14202   3 EFSRKDLIGHGAFAVVFKGRHKE----KHDLEVAVKCINKKNLAKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLkvrvppadHDMGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVG---------DTRT 713
Cdd:cd14202  79 VMEYCNGGDLADYL--------HTMRTLSEDTIRLFL--QQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRTSYGSDYYKMLHRSWMpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVA-N 792
Cdd:cd14202 149 IKIADFGFARYLQNNMMAATLCGSPM---YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEkN 224
                       250       260       270
                ....*....|....*....|....*....|....*
gi 71980965 793 RHLL-ECPHNCPTNIYSLMVECWHENIERRPTFSE 826
Cdd:cd14202 225 KSLSpNIPRETSSHLRQLLLGLLQRNQKDRMDFDE 259
Kringle pfam00051
Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, ...
328-403 7.09e-19

Kringle domain; Kringle domains have been found in plasminogen, hepatocyte growth factors, prothrombin, and apolipoprotein A. Structure is disulfide-rich, nearly all-beta.


Pssm-ID: 395005  Cd Length: 79  Bit Score: 81.58  E-value: 7.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965   328 CYVNSGTQYEGTVAQTSSGKQCAPWiDSTS----RDFNVHRFPELMNSKNYCRNPGGkKSRPWCYSK-PMGQEEYCDVPQ 402
Cdd:pfam00051   1 CYHGNGESYRGTVSTTESGRPCQAW-DSQTphrhSKYTPENFPAKGLGENYCRNPDG-DERPWCYTTdPRVRWEYCDIPR 78

                  .
gi 71980965   403 C 403
Cdd:pfam00051  79 C 79
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
568-829 7.74e-19

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 87.55  E-value: 7.74e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfAPEPMAVAVKKCRHdATNAERAQLEQEIRAVATFDHPNVIKLIGVCymDNSLLAVFEYM 647
Cdd:cd14025   2 EKVGSGGFGQVYKVRHKH---WKTWLAIKCPPSLH-VDDSERMELLEEAKKMEMAKFRHILPVYGIC--SEPVGLVMEYM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGITEanaeflyiatqIALGMEYLASMS--FVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd14025  76 ETGSLEKLLASEPLPWELRFRIIHE-----------TAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWN 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMlHRSWM--------PVRWMSKEAIeqgrFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIEL-VANRHLL 796
Cdd:cd14025 145 GLSHSHDL-SRDGLrgtiaylpPERFKEKNRC----PDTKHDVYSFAIVIWGILT-QKKPFAGENNILHIMVkVVKGHRP 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 797 EC-------PHNCpTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14025 219 SLspiprqrPSEC-QQMICLMKRCWDQDPRKRPTFQDITS 257
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
570-790 8.70e-19

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: 87.15  E-value: 8.70e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI-YTSGlfapePMAvAVK---KCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14098   8 LGSGTFAEVKKAVeVETG-----KMR-AIKqivKRKVAGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLkvrvppADHdmGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLV--GDTRTIKIADFGLMR 723
Cdd:cd14098  82 YVEGGDLMDFI------MAW--GAIPEQHAR--ELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAK 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKMLHRSW---MPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14098 152 VIHTGTFLVTFCGTMaylAPEILMSKEQNLQGGYSNLVDMWSVGCLVYVMLT-GALPFDGSSQLPVEKRI 220
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
568-829 9.62e-19

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: 87.05  E-value: 9.62e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGlfapEPMAVA-VKKCRHDATNAERAQ------LEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd06629   7 ELIGKGTYGRVYLAMnATTG----EMLAVKqVELPKTSSDRADSRQktvvdaLKSEIDTLKDLDHPNIVQYLGFEETEDY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLKvRVPPADHDMggiteanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd06629  83 FSIFLEYVPGGSIGSCLR-KYGKFEEDL---------VRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDF 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GLMRTS---YGSDYYKMLHRSwmpVRWMSKEAI---EQGrFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVI-ELVAN 792
Cdd:cd06629 153 GISKKSddiYGNNGATSMQGS---VFWMAPEVIhsqGQG-YSAKVDIWSLGCVVLEMLA-GRRPWSDDEAIAAMfKLGNK 227
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 793 RHLLECPHNcpTNIYSL----MVECWHENIERRPTFSEIRS 829
Cdd:cd06629 228 RSAPPVPED--VNLSPEaldfLNACFAIDPRDRPTAAELLS 266
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
568-773 1.61e-18

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: 86.82  E-value: 1.61e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfaPEPMaVAVKKCRHDATNAERAQLEQEIRAVATF-DHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd07830   5 KQLGDGTFGSVYLARNKE----TGEL-VAIKKMKKKFYSWEECMNLREVKSLRKLnEHPNIVKLKEVFRENDELYFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MvHGDLHELLKvrvppaDHDMGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR--- 723
Cdd:cd07830  80 M-EGNLYQLMK------DRKGKPFSESVIR--SIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAReir 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 -----TSYGSD-YYK----MLHRSWmpvrwmskeaieqgrFSEASDVWSFGVTLWEIWSF 773
Cdd:cd07830 151 srppyTDYVSTrWYRapeiLLRSTS---------------YSSPVDIWALGCIMAELYTL 195
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
569-829 2.14e-18

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 85.77  E-value: 2.14e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYT-SGlfapepMAVAVK--KCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14081   8 TLGKGQTGLVKLAKHCvTG------QKVAIKivNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVLE 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG----- 720
Cdd:cd14081  82 YVSGGELFDYLVKK--------GRLTEKEARKFF--RQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGmaslq 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 ----LMRTSYGSDYYkmlhrswmpvrwMSKEAIE----QGRfseASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVaN 792
Cdd:cd14081 152 pegsLLETSCGSPHY------------ACPEVIKgekyDGR---KADIWSCGVILYALLV-GALPFDDDNLRQLLEKV-K 214
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 793 RHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14081 215 RGVFHIPHFISPDAQDLLRRMLEVNPEKRITIEEIKK 251
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
595-831 2.21e-18

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: 86.11  E-value: 2.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCRHDATNAERAQLeQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppadhdmggiteAN 674
Cdd:cd14042  33 VAIKKVNKKRIDLTREVL-KELKHMRDLQHDNLTRFIGACVDPPNICILTEYCPKGSLQDIL----------------EN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 675 AEF----LYIA---TQIALGMEYL-ASMSFVHRDLATRNCLVgDTR-TIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMS 745
Cdd:cd14042  96 EDIkldwMFRYsliHDIVKGMHYLhDSEIKSHGNLKSSNCVV-DSRfVLKITDFGLHSFRSGQEPPDDSHAYYAKLLWTA 174
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 746 KEAIEQGRF----SEASDVWSFGVTLWEIwsFGRQ------PYEGASNQQVIELVAN------RHLLEcPHNCPTNIYSL 809
Cdd:cd14042 175 PELLRDPNPpppgTQKGDVYSFGIILQEI--ATRQgpfyeeGPDLSPKEIIKKKVRNgekppfRPSLD-ELECPDEVLSL 251
                       250       260
                ....*....|....*....|..
gi 71980965 810 MVECWHENIERRPTFSEIRSRL 831
Cdd:cd14042 252 MQRCWAEDPEERPDFSTLRNKL 273
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
570-829 2.77e-18

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: 85.46  E-value: 2.77e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfaPEpMAVAVKK-----CRHDATNaeraQLEQEIRAVATFDHPNVIKLIGvCYMDNSLLAVF 644
Cdd:cd14069   9 LGEGAFGEVFLAVNRN----TE-EAVAVKFvdmkrAPGDCPE----NIKKEVCIQKMLSHKNVVRFYG-HRREGEFQYLF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 -EYMVHGDLHEllkvRVPPadhDMGgITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd14069  79 lEYASGGELFD----KIEP---DVG-MPEDVAQFYF--QQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAT 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKMLHRSWMPVRWMSKEAIEQGRF-SEASDVWSFGVTLWEIWSfGRQPYEGASN--QQVIELVANRHLLECPH 800
Cdd:cd14069 149 VFRYKGKERLLNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLA-GELPWDQPSDscQEYSDWKENKKTYLTPW 227
                       250       260       270
                ....*....|....*....|....*....|
gi 71980965 801 N-CPTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14069 228 KkIDTAALSLLRKILTENPNKRITIEDIKK 257
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
568-827 2.81e-18

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 85.89  E-value: 2.81e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSglfapePMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd06641  10 EKIGKGSFGEVFKGIdNRT------QKVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEY 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKvrvpPADHDmggiteaNAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMrtsy 726
Cdd:cd06641  84 LGGGSALDLLE----PGPLD-------ETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVA---- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 727 GSDYYKMLHRSWM---PVrWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVA--NRHLLEcpHN 801
Cdd:cd06641 149 GQLTDTQIKRN*FvgtPF-WMAPEVIKQSAYDSKADIWSLGITAIEL-ARGEPPHSELHPMKVLFLIPknNPPTLE--GN 224
                       250       260
                ....*....|....*....|....*.
gi 71980965 802 CPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06641 225 YSKPLKEFVEACLNKEPSFRPTAKEL 250
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
561-827 3.03e-18

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: 85.88  E-value: 3.03e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 561 PSQLSVR-EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd06642   2 PEELFTKlERIGKGSFGEVYKGIDNR-----TKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGSYLKGTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLKVrvppadhdmGGITEAnaeflYIAT---QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd06642  77 LWIIMEYLGGGSALDLLKP---------GPLEET-----YIATilrEILKGLDYLHSERKIHRDIKAANVLLSEQGDVKL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMrtsyGSDYYKMLHRSWM---PVrWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVANR 793
Cdd:cd06642 143 ADFGVA----GQLTDTQIKRNTFvgtPF-WMAPEVIKQSAYDFKADIWSLGITAIEL-AKGEPPNSDLHPMRVLFLIPKN 216
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 794 H--LLECPHNCPtniYSLMVE-CWHENIERRPTFSEI 827
Cdd:cd06642 217 SppTLEGQHSKP---FKEFVEaCLNKDPRFRPTAKEL 250
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
568-830 5.32e-18

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


Pssm-ID: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 84.71  E-value: 5.32e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLFApepmAVAVKKCRHDATNAERAQLEQEIRAVATF----DHPNVIKLIGVCYMDNSLL 641
Cdd:cd13993   6 SPIGEGAYGVVYLAvdLRTGRKYA----IKCLYKSGPNSKDGNDFQKLPQLREIDLHrrvsRHPNIITLHDVFETEVAIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELL--KVRVPPADHDMGGiteanaeflyIATQIALGMEYLASMSFVHRDLATRNCLV-GDTRTIKIAD 718
Cdd:cd13993  82 IVLEYCPNGDLFEAIteNRIYVGKTELIKN----------VFLQLIDAVKHCHSLGIYHRDIKPENILLsQDEGTVKLCD 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLM---RTSY----GSDYYkmlhrswmpvrwMSKEAIEQ-GRFSE-----ASDVWSFGVTLWEIwSFGRQPYEGASNQQ 785
Cdd:cd13993 152 FGLAtteKISMdfgvGSEFY------------MAPECFDEvGRSLKgypcaAGDIWSLGIILLNL-TFGRNPWKIASESD 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 786 VIEL---VANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSR 830
Cdd:cd13993 219 PIFYdyyLNSPNLFDVILPMSDDFYNLLRQIFTVNPNNRILLPELQLL 266
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
568-793 6.86e-18

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 84.65  E-value: 6.86e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfapEPMAVA-VKKCRhdatnaeRAQLEQEIRAVATFDHPNVIKLIGvCY-MDNSLLAVFE 645
Cdd:cd14010   6 DEIGRGKHSVVYKGRRKGTI---EFVAIKcVDKSK-------RPEVLNEVRLTHELKHPNVLKFYE-WYeTSNHLWLVVE 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKvrvppadHDMGGITEANAEFlyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR-- 723
Cdd:cd14010  75 YCTGGDLETLLR-------QDGNLPESSVRKF---GRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARre 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 --------------TSYGSDYYKMLHRSwMPVrWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIEL 789
Cdd:cd14010 145 geilkelfgqfsdeGNVNKVSKKQAKRG-TPY-YMAPELFQGGVHSFASDLWALGCVLYEM-FTGKPPFVAESFTELVEK 221

                ....
gi 71980965 790 VANR 793
Cdd:cd14010 222 ILNE 225
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
568-803 7.93e-18

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: 84.57  E-value: 7.93e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGLfapepmAVAVKKC---------RHDATNAERAQLEQeiravatFDHPNVIKLIGVCYMD 637
Cdd:cd05581   7 KPLGEGSYSTVVLAKeKETGK------EYAIKVLdkrhiikekKVKYVTIEKEVLSR-------LAHPGIVKLYYTFQDE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05581  74 SKLYFVLEYAPNGDLLEYIR--------KYGSLDEKCTRF-YTA-EIVLALEYLHSKGIIHRDLKPENILLDEDMHIKIT 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFG------------LMRTSYGSDYYKMLHRSWMPV---RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:cd05581 144 DFGtakvlgpdsspeSTKGDADSQIAYNQARAASFVgtaEYVSPELLNEKPAGKSSDLWALGCIIYQMLT-GKPPFRGSN 222
                       250       260
                ....*....|....*....|.
gi 71980965 783 NQQVIELVANRHlLECPHNCP 803
Cdd:cd05581 223 EYLTFQKIVKLE-YEFPENFP 242
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
568-827 1.00e-17

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: 84.45  E-value: 1.00e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDH---PNVIKLIGvCYM-DNSLLAV 643
Cdd:cd06917   7 ELVGRGSYGAVYRGYHV-----KTGRVVALKVLNLDTDDDDVSDIQKEVALLSQLKLgqpKNIIKYYG-SYLkGPSLWII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVrvppadhdmGGITEANAEFLYIATQIALgmEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMr 723
Cdd:cd06917  81 MDYCEGGSIRTLMRA---------GPIAERYIAVIMREVLVAL--KFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVA- 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKmlhRSWM---PVrWMSKEAIEQGRFSEA-SDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVANRHllecP 799
Cdd:cd06917 149 ASLNQNSSK---RSTFvgtPY-WMAPEVITEGKYYDTkADIWSLGITTYEM-ATGNPPYSDVDALRAVMLIPKSK----P 219
                       250       260       270
                ....*....|....*....|....*....|...
gi 71980965 800 HNCPTNIYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd06917 220 PRLEGNGYSpllkeFVAACLDEEPKDRLSADEL 252
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
563-840 1.01e-17

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 83.98  E-value: 1.01e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd08530   1 DFKVLKKLGKGSYGSVYKVKRLS-----DNQVYALKEVNlGSLSQKEREDSVNEIRLLASVNHPNIIRYKEAFLDGNRLC 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELL----KVRVPpadhdmggITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd08530  76 IVMEYAPFGDLSKLIskrkKKRRL--------FPED--DIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIG 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFG--------LMRTSYGSDYYkmlhrswmpvrwMSKEaIEQGR-FSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIE 788
Cdd:cd08530 146 DLGiskvlkknLAKTQIGTPLY------------AAPE-VWKGRpYDYKSDIWSLGCLLYEMATF-RPPFEARTMQELRY 211
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 789 LVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIrsrlqswsLASPA 840
Cdd:cd08530 212 KVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKL--------LQSPA 255
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
562-829 1.13e-17

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: 83.59  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYTSGLfapepMAVAVKKCRHDATNAE--RAQLEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd14073   1 HRYELLETLGKGTYGKVKLAIERATG-----REVAIKSIKKDKIEDEqdMVRIRREIEIMSSLNHPHIIRIYEVFENKDK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd14073  76 IVIVMEYASGGELYDYISER--------RRLPEREARRIF--RQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADF 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GLmrtsygSDYY---KMLHRSWMPVRWMSKEAIE----QGrfsEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELVAN 792
Cdd:cd14073 146 GL------SNLYskdKLLQTFCGSPLYASPEIVNgtpyQG---PEVDCWSLGVLLYTL-VYGTMPFDGSDFKRLVKQISS 215
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 793 RHLLECPHncPTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14073 216 GDYREPTQ--PSDASGLIRWMLTVNPKRRATIEDIAN 250
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
605-827 1.38e-17

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: 83.24  E-value: 1.38e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 605 TNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYIATQI 684
Cdd:cd08220  39 TKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYAPGGTLFEYIQQR--------KGSLLSEEEILHFFVQI 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 685 ALGMEYLASMSFVHRDLATRNCLVGDTRTI-KIADFGLMR---------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRF 754
Cdd:cd08220 111 LLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKilsskskayTVVGTPCY------------ISPELCEGKPY 178
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 755 SEASDVWSFGVTLWEIWSFGRQpYEGASNQQVIelvanRHLLECPHNCPTNIYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd08220 179 NQKSDIWALGCVLYELASLKRA-FEAANLPALV-----LKIMRGTFAPISDRYSeelrhLILSMLHLDPNKRPTLSEI 250
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
614-778 1.59e-17

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 83.85  E-value: 1.59e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEIRAVATFDHPNVIKLIGVC--YMDNSLLAVFEYMVHGDLHELlkvrvpPADHDMggiTEANAEFLYiaTQIALGMEYL 691
Cdd:cd14200  72 QEIAILKKLDHVNIVKLIEVLddPAEDNLYMVFDLLRKGPVMEV------PSDKPF---SEDQARLYF--RDIVLGIEYL 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 692 ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDyyKMLHRSWMPVRWMSKEAIEQGR--FS-EASDVWSFGVTLW 768
Cdd:cd14200 141 HYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGND--ALLSSTAGTPAFMAPETLSDSGqsFSgKALDVWAMGVTLY 218
                       170
                ....*....|
gi 71980965 769 eIWSFGRQPY 778
Cdd:cd14200 219 -CFVYGKCPF 227
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
557-772 1.65e-17

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


Pssm-ID: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 84.66  E-value: 1.65e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPsQLSVREKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKC---RHDaTNAERAQleQEIRAVATFDHPNVIKLIGV 633
Cdd:cd07849   1 FDVGP-RYQNLSYIGEGAYGMVCSAVHK-----PTGQKVAIKKIspfEHQ-TYCLRTL--REIKILLRFKHENIIGILDI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 ------CYMdNSLLAVFEYMvHGDLHELLKVRVPPADHdmggiteaNAEFLYiatQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd07849  72 qrpptfESF-KDVYIVQELM-ETDLYKLIKTQHLSNDH--------IQYFLY---QILRGLKYIHSANVLHRDLKPSNLL 138
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 708 VGDTRTIKIADFGLMR-TSYGSDYYKMLhRSWMPVRWMSKEAI--EQGRFSEASDVWSFGVTLWEIWS 772
Cdd:cd07849 139 LNTNCDLKICDFGLARiADPEHDHTGFL-TEYVATRWYRAPEImlNSKGYTKAIDIWSVGCILAEMLS 205
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
569-783 1.95e-17

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: 83.93  E-value: 1.95e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSG--IYTSGLFapepmaVAVKKCRhdATNAERAQLEQEIRAVA------TFDHPNVIKLIGVCYM---- 636
Cdd:cd07862   8 EIGEGAYGKVFKArdLKNGGRF------VALKRVR--VQTGEEGMPLSTIREVAvlrhleTFEHPNVVRLFDVCTVsrtd 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 -DNSLLAVFEYmVHGDLHELLKvRVPpadhDMGGITEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd07862  80 rETKLTLVFEH-VDQDLTTYLD-KVP----EPGVPTETIKDMMF---QLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIK 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRTsYGsdyYKMLHRSWMPVRWM-SKEAIEQGRFSEASDVWSFGVTLWEIwsFGRQP-YEGASN 783
Cdd:cd07862 151 LADFGLARI-YS---FQMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAEM--FRRKPlFRGSSD 214
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
565-827 2.55e-17

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 82.70  E-value: 2.55e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 565 SVREKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCR-HDATNAE-RAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd08224   3 EIEKKIGKGQFSVVYRARCL-----LDGRLVALKKVQiFEMMDAKaRQDCLKEIDLLQQLNHPNIIKYLASFIENNELNI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRVppadHDMGGITEANAEFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd08224  78 VLELADAGDLSRLIKHFK----KQKRLIPERTIWKYFV--QLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLG 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 723 R----------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGaSNQQVIELVAN 792
Cdd:cd08224 152 RffsskttaahSLVGTPYY------------MSPERIREQGYDFKSDIWSLGCLLYEMAAL-QSPFYG-EKMNLYSLCKK 217
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 793 RHLLECPhNCPTNIYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd08224 218 IEKCEYP-PLPADLYSqelrdLVAACIQPDPEKRPDISYV 256
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
570-827 3.04e-17

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


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 82.45  E-value: 3.04e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd14663   8 LGEGTFAKVKFARNTK---TGESVAIKIIDKEQVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMELVTG 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKvrvppadhDMGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSD 729
Cdd:cd14663  85 GELFSKIA--------KNGRLKEDKARKYF--QQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFR 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 730 YYKMLHRSWMPVRWMSKEAIEQ-GRFSEASDVWSFGVTLWEIWSfGRQPYEgASNQQVIELVANRHLLECPHNCPTNIYS 808
Cdd:cd14663 155 QDGLLHTTCGTPNYVAPEVLARrGYDGAKADIWSCGVILFVLLA-GYLPFD-DENLMALYRKIMKGEFEYPRWFSPGAKS 232
                       250
                ....*....|....*....
gi 71980965 809 LMVECWHENIERRPTFSEI 827
Cdd:cd14663 233 LIKRILDPNPSTRITVEQI 251
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
563-832 3.32e-17

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 82.71  E-value: 3.32e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapepmAVAVKKCRHDATNAERAQL-EQEIRAVATFDHPNVIKLIGVCyMDNSLL 641
Cdd:cd14152   1 QIELGELIGQGRWGKVHRGRWHG--------EVAIRLLEIDGNNQDHLKLfKKEVMNYRQTRHENVVLFMGAC-MHPPHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHG-DLHELlkVRVPPADHDMGGITEanaeflyIATQIALGMEYLASMSFVHRDLATRNCLVgDTRTIKIADFG 720
Cdd:cd14152  72 AIITSFCKGrTLYSF--VRDPKTSLDINKTRQ-------IAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGR------------FSEASDVWSFGVTLWEI----WSFGRQP-----YE 779
Cdd:cd14152 142 LFGISGVVQEGRRENELKLPHDWLCYLAPEIVRemtpgkdedclpFSKAADVYAFGTIWYELqardWPLKNQPaealiWQ 221
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 780 GASNQQVIELVANRHLlecphncPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14152 222 IGSGEGMKQVLTTISL-------GKEVTEILSACWAFDLEERPSFTLLMDMLE 267
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
595-831 4.44e-17

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: 82.24  E-value: 4.44e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCRHDATNAERAQlEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHdmggiTEAN 674
Cdd:cd14044  34 VILKDLKNNEGNFTEKQ-KIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLRDVLNDKISYPDG-----TFMD 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 675 AEF-LYIATQIALGMEYL-ASMSFVHRDLATRNCLVGDTRTIKIADFGLmrtsygsdyykmlhRSWMPVR---WMSKEAI 749
Cdd:cd14044 108 WEFkISVMYDIAKGMSYLhSSKTEVHGRLKSTNCVVDSRMVVKITDFGC--------------NSILPPSkdlWTAPEHL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 750 EQGRFSEASDVWSFGVTLWEIWSFGRQPYEGA---SNQQVIELVANRHL--------LECPHNCPTNIYSLMVECWHENI 818
Cdd:cd14044 174 RQAGTSQKGDVYSYGIIAQEIILRKETFYTAAcsdRKEKIYRVQNPKGMkpfrpdlnLESAGEREREVYGLVKNCWEEDP 253
                       250
                ....*....|...
gi 71980965 819 ERRPTFSEIRSRL 831
Cdd:cd14044 254 EKRPDFKKIENTL 266
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
568-770 5.07e-17

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: 82.55  E-value: 5.07e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGlfapepMAVAVKKCRHDA-TNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd07860   6 EKIGEGTYGVVYKARnKLTG------EVVALKKIRLDTeTEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMvHGDLHELLKVrVPPADHDMGGITEanaeFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtS 725
Cdd:cd07860  80 FL-HQDLKKFMDA-SALTGIPLPLIKS----YLF---QLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLAR-A 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 726 YGsdyykmlhrswMPVR---------WMSKEAIEQG--RFSEASDVWSFGVTLWEI 770
Cdd:cd07860 150 FG-----------VPVRtythevvtlWYRAPEILLGckYYSTAVDIWSLGCIFAEM 194
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
570-832 6.96e-17

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: 82.18  E-value: 6.96e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLFApepmavaVKKCRHDAT---NAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14159   1 IGEGGFGCVYQAVMRNTEYA-------VKRLKEDSEldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGNYCLIYVY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELL--KVRVPPAdhdmggiteANAEFLYIATQIALGMEYL--ASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd14159  74 LPNGSLEDRLhcQVSCPCL---------SWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPKLGDFGLA 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 723 R----TSYGSDYYKMLHRSwmPVR----WMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYE--------------- 779
Cdd:cd14159 145 RfsrrPKQPGMSSTLARTQ--TVRgtlaYLPEEYVKTGTLSVEIDVYSFGVVLLELLT-GRRAMEvdscsptkylkdlvk 221
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 780 --------------GASNQ--QVIELVANRHL----LECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14159 222 eeeeaqhtpttmthSAEAQaaQLATSICQKHLdpqaGPCPPELGIEISQLACRCLHRRAKKRPPMTEVFQELE 294
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
568-772 7.87e-17

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: 81.70  E-value: 7.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIY-TSGLFapepmaVAVKKCRHDA------TNAERaqleqEIRAVATFDHPNVIKLIGVCYMDNSL 640
Cdd:cd07861   6 EKIGEGTYGVVYKGRNkKTGQI------VAMKKIRLESeeegvpSTAIR-----EISLLKELQHPNIVCLEDVLMQENRL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHgDLHELLKVRvpPADHDMGgiTEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd07861  75 YLVFEFLSM-DLKKYLDSL--PKGKYMD--AELVKSYLY---QILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFG 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 721 LMRtSYGsdyykmlhrswMPVRWMSKEAIE-----------QGRFSEASDVWSFGVTLWEIWS 772
Cdd:cd07861 147 LAR-AFG-----------IPVRVYTHEVVTlwyrapevllgSPRYSTPVDIWSIGTIFAEMAT 197
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
568-777 8.28e-17

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: 81.33  E-value: 8.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLFapepmaVAVKKCRHDATNAERAQ-----LEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd06631   7 NVLGKGAYGTVYCGLTSTGQL------IAVKQVELDTSDKEKAEkeyekLQEEVDLLKTLKHVNIVGYLGTCLEDNVVSI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKvRVPPADHDMggiteanaeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG-- 720
Cdd:cd06631  81 FMEFVPGGSIASILA-RFGALEEPV---------FCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGca 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 721 -----LMRTSYGSDYYKMLHRSwmPVrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfgRQP 777
Cdd:cd06631 151 krlciNLSSGSQSQLLKSMRGT--PY-WMAPEVINETGHGRKSDIWSIGCTVFEMAT--GKP 207
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
568-790 9.28e-17

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


Pssm-ID: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 82.41  E-value: 9.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYT-SGlfapepMAVAVKKCRH---DATNAERAQleQEIRAVATFDHPNVIKLIG-----VCYMD- 637
Cdd:cd07855  11 ETIGSGAYGVVCSAIDTkSG------QKVAIKKIPNafdVVTTAKRTL--RELKILRHFKHDNIIAIRDilrpkVPYADf 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMvHGDLHELLkvrvppadHDMGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd07855  83 KDVYVVLDLM-ESDLHHII--------HSDQPLTLEHIRyFLY---QLLRGLKYIHSANVIHRDLKPSNLLVNENCELKI 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMR-TSYGSDYYKMLHRSWMPVRWMskEAIE----QGRFSEASDVWSFGVTLWEIwsFGRQP-YEGASNQQVIELV 790
Cdd:cd07855 151 GDFGMARgLCTSPEEHKYFMTEYVATRWY--RAPElmlsLPEYTQAIDMWSVGCIFAEM--LGRRQlFPGKNYVHQLQLI 226
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
606-827 9.42e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 83.91  E-value: 9.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  606 NAER--AQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLH----ELLKVRVPPADHDMGgiteanaeFLY 679
Cdd:PTZ00267 104 NDERqaAYARSELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGDLNkqikQRLKEHLPFQEYEVG--------LLF 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  680 IatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR-----------TSY-GSDYYkmlhrswmpvrwMSKE 747
Cdd:PTZ00267 176 Y--QIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKqysdsvsldvaSSFcGTPYY------------LAPE 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  748 AIEQGRFSEASDVWSFGVTLWEIWSFGRqPYEGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:PTZ00267 242 LWERKRYSKKADMWSLGVILYELLTLHR-PFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRPTTQQL 320
I-set pfam07679
Immunoglobulin I-set domain;
13-101 1.12e-16

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 75.76  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    13 RLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAAS 92
Cdd:pfam07679   2 KFTQKPKDVEVQEGESARFTCTVTGTPDPEVSWFKDGQPLRSSDRFKVTYEGGTYTLTISNVQPDDSGKYTCVATNSAGE 81

                  ....*....
gi 71980965    93 VNTTSVLRV 101
Cdd:pfam07679  82 AEASAELTV 90
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
568-792 1.28e-16

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


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 81.59  E-value: 1.28e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIY-TSGlfapepMAVAVKKC-RHDATNAERAQLEQEIRAVATFDHPNVIKLI-------------- 631
Cdd:cd07866  14 GKLGEGTFGEVYKARQiKTG------RVVALKKIlMHNEKDGFPITALREIKILKKLKHPNVVPLIdmaverpdkskrkr 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 GVCYMdnsllaVFEYMVHgDLHELL---KVRVPPADHDMggiteanaeflyIATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd07866  88 GSVYM------VTPYMDH-DLSGLLenpSVKLTESQIKC------------YMLQLLEGINYLHENHILHRDIKAANILI 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 GDTRTIKIADFGLMRTSYGSDY-----YKMLHRSWMPV---RWMSKEAIEQG--RFSEASDVWSFGVTLWEIwsFGRQP- 777
Cdd:cd07866 149 DNQGILKIADFGLARPYDGPPPnpkggGGGGTRKYTNLvvtRWYRPPELLLGerRYTTAVDIWGIGCVFAEM--FTRRPi 226
                       250
                ....*....|....*
gi 71980965 778 YEGASNQQVIELVAN 792
Cdd:cd07866 227 LQGKSDIDQLHLIFK 241
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
568-769 1.49e-16

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 80.43  E-value: 1.49e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDATNaERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd06613   6 QRIGSGTYGDVYKArnIATGEL-------AAVKVIKLEPGD-DFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVME 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVrvppadhdMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM--- 722
Cdd:cd06613  78 YCGGGSLQDIYQV--------TGPLSEL--QIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSaql 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 723 ------RTSY-GSDYykmlhrswmpvrWMSKEAIE---QGRFSEASDVWSFGVTLWE 769
Cdd:cd06613 148 tatiakRKSFiGTPY------------WMAPEVAAverKGGYDGKCDIWALGITAIE 192
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
570-785 1.63e-16

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


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 80.00  E-value: 1.63e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTS-GLfapepmAVAVKKCRHDATNaeRAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd14006   1 LGRGRFGVVKRCIEKAtGR------EFAAKFIPKRDKK--KEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLkvrvppADHDMggITEANAEFlYIaTQIALGMEYLASMSFVHRDLATRNCLVGDTR--TIKIADFGLMRTSY 726
Cdd:cd14006  73 GGELLDRL------AERGS--LSEEEVRT-YM-RQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKLN 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 727 GSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQ 785
Cdd:cd14006 143 PGEELKEIFGT---PEFVAPEIVNGEPVSLATDMWSIGVLTYVLLS-GLSPFLGEDDQE 197
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
624-827 1.66e-16

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: 80.38  E-value: 1.66e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 624 HPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppADHDMGGITEAnaefLYIATQIALGMEYLASMSFVHRDLAT 703
Cdd:cd05078  62 HKHLVLNYGVCVCGDENILVQEYVKFGSLDTYLK-----KNKNCINILWK----LEVAKQLAWAMHFLEEKTLVHGNVCA 132
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 704 RNCLV--------GDTRTIKIADFGLMRTSYGSDYykMLHRswmpVRWMSKEAIEQGR-FSEASDVWSFGVTLWEIWSFG 774
Cdd:cd05078 133 KNILLireedrktGNPPFIKLSDPGISITVLPKDI--LLER----IPWVPPECIENPKnLSLATDKWSFGTTLWEICSGG 206
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 775 RQPYEGASNQQVIELVANRHLLECPHncPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05078 207 DKPLSALDSQRKLQFYEDRHQLPAPK--WTELANLINNCMDYEPDHRPSFRAI 257
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
569-800 2.89e-16

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: 80.49  E-value: 2.89e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSG-IYTSGlfapepMAVAVKKCRHDAtnaERAQLE----QEIRAVATFDHPNVIKLIGVCYMD--NSLL 641
Cdd:cd07845  14 RIGEGTYGIVYRArDTTSG------EIVALKKVRMDN---ERDGIPisslREITLLLNLRHPNIVELKEVVVGKhlDSIF 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHgDLHELLkvrvppaDHDMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd07845  85 LVMEYCEQ-DLASLL-------DNMPTPFSES--QVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRTsYGSDYYKMLHRswMPVRWMSKEAIEQG--RFSEASDVWSFGVTLWEIwsFGRQP-YEGASNQQVIELVANrhLLEC 798
Cdd:cd07845 155 ART-YGLPAKPMTPK--VVTLWYRAPELLLGctTYTTAIDMWAVGCILAEL--LAHKPlLPGKSEIEQLDLIIQ--LLGT 227

                ..
gi 71980965 799 PH 800
Cdd:cd07845 228 PN 229
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
570-827 3.83e-16

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 79.79  E-value: 3.83e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIY-TSGLFApepmavAVKKCRhdaTNAErAQLEQ---EIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd06611  13 LGDGAFGKVYKAQHkETGLFA------AAKIIQ---IESE-EELEDfmvEIDILSECKHPNIVGLYEAYFYENKLWILIE 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLkvrvppaDHDMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL---- 721
Cdd:cd06611  83 FCDGGALDSIM-------LELERGLTEP--QIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVsakn 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 -----MRTSY-GSDYykmlhrswmpvrWMSKEAIEQGRFSEA-----SDVWSFGVTLWEIwSFGRQPYEGASNQQVIELV 790
Cdd:cd06611 154 kstlqKRDTFiGTPY------------WMAPEVVACETFKDNpydykADIWSLGITLIEL-AQMEPPHHELNPMRVLLKI 220
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 791 ANRH--LLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06611 221 LKSEppTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAEL 259
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
570-790 4.31e-16

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: 78.97  E-value: 4.31e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapEPMAVAVK---KCRHDATNAERAQleQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14071   8 IGKGNFAVVKLARHRI-----TKTEVAIKiidKSQLDEENLKKIY--REVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLkvrvppADHdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLmrtsy 726
Cdd:cd14071  81 ASNGEIFDYL------AQH--GRMSEKEARKKF--WQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGF----- 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 727 gSDYYK--MLHRSWM---PvrWMSKEAIEQGRFSEAS-DVWSFGVTLWeIWSFGRQPYEGASNQQVIELV 790
Cdd:cd14071 146 -SNFFKpgELLKTWCgspP--YAAPEVFEGKEYEGPQlDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRV 211
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
568-771 4.48e-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: 79.26  E-value: 4.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVH------SGIYtsglfapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd13996  12 ELLGSGGFGSVYkvrnkvDGVT-----------YAIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLkvrvppadhDMGGITEANAEFLY--IATQIALGMEYLASMSFVHRDLATRNCLV-GDTRTIKIAD 718
Cdd:cd13996  81 IQMELCEGGTLRDWI---------DRRNSSSKNDRKLAleLFKQILKGVSYIHSKGIVHRDLKPSNIFLdNDDLQVKIGD 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 719 FGLMR-------TSYGSDYYKMLHRSWMPVR-----WMSKEAIEQGRFSEASDVWSFGVTLWEIW 771
Cdd:cd13996 152 FGLATsignqkrELNNLNNNNNGNTSNNSVGigtplYASPEQLDGENYNEKADIYSLGIILFEML 216
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
570-770 5.04e-16

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: 78.94  E-value: 5.04e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH------SGiytsglfapepMAVAVKKCRHDATNAERA----QLEQEIRAVATFDHPNVIKLIGvCYMDNS 639
Cdd:cd06625   8 LGQGAFGQVYlcydadTG-----------RELAVKQVEIDPINTEASkevkALECEIQLLKNLQHERIVQYYG-CLQDEK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVF-EYMVHGDLHELLKvrvppadhDMGGITEANAEfLYiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd06625  76 SLSIFmEYMPGGSVKDEIK--------AYGALTENVTR-KY-TRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGD 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 719 FG------------LMRTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06625 146 FGaskrlqticsstGMKSVTGTPY------------WMSPEVINGEGYGRKADIWSVGCTVVEM 197
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
570-779 7.55e-16

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


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 78.68  E-value: 7.55e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHD--ATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14076   9 LGEGEFGKVKLGWPLPKANHRSGVQVAIKLIRRDtqQENCQTSKIMREINILKGLTHPNIVRLLDVLKTKKYIGIVLEFV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG------- 720
Cdd:cd14076  89 SGGELFDYILAR--------RRLKDSVACRLF--AQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGfantfdh 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 721 ----LMRTSYGSDYYKmlhrswMPVRWMSKEAIEqGRfseASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd14076 159 fngdLMSTSCGSPCYA------APELVVSDSMYA-GR---KADIWSCGVILYAMLA-GYLPFD 210
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
568-724 1.08e-15

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: 78.37  E-value: 1.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDATN------AERaqleqEIRAVATFDHPNVIKLIGVCYMD-- 637
Cdd:cd07840   5 AQIGEGTYGQVYKArnKKTGEL-------VALKKIRMENEKegfpitAIR-----EIKLLQKLDHPNVVRLKEIVTSKgs 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 ----NSLLAVFEYMVHgDLHELLkvrvppaDHDMGGITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd07840  73 akykGSIYMVFEYMDH-DLTGLL-------DNPEVKFTESQIKC--YMKQLLEGLQYLHSNGILHRDIKGSNILINNDGV 142
                       170
                ....*....|.
gi 71980965 714 IKIADFGLMRT 724
Cdd:cd07840 143 LKLADFGLARP 153
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
558-827 1.11e-15

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 78.53  E-value: 1.11e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQL-SVREKIGEGQFGVVHSGIytsglfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd06644   7 DLDPNEVwEIIGELGDGAFGKVYKAK------NKETGALAAAKVIETKSEEELEDYMVEIEILATCNHPYIVKLLGAFYW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLkvrvppADHDMGgITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd06644  81 DGKLWIMIEFCPGGAVDAIM------LELDRG-LTEP--QIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGL---------MRTSY-GSDYykmlhrsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQV 786
Cdd:cd06644 152 ADFGVsaknvktlqRRDSFiGTPY-------WMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQI-EPPHHELNPMRV 223
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 71980965 787 IELVANRH--LLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06644 224 LLKIAKSEppTLSQPSKWSMEFRDFLKTALDKHPETRPSAAQL 266
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
568-827 1.22e-15

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


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 77.42  E-value: 1.22e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSgiytsglfAPEPM---AVAVKKCRHD-ATNAERAQLEQEIRAVATF-DHPNVIKLIGVCYMDNSLLA 642
Cdd:cd13997   6 EQIGSGSFSEVFK--------VRSKVdgcLYAVKKSKKPfRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGHLYI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRVPpadhdMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd13997  78 QMELCENGSLQDALEELSP-----ISKLSEA--EVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 723 RTsygsdyykmLHRSWM----PVRWMSKEAI-EQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRhLLE 797
Cdd:cd13997 151 TR---------LETSGDveegDSRYLAPELLnENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQWQQLRQGKLPL-PPG 220
                       250       260       270
                ....*....|....*....|....*....|
gi 71980965 798 CPHNcpTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd13997 221 LVLS--QELTRLLKVMLDPDPTRRPTADQL 248
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
561-827 1.23e-15

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: 78.17  E-value: 1.23e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 561 PSQLSVR-EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd06640   2 PEELFTKlERIGKGSFGEVFKGIDNR-----TQQVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKGTK 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLkvRVPPADhdmggiteanaEFlYIAT---QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd06640  77 LWIIMEYLGGGSALDLL--RAGPFD-----------EF-QIATmlkEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKL 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLM----------RTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQV 786
Cdd:cd06640 143 ADFGVAgqltdtqikrNTFVGTPF------------WMAPEVIQQSAYDSKADIWSLGITAIEL-AKGEPPNSDMHPMRV 209
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 787 IELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06640 210 LFLIPKNNPPTLVGDFSKPFKEFIDACLNKDPSFRPTAKEL 250
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
569-770 1.36e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 78.54  E-value: 1.36e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHsgiYTSGLFAPEpmAVAVKKCRHDA--TNAERAQLEQEIRAVATFDHPNVIKLIGvCYM-DNSLLAVFE 645
Cdd:cd06633  28 EIGHGSFGAVY---FATNSHTNE--VVAIKKMSYSGkqTNEKWQDIIKEVKFLQQLKHPNTIEYKG-CYLkDHTAWLVME 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVhGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGlmRTS 725
Cdd:cd06633 102 YCL-GSASDLLEVHKKPLQE---------VEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG--SAS 169
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 726 YGSDYYKMLHRSWmpvrWMSKE---AIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06633 170 IASPANSFVGTPY----WMAPEvilAMDEGQYDGKVDIWSLGITCIEL 213
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
569-777 1.76e-15

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


Pssm-ID: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 78.08  E-value: 1.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGI-YTSGLFapepmaVAVKKCRhdATNAERAQLEQEIRAVA------TFDHPNVIKLIGVCYM----- 636
Cdd:cd07863   7 EIGVGAYGTVYKARdPHSGHF------VALKSVR--VQTNEDGLPLSTVREVAllkrleAFDHPNIVRLMDVCATsrtdr 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYmVHGDLHELLKvRVPPADHDMGGITEANAEFLYiatqialGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd07863  79 ETKVTLVFEH-VDQDLRTYLD-KVPPPGLPAETIKDLMRQFLR-------GLDFLHANCIVHRDLKPENILVTSGGQVKL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 717 ADFGLMRT-SYGSDYYKMLHRSWmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIwsFGRQP 777
Cdd:cd07863 150 ADFGLARIySCQMALTPVVVTLW----YRAPEVLLQSTYATPVDMWSVGCIFAEM--FRRKP 205
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
563-786 2.31e-15

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: 77.36  E-value: 2.31e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd14201   7 EYSRKDLVGHGAFAVVFKGRHRK----KTDWEVAIKSINKKNLSKSQILLGKEIKILKELQHENIVALYDVQEMPNSVFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRvppadhdmGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTR--------- 712
Cdd:cd14201  83 VMEYCNGGDLADYLQAK--------GTLSEDTIRvFLQ---QIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgi 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 713 TIKIADFGLMRTSYGSDYYKMLHRSWMpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQV 786
Cdd:cd14201 152 RIKIADFGFARYLQSNMMAATLCGSPM---YMAPEVIMSQHYDAKADLWSIGTVIYQCL-VGKPPFQANSPQDL 221
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
573-827 2.71e-15

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 76.76  E-value: 2.71e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 573 GQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERaQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDL 652
Cdd:cd14057   1 TKINETHSGELWKGRWQGNDIVAKILKVRDVTTRISR-DFNEEYPRLRIFSHPNVLPVLGACNSPPNLVVISQYMPYGSL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 653 HELLkvrvppadHDMGGITEANAEFLYIATQIALGMEYLASMS--FVHRDLATRNCLVGDTRTIKIaDFGLMRTSYgSDY 730
Cdd:cd14057  80 YNVL--------HEGTGVVVDQSQAVKFALDIARGMAFLHTLEplIPRHHLNSKHVMIDEDMTARI-NMADVKFSF-QEP 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 731 YKMLHRSWMPVRWMSKEAIEQGRfsEASDVWSFGVTLWEIWSfgRQ-PYEGASNQQVIELVANRHL-LECPHNCPTNIYS 808
Cdd:cd14057 150 GKMYNPAWMAPEALQKKPEDINR--RSADMWSFAILLWELVT--REvPFADLSNMEIGMKIALEGLrVTIPPGISPHMCK 225
                       250
                ....*....|....*....
gi 71980965 809 LMVECWHENIERRPTFSEI 827
Cdd:cd14057 226 LMKICMNEDPGKRPKFDMI 244
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
569-827 2.76e-15

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: 76.84  E-value: 2.76e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSglfAPEPMAVAVKKCrhDATNAERAQLEQ----EIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd14080   7 TIGEGSYSKVKLAEYTK---SGLKEKVACKII--DKKKAPKDFLEKflprELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT 724
Cdd:cd14080  82 EYAEHGDLLEYIQKR--------GALSESQARIWF--RQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 725 sYGSDYYKMLhrswmpvrwmSK--------EAIE--QGR--FSEASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELVAN 792
Cdd:cd14080 152 -CPDDDGDVL----------SKtfcgsaayAAPEilQGIpyDPKKYDIWSLGVILY-IMLCGSMPFDDSNIKKMLKDQQN 219
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71980965 793 RHLlecphNCPTNIYSLMVEC-------WHENIERRPTFSEI 827
Cdd:cd14080 220 RKV-----RFPSSVKKLSPECkdlidqlLEPDPTKRATIEEI 256
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
544-778 2.93e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 78.33  E-value: 2.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  544 PSQEPIDDNSYKVFEITPSQLSVRE-----KIGEGQFGVVHSGIYTSglfAPEPMAVAVKKCRHDatNAERAQLEQEIRA 618
Cdd:PLN00034  51 SSSSSSSSSSSASGSAPSAAKSLSElervnRIGSGAGGTVYKVIHRP---TGRLYALKVIYGNHE--DTVRRQICREIEI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  619 VATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHellkvrvppadhdmgGITEANAEFLY-IATQIALGMEYLASMSFV 697
Cdd:PLN00034 126 LRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE---------------GTHIADEQFLAdVARQILSGIAYLHRRHIV 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  698 HRDLATRNCLVGDTRTIKIADFGLMRtsygsdyykMLHRSWMP-------VRWMSKEAI----EQGRFSE-ASDVWSFGV 765
Cdd:PLN00034 191 HRDIKPSNLLINSAKNVKIADFGVSR---------ILAQTMDPcnssvgtIAYMSPERIntdlNHGAYDGyAGDIWSLGV 261
                        250
                 ....*....|...
gi 71980965  766 TLWEIWsFGRQPY 778
Cdd:PLN00034 262 SILEFY-LGRFPF 273
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
549-790 3.03e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 77.98  E-value: 3.03e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 549 IDDNSYKVFEItpsqlsvREKIGEGQFGVVHSGI-YTSGlfapepMAVAVKKCrHDA----TNAERAQLE----QEIRav 619
Cdd:cd07852   1 IDKHILRRYEI-------LKKLGKGAYGIVWKAIdKKTG------EVVALKKI-FDAfrnaTDAQRTFREimflQELN-- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 620 atfDHPNVIKLIGVCYMDNS--LLAVFEYMvHGDLHELLKVRVPPADHDMggiteanaeflYIATQIALGMEYLASMSFV 697
Cdd:cd07852  65 ---DHPNIIKLLNVIRAENDkdIYLVFEYM-ETDLHAVIRANILEDIHKQ-----------YIMYQLLKALKYLHSGGVI 129
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 698 HRDLATRNCLVGDTRTIKIADFGLMRT-SYGSDYYKmlhrswMPV-------RWMSKEAIEQG--RFSEASDVWSFGVTL 767
Cdd:cd07852 130 HRDLKPSNILLNSDCRVKLADFGLARSlSQLEEDDE------NPVltdyvatRWYRAPEILLGstRYTKGVDMWSVGCIL 203
                       250       260
                ....*....|....*....|....*.
gi 71980965 768 WEIwsFGRQP-YEGAS--NQqvIELV 790
Cdd:cd07852 204 GEM--LLGKPlFPGTStlNQ--LEKI 225
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
568-830 4.53e-15

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: 76.15  E-value: 4.53e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGvvhsGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd08225   6 KKIGEGSFG----KIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRvppadhdmGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNC-LVGDTRTIKIADFG------ 720
Cdd:cd08225  82 DGGDLMKRINRQ--------RGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIfLSKNGMVAKLGDFGiarqln 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 ----LMRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIELVANRHLL 796
Cdd:cd08225 154 dsmeLAYTCVGTPYY------------LSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLHQLVLKICQGYFA 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 71980965 797 ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSR 830
Cdd:cd08225 221 PISPNFSRDLRSLISQLFKVSPRDRPSITSILKR 254
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
570-806 4.57e-15

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: 75.87  E-value: 4.57e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTsglfAPEPMAVAVKkCRHDaTNAERAQ--LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14120   1 IGHGAFAVVFKGRHR----KKPDLPVAIK-CITK-KNLSKSQnlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYC 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLkvrvppadHDMGGITEAN-AEFLyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTR---------TIKIA 717
Cdd:cd14120  75 NGGDLADYL--------QAKGTLSEDTiRVFL---QQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGLMRTSYGSDYYKMLHRSWMpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVielvanRHLLE 797
Cdd:cd14120 144 DFGFARFLQDGMMAATLCGSPM---YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQEL------KAFYE 213

                ....*....
gi 71980965 798 CPHNCPTNI 806
Cdd:cd14120 214 KNANLRPNI 222
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
568-764 6.15e-15

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: 76.17  E-value: 6.15e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDA------TNAERaqleqEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd07835   5 EKIGEGTYGVVYKArdKLTGEI-------VALKKIRLETedegvpSTAIR-----EISLLKELNHPNIVRLLDVVHSENK 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYmVHGDLHELL-KVRVPPADHDMggiteaNAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd07835  73 LYLVFEF-LDLDLKKYMdSSPLTGLDPPL------IKSYLY---QLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLAD 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 719 FGLMRtSYGsdyykmlhrswMPVRWMSKEAIE-----------QGRFSEASDVWSFG 764
Cdd:cd07835 143 FGLAR-AFG-----------VPVRTYTHEVVTlwyrapeillgSKHYSTPVDIWSVG 187
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
558-827 8.97e-15

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: 75.55  E-value: 8.97e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVhsgiyTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd06620   1 DLKNQDLETLKDLGAGNGGSV-----SKVLHIPTGTIMAKKVIHIDAKSSVRKQILRELQILHECHSPYIVSFYGAFLNE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 -NSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEflyiatqialGMEYLASM-SFVHRDLATRNCLVGDTRTIK 715
Cdd:cd06620  76 nNNIIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLE----------GLTYLYNVhRIIHRDIKPSNILVNSKGQIK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMR--------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEI------WSFGRQPYEGA 781
Cdd:cd06620 146 LCDFGVSGelinsiadTFVGTSTY------------MSPERIQGGKYSVKSDVWSLGLSIIELalgefpFAGSNDDDDGY 213
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 782 SNQQVIELVANRHLLECPHNCPTN-IYS----LMVE-CWHENIERRPTFSEI 827
Cdd:cd06620 214 NGPMGILDLLQRIVNEPPPRLPKDrIFPkdlrDFVDrCLLKDPRERPSPQLL 265
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
566-792 1.81e-14

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 74.51  E-value: 1.81e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSglfAPEPMAVAVKKCRhdatNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14104   4 IAEELGRGQFGIVHRCVETS---SKKTYMAKFVKVK----GADQVLVKKEISILNIARHRNILRLHESFESHEELVMIFE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLkvrvppADHDMgGITEanAEFLYIATQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIADFGLMR 723
Cdd:cd14104  77 FISGVDIFERI------TTARF-ELNE--REIVSYVRQVCEALEFLHSKNIGHFDIRPENiiYCTRRGSYIKIIEFGQSR 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 724 TSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVAN 792
Cdd:cd14104 148 QLKPGDKFRLQYTS---AEFYAPEVHQHESVSTATDMWSLGCLVYVLLS-GINPFEAETNQQTIENIRN 212
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
568-770 1.82e-14

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: 74.66  E-value: 1.82e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVhsgiytsgLFAPE---PMAVAVK--KCRHDATNAERAQLeQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd07833   7 GVVGEGAYGVV--------LKCRNkatGEIVAIKkfKESEDDEDVKKTAL-REVKVLRQLRHENIVNLKEAFRRKGRLYL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYmVHGDLHELLKVR---VPPAdhdmggiteanAEFLYIaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd07833  78 VFEY-VERTLLELLEASpggLPPD-----------AVRSYI-WQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDF 144
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 720 GLMR--TSYGSDYYKmlhrSWMPVRWMSKEAIEQG--RFSEASDVWSFGVTLWEI 770
Cdd:cd07833 145 GFARalTARPASPLT----DYVATRWYRAPELLVGdtNYGKPVDVWAIGCIMAEL 195
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
570-833 2.01e-14

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 74.22  E-value: 2.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYtsglfapEPMAVAVKKCRHDATNAeraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLlaVFEYMVH 649
Cdd:cd14068   2 LGDGGFGSVYRAVY-------RGEDVAVKIFNKHTSFR---LLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLHELLKvrvppadHDMGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRT-----IKIADFGL--- 721
Cdd:cd14068  70 GSLDALLQ-------QDNASLTRTLQH--RIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYPncaiiAKIADYGIaqy 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 -----MRTSYGSDYYKmlhrswmpvrwmskeAIEQGR----FSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVAN 792
Cdd:cd14068 141 ccrmgIKTSEGTPGFR---------------APEVARgnviYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAI 205
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 793 RHLLECP---HNCP--TNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14068 206 QGKLPDPvkeYGCApwPGVEALIKDCLKENPQCRPTSAQVFDILNS 251
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
568-833 2.40e-14

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: 74.71  E-value: 2.40e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDAtnaeRAQLEQEIRAVATFDHPNVIKLIGVC---YMDNSL--LA 642
Cdd:cd14054   1 QLIGQGRYGTVWKGSLDE-----RPVAVKVFPARHRQ----NFQNEKDIYELPLMEHSNILRFIGADerpTADGRMeyLL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRvppadhdmggiTEANAEFLYIATQIALGMEYLASM---------SFVHRDLATRNCLVGDTRT 713
Cdd:cd14054  72 VLEYAPKGSLCSYLREN-----------TLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGS 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGL-MRTSYGSDYYKMLH----RSWMPV---RWMSKEAIEQG---RFSEAS----DVWSFGVTLWEIW------S 772
Cdd:cd14054 141 CVICDFGLaMVLRGSSLVRGRPGaaenASISEVgtlRYMAPEVLEGAvnlRDCESAlkqvDVYALGLVLWEIAmrcsdlY 220
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 773 FGRQ------PYE---GA--SNQQVIELVAnRHLL--------ECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14054 221 PGESvppyqmPYEaelGNhpTFEDMQLLVS-REKArpkfpdawKENSLAVRSLKETIEDCWDQDAEARLTALCVEERLAE 299
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
563-832 2.56e-14

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: 74.27  E-value: 2.56e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapepmAVAVKKCRHDATNAERAQ-LEQEIRAVATFDHPNVIKLIGVCyMDNSLL 641
Cdd:cd14153   1 QLEIGELIGKGRFGQVYHGRWHG--------EVAIRLIDIERDNEEQLKaFKREVMAYRQTRHENVVLFMGAC-MSPPHL 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHG-DLHELLKvrvppadhDMGGITEANaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVgDTRTIKIADFG 720
Cdd:cd14153  72 AIITSLCKGrTLYSVVR--------DAKVVLDVN-KTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTS----YGSDYYKM-LHRSWM----P--VRWMSKEAIE-QGRFSEASDVWSFGVTLWEI----WSFGRQPYEGASNQ 784
Cdd:cd14153 142 LFTISgvlqAGRREDKLrIQSGWLchlaPeiIRQLSPETEEdKLPFSKHSDVFAFGTIWYELhareWPFKTQPAEAIIWQ 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 785 QVIELVANRHLLecphNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14153 222 VGSGMKPNLSQI----GMGKEISDILLFCWAYEQEERPTFSKLMEMLE 265
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
29-98 2.68e-14

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 68.51  E-value: 2.68e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  29 VRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSV 98
Cdd:cd00096   1 VTLTCSASGNPPPTITWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVASNSAGGSASASV 70
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
567-770 3.75e-14

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 73.25  E-value: 3.75e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 567 REkIGEGQFGVVHsgiYTSGLFAPEpmAVAVKKCRHDATNA-ERAQ-LEQEIRAVATFDHPNVIKLIGvCYM-DNSLLAV 643
Cdd:cd06607   7 RE-IGHGSFGAVY---YARNKRTSE--VVAIKKMSYSGKQStEKWQdIIKEVKFLRQLRHPNTIEYKG-CYLrEHTAWLV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVhGDLHELLKVRVPPADHDmggiteanaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-- 721
Cdd:cd06607  80 MEYCL-GSASDIVEVHKKPLQEV---------EIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSas 149
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 722 ----MRTSYGSDYykmlhrswmpvrWMSKE---AIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06607 150 lvcpANSFVGTPY------------WMAPEvilAMDEGQYDGKVDVWSLGITCIEL 193
PHA02988 PHA02988
hypothetical protein; Provisional
582-831 3.96e-14

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 73.62  E-value: 3.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  582 IYtSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVcYMDNS-----LLAVFEYMVHGDLHELL 656
Cdd:PHA02988  36 IY-KGIFNNKEVIIRTFKKFHKGHKVLIDITENEIKNLRRIDSNNILKIYGF-IIDIVddlprLSLILEYCTRGYLREVL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  657 kvrvppadhDMggitEANAEF---LYIATQIALGMEYL-ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYK 732
Cdd:PHA02988 114 ---------DK----EKDLSFktkLDMAIDCCKGLYNLyKYTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  733 ---MLHRSW-MPVRWMSKEAIEqgrfseaSDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHL-LECPHNCPTNIY 807
Cdd:PHA02988 181 vnfMVYFSYkMLNDIFSEYTIK-------DDIYSLGVVLWEIFT-GKIPFENLTTKEIYDLIINKNNsLKLPLDCPLEIK 252
                        250       260
                 ....*....|....*....|....
gi 71980965  808 SLMVECWHENIERRPTFSEIRSRL 831
Cdd:PHA02988 253 CIVEACTSHDSIKRPNIKEILYNL 276
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
566-793 4.24e-14

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 73.10  E-value: 4.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSglfapEPMAVAVK-KCRHDATNAERAQ-LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd14162   4 VGKTLGHGSYAVVKKAYSTK-----HKCKVAIKiVSKKKAPEDYLQKfLPREIEVIKGLKHPNLICFYEAIETTSRVYII 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd14162  79 MELAENGDLLDYIRKN--------GALPEPQARRWF--RQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSygsdyykmlHRSWMPVRWMSKEAIeqGRFSEA--------------SDVWSFGVTLWEIwSFGRQPYEGASNQQVIEL 789
Cdd:cd14162 149 GV---------MKTKDGKPKLSETYC--GSYAYAspeilrgipydpflSDIWSMGVVLYTM-VYGRLPFDDSNLKVLLKQ 216

                ....
gi 71980965 790 VANR 793
Cdd:cd14162 217 VQRR 220
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
568-791 4.90e-14

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 73.13  E-value: 4.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAE-------------------RAQLEQEIRAVATFDHPNVI 628
Cdd:cd14194  11 EELGSGQFAVV-------------------KKCREKSTGLQyaakfikkrrtkssrrgvsREDIEREVSILKEIQHPNVI 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 629 KLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANA-EFLyiaTQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd14194  72 TLHEVYENKTDVILILELVAGGELFDFLA--------EKESLTEEEAtEFL---KQILNGVYYLHSLQIAHFDLKPENIM 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 708 VGDTRT----IKIADFGLM-RTSYGSDYYKMLHRSwmpvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:cd14194 141 LLDRNVpkprIKIIDFGLAhKIDFGNEFKNIFGTP----EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDT 215

                ....*....
gi 71980965 783 NQQVIELVA 791
Cdd:cd14194 216 KQETLANVS 224
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
568-827 5.90e-14

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: 72.63  E-value: 5.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTS---GLFAPEPMAVAVKKCRHdaTNAERAQLEQEiRAVATFDHPNVIKLIGVCYMDNSLLaVF 644
Cdd:cd14208   5 ESLGKGSFTKIYRGLRTDeedDERCETEVLLKVMDPTH--GNCQESFLEAA-SIMSQISHKHLVLLHGVCVGKDSIM-VQ 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRvppadHDMGGITEANAefLYIATQIALGMEYLASMSFVHRDLATRNCLV---GDTRT---IKIAD 718
Cdd:cd14208  81 EFVCHGALDLYLKKQ-----QQKGPVAISWK--LQVVKQLAYALNYLEDKQLVHGNVSAKKVLLsreGDKGSppfIKLSD 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMrtsygsdyYKMLHRSWMPVR--WMSKEAI-EQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVANRHL 795
Cdd:cd14208 154 PGVS--------IKVLDEELLAERipWVAPECLsDPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQ 225
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 796 LECPHncPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd14208 226 LPAPH--WIELASLIQQCMSYNPLLRPSFRAI 255
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
562-834 7.16e-14

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 72.75  E-value: 7.16e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGiytSGLFAPEPmaVAVKKCR-HDATNAE-RAQLEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd08228   2 ANFQIEKKIGRGQFSEVYRA---TCLLDRKP--VALKKVQiFEMMDAKaRQDCVKEIDLLKQLNHPNVIKYLDSFIEDNE 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLKV-----RVPPadhdmggitEANAEFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd08228  77 LNIVLELADAGDLSQMIKYfkkqkRLIP---------ERTVWKYFV--QLCSAVEHMHSRRVMHRDIKPANVFITATGVV 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGLMRtsYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGaSNQQVIELVANRH 794
Cdd:cd08228 146 KLGDLGLGR--FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEMAAL-QSPFYG-DKMNLFSLCQKIE 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 795 LLECPhNCPTNIYS-----LMVECWHENIERRPTFS---EIRSRLQSW 834
Cdd:cd08228 222 QCDYP-PLPTEHYSeklreLVSMCIYPDPDQRPDIGyvhQIAKQMHVW 268
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
19-101 7.48e-14

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 67.53  E-value: 7.48e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965     19 RNATKSSGDEVRFKCEALGTPPLKFIWLKNNG-PVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTS 97
Cdd:smart00410   2 PSVTVKEGESVTLSCEASGSPPPEVTWYKQGGkLLAESGRFSVSRSGSTSTLTISNVTPEDSGTYTCAATNSSGSASSGT 81

                   ....
gi 71980965     98 VLRV 101
Cdd:smart00410  82 TLTV 85
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
568-790 7.63e-14

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: 72.84  E-value: 7.63e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfapePMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCY--MDNSLLAVFE 645
Cdd:cd06621   7 SSLGEGAGGSVTKCRLRNT-----KTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLdeQDSSIGIAME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLK-VRvppadhDMGGITEANAeFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG---- 720
Cdd:cd06621  82 YCEGGSLDSIYKkVK------KKGGRIGEKV-LGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGvsge 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 721 ----LMRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPY--EGASNQQVIELV 790
Cdd:cd06621 155 lvnsLAGTFTGTSYY------------MAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFppEGEPPLGPIELL 217
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
569-790 7.90e-14

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 72.58  E-value: 7.90e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSglfapEPMAVAVKK-CRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14097   8 KLGQGSFGVVIEATHKE-----TQTKWAIKKiNREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELC 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRvppadhdmGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLV-------GDTRTIKIADFG 720
Cdd:cd14097  83 EDGELKELLLRK--------GFFSEN--ETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFG 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTSYGSDyYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELV 790
Cdd:cd14097 153 LSVQKYGLG-EDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEI 220
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
570-790 8.50e-14

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: 72.17  E-value: 8.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQ-LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd14072   8 IGKGNFAKVKLARHV-----LTGREVAIKIIDKTQLNPSSLQkLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYAS 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLkvrvppADHDMGGITEANAEFlyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL------- 721
Cdd:cd14072  83 GGEVFDYL------VAHGRMKEKEARAKF----RQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFsneftpg 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 722 --MRTSYGSDYYkmlhrswmpvrwmSKEAIEQGRFSEAS--DVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14072 153 nkLDTFCGSPPY-------------AAPELFQGKKYDGPevDVWSLGVILYTLVS-GSLPFDGQNLKELRERV 211
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
570-780 9.58e-14

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 72.26  E-value: 9.58e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH--SGIYTSGLFApepmavaVKKCRHDATNAERAQ----LEQEIRAVAtfDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd05572   1 LGVGGFGRVElvQLKSKGRTFA-------LKCVKKRHIVQTRQQehifSEKEILEEC--NSPFIVKLYRTFKDKKYLYML 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLkvrvppadHDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd05572  72 MEYCLGGELWTIL--------RDRGLFDEYTARF-YTA-CVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSdyykmlHRSWMPV---RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEG 780
Cdd:cd05572 142 KLGSG------RKTWTFCgtpEYVAPEIILNKGYDFSVDYWSLGILLYELLT-GRPPFGG 194
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
563-830 9.92e-14

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


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 71.93  E-value: 9.92e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFG----VVHsgIYTSGLFAPEpmAVAVKKCRHDATNAERaqleqEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd08219   1 QYNVLRVVGEGSFGrallVQH--VNSDQKYAMK--EIRLPKSSSAVEDSRK-----EAVLLAKMKHPNIVAFKESFEADG 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd08219  72 HLYIVMEYCDGGDLMQKIK--------LQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMR----------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIE 788
Cdd:cd08219 144 FGSARlltspgayacTYVGTPYY------------VPPEIWENMPYNNKSDIWSLGCILYELCTL-KHPFQANSWKNLIL 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71980965 789 LVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSR 830
Cdd:cd08219 211 KVCQGSYKPLPSHYSYELRSLIKQMFKRNPRSRPSATTILSR 252
CRD_TK_ROR1 cd07467
Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) ...
177-306 1.07e-13

Cysteine-rich domain of tyrosine kinase-like orphan receptor 1; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor 1 (Ror1), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143576  Cd Length: 142  Bit Score: 68.91  E-value: 1.07e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 177 GDCVQYRGEACRQYLSNKFVMMtnESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVC-ESDSNNQIV 255
Cdd:cd07467   3 GFCQPYRGIACARFIGNRTIYM--ESLHMQGEIENQITAAFTMIGTSSHLSDKCSQFAIPSLCHYAFPYCdETSGMPKPR 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 256 SICKHDCDVIQNDECPSELALAAQHELVGDTPKalFPLCSRLSS-----TSNCIPV 306
Cdd:cd07467  81 DLCRDECEILENVLCQTEYIFARSNPMILMRLK--LPNCEDLAQpdspeAANCIRI 134
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
566-768 1.18e-13

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 71.92  E-value: 1.18e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYtsglfAPEPMAVAVKKC-RHDATNAERA-QLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd14079   6 LGKTLGVGSFGKVKLAEH-----ELTGHKVAVKILnRQKIKSLDMEeKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-- 721
Cdd:cd14079  81 MEYVSGGELFDYIVQK--------GRLSEDEARRFF--QQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLsn 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 722 -------MRTSYGSDYYKmlhrswmpvrwmSKEAIEqGRF---SEAsDVWSFGVTLW 768
Cdd:cd14079 151 imrdgefLKTSCGSPNYA------------APEVIS-GKLyagPEV-DVWSCGVILY 193
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
570-765 1.20e-13

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: 71.49  E-value: 1.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI-YTSGLFapepMAVAVKKCRHdatNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd14103   1 LGRGKFGTVYRCVeKATGKE----LAAKFIKCRK---AKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVA 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHEllkvRVPPADHDmggITEANAeFLYIaTQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIADFGLMRtSY 726
Cdd:cd14103  74 GGELFE----RVVDDDFE---LTERDC-ILFM-RQICEGVQYMHKQGILHLDLKPENilCVSRTGNQIKIIDFGLAR-KY 143
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 71980965 727 GSDyyKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGV 765
Cdd:cd14103 144 DPD--KKLKVLFGTPEFVAPEVVNYEPISYATDMWSVGV 180
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
562-776 1.37e-13

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 72.21  E-value: 1.37e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSgiytsglfAPEPM---AVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIgvcymdN 638
Cdd:cd14048   6 TDFEPIQCLGRGGFGVVFE--------AKNKVddcNYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYF------N 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLL------------AVFEYMV-----HGDLHELLKVRVPPADHDMGGIteanaefLYIATQIALGMEYLASMSFVHRDL 701
Cdd:cd14048  72 AWLerppegwqekmdEVYLYIQmqlcrKENLKDWMNRRCTMESRELFVC-------LNIFKQIASAVEYLHSKGLIHRDL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 702 ATRNCLVGDTRTIKIADFGLMrTSYGSDYYKMLHRSWMPVR-----------WMSKEAIEQGRFSEASDVWSFGVTLWE- 769
Cdd:cd14048 145 KPSNVFFSLDDVVKVGDFGLV-TAMDQGEPEQTVLTPMPAYakhtgqvgtrlYMSPEQIHGNQYSEKVDIFALGLILFEl 223

                ....*..
gi 71980965 770 IWSFGRQ 776
Cdd:cd14048 224 IYSFSTQ 230
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
568-788 1.38e-13

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: 1.38e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfAPEPMAV-AVKKCRHDATNAEraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14121   1 EKLGSGTYATVYKAYRKSG--AREVVAVkCVSKSSLNKASTE--NLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKVRvppadhdmGGITEANAE-FLyiaTQIALGMEYLASMSFVHRDLATRNCLV--GDTRTIKIADFGLMR 723
Cdd:cd14121  77 CSGGDLSRFIRSR--------RTLPESTVRrFL---QQLASALQFLREHNISHMDLKPQNLLLssRYNPVLKLADFGFAQ 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 724 TSYGSDYYKMLHRSwmPVrWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIE 788
Cdd:cd14121 146 HLKPNDEAHSLRGS--PL-YMAPEMILKKKYDARVDLWSVGVILYECL-FGRAPFASRSFEELEE 206
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
564-790 1.60e-13

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: 71.49  E-value: 1.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHSGIYT-SGLfapePMAVAVKKCRhdaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd14190   6 IHSKEVLGGGKFGKVHTCTEKrTGL----KLAAKVINKQ---NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHEllkvRVPPADHDMggiTEANAefLYIATQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIADFG 720
Cdd:cd14190  79 FMEYVEGGELFE----RIVDEDYHL---TEVDA--MVFVRQICEGIQFMHQMRVLHLDLKPENilCVNRTGHQVKIIDFG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTSYGSDYYKMlhrSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14190 150 LARRYNPREKLKV---NFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLLS-GLSPFLGDDDTETLNNV 215
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
563-768 1.66e-13

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: 71.29  E-value: 1.66e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIY-TSGlfapepMAVAVK---KCRHDATnaERAQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd14082   4 QIFPDEVLGSGQFGIVYGGKHrKTG------RDVAIKvidKLRFPTK--QESQLRNEVAILQQLSHPGVVNLECMFETPE 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMvHGDLHELLkvrvppADHDMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLV---GDTRTIK 715
Cdd:cd14082  76 RVFVVMEKL-HGDMLEMI------LSSEKGRLPERITKFL--VTQILVALRYLHSKNIVHCDLKPENVLLasaEPFPQVK 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 716 IADFGLMRTsYGSdyyKMLHRSWM--PVrWMSKEAIEQGRFSEASDVWSFGVTLW 768
Cdd:cd14082 147 LCDFGFARI-IGE---KSFRRSVVgtPA-YLAPEVLRNKGYNRSLDMWSVGVIIY 196
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
568-788 1.80e-13

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 71.36  E-value: 1.80e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVH------SGIYTSGLFapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd14105  11 EELGSGQFAVVKkcreksTGLEYAAKF------IKKRRSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTDVV 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLkvrvppADHDmgGITEANA-EFLyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRT----IKI 716
Cdd:cd14105  85 LILELVAGGELFDFL------AEKE--SLSEEEAtEFL---KQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKL 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 717 ADFGLMRTSYGSDYYKMLHRSwmPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIE 788
Cdd:cd14105 154 IDFGLAHKIEDGNEFKNIFGT--P-EFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGDTKQETLA 221
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
562-827 1.90e-13

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 71.80  E-value: 1.90e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06622   1 DEIEVLDELGKGNYGSVYKVLHR-----PTGVTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVY 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKvrvppADHDMGGITEANAEFlyIATQIALGMEYLAS-MSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd06622  76 MCMEYMDAGSLDKLYA-----GGVATEGIPEDVLRR--ITYAVVKGLKFLKEeHNIIHRDVKPTNVLVNGNGQVKLCDFG 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 --------LMRTSYGSdyykmlhRSWM-PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVI-ELV 790
Cdd:cd06622 149 vsgnlvasLAKTNIGC-------QSYMaPERIKSGGPNQNPTYTVQSDVWSLGLSILEM-ALGRYPYPPETYANIFaQLS 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71980965 791 ANRHllECPHNCPTNiYS-----LMVECWHENIERRPTFSEI 827
Cdd:cd06622 221 AIVD--GDPPTLPSG-YSddaqdFVAKCLNKIPNRRPTYAQL 259
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
569-827 1.91e-13

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 71.60  E-value: 1.91e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIytsglfAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd06643  12 ELGDGAFGKVYKAQ------NKETGILAAAKVIDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEFCA 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHE-LLKVRVPpadhdmggITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL------ 721
Cdd:cd06643  86 GGAVDAvMLELERP--------LTEP--QIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVsakntr 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 ---MRTSY-GSDYykmlhrsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIELVANRH--L 795
Cdd:cd06643 156 tlqRRDSFiGTPY-------WMAPEVVMCETSKDRPYDYKADVWSLGVTLIEMAQI-EPPHHELNPMRVLLKIAKSEppT 227
                       250       260       270
                ....*....|....*....|....*....|..
gi 71980965 796 LECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06643 228 LAQPSRWSPEFKDFLRKCLEKNVDARWTTSQL 259
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
568-770 2.04e-13

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: 71.68  E-value: 2.04e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFgvvhSGIYTSGLFAPEPMAVAVKKCRHDATNA-ERAQLEQEI---RAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd14052   6 ELIGSGEF----SQVYKVSERVPTGKVYAVKKLKPNYAGAkDRLRRLEEVsilRELTLDGHDNIVQLIDSWEYHGHLYIQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVRVppadhDMGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGlMR 723
Cdd:cd14052  82 TELCENGSLDVFLSELG-----LLGRLDEF--RVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFG-MA 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71980965 724 TSYGSDyyKMLHRSWMPVrWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd14052 154 TVWPLI--RGIEREGDRE-YIAPEILSEHMYDKPADIFSLGLILLEA 197
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
593-770 2.05e-13

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: 71.31  E-value: 2.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 593 MAVA-VKKCRHDATNAERA--QLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppadHDMGG 669
Cdd:cd06630  28 MAVKqVSFCRNSSSEQEEVveAIREEIRMMARLNHPNIVRMLGATQHKSHFNIFVEWMAGGSVASLL--------SKYGA 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 670 ITEaNAEFLYIaTQIALGMEYLASMSFVHRDLATRNCLVGDT-RTIKIADFG----LMRTSYGSDYYK--MLHrswmPVR 742
Cdd:cd06630 100 FSE-NVIINYT-LQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGaaarLASKGTGAGEFQgqLLG----TIA 173
                       170       180
                ....*....|....*....|....*...
gi 71980965 743 WMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06630 174 FMAPEVLRGEQYGRSCDVWSVGCVIIEM 201
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
609-829 2.13e-13

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 71.05  E-value: 2.13e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 609 RAQLEQEIRAVATFDHPNVIKLIGvCYMDNSllavFEYMV-----HGDLHELLKVRvppadhdmGGITEANAEflYIATQ 683
Cdd:cd14099  45 REKLKSEIKIHRSLKHPNIVKFHD-CFEDEE----NVYILlelcsNGSLMELLKRR--------KALTEPEVR--YFMRQ 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 684 IALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM----------RTSYGSDYYkmlhrswmpvrwMSKEAIEQGR 753
Cdd:cd14099 110 ILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAarleydgerkKTLCGTPNY------------IAPEVLEKKK 177
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 754 -FSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVANRHlLECPHNCPTNIY--SLMVECWHENIERRPTFSEIRS 829
Cdd:cd14099 178 gHSFEVDIWSLGVILYTLL-VGKPPFETSDVKETYKRIKKNE-YSFPSHLSISDEakDLIRSMLQPDPTKRPSLDEILS 254
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
568-806 2.19e-13

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 70.90  E-value: 2.19e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYtsgLFAPEPMAVAV-KKCRHDatNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14074   9 ETLGRGHFAVVKLARH---VFTGEKVAVKViDKTKLD--DVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLILEL 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLkvrvppADHDmGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTR-TIKIADFGL---- 721
Cdd:cd14074  84 GDGGDMYDYI------MKHE-NGLNEDLAR--KYFRQIVSAISYCHKLHVVHRDLKPENVVFFEKQgLVKLTDFGFsnkf 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 -----MRTSYGSDYYkmlhrswmpvrwmSKEAIEQGRFSEAS--DVWSFGVTLWEIWSfGRQPYEGASNQQVIElvanrH 794
Cdd:cd14074 155 qpgekLETSCGSLAY-------------SAPEILLGDEYDAPavDIWSLGVILYMLVC-GQPPFQEANDSETLT-----M 215
                       250
                ....*....|..
gi 71980965 795 LLECPHNCPTNI 806
Cdd:cd14074 216 IMDCKYTVPAHV 227
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
569-778 2.33e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 71.18  E-value: 2.33e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIY--TSGLFApepmavaVKKCR-HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd06626   7 KIGEGTFGKVYTAVNldTGELMA-------MKEIRfQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFME 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKvrvppadhdMGGITEANAEFLYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG----L 721
Cdd:cd06626  80 YCQEGTLEELLR---------HGRILDEAVIRVYTL-QLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGsavkL 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRTSYGSDYYKMLHRSWMPVrWMSKEAIEQGRFSE---ASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd06626 150 KNNTTTMAPGEVNSLVGTPA-YMAPEVITGNKGEGhgrAADIWSLGCVVLEMAT-GKRPW 207
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
568-779 2.35e-13

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: 71.32  E-value: 2.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLFAPEPMAVAVKKCRH-DATNAERAQLEQEIRAV------ATFDHPNVIKLIGVCYMDN 638
Cdd:cd14077   7 KTIGAGSMGKVKLAkhIRTGEKCAIKIIPRASNAGLKkEREKRLEKEISRDIRTIreaalsSLLNHPHICRLRDFLRTPN 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd14077  87 HYYMLFEYVDGGQLLDYIISH--------GKLKEKQAR--KFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIID 156
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 719 FGLmrtSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEAS-DVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd14077 157 FGL---SNLYDPRRLLRTFCGSLYFAAPELLQAQPYTGPEvDVWSFGVVLYVLVC-GKVPFD 214
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
570-785 2.55e-13

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: 70.75  E-value: 2.55e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAERAQ--------------LEQEIRAVATFDHPNVIKLIGVCY 635
Cdd:cd14185   8 IGDGNFAVV-------------------KECRHWNENQEYAMkiidksklkgkedmIESEILIIKSLSHPNIVKLFEVYE 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDLHELLKVRVPPADHDMGgiteanaeflYIATQIALGMEYLASMSFVHRDLATRNCLV----GDT 711
Cdd:cd14185  69 TEKEIYLILEYVRGGDLFDAIIESVKFTEHDAA----------LMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKS 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 712 RTIKIADFGLMRTSYGSdyykMLHRSWMPVrWMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQ 785
Cdd:cd14185 139 TTLKLADFGLAKYVTGP----IFTVCGTPT-YVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFRSPERDQ 206
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
623-779 2.72e-13

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: 70.82  E-value: 2.72e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 623 DHPNVIKLIGVCYMDNSLLaVF--EYMVHGDLHELLKVRVppadhdmgGITEANAEflYIATQIALGMEYLASMSFVHRD 700
Cdd:cd13987  48 VHPHIIKTYDVAFETEDYY-VFaqEYAPYGDLFSIIPPQV--------GLPEERVK--RCAAQLASALDFMHSKNLVHRD 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 701 LATRNCLVGDT--RTIKIADFGLMRtSYGSDYYKMLHrsWMPvrWMSKE---AIEQGRFS--EASDVWSFGVTL------ 767
Cdd:cd13987 117 IKPENVLLFDKdcRRVKLCDFGLTR-RVGSTVKRVSG--TIP--YTAPEvceAKKNEGFVvdPSIDVWAFGVLLfccltg 191
                       170
                ....*....|....*
gi 71980965 768 ---WEIWSFGRQPYE 779
Cdd:cd13987 192 nfpWEKADSDDQFYE 206
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
568-772 3.09e-13

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: 71.20  E-value: 3.09e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfapepmaVAVKKCRHdatnAERA--QLEQEIRAVATFDHPNVIKLIGV----CYMDNSLL 641
Cdd:cd14053   1 EIKARGRFGAVWKAQYLNRL-------VAVKIFPL----QEKQswLTEREIYSLPGMKHENILQFIGAekhgESLEAEYW 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRVppadhdmggITEAnaEFLYIATQIALGMEYLAS----------MSFVHRDLATRNCLVGDT 711
Cdd:cd14053  70 LITEFHERGSLCDYLKGNV---------ISWN--ELCKIAESMARGLAYLHEdipatngghkPSIAHRDFKSKNVLLKSD 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 712 RTIKIADFGL-MRTSYGSDYYKmLHRSWMPVRWMSKE----AIEqgrFSEAS----DVWSFGVTLWEIWS 772
Cdd:cd14053 139 LTACIADFGLaLKFEPGKSCGD-THGQVGTRRYMAPEvlegAIN---FTRDAflriDMYAMGLVLWELLS 204
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
568-833 3.49e-13

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: 71.15  E-value: 3.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfapepmAVAVKKCrhdATNAERAQL-EQEIRAVATFDHPNVIKLIGVCYMDNS----LLA 642
Cdd:cd14056   1 KTIGKGRYGEVWLGKYRGE-------KVAVKIF---SSRDEDSWFrETEIYQTVMLRHENILGFIAADIKSTGswtqLWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVRVppadhdmggITEAnaEFLYIATQIALGMEYLASMSF--------VHRDLATRNCLVGDTRTI 714
Cdd:cd14056  71 ITEYHEHGSLYDYLQRNT---------LDTE--EALRLAYSAASGLAHLHTEIVgtqgkpaiAHRDLKSKNILVKRDGTC 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGL-MRTSYGSDYYKML-HRSWMPVRWMSKEAIEQGR----FS--EASDVWSFGVTLWEIWSFG---------RQP 777
Cdd:cd14056 140 CIADLGLaVRYDSDTNTIDIPpNPRVGTKRYMAPEVLDDSInpksFEsfKMADIYSFGLVLWEIARRCeiggiaeeyQLP 219
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 778 YEG-----ASNQQVIELVANRHLLECP------HNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14056 220 YFGmvpsdPSFEEMRKVVCVEKLRPPIpnrwksDPVLRSMVKLMQECWSENPHARLTALRVKKTLAK 286
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
568-827 3.60e-13

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: 70.22  E-value: 3.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFG----VVHSgiyTSGlfapEPMAVA-VKKCRhdATNAERAQLEQEIRAVATFDHPNVikligVCYMDN---- 638
Cdd:cd08218   6 KKIGEGSFGkallVKSK---EDG----KQYVIKeINISK--MSPKEREESRKEVAVLSKMKHPNI-----VQYQESfeen 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 -SLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd08218  72 gNLYIVMDYCDGGDLYKRINAQ--------RGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLG 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFG----------LMRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVI 787
Cdd:cd08218 144 DFGiarvlnstveLARTCIGTPYY------------LSPEICENKPYNNKSDIWALGCVLYEMCTL-KHAFEAGNMKNLV 210
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 788 ELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd08218 211 LKIIRGSYPPVPSRYSYDLRSLVSQLFKRNPRDRPSINSI 250
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
570-793 4.05e-13

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: 70.20  E-value: 4.05e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH------SGIYtsglFAPEpmavAVKKCRHDATN------AERAQLEQEIravatfDHPNVIKLIGVCYMD 637
Cdd:cd05611   4 ISKGAFGSVYlakkrsTGDY----FAIK----VLKKSDMIAKNqvtnvkAERAIMMIQG------ESPYVAKLYYSFQSK 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVrvppadhdMGGITEANAEfLYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05611  70 DYLYLVMEYLNGGDCASLIKT--------LGGLPEDWAK-QYIA-EVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLT 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 718 DFGLMRTSYGSDYYKMLhrSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVANR 793
Cdd:cd05611 140 DFGLSRNGLEKRHNKKF--VGTP-DYLAPETILGVGDDKMSDWWSLGCVIFEFL-FGYPPFHAETPDAVFDNILSR 211
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
568-770 4.17e-13

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: 70.93  E-value: 4.17e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLFAPepmaVAVKKCR------HDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd14096   7 NKIGEGAFSNVYKAVPLRNTGKP----VAIKVVRkadlssDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDL-HELLKVRVppadhdmggITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLV------------ 708
Cdd:cd14096  83 IVLELADGGEIfHQIVRLTY---------FSEDLSRH--VITQVASAVKYLHEIGVVHRDIKPENLLFepipfipsivkl 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 ---------------------GDTRTIKIADFGL--------MRTSYGSdyykmlhrswmpVRWMSKEAIEQGRFSEASD 759
Cdd:cd14096 152 rkadddetkvdegefipgvggGGIGIVKLADFGLskqvwdsnTKTPCGT------------VGYTAPEVVKDERYSKKVD 219
                       250
                ....*....|.
gi 71980965 760 VWSFGVTLWEI 770
Cdd:cd14096 220 MWALGCVLYTL 230
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
566-827 4.46e-13

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: 70.26  E-value: 4.46e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDA-TNAERAQLEQEIRAVATFDHPNVIKligvcYMD------N 638
Cdd:cd08217   4 VLETIGKGSFGTVRKVRRKS-----DGKILVWKEIDYGKmSEKEKQQLVSEVNILRELKHPNIVR-----YYDrivdraN 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLL-AVFEYMVHGDLHELLKVRvpPADHDMggITEanaEFLY-IATQIALGMEY-----LASMSFVHRDLATRNCLVGDT 711
Cdd:cd08217  74 TTLyIVMEYCEGGDLAQLIKKC--KKENQY--IPE---EFIWkIFTQLLLALYEchnrsVGGGKILHRDLKPANIFLDSD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 712 RTIKIADFGLMR----------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGA 781
Cdd:cd08217 147 NNVKLGDFGLARvlshdssfakTYVGTPYY------------MSPELLNEQSYDEKSDIWSLGCLIYELCA-LHPPFQAA 213
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 782 SNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd08217 214 NQLELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEEL 259
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
570-827 4.58e-13

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 70.13  E-value: 4.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapEPMAVAVKKCrhDATNAERAQ-LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd06624  16 LGKGTFGVVYAARDLS-----TQVRIAIKEI--PERDSREVQpLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVP 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKVRVPPADHDMGGITeanaeflYIATQIALGMEYLASMSFVHRDLATRNCLVgDTRT--IKIADFGLMRTSY 726
Cdd:cd06624  89 GGSLSALLRSKWGPLKDNENTIG-------YYTKQILEGLKYLHDNKIVHRDIKGDNVLV-NTYSgvVKISDFGTSKRLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 727 GSDYYKMLHRSWMpvRWMSKEAIEQGR--FSEASDVWSFGVTLWEIWSFGRQPYEGASNQQVIELVA--NRHlLECPHNC 802
Cdd:cd06624 161 GINPCTETFTGTL--QYMAPEVIDKGQrgYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGmfKIH-PEIPESL 237
                       250       260
                ....*....|....*....|....*
gi 71980965 803 PTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06624 238 SEEAKSFILRCFEPDPDKRATASDL 262
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
569-721 5.30e-13

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


Pssm-ID: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 70.05  E-value: 5.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAERA--------------QLEQEIRAVATFDHPNVIKLIGVC 634
Cdd:cd14095   7 VIGDGNFAVV-------------------KECRDKATDKEYAlkiidkakckgkehMIENEVAILRRVKHPNIVQLIEEY 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 635 YMDNSLLAVFEYMVHGDLHELLKVRVPpadhdmggITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGD---- 710
Cdd:cd14095  68 DTDTELYLVMELVKGGDLFDAITSSTK--------FTERDASRMV--TDLAQALKYLHSLSIVHRDIKPENLLVVEhedg 137
                       170
                ....*....|.
gi 71980965 711 TRTIKIADFGL 721
Cdd:cd14095 138 SKSLKLADFGL 148
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
566-827 5.59e-13

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


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 69.76  E-value: 5.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHsgiYTSGLFAPEPMAVAVKK--CRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd08222   4 VVRKLGSGNFGTVY---LVSDLKATADEELKVLKeiSVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKvrvppaDHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTrTIKIADFGLMR 723
Cdd:cd08222  81 TEYCEGGDLDDKIS------EYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNN-VIKVGDFGISR 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 ----------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIELVANR 793
Cdd:cd08222 154 ilmgtsdlatTFTGTPYY------------MSPEVLKHEGYNSKSDIWSLGCILYEMCCL-KHAFDGQNLLSVMYKIVEG 220
                       250       260       270
                ....*....|....*....|....*....|....
gi 71980965 794 HLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd08222 221 ETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEI 254
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
594-827 5.65e-13

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: 70.13  E-value: 5.65e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 594 AVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGvCYMDNSLLA-VFEYMVHGDLHELLkvrvppADHDMGGITE 672
Cdd:cd14043  25 WVWLKKFPGGSHTELRPSTKNVFSKLRELRHENVNLFLG-LFVDCGILAiVSEHCSRGSLEDLL------RNDDMKLDWM 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 673 ANAEFLyiaTQIALGMEYLASMSFVHRDLATRNCLVgDTR-TIKIADFGLMRTsYGSdyykmlHRSWMPVR------WMS 745
Cdd:cd14043  98 FKSSLL---LDLIKGMRYLHHRGIVHGRLKSRNCVV-DGRfVLKITDYGYNEI-LEA------QNLPLPEPapeellWTA 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 746 KEAIE----QGRFSEASDVWSFGVTLWEIWSFGrQPY--EGASNQQVIELVANRHLLeC-----PHNCPTNIYSLMVECW 814
Cdd:cd14043 167 PELLRdprlERRGTFPGDVFSFAIIMQEVIVRG-APYcmLGLSPEEIIEKVRSPPPL-CrpsvsMDQAPLECIQLMKQCW 244
                       250
                ....*....|...
gi 71980965 815 HENIERRPTFSEI 827
Cdd:cd14043 245 SEAPERRPTFDQI 257
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
570-790 5.95e-13

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


Pssm-ID: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 70.89  E-value: 5.95e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH-----SGIYTSGLFAPEPMAVAVKKCRhdatNAERAQLEQEIraVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd05582   3 LGQGSFGKVFlvrkiTGPDAGTLYAMKVLKKATLKVR----DRVRTKMERDI--LADVNHPFIVKLHYAFQTEGKLYLIL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRVppadhdMggITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT 724
Cdd:cd05582  77 DFLRGGDLFTRLSKEV------M--FTEEDVKF-YLA-ELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKE 146
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 725 SYgsDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd05582 147 SI--DHEKKAYSFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMI 209
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
563-778 7.01e-13

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 69.91  E-value: 7.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd06619   2 DIQYQEILGHGNGGTVYKAYHL-----LTRRILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFFVENRISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVrvppADHDMGgiteanaeflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd06619  77 CTEFMDGGSLDVYRKI----PEHVLG----------RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVS 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 723 R--------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPY 778
Cdd:cd06619 143 TqlvnsiakTYVGTNAY------------MAPERISGEQYGIHSDVWSLGISFMEL-ALGRFPY 193
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
598-779 7.83e-13

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 69.50  E-value: 7.83e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 598 KKCRHDATNAERAQLEQEIRAvaTFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADHDmggitEAnAEF 677
Cdd:cd14186  36 KKAMQKAGMVQRVRNEVEIHC--QLKHPSILELYNYFEDSNYVYLVLEMCHNGEMSRYLKNRKKPFTED-----EA-RHF 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 678 LYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLmrtsygSDYYKMLHRSWMPV----RWMSKEAIEQGR 753
Cdd:cd14186 108 MH---QIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGL------ATQLKMPHEKHFTMcgtpNYISPEIATRSA 178
                       170       180
                ....*....|....*....|....*.
gi 71980965 754 FSEASDVWSFGVTLWEIWsFGRQPYE 779
Cdd:cd14186 179 HGLESDVWSLGCMFYTLL-VGRPPFD 203
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
529-780 8.36e-13

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 70.06  E-value: 8.36e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 529 PPYPMDQhlqqarrfPSQEPIDDNSYKvfeiTPSQLSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCR-HDATNA 607
Cdd:cd08229   3 PPVPQFQ--------PQKALRPDMGYN----TLANFRIEKKIGRGQFSEVYRATCLL-----DGVPVALKKVQiFDLMDA 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 608 E-RAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvpPADHDMGGITEANAEFLYIatQIAL 686
Cdd:cd08229  66 KaRADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADAGDLSRMIK----HFKKQKRLIPEKTVWKYFV--QLCS 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 687 GMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtsYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVT 766
Cdd:cd08229 140 ALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGR--FFSSKTTAAHSLVGTPYYMSPERIHENGYNFKSDIWSLGCL 217
                       250
                ....*....|....
gi 71980965 767 LWEIWSFgRQPYEG 780
Cdd:cd08229 218 LYEMAAL-QSPFYG 230
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
568-784 8.89e-13

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


Pssm-ID: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 69.82  E-value: 8.89e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGLFapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd07836   6 EKLGEGTYATVYKGRnRTTGEI------VALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MvHGDLHELLKVRVPPadhdmGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRtS 725
Cdd:cd07836  80 M-DKDLKKYMDTHGVR-----GALDPNTVKsFTY---QLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLAR-A 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGsdyykmlhrswMPVRWMSKEAIE-----------QGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ 784
Cdd:cd07836 150 FG-----------IPVNTFSNEVVTlwyrapdvllgSRTYSTSIDIWSVGCIMAEMIT-GRPLFPGTNNE 207
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
568-785 1.09e-12

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


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 69.96  E-value: 1.09e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVH----SGiyTSGLFApepMAVAVKKCRHDATNAERAQLEQEIraVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd05574   7 KLLGKGDVGRVYlvrlKG--TGKLFA---MKVLDKEEMIKRNKVKRVLTEREI--LATLDHPFLPTLYASFQTSTHLCFV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKVRvpPadhdMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-- 721
Cdd:cd05574  80 MDYCPGGELFRLLQKQ--P----GKRLPEEVARF-YAA-EVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFDLsk 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 --------MRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGR-F-----------------SEASDVWSFGVTLWEIwSFGR 775
Cdd:cd05574 152 qssvtpppVRKSLRKGSRRS-SVKSIEKETFVAEPSARSNsFvgteeyiapevikgdghGSAVDWWTLGILLYEM-LYGT 229
                       250
                ....*....|
gi 71980965 776 QPYEGASNQQ 785
Cdd:cd05574 230 TPFKGSNRDE 239
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
568-782 1.17e-12

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 69.38  E-value: 1.17e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGLFapepmaVAVKKCRHD------ATNAERaqleqEIRAVATFDHPNVIKLIGVCYMDNSL 640
Cdd:cd07839   6 EKIGEGTYGTVFKAKnRETHEI------VALKRVRLDdddegvPSSALR-----EICLLKELKHKNIVRLYDVLHSDKKL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYmVHGDLHELLkvrvppaDHDMGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd07839  75 TLVFEY-CDQDLKKYF-------DSCNGDIDPEIVKsFMF---QLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADF 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 720 GLMRtSYGsdyykmlhrswMPVRWMSKEAIE-----------QGRFSEASDVWSFGVTLWEIWSFGRQPYEGAS 782
Cdd:cd07839 144 GLAR-AFG-----------IPVRCYSAEVVTlwyrppdvlfgAKLYSTSIDMWSAGCIFAELANAGRPLFPGND 205
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
570-769 1.43e-12

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 70.01  E-value: 1.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGlfapePMAVAVKKCR---HDATNAERAQleQEIRAVATFDHPNVIKLIGVcYMDNSLLAVFE- 645
Cdd:cd07851  23 VGSGAYGQVCSAFDTKT-----GRKVAIKKLSrpfQSAIHAKRTY--RELRLLKHMKHENVIGLLDV-FTPASSLEDFQd 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 -YMVH----GDLHELLKVRVPPADHdmggITeanaeflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd07851  95 vYLVThlmgADLNNIVKCQKLSDDH----IQ-------FLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFG 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMR------TSY-GSDYYK----MLhrSWMpvrwmskeaieqgRFSEASDVWSFGVTLWE 769
Cdd:cd07851 164 LARhtddemTGYvATRWYRapeiML--NWM-------------HYNQTVDIWSVGCIMAE 208
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
568-787 1.43e-12

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: 68.79  E-value: 1.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYT-SGLfapePMAVAVKKCRhdaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14193  10 EILGGGRFGQVHKCEEKsSGL----KLAAKIIKAR---SQKEKEEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLVMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHEllkvRVPPADHDMggiTEANAeFLYIaTQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIADFGLMRT 724
Cdd:cd14193  83 VDGGELFD----RIIDENYNL---TELDT-ILFI-KQICEGIQYMHQMYILHLDLKPENilCVSREANQVKIIDFGLARR 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 725 sygsdyYK---MLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVI 787
Cdd:cd14193 154 ------YKpreKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLS-GLSPFLGEDDNETL 212
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
569-829 1.61e-12

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


Pssm-ID: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 68.42  E-value: 1.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTS-GLfapePMAV--AVKKCRHDATNAERAQ-LEQEI---RAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd14005   7 LLGKGGFGTVYSGVRIRdGL----PVAVkfVPKSRVTEWAMINGPVpVPLEIallLKASKPGVPGVIRLLDWYERPDGFL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEY----MvhgDLHELLKVRvppadhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVgDTRT--IK 715
Cdd:cd14005  83 LIMERpepcQ---DLFDFITER--------GALSENLARIIF--RQVVEAVRHCHQRGVLHRDIKDENLLI-NLRTgeVK 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFG---LMRTSYGSDYYKMlhRSWMPvrwmsKEAIEQGRF-SEASDVWSFGVTLWEIwSFGRQPYEgaSNQQVI--EL 789
Cdd:cd14005 149 LIDFGcgaLLKDSVYTDFDGT--RVYSP-----PEWIRHGRYhGRPATVWSLGILLYDM-LCGDIPFE--NDEQILrgNV 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 71980965 790 VANRHLL-ECPHncptniysLMVECWHENIERRPTFSEIRS 829
Cdd:cd14005 219 LFRPRLSkECCD--------LISRCLQFDPSKRPSLEQILS 251
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
557-770 1.72e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 69.31  E-value: 1.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQL--SVREkIGEGQFGVVH--SGIYTSGLFAPEPMAVAVKKcrhdaTNAERAQLEQEIRAVATFDHPNVIKLIG 632
Cdd:cd06635  19 FKEDPEKLfsDLRE-IGHGSFGAVYfaRDVRTSEVVAIKKMSYSGKQ-----SNEKWQDIIKEVKFLQRIKHPNSIEYKG 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 vCYM-DNSLLAVFEYMVhGDLHELLKVRVPPADH-DMGGITEANAEflyiatqialGMEYLASMSFVHRDLATRNCLVGD 710
Cdd:cd06635  93 -CYLrEHTAWLVMEYCL-GSASDLLEVHKKPLQEiEIAAITHGALQ----------GLAYLHSHNMIHRDIKAGNILLTE 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 711 TRTIKIADFGlmRTSYGSDYYKMLHRSWmpvrWMSKE---AIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06635 161 PGQVKLADFG--SASIASPANSFVGTPY----WMAPEvilAMDEGQYDGKVDVWSLGITCIEL 217
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
568-792 1.72e-12

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: 68.45  E-value: 1.72e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI-YTSGLfapePMAVAVKKCRhdaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14192  10 EVLGGGRFGQVHKCTeLSTGL----TLAAKIIKVK---GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEY 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHEllkvRVPPADHDMggiTEANAefLYIATQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIADFGLMRT 724
Cdd:cd14192  83 VDGGELFD----RITDESYQL---TELDA--ILFTRQICEGVHYLHQHYILHLDLKPENilCVNSTGNQIKIIDFGLARR 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 725 SYGSDYYKMlhrSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVAN 792
Cdd:cd14192 154 YKPREKLKV---NFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLS-GLSPFLGETDAETMNNIVN 217
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
10-88 1.72e-12

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 433584 [Multi-domain]  Cd Length: 75  Bit Score: 63.37  E-value: 1.72e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965    10 PYIrlTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKtkrVKIRDKENSSRLVITQLDVLDSGYYQCIVSN 88
Cdd:pfam13927   2 PVI--TVSPSSVVVVEGETVTLTCEASGSPPPTITWYKNGGKLSS---GRTSLVGGNGTLTISNVTREDSGTYTCTASN 75
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
561-785 1.99e-12

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


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 68.48  E-value: 1.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 561 PSQLSVREK----IGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRhdatnAERAQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd14183   1 PASISERYKvgrtIGDGNFAVVKECVERSTGREYALKIINKSKCR-----GKEHMIQNEVSILRRVKHPNIVLLIEEMDM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRVPPADHDMGGIteanaefLYiatQIALGMEYLASMSFVHRDLATRNCLVGD----TR 712
Cdd:cd14183  76 PTELYLVMELVKGGDLFDAITSTNKYTERDASGM-------LY---NLASAIKYLHSLNIVHRDIKPENLLVYEhqdgSK 145
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 713 TIKIADFGLMRTSYGSdyykmLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQ 785
Cdd:cd14183 146 SLKLGDFGLATVVDGP-----LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRGSGDDQ 212
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
563-772 2.29e-12

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: 68.29  E-value: 2.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGiyTSGLfapEPMAVAVKKCRHDATNAERaqleqEIRAVATFDHPNVIKLIGvCY------M 636
Cdd:cd14047   7 DFKEIELIGSGGFGQVFKA--KHRI---DGKTYAIKRVKLNNEKAER-----EVKALAKLDHPNIVRYNG-CWdgfdydP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNS-----------LLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRN 705
Cdd:cd14047  76 ETSssnssrsktkcLFIQMEFCEKGTLESWIE--------KRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSN 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 706 CLVGDTRTIKIADFGLMRTSYGsdyYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWS 772
Cdd:cd14047 148 IFLVDTGKVKIGDFGLVTSLKN---DGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLH 211
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
569-768 2.43e-12

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: 67.92  E-value: 2.43e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYtsgLFAPEPMAVAV---KKCRHDA---TNAER-AQLEQEIRavatfdHPNVIKLIGVCYMDNSLL 641
Cdd:cd14070   9 KLGEGSFAKVREGLH---AVTGEKVAIKVidkKKAKKDSyvtKNLRReGRIQQMIR------HPNITQLLDILETENSYY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLkvrvppadHDMGGITEANAEfLYIaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd14070  80 LVMELCPGGNLMHRI--------YDKKRLEEREAR-RYI-RQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGL 149
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 71980965 722 MRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLW 768
Cdd:cd14070 150 SNCAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMY 196
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
566-784 2.56e-12

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 68.19  E-value: 2.56e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKC-RHDATNAERAQ------LEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd14084  10 MSRTLGSGACGEVKLAYDKS-----TCKKVAIKIInKRKFTIGSRREinkprnIETEIEILKKLSHPCIIKIEDFFDAED 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHEllKVRvppadhDMGGITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRT---IK 715
Cdd:cd14084  85 DYYIVLELMEGGELFD--RVV------SNKRLKEAICKL--YFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIK 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFG---------LMRTSYGSDYYKmlhrswMP--VRWMSKEAieqgrFSEASDVWSFGVTLWEIWSfGRQPYEGASNQ 784
Cdd:cd14084 155 ITDFGlskilgetsLMKTLCGTPTYL------APevLRSFGTEG-----YTRAVDCWSLGVILFICLS-GYPPFSEEYTQ 222
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
563-779 2.59e-12

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 68.91  E-value: 2.59e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREK-IGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAE----------RAQLEQEIRAVATFD-HPNVIKL 630
Cdd:cd14179   7 ELDLKDKpLGEGSFSIC-------------------RKCLHKKTNQEyavkivskrmEANTQREIAALKLCEgHPNIVKL 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 631 IGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADhdmggiTEANaeflYIATQIALGMEYLASMSFVHRDLATRNCLV-- 708
Cdd:cd14179  68 HEVYHDQLHTFLVMELLKGGELLERIKKKQHFSE------TEAS----HIMRKLVSAVSHMHDVGVVHRDLKPENLLFtd 137
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 709 -GDTRTIKIADFGLMRTSYGSDyyKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd14179 138 eSDNSEIKIIDFGFARLKPPDN--QPLKTPCFTLHYAAPELLNYNGYDESCDLWSLGVILYTMLS-GQVPFQ 206
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
557-790 2.92e-12

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 68.16  E-value: 2.92e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVREKIGEGQFGVVHSGiytsgLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAV-ATFDHPNVIKLIG--- 632
Cdd:cd06616   1 YEFTAEDLKDLGEIGRGAFGTVNKM-----LHKPSGTIMAVKRIRSTVDEKEQKRLLMDLDVVmRSSDCPYIVKFYGalf 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 ---VCY-----MDNSLLAVFEYmvhgdLHELLKVRVPpaDHDMGGITeanaeflyIATQIALgmEYLAS-MSFVHRDLAT 703
Cdd:cd06616  76 regDCWicmelMDISLDKFYKY-----VYEVLDSVIP--EEILGKIA--------VATVKAL--NYLKEeLKIIHRDVKP 138
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 704 RNCLVGDTRTIKIADFGLmrtsygSDYykmLHRSWMPVR------WMSKEAIEQGRFSEA----SDVWSFGVTLWEIwSF 773
Cdd:cd06616 139 SNILLDRNGNIKLCDFGI------SGQ---LVDSIAKTRdagcrpYMAPERIDPSASRDGydvrSDVWSLGITLYEV-AT 208
                       250
                ....*....|....*....
gi 71980965 774 GRQPYEGASN--QQVIELV 790
Cdd:cd06616 209 GKFPYPKWNSvfDQLTQVV 227
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
566-770 2.95e-12

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 69.04  E-value: 2.95e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYT-SGlfapepMAVAVKKCRH------DATNAERaqleqEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd07859   4 IQEVIGKGSYGVVCSAIDThTG------EKVAIKKINDvfehvsDATRILR-----EIKLLRLLRHPDIVEIKHIMLPPS 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 -----SLLAVFEYMvHGDLHELLKvrvppADHDMggITEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd07859  73 rrefkDIYVVFELM-ESDLHQVIK-----ANDDL--TPEHHQFFLY---QLLRALKYIHTANVFHRDLKPKNILANADCK 141
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 714 IKIADFGLMRTSYGSDYYKMLHRSWMPVRWMskEAIEQ-----GRFSEASDVWSFGVTLWEI 770
Cdd:cd07859 142 LKICDFGLARVAFNDTPTAIFWTDYVATRWY--RAPELcgsffSKYTPAIDIWSIGCIFAEV 201
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
570-785 3.14e-12

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


Pssm-ID: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 67.67  E-value: 3.14e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSGLFApEPMAVAVKKCRHDAtnAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVH 649
Cdd:cd14116  13 LGKGKFGNVYLAREKQSKFI-LALKVLFKAQLEKA--GVEHQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEYAPL 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 650 GDLH-ELLKVrvppadhdmgGITEANAEFLYIaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGS 728
Cdd:cd14116  90 GTVYrELQKL----------SKFDEQRTATYI-TELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 729 dyykmlHRSWM--PVRWMSKEAIEQGRFSEASDVWSFGVTLWEiWSFGRQPYEGASNQQ 785
Cdd:cd14116 159 ------RRTTLcgTLDYLPPEMIEGRMHDEKVDLWSLGVLCYE-FLVGKPPFEANTYQE 210
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
566-832 3.27e-12

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: 68.09  E-value: 3.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVH--SGIYTSGLFApepmavaVKKCR-HDATNAERAQleQEIRAVATFDHPNVIKLIGVCYM-----D 637
Cdd:cd13986   4 IQRLLGEGGFSFVYlvEDLSTGRLYA-------LKKILcHSKEDVKEAM--REIENYRLFNHPNILRLLDSQIVkeaggK 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVRVPPADHdmggITEAnaEFLYIATQIALGMEYL---ASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd13986  75 KEVYLLLPYYKRGSLQDEIERRLVKGTF----FPED--RILHIFLGICRGLKAMhepELVPYAHRDIKPGNVLLSEDDEP 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGLMRTSY----GSDYYKML-----HRSWMPVRWMSKEAIEQGR-FSEASDVWSFGVTLWEIwSFGRQPYEGASNQ 784
Cdd:cd13986 149 ILMDLGSMNPARieieGRREALALqdwaaEHCTMPYRAPELFDVKSHCtIDEKTDIWSLGCTLYAL-MYGESPFERIFQK 227
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 71980965 785 -QVIELVANRHLLECPHNC--PTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd13986 228 gDSLALAVLSGNYSFPDNSrySEELHQLVKSMLVVNPAERPSIDDLLSRVH 278
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
563-813 3.41e-12

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 68.20  E-value: 3.41e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVV----HSGiyTSGLFAPEPMA----VAVKKCRHDATnaeraqleqEIRAVATFDHPNVIKLIgVC 634
Cdd:cd14209   2 DFDRIKTLGTGSFGRVmlvrHKE--TGNYYAMKILDkqkvVKLKQVEHTLN---------EKRILQAINFPFLVKLE-YS 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 635 YMDNS-LLAVFEYMVHGDLHELLKvRVppadhdmGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd14209  70 FKDNSnLYMVMEYVPGGEMFSHLR-RI-------GRFSEPHARFY--AAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGY 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRTSYGsdyykmlhRSW----MPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEgasnqqviel 789
Cdd:cd14209 140 IKVTDFGFAKRVKG--------RTWtlcgTP-EYLAPEIILSKGYNKAVDWWALGVLIYEM-AAGYPPFF---------- 199
                       250       260
                ....*....|....*....|....
gi 71980965 790 vanrhllecpHNCPTNIYSLMVEC 813
Cdd:cd14209 200 ----------ADQPIQIYEKIVSG 213
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
608-795 3.84e-12

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: 67.63  E-value: 3.84e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 608 ERAQLEQEIRAVATfdHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppadHDMGGITEANAEFlYIAtQIALG 687
Cdd:cd05579  38 DSVLAERNILSQAQ--NPFVVKLYYSFQGKKNLYLVMEYLPGGDLYSLL--------ENVGALDEDVARI-YIA-EIVLA 105
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 688 MEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLmrTSYGSdYYKMLHRSWMPVR----------------WMSKEAIEQ 751
Cdd:cd05579 106 LEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGL--SKVGL-VRRQIKLSIQKKSngapekedrrivgtpdYLAPEILLG 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 71980965 752 GRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVANRHL 795
Cdd:cd05579 183 QGHGKTVDWWSLGVILYEFL-VGIPPFHAETPEEIFQNILNGKI 225
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
570-827 3.91e-12

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 67.50  E-value: 3.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGiYTSGLfapePMAVAVKKCrhDATNAERAQLEQ----EIRAVATFDHPNVIKLIGVCYM-DNSLLAVF 644
Cdd:cd14165   9 LGEGSYAKVKSA-YSERL----KCNVAIKII--DKKKAPDDFVEKflprELEILARLNHKSIIKTYEIFETsDGKVYIVM 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVRVPPADHDmggiteANAEFlyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR- 723
Cdd:cd14165  82 ELGVQGDLLEFIKLRGALPEDV------ARKMF----HQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKr 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSE--ASDVWSFGVTLWeIWSFGRQPYEgASNQQVIELVANRHLLECPHN 801
Cdd:cd14165 152 CLRDENGRIVLSKTFCGSAAYAAPEVLQGIPYDprIYDIWSLGVILY-IMVCGSMPYD-DSNVKKMLKIQKEHRVRFPRS 229
                       250       260
                ....*....|....*....|....*...
gi 71980965 802 C--PTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd14165 230 KnlTSECKDLIYRLLQPDVSQRLCIDEV 257
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
568-790 4.66e-12

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


Pssm-ID: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 68.09  E-value: 4.66e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd07872  12 EKLGEGTYATVFKGrsKLTENL-------VALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDKSLTLVFE 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMvHGDLHELLKvrvppadhDMGGITEAN--AEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd07872  85 YL-DKDLKQYMD--------DCGNIMSMHnvKIFLY---QILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 724 T------SYGSDYYKMLHRSwmpvrwmSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd07872 153 AksvptkTYSNEVVTLWYRP-------PDVLLGSSEYSTQIDMWGVGCIFFEMAS-GRPLFPGSTVEDELHLI 217
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
563-764 5.03e-12

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 67.53  E-value: 5.03e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGI-YTSGlfapepMAVAVKKCRHDATNAERaqlEQEI-RAVatfDHPNVIKLIGVCYM---- 636
Cdd:cd14137   5 SYTIEKVIGSGSFGVVYQAKlLETG------EVVAIKKVLQDKRYKNR---ELQImRRL---KHPNIVKLKYFFYSsgek 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 --DNSLLAVFEYM---VHGDLHELLKVRVPPAdhdmggiteanaeFLYI---ATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd14137  73 kdEVYLNLVMEYMpetLYRVIRHYSKNKQTIP-------------IIYVklySYQLFRGLAYLHSLGICHRDIKPQNLLV 139
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 -GDTRTIKIADFG---LMR-----TSY-GSDYYKmlhrswmpvrwmskeAIE--QG--RFSEASDVWSFG 764
Cdd:cd14137 140 dPETGVLKLCDFGsakRLVpgepnVSYiCSRYYR---------------APEliFGatDYTTAIDIWSAG 194
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
568-770 5.42e-12

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: 67.45  E-value: 5.42e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVhsgiytsglfapepmavavKKCRHDATN---AERAQLE------------QEIRAVATFDHPNVIKLIG 632
Cdd:cd07846   7 GLVGEGSYGMV-------------------MKCRHKETGqivAIKKFLEseddkmvkkiamREIKMLKQLRHENLVNLIE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDLHELlkvrvppaDHDMGGITEANA-EFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDT 711
Cdd:cd07846  68 VFRRKKRWYLVFEFVDHTVLDDL--------EKYPNGLDESRVrKYLF---QILRGIDFCHSHNIIHRDIKPENILVSQS 136
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 712 RTIKIADFGLMRT--SYGSDYykmlhRSWMPVRWMSKEAIEQG--RFSEASDVWSFGVTLWEI 770
Cdd:cd07846 137 GVVKLCDFGFARTlaAPGEVY-----TDYVATRWYRAPELLVGdtKYGKAVDVWAVGCLVTEM 194
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
568-790 5.49e-12

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 67.34  E-value: 5.49e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd07871  11 DKLGEGTYATVFKGrsKLTENL-------VALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTERCLTLVFE 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMvHGDLHELLkvrvppaDHDMGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT 724
Cdd:cd07871  84 YL-DSDLKQYL-------DNCGNLMSMHNVKiFMF---QLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 725 ------SYGSDYYKMLHRSwmP-VRWMSKEaieqgrFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd07871 153 ksvptkTYSNEVVTLWYRP--PdVLLGSTE------YSTPIDMWGVGCILYEMAT-GRPMFPGSTVKEELHLI 216
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
570-774 5.76e-12

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 67.86  E-value: 5.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  570 IGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLEQ-------------EIRAVATFDHPNVIKLIGVCYM 636
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTL-----TGKIVAIKKVKIIEISNDVTKDRQlvgmcgihfttlrELKIMNEIKHENIMGLVDVYVE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  637 DNSLLAVFEYMvHGDLHELL--KVRvppadhdmggITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:PTZ00024  92 GDFINLVMDIM-ASDLKKVVdrKIR----------LTESQVKC--ILLQILNGLNVLHKWYFMHRDLSPANIFINSKGIC 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965  715 KIADFGLMRtSYGSDYYkmlhrswmpVRWMSKEAIEQGRFSEASDVwsfgVTLW-----------------EIWSFG 774
Cdd:PTZ00024 159 KIADFGLAR-RYGYPPY---------SDTLSKDETMQRREEMTSKV----VTLWyrapellmgaekyhfavDMWSVG 221
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
570-816 5.85e-12

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 68.23  E-value: 5.85e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSgiytsglfAPEPM---AVAVKK---CRHDATNAERAQleQEIRAVATFDHPNVIKLIGVcyMDNSLLAV 643
Cdd:cd07853   8 IGYGAFGVVWS--------VTDPRdgkRVALKKmpnVFQNLVSCKRVF--RELKMLCFFKHDNVLSALDI--LQPPHIDP 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYM------VHGDLHELLkVRVPP--ADHdmggiteaNAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd07853  76 FEEIyvvtelMQSDLHKII-VSPQPlsSDH--------VKVFLY---QILRGLKYLHSAGILHRDIKPGNLLVNSNCVLK 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRTsygsdyykmlhrsWMP--VRWMSKEAIEQ-----------GRFSEASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:cd07853 144 ICDFGLARV-------------EEPdeSKHMTQEVVTQyyrapeilmgsRHYTSAVDIWSVGCIFAELLG-RRILFQAQS 209
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 783 NQQVIELV------------------ANRHLLECPHNCP--TNIYSLMVECWHE 816
Cdd:cd07853 210 PIQQLDLItdllgtpsleamrsacegARAHILRGPHKPPslPVLYTLSSQATHE 263
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
566-827 5.99e-12

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 67.34  E-value: 5.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSGlfaPEPMAVAVKKCRHDatnaeraqLEQEIRA-----VATFDHPNVIKLIGVCYMDN-- 638
Cdd:cd06638  22 IIETIGKGTYGKVFKVLNKKN---GSKAAVKILDPIHD--------IDEEIEAeynilKALSDHPNVVKFYGMYYKKDvk 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 ---SLLAVFEYMVHGDLHELLKVRVPPADHdMGGITEAnaeflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd06638  91 ngdQLWLVLELCNGGSVTDLVKGFLKRGER-MEEPIIA-----YILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVK 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGL----------MRTSYGSDYykmlhrswmpvrWMSKEAI--EQ---GRFSEASDVWSFGVTLWEIwsfgrqpyeG 780
Cdd:cd06638 165 LVDFGVsaqltstrlrRNTSVGTPF------------WMAPEVIacEQqldSTYDARCDVWSLGITAIEL---------G 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 781 ASNQQVIELVANRHLLECPHNCPTNIYS----------LMVECWHENIERRPTFSEI 827
Cdd:cd06638 224 DGDPPLADLHPMRALFKIPRNPPPTLHQpelwsnefndFIRKCLTKDYEKRPTVSDL 280
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
568-843 6.04e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 67.44  E-value: 6.04e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06654  26 EKIGQGASGTVYTAMDVA-----TGQEVAIRQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELlkvrVPPADHDMGGITEANAEFLYiatqialGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR--TS 725
Cdd:cd06654 100 AGGSLTDV----VTETCMDEGQIAAVCRECLQ-------ALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqiTP 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSWmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHL--LECPHNCP 803
Cdd:cd06654 169 EQSKRSTMVGTPY----WMAPEVVTRKAYGPKVDIWSLGIMAIEMIE-GEPPYLNENPLRALYLIATNGTpeLQNPEKLS 243
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 71980965 804 TNIYSLMVECWHENIERRPTFSEIRSRlQSWSLASPAHSI 843
Cdd:cd06654 244 AIFRDFLNRCLEMDVEKRGSAKELLQH-QFLKIAKPLSSL 282
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
562-770 6.47e-12

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 67.22  E-value: 6.47e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYT-SGlfapEPMAVavkKCRHDATNAERAQLEQ---EIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd05580   1 DDFEFLKTLGTGSFGRVRLVKHKdSG----KYYAL---KILKKAKIIKLKQVEHvlnEKRILSEVRHPFIVNLLGSFQDD 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELL-KVRVPPADHdmggiteanAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05580  74 RNLYMVMEYVPGGELFSLLrRSGRFPNDV---------AKF-YAA-EVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKI 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 717 ADFGLMRtsygsdyyKMLHRSW----MPvRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd05580 143 TDFGFAK--------RVKDRTYtlcgTP-EYLAPEIILSKGHGKAVDWWALGILIYEM 191
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
568-827 7.52e-12

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 67.06  E-value: 7.52e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGiyTSGLFAPEpmaVAVKKCRHDaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06655  25 EKIGQGASGTVFTA--IDVATGQE---VAIKQINLQ-KQPKKELIINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELlkvrvppadhdmggITEA---NAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR- 723
Cdd:cd06655  99 AGGSLTDV--------------VTETcmdEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAq 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 -TSYGSDYYKMLHRSWmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHL--LECPH 800
Cdd:cd06655 165 iTPEQSKRSTMVGTPY----WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTpeLQNPE 239
                       250       260
                ....*....|....*....|....*..
gi 71980965 801 NCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06655 240 KLSPIFRDFLNRCLEMDVEKRGSAKEL 266
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
569-773 7.64e-12

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 66.91  E-value: 7.64e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSG--IYTSGLFAPEPMavavKKCRHDATNAERAQLEQEIRAVAtfDHPNVIKLIGVCY--MDNSLLAVF 644
Cdd:cd07831   6 KIGEGTFSEVLKAqsRKTGKYYAIKCM----KKHFKSLEQVNNLREIQALRRLS--PHPNILRLIEVLFdrKTGRLALVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMvHGDLHELLKVRVPPadhdmggITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDtRTIKIADFGLMR 723
Cdd:cd07831  80 ELM-DMNLYELIKGRKRP-------LPEKRVKnYMY---QLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGSCR 147
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 724 TSYGsdyyKMLHRSWMPVRWM-SKEAI-EQGRFSEASDVWSFGVTLWEIWSF 773
Cdd:cd07831 148 GIYS----KPPYTEYISTRWYrAPECLlTDGYYGPKMDIWAVGCVFFEILSL 195
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
568-827 9.82e-12

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 66.10  E-value: 9.82e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCrHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06647  13 EKIGQGASGTVYTAIDVA-----TGQEVAIKQM-NLQQQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELlkvrVPPADHDMGGITEANAEFLYiatqialGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR--TS 725
Cdd:cd06647  87 AGGSLTDV----VTETCMDEGQIAAVCRECLQ-------ALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqiTP 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSWmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHLLECPHncPTN 805
Cdd:cd06647 156 EQSKRSTMVGTPY----WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTPELQN--PEK 228
                       250       260
                ....*....|....*....|....*.
gi 71980965 806 IYSL----MVECWHENIERRPTFSEI 827
Cdd:cd06647 229 LSAIfrdfLNRCLEMDVEKRGSAKEL 254
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
570-834 1.10e-11

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


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 66.16  E-value: 1.10e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH--SGIYTSGLfapepmaVAVKKCRHDATNAERAQleQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14665   8 IGSGNFGVARlmRDKQTKEL-------VAVKYIERGEKIDENVQ--REIINHRSLRHPNIVRFKEVILTPTHLAIVMEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHEllkvRVPPAdhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRT--IKIADFGLMRTS 725
Cdd:cd14665  79 AGGELFE----RICNA----GRFSEDEARFFF--QQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 ygsdyykMLHRS-----WMPVrWMSKEAIEQGRFS-EASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELVANRhLLECP 799
Cdd:cd14665 149 -------VLHSQpkstvGTPA-YIAPEVLLKKEYDgKIADVWSCGVTLY-VMLVGAYPFEDPEEPRNFRKTIQR-ILSVQ 218
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71980965 800 HNCPTNIYsLMVECWH-------ENIERRPTFSEIRSrlQSW 834
Cdd:cd14665 219 YSIPDYVH-ISPECRHlisrifvADPATRITIPEIRN--HEW 257
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
570-790 1.22e-11

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 66.95  E-value: 1.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVV------HSGIYTSGLFAPEPMAVAVKKCRHDATnaeraqleqEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd05595   3 LGKGTFGKVilvrekATGRYYAMKILRKEVIIAKDEVAHTVT---------ESRVLQNTRHPFLTALKYAFQTHDRLCFV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLH-ELLKVRVppadhdmggITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd05595  74 MEYANGGELFfHLSRERV---------FTEDRARFY--GAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLC 142
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 723 RTSYgSDYYKMLHRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd05595 143 KEGI-TDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHERLFELI 207
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
568-827 1.38e-11

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 66.17  E-value: 1.38e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKcrHDATNAERAQLEQEIRAVATF-DHPNVIKLIGVCY------MDNSL 640
Cdd:cd06608  12 EVIGEGTYGKVYKARHKK-----TGQLAAIKI--MDIIEDEEEEIKLEINILRKFsNHPNIATFYGAFIkkdppgGDDQL 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHGDLHELLKvrvppADHDMGGITEANaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd06608  85 WLVMEYCGGGSVTDLVK-----GLRKKGKRLKEE-WIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFG 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMR----------TSYGSDYykmlhrswmpvrWMSKEAI--EQGR---FSEASDVWSFGVTLWEIwSFGRQPYegasnqq 785
Cdd:cd06608 159 VSAqldstlgrrnTFIGTPY------------WMAPEVIacDQQPdasYDARCDVWSLGITAIEL-ADGKPPL------- 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 786 vIELVANRHLLECPHNCP----------TNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06608 219 -CDMHPMRALFKIPRNPPptlkspekwsKEFNDFISECLIKNYEQRPFTEEL 269
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
557-777 1.41e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20. The TEY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 66.63  E-value: 1.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQLSVReKIGEGQFGVVHSGIYTSglfapEPMAVAVKKC------RHDATNAERaqleqEIRAVATFDHPNVIKL 630
Cdd:cd07858   1 FEVDTKYVPIK-PIGRGAYGIVCSAKNSE-----TNEKVAIKKIanafdnRIDAKRTLR-----EIKLLRHLDHENVIAI 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 631 IGVC---YMD--NSLLAVFEYMvHGDLHELLKVRVPPADhdmggitEANAEFLYiatQIALGMEYLASMSFVHRDLATRN 705
Cdd:cd07858  70 KDIMpppHREafNDVYIVYELM-DTDLHQIIRSSQTLSD-------DHCQYFLY---QLLRGLKYIHSANVLHRDLKPSN 138
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 706 CLVGDTRTIKIADFGLMRTSYGSDYYKMlhrSWMPVRW--MSKEAIEQGRFSEASDVWSFGVTLWEIwsFGRQP 777
Cdd:cd07858 139 LLLNANCDLKICDFGLARTTSEKGDFMT---EYVVTRWyrAPELLLNCSEYTTAIDVWSVGCIFAEL--LGRKP 207
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
568-777 1.55e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 66.62  E-value: 1.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEgqFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06650   8 EKISE--LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHM 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKV--RVPpaDHDMGGITEAnaeflyiatqIALGMEYL-ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT 724
Cdd:cd06650  86 DGGSLDQVLKKagRIP--EQILGKVSIA----------VIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQ 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 725 SYGSdyykmLHRSWMPVR-WMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQP 777
Cdd:cd06650 154 LIDS-----MANSFVGTRsYMSPERLQGTHYSVQSDIWSMGLSLVEM-AVGRYP 201
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
569-777 1.60e-11

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 66.66  E-value: 1.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSglfAPEPMAVAVKKcrhdATN-------AERAQleQEIRAVATF-DHPNVIKLIGvcyMDNSL 640
Cdd:cd07857   7 ELGQGAYGIVCSARNAE---TSEEETVAIKK----ITNvfskkilAKRAL--RELKLLRHFrGHKNITCLYD---MDIVF 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 ------LAVFEYMVHGDLHELLKVRVPpadhdmggITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd07857  75 pgnfneLYLYEELMEADLHQIIRSGQP--------LTDAHFQsFIY---QILCGLKYIHSANVLHRDLKPGNLLVNADCE 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 714 IKIADFGLMRtSYGSDYYKM--LHRSWMPVRWMSKEAI--EQGRFSEASDVWSFGVTLWEIwsFGRQP 777
Cdd:cd07857 144 LKICDFGLAR-GFSENPGENagFMTEYVATRWYRAPEImlSFQSYTKAIDVWSVGCILAEL--LGRKP 208
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
568-831 1.78e-11

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: 65.92  E-value: 1.78e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVkkcrHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNS----LLAV 643
Cdd:cd13998   1 EVIGKGRFGEVWKASLKN-----EPVAVKI----FSSRDKQSWFREKEIYRTPMLKHENILQFIAADERDTAlrteLWLV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKvrvppadhdmgGITEANAEFLYIATQIALGMEYLAS---------MSFVHRDLATRNCLVGDTRTI 714
Cdd:cd13998  72 TAFHPNGSL*DYLS-----------LHTIDWVSLCRLALSVARGLAHLHSeipgctqgkPAIAHRDLKSKNILVKNDGTC 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 715 KIADFGL-MRTSYGSDYYKMLHRSWM-PVRWMSKEAIE---QGRFSEA---SDVWSFGVTLWEIWS-------------- 772
Cdd:cd13998 141 CIADFGLaVRLSPSTGEEDNANNGQVgTKRYMAPEVLEgaiNLRDFESfkrVDIYAMGLVLWEMASrctdlfgiveeykp 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 773 -FGRQPYEGASNQQVIELVANR--------HLLECPHncPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd13998 221 pFYSEVPNHPSFEDMQEVVVRDkqrpnipnRWLSHPG--LQSLAETIEECWDHDAEARLTAQCIEERL 286
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
568-827 2.20e-11

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 65.90  E-value: 2.20e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06656  25 EKIGQGASGTVYTAIDIA-----TGQEVAIKQMNLQ-QQPKKELIINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELlkvrVPPADHDMGGITEANAEFLYiatqialGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR--TS 725
Cdd:cd06656  99 AGGSLTDV----VTETCMDEGQIAAVCRECLQ-------ALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAqiTP 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 YGSDYYKMLHRSWmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANRHL--LECPHNCP 803
Cdd:cd06656 168 EQSKRSTMVGTPY----WMAPEVVTRKAYGPKVDIWSLGIMAIEMVE-GEPPYLNENPLRALYLIATNGTpeLQNPERLS 242
                       250       260
                ....*....|....*....|....
gi 71980965 804 TNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd06656 243 AVFRDFLNRCLEMDVDRRGSAKEL 266
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
557-770 2.33e-11

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 65.81  E-value: 2.33e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQL--SVREkIGEGQFGVVHsgiYTSGLFAPEpmAVAVKKCRHDA--TNAERAQLEQEIRAVATFDHPNVIKLIG 632
Cdd:cd06634   9 FKDDPEKLfsDLRE-IGHGSFGAVY---FARDVRNNE--VVAIKKMSYSGkqSNEKWQDIIKEVKFLQKLRHPNTIEYRG 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 vCYM-DNSLLAVFEYMVhGDLHELLKV-RVPPADHDMGGITEANAEflyiatqialGMEYLASMSFVHRDLATRNCLVGD 710
Cdd:cd06634  83 -CYLrEHTAWLVMEYCL-GSASDLLEVhKKPLQEVEIAAITHGALQ----------GLAYLHSHNMIHRDVKAGNILLTE 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 711 TRTIKIADFG---LMRTS---YGSDYykmlhrswmpvrWMSKE---AIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06634 151 PGLVKLGDFGsasIMAPAnsfVGTPY------------WMAPEvilAMDEGQYDGKVDVWSLGITCIEL 207
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
561-770 2.45e-11

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 65.07  E-value: 2.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 561 PSQLSVREKIGEGQFGVVHSgIYTsglfAPEPMAVAVKKCRHDA----TNAERAQLEQEIRAVATFDHPNVIKLIGvCYM 636
Cdd:cd06652   1 PTNWRLGKLLGQGAFGRVYL-CYD----ADTGRELAVKQVQFDPespeTSKEVNALECEIQLLKNLLHERIVQYYG-CLR 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 D--NSLLAVF-EYMVHGDLHELLKVrvppadhdMGGITEaNAEFLYiATQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd06652  75 DpqERTLSIFmEYMPGGSIKDQLKS--------YGALTE-NVTRKY-TRQILEGVHYLHSNMIVHRDIKGANILRDSVGN 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGL-------------MRTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06652 145 VKLGDFGAskrlqticlsgtgMKSVTGTPY------------WMSPEVISGEGYGRKADIWSVGCTVVEM 202
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
568-790 2.52e-11

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 65.41  E-value: 2.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd07873   8 DKLGEGTYATVYKGrsKLTDNL-------VALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFE 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMvHGDLHELLKvrvppadhDMGGITEANAEFLYIaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT- 724
Cdd:cd07873  81 YL-DKDLKQYLD--------DCGNSINMHNVKLFL-FQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAk 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 725 -----SYGSDYYKMlhrswmpvrWMSKEAIEQG--RFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVIELV 790
Cdd:cd07873 151 siptkTYSNEVVTL---------WYRPPDILLGstDYSTQIDMWGVGCIFYEM-STGRPLFPGSTVEEQLHFI 213
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
568-723 2.79e-11

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 65.09  E-value: 2.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGI--YTSGLfapepmaVAVKKCRhdatnaeraqLEQE-------IRAVA---TFDHPNVIKLIGVCY 635
Cdd:cd07844   6 DKLGEGSYATVYKGRskLTGQL-------VALKEIR----------LEHEegapftaIREASllkDLKHANIVTLHDIIH 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMvHGDLHELLkvrvppaDHDMGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd07844  69 TKKTLTLVFEYL-DTDLKQYM-------DDCGGGLSMHNVRlFLF---QLLRGLAYCHQRRVLHRDLKPQNLLISERGEL 137

                ....*....
gi 71980965 715 KIADFGLMR 723
Cdd:cd07844 138 KLADFGLAR 146
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
570-720 2.90e-11

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 61.69  E-value: 2.90e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIytsglFAPEPMAVAVKKCRhDATNAERAQLEQEIRAV--ATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd13968   1 MGEGASAKVFWAE-----GECTTIGVAVKIGD-DVNNEEGEDLESEMDILrrLKGLELNIPKVLVTEDVDGPNILLMELV 74
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 648 VHGDLHELLKVRvppadhdmggiTEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd13968  75 KGGTLIAYTQEE-----------ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
566-785 3.21e-11

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 65.77  E-value: 3.21e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVH--SGIYTSGLFApepMAVaVKKC----RHD--ATNAERaqleqEIRAVAtfDHPNVIKLigVCYM- 636
Cdd:cd05573   5 VIKVIGRGAFGEVWlvRDKDTGQVYA---MKI-LRKSdmlkREQiaHVRAER-----DILADA--DSPWIVRL--HYAFq 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 -DNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd05573  72 dEDHLYLVMEYMPGGDLMNLLI--------KYDVFPEETARF-YIA-ELVLALDSLHKLGFIHRDIKPDNILLDADGHIK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGL--------MRTSYGSDYYKML-------HRSWMPVR------------WMSKEAIEQGRFSEASDVWSFGVTLW 768
Cdd:cd05573 142 LADFGLctkmnksgDRESYLNDSVNTLfqdnvlaRRRPHKQRrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILY 221
                       250
                ....*....|....*..
gi 71980965 769 EIWsFGRQPYEGASNQQ 785
Cdd:cd05573 222 EML-YGFPPFYSDSLVE 237
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
566-768 3.31e-11

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 64.71  E-value: 3.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIY-TSGlfapepMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd14078   7 LHETIGSGGFAKVKLATHiLTG------EKVAIKIMDKKALGDDLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELL--KVRVPPadhdmggiTEANAEFLYIATQIAlgmeYLASMSFVHRDLATRNCLVGDTRTIKIADFGL- 721
Cdd:cd14078  81 EYCPGGELFDYIvaKDRLSE--------DEARVFFRQIVSAVA----YVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLc 148
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 722 ----------MRTSYGSDYYKmlhrswmpvrwmSKEAIEQGRF--SEAsDVWSFGVTLW 768
Cdd:cd14078 149 akpkggmdhhLETCCGSPAYA------------APELIQGKPYigSEA-DVWSMGVLLY 194
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
566-778 3.39e-11

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 65.05  E-value: 3.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAERA---------QLEQEIRAVATF-DHPNVIKLIGVCY 635
Cdd:cd14175   5 VKETIGVGSYSVC-------------------KRCVHKATNMEYAvkvidkskrDPSEEIEILLRYgQHPNIITLKDVYD 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDL-HELLKVRVppadhdmggITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLV----GD 710
Cdd:cd14175  66 DGKHVYLVTELMRGGELlDKILRQKF---------FSEREASS--VLHTICKTVEYLHSQGVVHRDLKPSNILYvdesGN 134
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965 711 TRTIKIADFGL---MRTSYGsdyykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd14175 135 PESLRICDFGFakqLRAENG-----LLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPF 199
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
570-770 3.46e-11

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: 64.66  E-value: 3.46e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSgIYTsglfAPEPMAVAVKKCRHDA----TNAERAQLEQEIRAVATFDHPNVIKLIGvCYMDNS--LLAV 643
Cdd:cd06653  10 LGRGAFGEVYL-CYD----ADTGRELAVKQVPFDPdsqeTSKEVNALECEIQLLKNLRHDRIVQYYG-CLRDPEekKLSI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 F-EYMVHGDLHELLKVrvppadhdMGGITEaNAEFLYiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGlm 722
Cdd:cd06653  84 FvEYMPGGSVKDQLKA--------YGALTE-NVTRRY-TRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFG-- 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 723 rtsyGSDYYKMLHRSWMPVR-------WMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06653 152 ----ASKRIQTICMSGTGIKsvtgtpyWMSPEVISGEGYGRKADVWSVACTVVEM 202
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
595-782 3.80e-11

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 66.74  E-value: 3.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  595 VAVKKCRHD-ATNAE-RAQLEQEIRAVATFDHPNVIKLI------GVCYMdnsllaVFEYmVHG-DLHELLKVR--VPPA 663
Cdd:NF033483  35 VAVKVLRPDlARDPEfVARFRREAQSAASLSHPNIVSVYdvgedgGIPYI------VMEY-VDGrTLKDYIREHgpLSPE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  664 dhdmggitEAnaefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR----TSY-------GSDYYk 732
Cdd:NF033483 108 --------EA----VEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARalssTTMtqtnsvlGTVHY- 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 71980965  733 mlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:NF033483 175 -----------LSPEQARGGTVDARSDIYSLGIVLYEMLT-GRPPFDGDS 212
Ig_Pro_neuregulin cd05750
Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the ...
17-101 4.07e-11

Immunoglobulin (Ig)-like domain in neuregulins; The members here are composed of the immunoglobulin (Ig)-like domain in neuregulins (NRGs). NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. There are four members of the neuregulin gene family (NRG-1, NRG-2, NRG-3, and NRG-4). The NRG-1 protein, binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. The other NRGs proteins bind one or the other or both of these ErbBs. NRG-1 has multiple functions: in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors, while in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. Less is known of the functions of the other NRGs. NRG-2 and NRG-3 are expressed predominantly in the nervous system. NRG-2 is expressed by motor neurons and terminal Schwann cells, and is concentrated near synaptic sites and may be a signal that regulates synaptic differentiation. NRG-4 has been shown to direct pancreatic islet cell development towards the delta-cell lineage.


Pssm-ID: 409408 [Multi-domain]  Cd Length: 92  Bit Score: 60.22  E-value: 4.07e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  17 QLRNATKSSGDEVRFKCEALG-TPPLKFIWLKNNGPV--EKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASV 93
Cdd:cd05750   5 EMKSQTVQEGSKLVLKCEATSeNPSPRYRWFKDGKELnrKRPKNIKIRNKKKNSELQINKAKLEDSGEYTCVVENILGKD 84

                ....*...
gi 71980965  94 NTTSVLRV 101
Cdd:cd05750  85 TVTGNVTV 92
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
562-790 4.53e-11

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: 64.53  E-value: 4.53e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVhsgiytsgLFAPEPMA---VAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDN 638
Cdd:cd14169   3 SVYELKEKLGEGAFSEV--------VLAQERGSqrlVALKCIPKKALRGKEAMVENEIAVLRRINHENIVSLEDIYESPT 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVG---DTRTIK 715
Cdd:cd14169  75 HLYLAMELVTGGELFDRIIER--------GSYTEKDASQL--IGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIM 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 716 IADFGLMRTSYGSdyykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELV 790
Cdd:cd14169 145 ISDFGLSKIEAQG----MLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPFYDENDSELFNQI 214
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
595-769 4.97e-11

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: 64.60  E-value: 4.97e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIK-------LIGVCYMDNSLLAVfEYMVHGDLHELLKVRvppadHDM 667
Cdd:cd14038  22 VAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPLLAM-EYCQGGDLRKYLNQF-----ENC 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 668 GGITEanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLV--GDTRTI-KIADFGlmrtsygsdYYKMLHRSWM----- 739
Cdd:cd14038  96 CGLRE--GAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqGEQRLIhKIIDLG---------YAKELDQGSLctsfv 164
                       170       180       190
                ....*....|....*....|....*....|.
gi 71980965 740 -PVRWMSKEAIEQGRFSEASDVWSFGVTLWE 769
Cdd:cd14038 165 gTLQYLAPELLEQQKYTVTVDYWSFGTLAFE 195
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
568-793 5.12e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 64.76  E-value: 5.12e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGE---GQFGVVHSGIYT-SGLFapepMAvavKKCRH-DATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd06615   4 EKLGElgaGNGGVVTKVLHRpSGLI----MA---RKLIHlEIKPAIRNQIIRELKVLHECNSPYIVGFYGAFYSDGEISI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKV--RVPpaDHDMGGITEAnaeflyiatqIALGMEYLAS-MSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd06615  77 CMEHMDGGSLDQVLKKagRIP--ENILGKISIA----------VLRGLTYLREkHKIMHRDVKPSNILVNSRGEIKLCDF 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GL-------MRTSY-GSdyykmlhRSWMpvrwmSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEgASNQQVIELVA 791
Cdd:cd06615 145 GVsgqlidsMANSFvGT-------RSYM-----SPERLQGTHYTVQSDIWSLGLSLVEM-AIGRYPIP-PPDAKELEAMF 210

                ..
gi 71980965 792 NR 793
Cdd:cd06615 211 GR 212
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
568-764 5.29e-11

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


Pssm-ID: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 64.32  E-value: 5.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHsgiytsglfapepmavavkKCRHDATN---AERAQLE------------QEIRAVATFDHPNVIKLIG 632
Cdd:cd07847   7 SKIGEGSYGVVF-------------------KCRNRETGqivAIKKFVEseddpvikkialREIRMLKQLKHPNLVNLIE 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDLHELlkvrvppaDHDMGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:cd07847  68 VFRRKRKLHLVFEYCDHTVLNEL--------EKNPRGVPEHLIK--KIIWQTLQAVNFCHKHNCIHRDVKPENILITKQG 137
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 713 TIKIADFGLMRT-SYGSDYYKmlhrSWMPVRWMSKEAIEQG--RFSEASDVWSFG 764
Cdd:cd07847 138 QIKLCDFGFARIlTGPGDDYT----DYVATRWYRAPELLVGdtQYGPPVDVWAIG 188
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
570-803 5.88e-11

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 64.44  E-value: 5.88e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI--YTSGLfapepmaVAVKKCRHDAtnaERAQLE----QEIRAVATFDHPNVIKLIGVCY-----MD- 637
Cdd:cd07864  15 IGEGTYGQVYKAKdkDTGEL-------VALKKVRLDN---EKEGFPitaiREIKILRQLNHRSVVNLKEIVTdkqdaLDf 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 ----NSLLAVFEYMVHgDLHELLKVRVPPADHDMggiteaNAEFLyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd07864  85 kkdkGAFYLVFEYMDH-DLMGLLESGLVHFSEDH------IKSFM---KQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQ 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGLMRTsYGSDyYKMLHRSWMPVRWMSKEAIEQG--RFSEASDVWSFGVTLWEIwsFGRQPYEGASNQQV-IELV 790
Cdd:cd07864 155 IKLADFGLARL-YNSE-ESRPYTNKVITLWYRPPELLLGeeRYGPAIDVWSCGCILGEL--FTKKPIFQANQELAqLELI 230
                       250
                ....*....|...
gi 71980965 791 ANRHLLECPHNCP 803
Cdd:cd07864 231 SRLCGSPCPAVWP 243
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
570-829 7.57e-11

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 63.51  E-value: 7.57e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI--YTSGLFAPEPMAVAvkKCRhdatnAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14184   9 IGDGNFAVVKECVerSTGKEFALKIIDKA--KCC-----GKEHLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADHDMGGITeanaeflyiaTQIALGMEYLASMSFVHRDLATRNCLVGD----TRTIKIADFGLMR 723
Cdd:cd14184  82 KGGDLFDAITSSTKYTERDASAMV----------YNLASALKYLHGLCIVHRDIKPENLLVCEypdgTKSLKLGDFGLAT 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 724 TSYGSdyykmLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQ---VIELVANRHLLECPH 800
Cdd:cd14184 152 VVEGP-----LYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRSENNLQedlFDQILLGKLEFPSPY 225
                       250       260       270
                ....*....|....*....|....*....|.
gi 71980965 801 --NCPTNIYSLMVECWHENIERRPTFSEIRS 829
Cdd:cd14184 226 wdNITDSAKELISHMLQVNVEARYTAEQILS 256
CRD_TK_ROR2 cd07468
Cysteine-rich domain of tyrosine kinase-like orphan receptor 2; The cysteine-rich domain (CRD) ...
177-306 7.83e-11

Cysteine-rich domain of tyrosine kinase-like orphan receptor 2; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror2), a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands. In addition, a number of Wnt-independent functions have been proposed for both Ror1 and Ror2.


Pssm-ID: 143577  Cd Length: 140  Bit Score: 60.80  E-value: 7.83e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 177 GDCVQYRGEACRQYLSNKFVMMtnESREEMYDIDRNLRAAMLFINGAPTISQKCRQLSQAVACHHMYKVCESDSNN-QIV 255
Cdd:cd07468   3 GFCQPYRGIACARFIGNRTIYV--DSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLCDDRSRTpKPR 80
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 256 SICKHDCDVIQNDECPSELALAAQHELVgdTPKALFPLCSRLS-----STSNCIPV 306
Cdd:cd07468  81 ELCRDECEVLENDLCRQEYNIARSNPLI--LMQLQLPKCEELPlpespEAANCMRI 134
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
613-802 7.87e-11

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


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 64.26  E-value: 7.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 613 EQEIRAVAtfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkVRvppadhdMGGITEANAEFlYIAtQIALGMEYLA 692
Cdd:cd05598  51 ERDILAEA--DNEWVVKLYYSFQDKENLYFVMDYIPGGDLMSLL-IK-------KGIFEEDLARF-YIA-ELVCAIESVH 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 693 SMSFVHRDLATRNCLVGDTRTIKIADFGL---MRTSYGSDYYkMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWE 769
Cdd:cd05598 119 KMGFIHRDIKPDNILIDRDGHIKLTDFGLctgFRWTHDSKYY-LAHSLVGTPNYIAPEVLLRTGYTQLCDWWSVGVILYE 197
                       170       180       190
                ....*....|....*....|....*....|....
gi 71980965 770 IWsFGRQPYEGASNQQVIELVAN-RHLLECPHNC 802
Cdd:cd05598 198 ML-VGQPPFLAQTPAETQLKVINwRTTLKIPHEA 230
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
561-791 8.06e-11

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


Pssm-ID: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 64.68  E-value: 8.06e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 561 PSQLSVREKIGEGQFGVVHSGIYTSGLFApepmaVAVKKCR---HDATNAERAQleQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd07877  16 PERYQNLSPVGSGAYGSVCAAFDTKTGLR-----VAVKKLSrpfQSIIHAKRTY--RELRLLKHMKHENVIGLLDVFTPA 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSL-----LAVFEYMVHGDLHELLKVRVPPADHdmggiteanAEFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:cd07877  89 RSLeefndVYLVTHLMGADLNNIVKCQKLTDDH---------VQFLIY--QILRGLKYIHSADIIHRDLKPSNLAVNEDC 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 713 TIKIADFGLMR------TSY-GSDYYKMLHrswMPVRWMskeaieqgRFSEASDVWSFGVTLWEIWSfGRQPYEGASN-- 783
Cdd:cd07877 158 ELKILDFGLARhtddemTGYvATRWYRAPE---IMLNWM--------HYNQTVDIWSVGCIMAELLT-GRTLFPGTDHid 225
                       250
                ....*....|
gi 71980965 784 --QQVIELVA 791
Cdd:cd07877 226 qlKLILRLVG 235
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
566-720 8.11e-11

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 63.51  E-value: 8.11e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYtsglfAPEPMAVAVK---KCRHDAtnaeRAQ--LEQEIRAVATFDHPNVIKLIGVCYMDNSL 640
Cdd:cd14075   6 IRGELGSGNFSQVKLGIH-----QLTKEKVAIKildKTKLDQ----KTQrlLSREISSMEKLHHPNIIRLYEVVETLSKL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHGDLHEllKVrvppadHDMGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd14075  77 HLVMEYASGGELYT--KI------STEGKLSESEAKPLF--AQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFG 146
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
604-827 8.29e-11

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: 63.22  E-value: 8.29e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 604 ATNAERAQLEQEIRAVATFDHPNVikligVCYMDN------SLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEF 677
Cdd:cd08223  38 ASKRERKAAEQEAKLLSKLKHPNI-----VSYKESfegedgFLYIVMGFCEGGDLYTRLKEQ--------KGVLLEERQV 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 678 LYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR----------TSYGSDYYkmlhrswmpvrwMSKE 747
Cdd:cd08223 105 VEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARvlesssdmatTLIGTPYY------------MSPE 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 748 AIEQGRFSEASDVWSFGVTLWEIWSFgRQPYEGASNQQVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd08223 173 LFSNKPYNHKSDVWALGCCVYEMATL-KHAFNAKDMNSLVYKILEGKLPPMPKQYSPELGELIKAMLHQDPEKRPSVKRI 251
IgI_2_FGFR_like cd05729
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar ...
10-101 8.34e-11

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor, and similar domains; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three Ig-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans. This group also contains fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409393 [Multi-domain]  Cd Length: 95  Bit Score: 59.16  E-value: 8.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  10 PYIRLTSQLRNATKS--SGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKI-RDKENSSRLVITQLDVLDSGYYQCIV 86
Cdd:cd05729   1 PRFTDTEKMEEREHAlpAANKVRLECGAGGNPMPNITWLKDGKEFKKEHRIGGtKVEEKGWSLIIERAIPRDKGKYTCIV 80
                        90
                ....*....|....*
gi 71980965  87 SNPAASVNTTSVLRV 101
Cdd:cd05729  81 ENEYGSINHTYDVDV 95
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
624-827 8.99e-11

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: 63.39  E-value: 8.99e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 624 HPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELL---KVRVPPADHdmggiteanaefLYIATQIALGMEYLASMSFVHRD 700
Cdd:cd05076  74 HTHLVFVHGVCVRGSENIMVEEFVEHGPLDVWLrkeKGHVPMAWK------------FVVARQLASALSYLENKNLVHGN 141
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 701 LATRNCLV-------GDTRTIKIADFGLMRTSYGSDyyKMLHRswmpVRWMSKEAIEQG-RFSEASDVWSFGVTLWEIWS 772
Cdd:cd05076 142 VCAKNILLarlgleeGTSPFIKLSDPGVGLGVLSRE--ERVER----IPWIAPECVPGGnSLSTAADKWGFGATLLEICF 215
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 773 FGRQPYEGASNQQVIELVANRHLLECPhNCPtNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05076 216 NGEAPLQSRTPSEKERFYQRQHRLPEP-SCP-ELATLISQCLTYEPTQRPSFRTI 268
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
563-784 9.70e-11

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 63.86  E-value: 9.70e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKI-GEGQFGVVhsgiytsglfapepmavavKKCRHDATNAE--------RAQLEQEIRAVATFD-HPNVIKLIG 632
Cdd:cd14092   6 ELDLREEAlGDGSFSVC-------------------RKCVHKKTGQEfavkivsrRLDTSREVQLLRLCQgHPNIVKLHE 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGdlhELLKvRVPPADHdmggITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLV---G 709
Cdd:cd14092  67 VFQDELHTYLVMELLRGG---ELLE-RIRKKKR----FTESEAS--RIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeD 136
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 710 DTRTIKIADFGLMRTSYGSdyyKMLHRSWMPVRWMSKEAIEQGR----FSEASDVWSFGVTLWEIWSfGRQPYEGASNQ 784
Cdd:cd14092 137 DDAEIKIVDFGFARLKPEN---QPLKTPCFTLPYAAPEVLKQALstqgYDESCDLWSLGVILYTMLS-GQVPFQSPSRN 211
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
570-832 1.24e-10

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: 63.06  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVhsgIYTSGlFAPEPMAVA---VKKC------------RH-DATNAER--AQLEQEIRAVATFDHPNVIKLI 631
Cdd:cd14067   1 LGQGGSGTV---IYRAR-YQGQPVAVKrfhIKKCkkrtdgsadtmlKHlRAADAMKnfSEFRQEASMLHSLQHPCIVYLI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 GVCYmdNSLLAVFEYMVHGDLHELLkvrvppADHDMGGITEANAEFLY--IATQIALGMEYLASMSFVHRDLATRNCLVG 709
Cdd:cd14067  77 GISI--HPLCFALELAPLGSLNTVL------EENHKGSSFMPLGHMLTfkIAYQIAAGLAYLHKKNIIFCDLKSDNILVW 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 710 --DTR---TIKIADFGLMRTSYgsdyykmlHRSWMPVR----WMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEG 780
Cdd:cd14067 149 slDVQehiNIKLSDYGISRQSF--------HEGALGVEgtpgYQAPEIRPRIVYDEKVDMFSYGMVLYELLS-GQRPSLG 219
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 781 ASNQQVIELVAN--RHLLECPHNCP-TNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14067 220 HHQLQIAKKLSKgiRPVLGQPEEVQfFRLQALMMECWDTKPEKRPLACSVVEQMK 274
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
566-780 1.24e-10

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


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 63.87  E-value: 1.24e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVH-------SGIYtsglfapepmavAVKKCRHDATNAER--AQLEQEIRAVATFDHPNVIKLIGVCYM 636
Cdd:cd05601   5 VKNVIGRGHFGEVQvvkekatGDIY------------AMKVLKKSETLAQEevSFFEEERDIMAKANSPWITKLQYAFQD 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKVRVPPADHDMggiteanAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd05601  73 SENLYLVMEYHPGGDLLSLLSRYDDIFEESM-------ARF-YLA-ELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKL 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 717 ADFGlmrtSYGSDYYKMLHRSWMPV---RWMSKEAIE------QGRFSEASDVWSFGVTLWEIwSFGRQPYEG 780
Cdd:cd05601 144 ADFG----SAAKLSSDKTVTSKMPVgtpDYIAPEVLTsmnggsKGTYGVECDWWSLGIVAYEM-LYGKTPFTE 211
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
568-790 1.26e-10

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: 63.01  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVA---VKKcrHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd13983   7 EVLGRGSFKTVYRAFDTE-----EGIEVAwneIKL--RKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKKEVIF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 --EYMVHGDLHELLKvrvppadhDMGGITEANaeFLYIATQIALGMEYLASM--SFVHRDLATRNCLV-GDTRTIKIADF 719
Cdd:cd13983  80 itELMTSGTLKQYLK--------RFKRLKLKV--IKSWCRQILEGLNYLHTRdpPIIHRDLKCDNIFInGNTGEVKIGDL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GL---MRTSY-----GSDYYkmlhrswmpvrwMSKEAIEQGrFSEASDVWSFGVTLWEIWSfGRQPY-EGASNQQVIELV 790
Cdd:cd13983 150 GLatlLRQSFaksviGTPEF------------MAPEMYEEH-YDEKVDIYAFGMCLLEMAT-GEYPYsECTNAAQIYKKV 215
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
562-779 1.26e-10

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 63.22  E-value: 1.26e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYTSG--LFAPEPMA----VAVKKCRHdatnaeraqLEQEIRAVATFDHPNVIKLIGVCY 635
Cdd:cd05612   1 DDFERIKTIGTGTFGRVHLVRDRISehYYALKVMAipevIRLKQEQH---------VHNEKRVLKEVSHPFIIRLFWTEH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd05612  72 DQRFLYMLMEYVPGGELFSYLR--------NSGRFSNSTGLFY--ASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIK 141
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 716 IADFGLMRtsygsdyyKMLHRSW----MPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWS-----FGRQPYE 779
Cdd:cd05612 142 LTDFGFAK--------KLRDRTWtlcgTP-EYLAPEVIQSKGHNKAVDWWALGILIYEMLVgyppfFDDNPFG 205
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
562-768 1.37e-10

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: 63.21  E-value: 1.37e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 562 SQLSVREKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNaeraQLEQEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd14086   1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQ----KLEREARICRLLKHPNIVRLHDSISEEGFHY 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRvppaDHdmggITEANAEFlyIATQIALGMEYLASMSFVHRDLATRNCLVGDTR---TIKIAD 718
Cdd:cd14086  77 LVFDLVTGGELFEDIVAR----EF----YSEADASH--CIQQILESVNHCHQNGIVHRDLKPENLLLASKSkgaAVKLAD 146
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 719 FGLMRTSYGSdyykmlHRSWM-----PVrWMSKEAIEQGRFSEASDVWSFGVTLW 768
Cdd:cd14086 147 FGLAIEVQGD------QQAWFgfagtPG-YLSPEVLRKDPYGKPVDIWACGVILY 194
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
568-770 1.71e-10

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 62.91  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  568 EKIGEGQFGVVHSGI--YTSGLfapepmaVAVKKCRhdatnaeraqLEQE--------IRAVA---TFDHPNVIKLIGVC 634
Cdd:PLN00009   8 EKIGEGTYGVVYKARdrVTNET-------IALKKIR----------LEQEdegvpstaIREISllkEMQHGNIVRLQDVV 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  635 YMDNSLLAVFEYMvhgDLHelLKVRVPPADhDMGGITEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVgDTRT- 713
Cdd:PLN00009  71 HSEKRLYLVFEYL---DLD--LKKHMDSSP-DFAKNPRLIKTYLY---QILRGIAYCHSHRVLHRDLKPQNLLI-DRRTn 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965  714 -IKIADFGLMRtSYGsdyykmlhrswMPVR---------WMSKEAIEQG--RFSEASDVWSFGVTLWEI 770
Cdd:PLN00009 141 aLKLADFGLAR-AFG-----------IPVRtfthevvtlWYRAPEILLGsrHYSTPVDIWSVGCIFAEM 197
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
567-765 1.85e-10

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: 62.39  E-value: 1.85e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 567 REKIGEGQFG-VVHSGIYTSGLFapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14083   8 KEVLGTGAFSeVVLAEDKATGKL------VAIKCIDKKALKGKEDSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVME 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRvppadhdmGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLV---GDTRTIKIADFGL- 721
Cdd:cd14083  82 LVTGGELFDRIVEK--------GSYTEKDASHL--IRQVLEAVDYLHSLGIVHRDLKPENLLYyspDEDSKIMISDFGLs 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 71980965 722 -------MRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGV 765
Cdd:cd14083 152 kmedsgvMSTACGTPGY------------VAPEVLAQKPYGKAVDCWSIGV 190
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
568-723 1.97e-10

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: 62.79  E-value: 1.97e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYm 647
Cdd:cd07869  11 EKLGEGSYATVYKGKSKV-----NGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEY- 84
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 648 VHGDLHELLkvrvppaDHDMGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd07869  85 VHTDLCQYM-------DKHPGGLHPENVKlFLF---QLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR 151
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
568-783 2.05e-10

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


Pssm-ID: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 62.67  E-value: 2.05e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIY-TSGLFapepmaVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd07870   6 EKLGEGSYATVYKGISrINGQL------VALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIHTKETLTFVFEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MvHGDLHELLkvrvppADHDmGGITEANAE-FLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT- 724
Cdd:cd07870  80 M-HTDLAQYM------IQHP-GGLHPYNVRlFMF---QLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAk 148
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 725 -----SYGSDYYKMLHRSwmPVRWMSKEaieqgRFSEASDVWSFGVTLWEIWSfGRQPYEGASN 783
Cdd:cd07870 149 sipsqTYSSEVVTLWYRP--PDVLLGAT-----DYSSALDIWGAGCIFIEMLQ-GQPAFPGVSD 204
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
570-782 2.11e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 62.71  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQLE-QEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYmV 648
Cdd:cd07848   9 VGEGAYGVVLKCRHKE-----TKEIVAIKKFKDSEENEEVKETTlRELKMLRTLKQENIVELKEAFRRRGKLYLVFEY-V 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLKvrvppaDHDMGGITEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRT-SYG 727
Cdd:cd07848  83 EKNMLELLE------EMPNGVPPEKVRSYIY---QLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNlSEG 153
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 728 SDYYkmlHRSWMPVRWM-SKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQPYEGAS 782
Cdd:cd07848 154 SNAN---YTEYVATRWYrSPELLLGAPYGKAVDMWSVGCILGEL-SDGQPLFPGES 205
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
566-765 2.11e-10

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 62.21  E-value: 2.11e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVH------SGIYTSGLFAPepmavavkkcrhdATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd14107   6 VKEEIGRGTFGFVKrvthkgNGECCAAKFIP-------------LRSSTRARAFQERDILARLSHRRLTCLLDQFETRKT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEfLYIaTQIALGMEYLASMSFVHRDLATRNCL-VGDTRT-IKIA 717
Cdd:cd14107  73 LILILELCSSEELLDRLFLK--------GVVTEAEVK-LYI-QQVLEGIGYLHGMNILHLDIKPDNILmVSPTREdIKIC 142
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 718 DFGLMR---------TSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGV 765
Cdd:cd14107 143 DFGFAQeitpsehqfSKYGSPEF------------VAPEIVHQEPVSAATDIWALGV 187
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
18-101 2.32e-10

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205  Cd Length: 85  Bit Score: 57.61  E-value: 2.32e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  18 LRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKEnssrLVITQLDVLDSGYYQCIVSNPAASVNTTS 97
Cdd:cd05728   6 ISDTEADIGSSLRWECKASGNPRPAYRWLKNGQPLASENRIEVEAGD----LRITKLSLSDSGMYQCVAENKHGTIYASA 81

                ....
gi 71980965  98 VLRV 101
Cdd:cd05728  82 ELAV 85
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
551-770 2.71e-10

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


Pssm-ID: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 63.14  E-value: 2.71e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 551 DNSYKVFEITPSQLSVREK------IGEGQFGVVhsgiyTSGLFAPEPMAVAVKKCR---HDATNAERAQleQEIRAVAT 621
Cdd:cd07875   7 DNNFYSVEIGDSTFTVLKRyqnlkpIGSGAQGIV-----CAAYDAILERNVAIKKLSrpfQNQTHAKRAY--RELVLMKC 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 622 FDHPNVIKLIGVCYMDNSL-----LAVFEYMVHGDLHELLKVRVppaDHDmggiteanaEFLYIATQIALGMEYLASMSF 696
Cdd:cd07875  80 VNHKNIIGLLNVFTPQKSLeefqdVYIVMELMDANLCQVIQMEL---DHE---------RMSYLLYQMLCGIKHLHSAGI 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 697 VHRDLATRNCLVGDTRTIKIADFGLMRTSyGSDYykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd07875 148 IHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSF--MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEM 218
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
570-829 2.82e-10

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 61.71  E-value: 2.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH--SGIYTSGLfapepmaVAVKKCRHDATNAERAQleQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14662   8 IGSGNFGVARlmRNKETKEL-------VAVKYIERGLKIDENVQ--REIINHRSLRHPNIIRFKEVVLTPTHLAIVMEYA 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHEllkvRVPPAdhdmGGITEANAEFLYiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRT--IKIADFGLMRTS 725
Cdd:cd14662  79 AGGELFE----RICNA----GRFSEDEARYFF--QQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSS 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 726 ygsdyykMLHRS-----WMPVrWMSKEAIEQGRFS-EASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELVANRhLLECP 799
Cdd:cd14662 149 -------VLHSQpkstvGTPA-YIAPEVLSRKEYDgKVADVWSCGVTLY-VMLVGAYPFEDPDDPKNFRKTIQR-IMSVQ 218
                       250       260       270
                ....*....|....*....|....*....|....*..
gi 71980965 800 HNCPTNIYSLMvECWH-------ENIERRPTFSEIRS 829
Cdd:cd14662 219 YKIPDYVRVSQ-DCRHllsrifvANPAKRITIPEIKN 254
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
558-788 2.86e-10

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: 62.63  E-value: 2.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVH-SGIYTSGLFapepmaVAVKKCRHDAT----NAERAQLEQEIRAVAtFDHPNVIKLIG 632
Cdd:cd05619   1 KLTIEDFVLHKMLGKGSFGKVFlAELKGTNQF------FAIKALKKDVVlmddDVECTMVEKRVLSLA-WEHPFLTHLFC 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFEYMVHGDL----HELLKVRVPPADhdmggiteanaeflYIATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd05619  74 TFQTKENLFFVMEYLNGGDLmfhiQSCHKFDLPRAT--------------FYAAEIICGLQFLHSKGIVYRDLKLDNILL 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 GDTRTIKIADFGLMRTSYGSDyYKMLHRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIE 788
Cdd:cd05619 140 DKDGHIKIADFGMCKENMLGD-AKTSTFCGTP-DYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFHGQDEEELFQ 216
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
569-778 3.08e-10

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 61.69  E-value: 3.08e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVV------HSGiytsglfapepMAVAVKKCrhDATNAERAQLE-QEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06648  14 KIGEGSTGIVciatdkSTG-----------RQVAVKKM--DLRKQQRRELLfNEVVIMRDYQHPNIVEMYSSYLVGDELW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELlkvrvppadhdmggITEANAEFLYIAT---QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd06648  81 VVMEFLEGGALTDI--------------VTHTRMNEEQIATvcrAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSD 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGL----------MRTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd06648 147 FGFcaqvskevprRKSLVGTPY------------WMAPEVISRLPYGTEVDIWSLGIMVIEMVD-GEPPY 203
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
556-770 3.18e-10

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 62.59  E-value: 3.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 556 VFEITpSQLSVREKIGEGQFGVVHSGiyTSGLFApepMAVAVKKCRHD-ATNAERAQLEQEIRAVATFDHPNVIKLIGV- 633
Cdd:cd07856   5 VFEIT-TRYSDLQPVGMGAFGLVCSA--RDQLTG---QNVAVKKIMKPfSTPVLAKRTYRELKLLKHLRHENIISLSDIf 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 634 ------CYMDNSLLAVfeymvhgDLHELLKVRvpPADhdmggiTEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd07856  79 ispledIYFVTELLGT-------DLHRLLTSR--PLE------KQFIQYFLY---QILRGLKYVHSAGVIHRDLKPSNIL 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 708 VGDTRTIKIADFGLMR------TSYGSD-YYK----MLhrSWMpvrwmskeaieqgRFSEASDVWSFGVTLWEI 770
Cdd:cd07856 141 VNENCDLKICDFGLARiqdpqmTGYVSTrYYRapeiML--TWQ-------------KYDVEVDIWSAGCIFAEM 199
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
567-790 3.31e-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: 61.58  E-value: 3.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 567 REKIGEGQFGVVhsgiytsgLFAPEPMA---VAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd14167   8 REVLGTGAFSEV--------VLAEEKRTqklVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYESGGHLYLI 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLHELLKvrvppadhDMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCL---VGDTRTIKIADFG 720
Cdd:cd14167  80 MQLVSGGELFDRIV--------EKGFYTERDASKL--IFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 721 L---------MRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQVIELV 790
Cdd:cd14167 150 LskiegsgsvMSTACGTPGY------------VAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDAKLFEQI 215
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
624-827 3.59e-10

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits, common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a cytoplasmic (or nonreceptor) PTK containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270662 [Multi-domain]  Cd Length: 266  Bit Score: 61.49  E-value: 3.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 624 HPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPAdhdmggiteANAEFLYIATQIALGMEYLASMSFVHRDLAT 703
Cdd:cd05077  67 HKHIVLLYGVCVRDVENIMVEEFVEFGPLDLFMHRKSDVL---------TTPWKFKVAKQLASALSYLEDKDLVHGNVCT 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 704 RNCLVG----DTRT---IKIADFGLMRTsygsdyykMLHRSWMPVR--WMSKEAIEQGR-FSEASDVWSFGVTLWEIWSF 773
Cdd:cd05077 138 KNILLAregiDGECgpfIKLSDPGIPIT--------VLSRQECVERipWIAPECVEDSKnLSIAADKWSFGTTLWEICYN 209
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 71980965 774 GRQPYEGASNQQVIELVANRHLLECPhNCpTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd05077 210 GEIPLKDKTLAEKERFYEGQCMLVTP-SC-KELADLMTHCMNYDPNQRPFFRAI 261
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
570-833 3.65e-10

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: 61.82  E-value: 3.65e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapepMAVAVKKCRHDATNAERAQLEQ---EIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd14160   1 IGEGEIFEVYRVRIGN-------RSYAVKLFKQEKKMQWKKHWKRflsELEVLLLFQHPNILELAAYFTETEKFCLVYPY 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDL-HELLKVRV--PPADHdmggiteanaEFLYIATQIALGMEYLASM---SFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd14160  74 MQNGTLfDRLQCHGVtkPLSWH----------ERINILIGIAKAIHYLHNSqpcTVICGNISSANILLDDQMQPKLTDFA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMR----TSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQ----VIELVAN 792
Cdd:cd14160 144 LAHfrphLEDQSCTINMTTALHKHLWYMPEEYIRQGKLSVKTDVYSFGIVIMEVLTGCKVVLDDPKHLQlrdlLHELMEK 223
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 793 RHLLEC--------PHnCPTN----IYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd14160 224 RGLDSClsfldlkfPP-CPRNfsakLFRLAGRCTATKAKLRPDMDEVLQRLES 275
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
595-769 3.86e-10

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: 61.86  E-value: 3.86e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGV------CYMDNSLLAVfEYMVHGDLHELLKvrvppADHDMG 668
Cdd:cd14039  21 IAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVpeemnfLVNDVPLLAM-EYCSGGDLRKLLN-----KPENCC 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 669 GITEanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDT--RTI-KIADFGlmrtsYGSDYYK-MLHRSWM-PVRW 743
Cdd:cd14039  95 GLKE--SQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEIngKIVhKIIDLG-----YAKDLDQgSLCTSFVgTLQY 167
                       170       180
                ....*....|....*....|....*.
gi 71980965 744 MSKEAIEQGRFSEASDVWSFGVTLWE 769
Cdd:cd14039 168 LAPELFENKSYTVTVDYWSFGTMVFE 193
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
569-777 3.89e-10

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: 62.37  E-value: 3.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTsglfaPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMV 648
Cdd:cd06649  12 ELGAGNGGVVTKVQHK-----PSGLIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMD 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 649 HGDLHELLK--VRVPpaDHDMGGITEAnaeflyiatqIALGMEYL-ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:cd06649  87 GGSLDQVLKeaKRIP--EEILGKVSIA----------VLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 726 YGSdyykmLHRSWMPVR-WMSKEAIEQGRFSEASDVWSFGVTLWEIwSFGRQP 777
Cdd:cd06649 155 IDS-----MANSFVGTRsYMSPERLQGTHYSVQSDIWSMGLSLVEL-AIGRYP 201
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
565-792 3.93e-10

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 61.56  E-value: 3.93e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 565 SVREKIGEGQFGVVHSgiytsgLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd14191   5 DIEERLGSGKFGQVFR------LVEKKTKKVWAGKFFKAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHEllkvRVPPADHDMggiTEanAEFLYIATQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIADFGLM 722
Cdd:cd14191  79 EMVSGGELFE----RIIDEDFEL---TE--RECIKYMRQISEGVEYIHKQGIVHLDLKPENimCVNKTGTKIKLIDFGLA 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 723 RTSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVAN 792
Cdd:cd14191 150 RRLENAGSLKVLFGT---PEFVAPEVINYEPIGYATDMWSIGVICYILVS-GLSPFMGDNDNETLANVTS 215
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
558-785 4.49e-10

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: 61.42  E-value: 4.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREKIGEGQFGVVHSGIYTSGLFApepMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMD 637
Cdd:cd14117   2 KFTIDDFDIGRPLGKGKFGNVYLAREKQSKFI---VALKVLFKSQIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDR 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLHELLKVRVPPADHDMGGITEanaeflyiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd14117  79 KRIYLILEYAPRGELYKELQKHGRFDEQRTATFME----------ELADALHYCHEKKVIHRDIKPENLLMGYKGELKIA 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGLmrtsygSDYYKMLHRSWM--PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQ 785
Cdd:cd14117 149 DFGW------SVHAPSLRRRTMcgTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGMPPFESASHTE 211
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
569-723 4.73e-10

Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK8, CDC2L6, and similar proteins. CDK8 functions as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK8-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 61.92  E-value: 4.73e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSGlfaPEPMAVAVKKCRhdATNAERAQLEQE-IRAVATF---DHPNVIKLIGVC--YMDNSLLA 642
Cdd:cd07842   7 CIGRGTYGRVYKAKRKNG---KDGKEYAIKKFK--GDKEQYTGISQSaCREIALLrelKHENVVSLVEVFleHADKSVYL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYmvhgdlhellkvrvppADHDMGGI----TEANAEFLYIAT------QIALGMEYLASMSFVHRDLATRNCLV---G 709
Cdd:cd07842  82 LFDY----------------AEHDLWQIikfhRQAKRVSIPPSMvksllwQILNGIHYLHSNWVLHRDLKPANILVmgeG 145
                       170
                ....*....|....*
gi 71980965 710 DTR-TIKIADFGLMR 723
Cdd:cd07842 146 PERgVVKIGDLGLAR 160
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
615-795 4.89e-10

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: 61.94  E-value: 4.89e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVATFDHPNVIKLIGVCY--MDNsLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLyiATQIALGMEYLA 692
Cdd:cd05616  50 EKRVLALSGKPPFLTQLHSCFqtMDR-LYFVMEYVNGGDLMYHIQ--------QVGRFKEPHAVFY--AAEIAIGLFFLQ 118
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 693 SMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYgSDYYKMLHRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWS 772
Cdd:cd05616 119 SKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENI-WDGVTTKTFCGTP-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA 196
                       170       180
                ....*....|....*....|...
gi 71980965 773 fGRQPYEGASNQQVIELVANRHL 795
Cdd:cd05616 197 -GQAPFEGEDEDELFQSIMEHNV 218
IgI_3_NCAM-1 cd05730
Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of ...
10-101 5.14e-10

Third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule 1 (NCAM-1); member of the I-set of IgSF domains; The members here are composed of the third immunoglobulin (Ig)-like domain of Neural Cell Adhesion Molecule (NCAM-1). NCAM plays important roles in the development and regeneration of the central nervous system, in synaptogenesis and neural migration. NCAM mediates cell-cell and cell-substratum recognition and adhesion via homophilic (NCAM-NCAM), and heterophilic (NCAM-non-NCAM), interactions. NCAM is expressed as three major isoforms having different intracellular extensions. The extracellular portion of NCAM has five N-terminal Ig-like domains and two fibronectin type III domains. The double zipper adhesion complex model for NCAM homophilic binding involves Ig1, Ig2, and Ig3. By this model, Ig1 and Ig2 mediate dimerization of NCAM molecules situated on the same cell surface (cis interactions), and Ig3 domains mediate interactions between NCAM molecules expressed on the surface of opposing cells (trans interactions) through binding to the Ig1 and Ig2 domains. The adhesive ability of NCAM is modulated by the addition of polysialic acid chains to the fifth Ig-like domain.


Pssm-ID: 143207 [Multi-domain]  Cd Length: 95  Bit Score: 56.86  E-value: 5.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  10 PYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRvKIRDKENSSRLVITQLDVLDSGYYQCIVSNP 89
Cdd:cd05730   2 PTIRARQSEVNATANLGQSVTLACDADGFPEPTMTWTKDGEPIESGEE-KYSFNEDGSEMTILDVDKLDEAEYTCIAENK 80
                        90
                ....*....|..
gi 71980965  90 AASVNTTSVLRV 101
Cdd:cd05730  81 AGEQEAEIHLKV 92
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
608-827 5.28e-10

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 61.10  E-value: 5.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 608 ERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEflYIATQIALG 687
Cdd:cd14187  50 QKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSLLELHKRR--------KALTEPEAR--YYLRQIILG 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 688 MEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-MRTSYGSDYYKMLHRSwmPvRWMSKEAIEQGRFSEASDVWSFGVT 766
Cdd:cd14187 120 CQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLaTKVEYDGERKKTLCGT--P-NYIAPEVLSKKGHSFEVDIWSIGCI 196
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 767 LWEIWsFGRQPYEGAS-NQQVIELVANRHLLecPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd14187 197 MYTLL-VGKPPFETSClKETYLRIKKNEYSI--PKHINPVAASLIQKMLQTDPTARPTINEL 255
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
570-770 6.23e-10

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: 60.87  E-value: 6.23e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDA----TNAERAQLEQEIRAVATFDHPNVIKLIGvCYMDN---SLLA 642
Cdd:cd06651  15 LGQGAFGRVYLCYDVD-----TGRELAAKQVQFDPespeTSKEVSALECEIQLLKNLQHERIVQYYG-CLRDRaekTLTI 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKVrvppadhdMGGITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL- 721
Cdd:cd06651  89 FMEYMPGGSVKDQLKA--------YGALTESVTR--KYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGAs 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965 722 ------------MRTSYGSDYykmlhrswmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06651 159 krlqticmsgtgIRSVTGTPY------------WMSPEVISGEGYGRKADVWSLGCTVVEM 207
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
615-764 8.42e-10

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


Pssm-ID: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 60.70  E-value: 8.42e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVATFDHPNVIKL--IGVCYMDNSLLAVFEYMVHgDLHELLKVRVPPadhdmggITEANAEFLYIatQIALGMEYLA 692
Cdd:cd07843  54 EINILLKLQHPNIVTVkeVVVGSNLDKIYMVMEYVEH-DLKSLMETMKQP-------FLQSEVKCLML--QLLSGVAHLH 123
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 693 SMSFVHRDLATRNCLVGDTRTIKIADFGLMRtSYGSDYYKMLHrswmPVRWMSKEAIE----QGRFSEASDVWSFG 764
Cdd:cd07843 124 DNWILHRDLKTSNLLLNNRGILKICDFGLAR-EYGSPLKPYTQ----LVVTLWYRAPElllgAKEYSTAIDMWSVG 194
IgI_Myotilin_C_like cd05744
Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of ...
26-101 1.06e-09

Immunoglobulin (Ig)-like domain of myotilin, palladin, and myopalladin; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the immunoglobulin (Ig)-like domain in myotilin, palladin, and myopalladin. Myotilin, palladin, and myopalladin function as scaffolds that regulate actin organization. Myotilin and myopalladin are most abundant in skeletal and cardiac muscle; palladin is ubiquitously expressed in the organs of developing vertebrates and plays a key role in cellular morphogenesis. The three family members each interact with specific molecular partners with all three binding to alpha-actinin; In addition, palladin also binds to vasodilator-stimulated phosphoprotein (VASP) and ezrin, myotilin binds to filamin and actin, and myopalladin also binds to nebulin and cardiac ankyrin repeat protein (CARP). This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409405 [Multi-domain]  Cd Length: 91  Bit Score: 55.96  E-value: 1.06e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965  26 GDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSR-LVITQLDVLDSGYYQCIVSNPAASVNTTSVLRV 101
Cdd:cd05744  15 GRLCRFDCKVSGLPTPDLFWQLNGKPVRPDSAHKMLVRENGRHsLIIEPVTKRDAGIYTCIARNRAGENSFNAELVV 91
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
568-787 1.12e-09

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: 60.40  E-value: 1.12e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGlfAPEPMAVAVKKCRHDAT--NAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFE 645
Cdd:cd14195  11 EELGSGQFAIVRKCREKGT--GKEYAAKFIKKRRLSSSrrGVSREEIEREVNILREIQHPNIITLHDIFENKTDVVLILE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 YMVHGDLHELLKVRvppadhdmGGITEANA-EFLyiaTQIALGMEYLASMSFVHRDLATRNCLVGDTRT----IKIADFG 720
Cdd:cd14195  89 LVSGGELFDFLAEK--------ESLTEEEAtQFL---KQILDGVHYLHSKRIAHFDLKPENIMLLDKNVpnprIKLIDFG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 721 LMRTSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVI 787
Cdd:cd14195 158 IAHKIEAGNEFKNIFGT---PEFVAPEIVNYEPLGLEADMWSIGVITYILLS-GASPFLGETKQETL 220
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
598-791 1.16e-09

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 60.41  E-value: 1.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 598 KKCRHDATNAERA---------QLEQEIRAVATF-DHPNVIKLIGVcYMDNSLL-AVFEYMVHGDL-HELLKVRVPPAdh 665
Cdd:cd14178  20 KRCVHKATSTEYAvkiidkskrDPSEEIEILLRYgQHPNIITLKDV-YDDGKFVyLVMELMRGGELlDRILRQKCFSE-- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 666 dmggiTEANAeflyIATQIALGMEYLASMSFVHRDLATRNCL----VGDTRTIKIADFGL---MRTSYGsdyykMLHRSW 738
Cdd:cd14178  97 -----REASA----VLCTITKTVEYLHSQGVVHRDLKPSNILymdeSGNPESIRICDFGFakqLRAENG-----LLMTPC 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 739 MPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVA 791
Cdd:cd14178 163 YTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFTPFANGPDDTPEEILA 214
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
570-800 1.26e-09

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: 60.73  E-value: 1.26e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFG-VVHSGIYTSGLFapepmaVAVKKCRHDAT----NAERAQLEQEIRAVAtFDHPNVIKLIGVCYMDNSLLAVF 644
Cdd:cd05620   3 LGKGSFGkVLLAELKGKGEY------FAVKALKKDVVliddDVECTMVEKRVLALA-WENPFLTHLYCTFQTKEHLFFVM 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLhellkvrvppadhdMGGITEANAEFLYIAT----QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd05620  76 EFLNGGDL--------------MFHIQDKGRFDLYRATfyaaEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFG 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTS-YGSDyyKMLHRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVAnrhlLECP 799
Cdd:cd05620 142 MCKENvFGDN--RASTFCGTP-DYIAPEILQGLKYTFSVDWWSFGVLLYEML-IGQSPFHGDDEDELFESIR----VDTP 213

                .
gi 71980965 800 H 800
Cdd:cd05620 214 H 214
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
558-790 1.37e-09

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


Pssm-ID: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 60.74  E-value: 1.37e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 558 EITPSQLSVREK------IGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATN---AERAQleQEIRAVATFDHPNVI 628
Cdd:cd07880   5 EVNKTIWEVPDRyrdlkqVGSGAYGTVCSALDRR-----TGAKVAIKKLYRPFQSelfAKRAY--RELRLLKHMKHENVI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 629 KLIGVCYMDNSL------LAVFEYMvHGDLHELLKvrvppadhdMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLA 702
Cdd:cd07880  78 GLLDVFTPDLSLdrfhdfYLVMPFM-GTDLGKLMK---------HEKLSEDRIQFL--VYQMLKGLKYIHAAGIIHRDLK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 703 TRNCLVGDTRTIKIADFGLMRTSyGSDYYKMLHRSW-----MPVRWMskeaieqgRFSEASDVWSFGVTLWEIWSfGRQP 777
Cdd:cd07880 146 PGNLAVNEDCELKILDFGLARQT-DSEMTGYVVTRWyrapeVILNWM--------HYTQTVDIWSVGCIMAEMLT-GKPL 215
                       250
                ....*....|....
gi 71980965 778 YEGASN-QQVIELV 790
Cdd:cd07880 216 FKGHDHlDQLMEIM 229
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
623-787 1.47e-09

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 59.59  E-value: 1.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 623 DHPNVIKLIGVCYMDNSLLAVFEyMVHGDLHELLK-VRVPPADHDMggiteanaeFLYIATQIALGMEYLASMSFVHRDL 701
Cdd:cd14133  59 DKYHIVRLKDVFYFKNHLCIVFE-LLSQNLYEFLKqNKFQYLSLPR---------IRKIAQQILEALVFLHSLGLIHCDL 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 702 ATRNCLVGDTR--TIKIADFGLMRTSYGSDYYKMLHRSwmpvrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd14133 129 KPENILLASYSrcQIKIIDFGSSCFLTQRLYSYIQSRY-----YRAPEVILGLPYDEKIDMWSLGCILAELYT-GEPLFP 202

                ....*...
gi 71980965 780 GASNQQVI 787
Cdd:cd14133 203 GASEVDQL 210
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
604-787 1.58e-09

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: 60.03  E-value: 1.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 604 ATNAERAQLEQEIRAvaTFDHPNVIKLIGVCYMD-NSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFlyIAT 682
Cdd:cd13990  45 QNYIKHALREYEIHK--SLDHPRIVKLYDVFEIDtDSFCTVLEYCDGNDLDFYLK--------QHKSIPEREARS--IIM 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 683 QIALGMEYLASMS--FVHRDLATRNCLVGDTRT---IKIADFGLMR--------------TSYGSDYYkmlhrsWmpvrW 743
Cdd:cd13990 113 QVVSALKYLNEIKppIIHYDLKPGNILLHSGNVsgeIKITDFGLSKimddesynsdgmelTSQGAGTY------W----Y 182
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 744 MSKEAIEQG----RFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVI 787
Cdd:cd13990 183 LPPECFVVGktppKISSKVDVWSVGVIFYQML-YGRKPFGHNQSQEAI 229
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
602-827 1.63e-09

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: 59.36  E-value: 1.63e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 602 HDATNAERAQLEQEIRAVATFDHPNVIKLIGvCYMDN-SLLAVFEYMVHGDLHEllKVRvppadHDMGGI--TEANAEFL 678
Cdd:cd08221  36 SRLSEKERRDALNEIDILSLLNHDNIITYYN-HFLDGeSLFIEMEYCNGGNLHD--KIA-----QQKNQLfpEEVVLWYL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 679 YiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL---------MRTSY-GSDYYkmlhrswmpvrwMSKEA 748
Cdd:cd08221 108 Y---QIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGIskvldsessMAESIvGTPYY------------MSPEL 172
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 749 IEQGRFSEASDVWSFGVTLWEIWSFGRQpyEGASNQ--QVIELVANRHLLECPhNCPTNIYSLMVECWHENIERRPTFSE 826
Cdd:cd08221 173 VQGVKYNFKSDIWAVGCVLYELLTLKRT--FDATNPlrLAVKIVQGEYEDIDE-QYSEEIIQLVHDCLHQDPEDRPTAEE 249

                .
gi 71980965 827 I 827
Cdd:cd08221 250 L 250
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
568-770 1.78e-09

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


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 60.12  E-value: 1.78e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLFAPEPMavavkkcrhDATNAERAQLEQEIRAVATFDH-PNVIKLIGVCY------MDN 638
Cdd:cd06637  12 ELVGNGTYGQVYKGrhVKTGQLAAIKVM---------DVTGDEEEEIKQEINMLKKYSHhRNIATYYGAFIkknppgMDD 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd06637  83 QLWLVMEFCGAGSVTDLIK--------NTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVD 154
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 719 FGL----------MRTSYGSDYykmlhrsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd06637 155 FGVsaqldrtvgrRNTFIGTPY-------WMAPEVIACDENPDATYDFKSDLWSLGITAIEM 209
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
568-770 1.80e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 59.66  E-value: 1.80e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGiytSGLFAPEPMAVAVKKCRhdaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06646  15 QRVGSGTYGDVYKA---RNLHTGELAAVKIIKLE---PGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADhdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM----- 722
Cdd:cd06646  89 GGGSLQDIYHVTGPLSE----------LQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAakita 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 723 ----RTSY-GSDYykmlhrswmpvrWMSKE--AIEQ-GRFSEASDVWSFGVTLWEI 770
Cdd:cd06646 159 tiakRKSFiGTPY------------WMAPEvaAVEKnGGYNQLCDIWAVGITAIEL 202
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
569-792 1.82e-09

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK9 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 60.08  E-value: 1.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSG--IYTSGLfapepmaVAVKKCRHDatNAERA---QLEQEIRAVATFDHPNVIKLIGVCY----MDN- 638
Cdd:cd07865  19 KIGQGTFGEVFKArhRKTGQI-------VALKKVLME--NEKEGfpiTALREIKILQLLKHENVVNLIEICRtkatPYNr 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 ---SLLAVFEYMVHgDLHELLKVrvPPADHDMGGITEanaeflyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd07865  90 ykgSIYLVFEFCEH-DLAGLLSN--KNVKFTLSEIKK-------VMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLK 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 716 IADFGLMRT---SYGSDYYKMLHRswMPVRWMSKEAIEQG--RFSEASDVWSFGVTLWEIWSfgRQP-YEGASNQQVIEL 789
Cdd:cd07865 160 LADFGLARAfslAKNSQPNRYTNR--VVTLWYRPPELLLGerDYGPPIDMWGAGCIMAEMWT--RSPiMQGNTEQHQLTL 235

                ...
gi 71980965 790 VAN 792
Cdd:cd07865 236 ISQ 238
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
570-790 1.86e-09

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 60.48  E-value: 1.86e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVV------HSGIYTSGLFAPEPMAVAVKKCRHDATnaeraqleqEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd05593  23 LGKGTFGKVilvrekASGKYYAMKILKKEVIIAKDEVAHTLT---------ESRVLKNTRHPFLTSLKYSFQTKDRLCFV 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLH-ELLKVRVPPADHDMggiteanaeflYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd05593  94 MEYVNGGELFfHLSRERVFSEDRTR-----------FYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLC 162
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 723 RTSYgSDYYKMLHRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd05593 163 KEGI-TDAATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 227
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
566-778 1.98e-09

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 59.57  E-value: 1.98e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAERA---------QLEQEIRAVATF-DHPNVIKLIGVCY 635
Cdd:cd14091   4 IKEEIGKGSYSVC-------------------KRCIHKATGKEYAvkiidkskrDPSEEIEILLRYgQHPNIITLRDVYD 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNSLLAVFEYMVHGDLHE-LLKVRVppadhdmggITEANAEflYIATQIALGMEYLASMSFVHRDLATRNCLV----GD 710
Cdd:cd14091  65 DGNSVYLVTELLRGGELLDrILRQKF---------FSEREAS--AVMKTLTKTVEYLHSQGVVHRDLKPSNILYadesGD 133
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965 711 TRTIKIADFGL---MRTSYGsdyykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd14091 134 PESLRICDFGFakqLRAENG-----LLMTPCYTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLA-GYTPF 198
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
568-780 2.00e-09

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 59.10  E-value: 2.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGiyTSGLFAPePMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd14164   6 TTIGEGSFSKVKLA--TSQKYCC-KVAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIEVANGRLYIVMEA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLkvrvppadHDMGGITEANAEFLYIatQIALGMEYLASMSFVHRDLATRNCLV-GDTRTIKIADFGLMRtsY 726
Cdd:cd14164  83 AATDLLQKI--------QEVHHIPKDLARDMFA--QMVGAVNYLHDMNIVHRDLKCENILLsADDRKIKIADFGFAR--F 150
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 727 GSDYYKMLHRSWMPVRWMSKEAIEQGRF-SEASDVWSFGVTLWEIWSfGRQPYEG 780
Cdd:cd14164 151 VEDYPELSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVLYVMVT-GTMPFDE 204
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
595-764 2.27e-09

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 60.12  E-value: 2.27e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCR---HDATNAERAQleQEIRAVATFDHPNVIKLIGVCYMDNSL------LAVFEYMVHgDLHELLKVRVppaDH 665
Cdd:cd07850  28 VAIKKLSrpfQNVTHAKRAY--RELVLMKLVNHKNIIGLLNVFTPQKSLeefqdvYLVMELMDA-NLCQVIQMDL---DH 101
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 666 dmggitEANAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGS---------DYYKmlhr 736
Cdd:cd07850 102 ------ERMSYLLY---QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfmmtpyvvtRYYR---- 168
                       170       180
                ....*....|....*....|....*...
gi 71980965 737 swmpvrwmSKEAIEQGRFSEASDVWSFG 764
Cdd:cd07850 169 --------APEVILGMGYKENVDIWSVG 188
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
551-785 2.29e-09

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


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 59.17  E-value: 2.29e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 551 DNSYKVFEITPSQLsvrekiGEGQFGVVHSGIYTSGlfAPEPMAVAVKKCRHDATNaeRAQLEQEIRAV-ATFDHPNVIK 629
Cdd:cd14198   3 DNFNNFYILTSKEL------GRGKFAVVRQCISKST--GQEYAAKFLKKRRRGQDC--RAEILHEIAVLeLAKSNPRVVN 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 630 LIGVCYMDNSLLAVFEYMVHGDLHEL----LKVRVPPADhdmggiteanaeFLYIATQIALGMEYLASMSFVHRDLATRN 705
Cdd:cd14198  73 LHEVYETTSEIILILEYAAGGEIFNLcvpdLAEMVSEND------------IIRLIRQILEGVYYLHQNNIVHLDLKPQN 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 706 CLV------GDtrtIKIADFGLMRTSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd14198 141 ILLssiyplGD---IKIVDFGMSRKIGHACELREIMGT---PEYLAPEILNYDPITTATDMWNIGVIAYMLLT-HESPFV 213

                ....*.
gi 71980965 780 GASNQQ 785
Cdd:cd14198 214 GEDNQE 219
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
570-794 2.41e-09

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: 58.81  E-value: 2.41e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH--SGIYTSGLFAPEPMavavKKCRHDATNAERAQLeQEIRAVATFDHPNVIKLigvCYM---DNSLLAVF 644
Cdd:cd05578   8 IGKGSFGKVCivQKKDTKKMFAMKYM----NKQKCIEKDSVRNVL-NELEILQELEHPFLVNL---WYSfqdEEDMYMVV 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDL--HELLKVRVppadhdmggiTEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd05578  80 DLLLGGDLryHLQQKVKF----------SEETVKF-YIC-EIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIA 147
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 723 RtsygsdyykMLHRSWMPVR------WMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVIELVANRH 794
Cdd:cd05578 148 T---------KLTDGTLATStsgtkpYMAPEVFMRAGYSFAVDWWSLGVTAYEML-RGKRPYEIHSRTSIEEIRAKFE 215
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
570-770 2.42e-09

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


Pssm-ID: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 60.04  E-value: 2.42e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSgLFAPepmaVAVKK-CR--HDATNAERAQleQEIRAVATFDHPNVIKLIGVcYMDNSLLAVFE- 645
Cdd:cd07876  29 IGSGAQGIVCAAFDTV-LGIN----VAVKKlSRpfQNQTHAKRAY--RELVLLKCVNHKNIISLLNV-FTPQKSLEEFQd 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 646 -YMVHgdlhELLKVRVPPADHdmggiTEANAEFL-YIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMR 723
Cdd:cd07876 101 vYLVM----ELMDANLCQVIH-----MELDHERMsYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 724 TSYGSdyykMLHRSWMPVRWM-SKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd07876 172 TACTN----FMMTPYVVTRYYrAPEVILGMGYKENVDIWSVGCIMGEL 215
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
563-770 2.45e-09

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: 59.38  E-value: 2.45e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAEraqlEQEIRAVATFDHPNVIKLIG----VCYMDN 638
Cdd:cd14142   6 QITLVECIGKGRYGEVWRGQWQG-----ESVAVKIFSSRDEKSWFR----ETEIYNTVLLRHENILGFIAsdmtSRNSCT 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvRVPPADHDMggiteanaefLYIATQIALGMEYLASMSF--------VHRDLATRNCLVGD 710
Cdd:cd14142  77 QLWLITHYHENGSLYDYLQ-RTTLDHQEM----------LRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKS 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 711 TRTIKIADFGLMRT-SYGSDYYKMLHRSWMPV-RWMSKEAIEQGRFSEA------SDVWSFGVTLWEI 770
Cdd:cd14142 146 NGQCCIADLGLAVThSQETNQLDVGNNPRVGTkRYMAPEVLDETINTDCfesykrVDIYAFGLVLWEV 213
Ig_Pro_neuregulin-1 cd05895
Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of ...
17-96 2.76e-09

Immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1; The members here are composed of the immunoglobulin (Ig)-like domain found in neuregulin (NRG)-1. There are many NRG-1 isoforms which arise from the alternative splicing of mRNA. NRG-1 belongs to the neuregulin gene family which is comprised of four genes. This group represents NRG-1. NRGs are signaling molecules which participate in cell-cell interactions in the nervous system, breast, and heart, and other organ systems, and are implicated in the pathology of diseases including schizophrenia, multiple sclerosis, and breast cancer. The NRG-1 protein binds to and activates the tyrosine kinases receptors ErbB3 and ErbB4, initiating signaling cascades. NRG-1 has multiple functions, for example, in the brain it regulates various processes such as radial glia formation and neuronal migration, dendritic development, and expression of neurotransmitters receptors in the peripheral nervous system NRG-1 regulates processes such as target cell differentiation, and Schwann cell survival.


Pssm-ID: 409476  Cd Length: 93  Bit Score: 55.00  E-value: 2.76e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  17 QLRNATKSSGDEVRFKCEALGT-PPLKFIWLKNNGPVEKTKR---VKIRDKENSSRLVITQLDVLDSGYYQCIVS----N 88
Cdd:cd05895   5 EMKSQEVAAGSKLVLRCETSSEyPSLRFKWFKNGKEINRKNKpenIKIQKKKKKSELRINKASLADSGEYMCKVSsklgN 84

                ....*...
gi 71980965  89 PAASVNTT 96
Cdd:cd05895  85 DSASANVT 92
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
609-770 3.24e-09

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 58.96  E-value: 3.24e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 609 RAQLEQEI--RAVATF-DHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEfLYIATQIa 685
Cdd:cd05609  41 RNQIQQVFveRDILTFaENPFVVSMYCSFETKRHLCMVMEYVEGGDCATLLK--------NIGPLPVDMAR-MYFAETV- 110
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 686 LGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-------MRTSYGSDYYKMLHRSWMPVR------WMSKEAIEQG 752
Cdd:cd05609 111 LALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLskiglmsLTTNLYEGHIEKDTREFLDKQvcgtpeYIAPEVILRQ 190
                       170
                ....*....|....*...
gi 71980965 753 RFSEASDVWSFGVTLWEI 770
Cdd:cd05609 191 GYGKPVDWWAMGIILYEF 208
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
563-781 3.82e-09

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


Pssm-ID: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 59.09  E-value: 3.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREKIGEGQFGVVHSGIY--TSGLFAPEpmAVAVKKCRHdATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSL 640
Cdd:cd14094   4 VYELCEVIGKGPFSVVRRCIHreTGQQFAVK--IVDVAKFTS-SPGLSTEDLKREASICHMLKHPHIVELLETYSSDGML 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 LAVFEYMVHGDL-HELLKvrvppadhdmggitEANAEFLY---IAT----QIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:cd14094  81 YMVFEFMDGADLcFEIVK--------------RADAGFVYseaVAShymrQILEALRYCHDNNIIHRDVKPHCVLLASKE 146
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 713 T---IKIADFGLMRTSygSDYYKMLH-RSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGA 781
Cdd:cd14094 147 NsapVKLGGFGVAIQL--GESGLVAGgRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILFILLS-GCLPFYGT 215
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
570-788 4.00e-09

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


Pssm-ID: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 59.15  E-value: 4.00e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVV----HSGiyTSGLFAPEpmavAVKKCR------HDATNAERAQLEQEIRavatfdHPNVIKLIGVCYMDNS 639
Cdd:cd05570   3 LGKGSFGKVmlaeRKK--TDELYAIK----VLKKEViiedddVECTMTEKRVLALANR------HPFLTGLHACFQTEDR 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDL-HELLKVRVppadhdmggITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05570  71 LYFVMEYVNGGDLmFHIQRARR---------FTEERARF-YAA-EICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIAD 139
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMR--TSYGS---------DYykmlhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVI 787
Cdd:cd05570 140 FGMCKegIWGGNttstfcgtpDY-------------IAPEILREQDYGFSVDWWALGVLLYEMLA-GQSPFEGDDEDELF 205

                .
gi 71980965 788 E 788
Cdd:cd05570 206 E 206
IgI_telokin-like cd20973
immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF ...
18-101 4.09e-09

immunoglobulin-like domain of telokin and similar proteins; a member of the I-set of IgSF domains; The members here are composed of the immunoglobulin (Ig) domain in telokin, the C-terminal domain of myosin light chain kinase which is identical to telokin, and similar proteins. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the telokin Ig domain lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409565 [Multi-domain]  Cd Length: 88  Bit Score: 54.12  E-value: 4.09e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  18 LRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKI-RDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTT 96
Cdd:cd20973   4 LRDKEVVEGSAARFDCKVEGYPDPEVKWMKDDNPIVESRRFQIdQDEDGLCSLIISDVCGDDSGKYTCKAVNSLGEATCS 83

                ....*
gi 71980965  97 SVLRV 101
Cdd:cd20973  84 AELTV 88
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
549-827 4.19e-09

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: 58.92  E-value: 4.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 549 IDDNSYKVfeiTPSQLSVREKIGEGQFGVVhsgiyTSGLFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVA-TFDHPNV 627
Cdd:cd06618   5 IDGKKYKA---DLNDLENLGEIGSGTCGQV-----YKMRHKKTGHVMAVKQMRRSGNKEENKRILMDLDVVLkSHDCPYI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 628 IKLIGVCYMDNSLLAVFEYMvhGDLHELLKVRVppadhdMGGITEANAEFLYIATQIALgmEYL-ASMSFVHRDLATRNC 706
Cdd:cd06618  77 VKCYGYFITDSDVFICMELM--STCLDKLLKRI------QGPIPEDILGKMTVSIVKAL--HYLkEKHGVIHRDVKPSNI 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 707 LVGDTRTIKIADFGLMrtsyGSDYYKMLH-RSWMPVRWMSKEAIEQGRFSE---ASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:cd06618 147 LLDESGNVKLCDFGIS----GRLVDSKAKtRSAGCAAYMAPERIDPPDNPKydiRADVWSLGISLVELAT-GQFPYRNCK 221
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 71980965 783 NQ-QVIELVANRHLLECPHNCPTNI--YSLMVECWHENIERRPTFSEI 827
Cdd:cd06618 222 TEfEVLTKILNEEPPSLPPNEGFSPdfCSFVDLCLTKDHRYRPKYREL 269
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
568-770 4.19e-09

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 58.52  E-value: 4.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSglfAPEPMAVAVKKCRhdaTNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd06645  17 QRIGSGTYGDVYKARNVN---TGELAAIKVIKLE---PGEDFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFC 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLKVRVPPADhdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL------ 721
Cdd:cd06645  91 GGGSLQDIYHVTGPLSE----------SQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVsaqita 160
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 722 ---MRTSY-GSDYykmlhrswmpvrWMSKE--AIE-QGRFSEASDVWSFGVTLWEI 770
Cdd:cd06645 161 tiaKRKSFiGTPY------------WMAPEvaAVErKGGYNQLCDIWAVGITAIEL 204
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
568-833 4.36e-09

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: 58.27  E-value: 4.36e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLFAPEPMAVAVKKCRHDATNAeraqLE-QEIRAVAtfDHPNVIKLIGVC----YMDNSLLA 642
Cdd:cd13975   6 RELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLA----LEfHYTRSLP--KHERIVSLHGSVidysYGGGSSIA 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYM--VHGDLHELLKvrvppadhdmGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd13975  80 VLLIMerLHRDLYTGIK----------AGLSLE--ERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLG 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LMRTSygsdyyKMLHRSWM--PVRwMSKEAIEqGRFSEASDVWSFGVTLWEIWSFG-RQPY---EGASNQQVIELVANRH 794
Cdd:cd13975 148 FCKPE------AMMSGSIVgtPIH-MAPELFS-GKYDNSVDVYAFGILFWYLCAGHvKLPEafeQCASKDHLWNNVRKGV 219
                       250       260       270
                ....*....|....*....|....*....|....*....
gi 71980965 795 LLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQS 833
Cdd:cd13975 220 RPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQG 258
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
568-835 5.31e-09

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: 58.22  E-value: 5.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSGIYTSGLfapepmaVAVKKCrhdATNAERAQL-EQEIRAVATFDHPNVIKLIGVCYMDN----SLLA 642
Cdd:cd14143   1 ESIGKGRFGEVWRGRWRGED-------VAVKIF---SSREERSWFrEAEIYQTVMLRHENILGFIAADNKDNgtwtQLWL 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKvRVPPadhDMGGITEANaefLYIATQIA-LGMEYLASM---SFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd14143  71 VSDYHEHGSLFDYLN-RYTV---TVEGMIKLA---LSIASGLAhLHMEIVGTQgkpAIAHRDLKSKNILVKKNGTCCIAD 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGL-MRTSYGSDYYKML--HRSWMPvRWMSKEAIEQG-------RFSEAsDVWSFGVTLWEIwsfGRQPYEGASNQQ--- 785
Cdd:cd14143 144 LGLaVRHDSATDTIDIApnHRVGTK-RYMAPEVLDDTinmkhfeSFKRA-DIYALGLVFWEI---ARRCSIGGIHEDyql 218
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 786 -VIELVANRHLLE------CPHNCPTNI-------------YSLMVECWHENIERRPTFSEIRSRLQSWS 835
Cdd:cd14143 219 pYYDLVPSDPSIEemrkvvCEQKLRPNIpnrwqscealrvmAKIMRECWYANGAARLTALRIKKTLSQLS 288
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
566-790 5.61e-09

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 57.98  E-value: 5.61e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVH------SGIYTSGLFAPEPMAVavkkcrhdatnaERAQLEQEIRAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd14114   6 ILEELGTGAFGVVHrcteraTGNNFAAKFIMTPHES------------DKETVRKEIQIMNQLHHPKLINLHDAFEDDNE 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHEllkvRVPPADHDMggiteANAEFLYIATQIALGMEYLASMSFVHRDLATRN--CLVGDTRTIKIA 717
Cdd:cd14114  74 MVLILEFLSGGELFE----RIAAEHYKM-----SEAEVINYMRQVCEGLCHMHENNIVHLDIKPENimCTTKRSNEVKLI 144
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 718 DFGLMRTSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14114 145 DFGLATHLDPKESVKVTTGT---AEFAAPEIVEREPVGFYTDMWAVGVLSYVLLS-GLSPFAGENDDETLRNV 213
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
683-786 5.65e-09

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 57.91  E-value: 5.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 683 QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTsYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWS 762
Cdd:cd14111 107 QILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQS-FNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWS 185
                        90       100
                ....*....|....*....|....
gi 71980965 763 FGVTLWEIWSfGRQPYEGASNQQV 786
Cdd:cd14111 186 IGVLTYIMLS-GRSPFEDQDPQET 208
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
564-850 5.94e-09

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 58.20  E-value: 5.94e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHSGIYtsglfAPEPMAVAVKKCRHDATNAERAQLEQEIR-AVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd06617   3 LEVIEELGRGAYGVVDKMRH-----VPTGTIMAVKRIRATVNSQEQKRLLMDLDiSMRSVDCPYTVTFYGALFREGDVWI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMvHGDLHELLKVRVppaDHDMGgITEanaEFL-YIATQIALGMEYLAS-MSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd06617  78 CMEVM-DTSLDKFYKKVY---DKGLT-IPE---DILgKIAVSIVKALEYLHSkLSVIHRDVKPSNVLINRNGQVKLCDFG 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 LmrTSYGSD-YYKMLHRSWMPvrWMSKEAI----EQGRFSEASDVWSFGVTLWEIwSFGRQPYE--GASNQQVIELVAnr 793
Cdd:cd06617 150 I--SGYLVDsVAKTIDAGCKP--YMAPERInpelNQKGYDVKSDVWSLGITMIEL-ATGRFPYDswKTPFQQLKQVVE-- 222
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71980965 794 hllECPHNCPTNIYSLMVE-----CWHENIERRPTFSEIRsrlqswslaspAHSILQQHNNR 850
Cdd:cd06617 223 ---EPSPQLPAEKFSPEFQdfvnkCLKKNYKERPNYPELL-----------QHPFFELHLSK 270
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
568-827 6.65e-09

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: 57.70  E-value: 6.65e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVhsgiytsglfapepMAV---------AVKKCRHDATN-AERAQLEQEIRAVATF-DHPNVIKLI----- 631
Cdd:cd14050   7 SKLGEGSFGEV--------------FKVrsredgklyAVKRSRSRFRGeKDRKRKLEEVERHEKLgEHPNCVRFIkawee 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 -GVCYM-----DNSLLAVFEymVHGDLHEllkvrvppadhdmggiteanAEFLYIATQIALGMEYLASMSFVHRDLATRN 705
Cdd:cd14050  73 kGILYIqtelcDTSLQQYCE--ETHSLPE--------------------SEVWNILLDLLKGLKHLHDHGLIHLDIKPAN 130
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 706 CLVGDTRTIKIADFGLMRTSYGSDyykMLHRSWMPVRWMSKEAIeQGRFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQ 785
Cdd:cd14050 131 IFLSKDGVCKLGDFGLVVELDKED---IHDAQEGDPRYMAPELL-QGSFTKAADIFSLGITILELACNLELPSGGDGWHQ 206
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 786 vielVANRHLlecPHNC----PTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd14050 207 ----LRQGYL---PEEFtaglSPELRSIIKLMMDPDPERRPTAEDL 245
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
568-808 8.33e-09

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


Pssm-ID: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 57.71  E-value: 8.33e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLFAPEPMavavkkcrhDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYM-------DN 638
Cdd:cd06636  22 EVVGNGTYGQVYKGrhVKTGQLAAIKVM---------DVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIkksppghDD 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd06636  93 QLWLVMEFCGAGSVTDLVK--------NTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVD 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGL----------MRTSYGSDYykmlhrsWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIwsfgrqpYEGASnqQVIE 788
Cdd:cd06636 165 FGVsaqldrtvgrRNTFIGTPY-------WMAPEVIACDENPDATYDYRSDIWSLGITAIEM-------AEGAP--PLCD 228
                       250       260
                ....*....|....*....|
gi 71980965 789 LVANRHLLECPHNCPTNIYS 808
Cdd:cd06636 229 MHPMRALFLIPRNPPPKLKS 248
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
612-792 1.04e-08

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: 57.78  E-value: 1.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 612 LEQEIRAVATfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLheLLKVRvppadhDMGGITEANAEFlYIAtQIALGMEYL 691
Cdd:cd05592  44 IERRVLALAS-QHPFLTHLFCTFQTESHLFFVMEYLNGGDL--MFHIQ------QSGRFDEDRARF-YGA-EIICGLQFL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 692 ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS-YGS----------DYykmlhrswmpvrwMSKEAIEQGRFSEASDV 760
Cdd:cd05592 113 HSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENiYGEnkastfcgtpDY-------------IAPEILKGQKYNQSVDW 179
                       170       180       190
                ....*....|....*....|....*....|..
gi 71980965 761 WSFGVTLWEIWsFGRQPYEGASNQQVIELVAN 792
Cdd:cd05592 180 WSFGVLLYEML-IGQSPFHGEDEDELFWSICN 210
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
605-790 1.06e-08

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 57.80  E-value: 1.06e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 605 TNAERAQLEqeirAVatfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFlYIAtQI 684
Cdd:cd05584  47 TKAERNILE----AV---KHPFIVDLHYAFQTGGKLYLILEYLSGGELFMHLERE--------GIFMEDTACF-YLA-EI 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 685 ALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDyyKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFG 764
Cdd:cd05584 110 TLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESIHDG--TVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLG 187
                       170       180
                ....*....|....*....|....*.
gi 71980965 765 VTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd05584 188 ALMYDMLT-GAPPFTAENRKKTIDKI 212
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
665-778 1.08e-08

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: 57.37  E-value: 1.08e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 665 HDMG--GITEANAEFlYiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL-MRTSYGsdyyKMLHRSWMPV 741
Cdd:cd05605  92 YNMGnpGFEEERAVF-Y-AAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLaVEIPEG----ETIRGRVGTV 165
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 71980965 742 RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd05605 166 GYMAPEVVKNERYTFSPDWWGLGCLIYEMIE-GQAPF 201
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
640-779 1.13e-08

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: 57.15  E-value: 1.13e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLkvrvppADHDMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd05577  68 LCLVLTLMNGGDLKYHI------YNVGTRGFSEARAIFY--AAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDL 139
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965 720 GLMRTSYGSdyyKMLHRSWMPVRWMSKEAIEQGR-FSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd05577 140 GLAVEFKGG---KKIKGRVGTHGYMAPEVLQKEVaYDFSVDWFALGCMLYEMIA-GRSPFR 196
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
608-827 1.14e-08

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


Pssm-ID: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 56.94  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 608 ERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADhdmggiteanAEFLYIATQIALG 687
Cdd:cd14188  44 QREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTE----------PEVRYYLRQIVSG 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 688 MEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM----------RTSYGSDYYkmlhrswmpvrwMSKEAI-EQGRFSE 756
Cdd:cd14188 114 LKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAarleplehrrRTICGTPNY------------LSPEVLnKQGHGCE 181
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 757 aSDVWSFGVTLWEIWsFGRQPYEGASNQQVIelvanRHLLECPHNCPTNIYS----LMVECWHENIERRPTFSEI 827
Cdd:cd14188 182 -SDIWALGCVMYTML-LGRPPFETTNLKETY-----RCIREARYSLPSSLLApakhLIASMLSKNPEDRPSLDEI 249
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
570-770 1.40e-08

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 57.68  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  570 IGEGQFGVVHSGIYTSGLFAPepmaVAVKKCRHDATNAERA--QLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:PTZ00426  38 LGTGSFGRVILATYKNEDFPP----VAIKRFEKSKIIKQKQvdHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  648 VHGDLHELLK--VRVPpadHDMGgiteanaefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTS 725
Cdd:PTZ00426 114 IGGEFFTFLRrnKRFP---NDVG---------CFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVV 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 71980965  726 YGSDYYkmlhRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:PTZ00426 182 DTRTYT----LCGTP-EYIAPEILLNVGHGKAADWWTLGIFIYEI 221
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
568-827 1.47e-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: 56.92  E-value: 1.47e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHS-GIYTSGLFApepmavAVKKCrhDATNAERAQLEQEIRAVATF-DHPNVIKLIGVCYMDNSLLA--- 642
Cdd:cd06639  28 ETIGKGTYGKVYKvTNKKDGSLA------AVKIL--DPISDVDEEIEAEYNILRSLpNHPNVVKFYGMFYKADQYVGgql 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 --VFEYMVHGDLHELLKVRVppadhdMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd06639 100 wlVLELCNGGSVTELVKGLL------KCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 721 ---------LMR-TSYGSDYykmlhrswmpvrWMSKEAI--EQG---RFSEASDVWSFGVTLWEIwsfgrqpyeGASNQQ 785
Cdd:cd06639 174 vsaqltsarLRRnTSVGTPF------------WMAPEVIacEQQydySYDARCDVWSLGITAIEL---------ADGDPP 232
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 71980965 786 VIELVANRHLLECPHNCPTNIYS----------LMVECWHENIERRPTFSEI 827
Cdd:cd06639 233 LFDMHPVKALFKIPRNPPPTLLNpekwcrgfshFISQCLIKDFEKRPSVTHL 284
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
552-782 1.50e-08

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 57.70  E-value: 1.50e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 552 NSYKVFEITPSQLSVREKIGEGQFGVVH-------SGIYTSGLFAPEPMavaVKKcrhdatnAERAQLEQEIRAVATFDH 624
Cdd:cd05621  42 NKIRELQMKAEDYDVVKVIGRGAFGEVQlvrhkasQKVYAMKLLSKFEM---IKR-------SDSAFFWEERDIMAFANS 111
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 625 PNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppADHDmggITEANAEFlYIAtQIALGMEYLASMSFVHRDLATR 704
Cdd:cd05621 112 PWVVQLFCAFQDDKYLYMVMEYMPGGDLVNLM------SNYD---VPEKWAKF-YTA-EVVLALDAIHSMGLIHRDVKPD 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 705 NCLVGDTRTIKIADFGlmrTSYGSDYYKMLH--RSWMPVRWMSKEAIEQ----GRFSEASDVWSFGVTLWEIWsFGRQPY 778
Cdd:cd05621 181 NMLLDKYGHLKLADFG---TCMKMDETGMVHcdTAVGTPDYISPEVLKSqggdGYYGRECDWWSVGVFLFEML-VGDTPF 256

                ....
gi 71980965 779 EGAS 782
Cdd:cd05621 257 YADS 260
IgI_2_FGFR cd05857
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of ...
24-101 1.94e-08

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor; member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor. FGF receptors bind FGF signaling polypeptides. FGFs participate in multiple processes such as morphogenesis, development, and angiogenesis. FGFs bind to four FGF receptor tyrosine kinases (FGFR1, FGFR2, FGFR3, FGFR4). Receptor diversity is controlled by alternative splicing producing splice variants with different ligand binding characteristics and different expression patterns. FGFRs have an extracellular region comprised of three IG-like domains, a single transmembrane helix, and an intracellular tyrosine kinase domain. Ligand binding and specificity reside in the Ig-like domains 2 and 3, and the linker region that connects these two. FGFR activation and signaling depend on FGF-induced dimerization, a process involving cell surface heparin or heparin sulfate proteoglycans.


Pssm-ID: 409443 [Multi-domain]  Cd Length: 95  Bit Score: 52.55  E-value: 1.94e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  24 SSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRV---KIRDKENSsrLVITQLDVLDSGYYQCIVSNPAASVNTTSVLR 100
Cdd:cd05857  17 PAANTVKFRCPAAGNPTPTMRWLKNGKEFKQEHRIggyKVRNQHWS--LIMESVVPSDKGNYTCVVENEYGSINHTYHLD 94

                .
gi 71980965 101 V 101
Cdd:cd05857  95 V 95
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
562-770 2.01e-08

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 57.14  E-value: 2.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  562 SQLSVREKIGEGQFGVV----HSGiytSGlfapEPMAVAVKKCRHDATNAERAQLEQEIRAVATFDHPNVIKLIgVCYMD 637
Cdd:PTZ00263  18 SDFEMGETLGTGSFGRVriakHKG---TG----EYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMM-CSFQD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  638 -NSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:PTZ00263  90 eNRVYFLLEFVVGGELFTHLR--------KAGRFPNDVAKF-YHA-ELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKV 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965  717 ADFGLMRtsygsdyyKMLHRSW----MPvRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:PTZ00263 160 TDFGFAK--------KVPDRTFtlcgTP-EYLAPEVIQSKGHGKAVDWWTMGVLLYEF 208
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
566-791 2.04e-08

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


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 56.95  E-value: 2.04e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 566 VREKIGEGQFGVVHSGIYTSglfapEPMAVAVK---KCRHDATnaeraqleQEIRAVATF-DHPNVIKLIGVCYMDNSLL 641
Cdd:cd14176  23 VKEDIGVGSYSVCKRCIHKA-----TNMEFAVKiidKSKRDPT--------EEIEILLRYgQHPNIITLKDVYDDGKYVY 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDL-HELLKVRVPPAdhdmggiTEANAeFLYIATQIAlgmEYLASMSFVHRDLATRNCLV----GDTRTIKI 716
Cdd:cd14176  90 VVTELMKGGELlDKILRQKFFSE-------REASA-VLFTITKTV---EYLHAQGVVHRDLKPSNILYvdesGNPESIRI 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 717 ADFGL---MRTSYGsdyykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVA 791
Cdd:cd14176 159 CDFGFakqLRAENG-----LLMTPCYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFANGPDDTPEEILA 230
IgI_4_hemolin-like cd20978
Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set ...
10-101 2.28e-08

Fourth immunoglobulin (Ig)-like domain of hemolin, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin (Ig)-like domain of hemolin and similar proteins. Hemolin, an insect immunoglobulin superfamily (IgSF) member containing four Ig-like domains, is a lipopolysaccharide-binding immune protein induced during bacterial infection. Hemolin shares significant sequence similarity with the first four Ig-like domains of the transmembrane cell adhesion molecules (CAMs) of the L1 family. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The fourth Ig-like domain of hemolin is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set domains, members of the I-set have a discontinuous A strand but lack a C" strand. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409570 [Multi-domain]  Cd Length: 88  Bit Score: 52.01  E-value: 2.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  10 PYIrLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTK-RVKIRDkensSRLVITQLDVLDSGYYQCIVSN 88
Cdd:cd20978   1 PKF-IQKPEKNVVVKGGQDVTLPCQVTGVPQPKITWLHNGKPLQGPMeRATVED----GTLTIINVQPEDTGYYGCVATN 75
                        90
                ....*....|...
gi 71980965  89 PAASVNTTSVLRV 101
Cdd:cd20978  76 EIGDIYTETLLHV 88
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
556-770 2.35e-08

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 56.98  E-value: 2.35e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 556 VFEItPSQLSVREKIGEGQFGVVHSGiYTSGLfapePMAVAVKKCR---HDATNAERAQleQEIRAVATFDHPNVIKLIG 632
Cdd:cd07878  10 VWEV-PERYQNLTPVGSGAYGSVCSA-YDTRL----RQKVAVKKLSrpfQSLIHARRTY--RELRLLKHMKHENVIGLLD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 633 VCYMDNSLLAVFE-YMVH----GDLHELLKVRVPPADHdmggiteanAEFLyiATQIALGMEYLASMSFVHRDLATRNCL 707
Cdd:cd07878  82 VFTPATSIENFNEvYLVTnlmgADLNNIVKCQKLSDEH---------VQFL--IYQLLRGLKYIHSAGIIHRDLKPSNVA 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 708 VGDTRTIKIADFGLMR------TSY-GSDYYK----MLhrSWMpvrwmskeaieqgRFSEASDVWSFGVTLWEI 770
Cdd:cd07878 151 VNEDCELRILDFGLARqaddemTGYvATRWYRapeiML--NWM-------------HYNQTVDIWSVGCIMAEL 209
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
545-785 2.68e-08

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 55.82  E-value: 2.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 545 SQEPIDDnsykVFEITPsqlsvrEKIGEGQFGVVhsgiytsglfapepmavavKKCRHDATNAE----------RAQ-LE 613
Cdd:cd14106   1 STENINE----VYTVES------TPLGRGKFAVV-------------------RKCIHKETGKEyaakflrkrrRGQdCR 51
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEI-RAVATF----DHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppaDHDmGGITEANAEFLYIatQIALGM 688
Cdd:cd14106  52 NEIlHEIAVLelckDCPRVVNLHEVYETRSELILILELAAGGELQTLL-------DEE-ECLTEADVRRLMR--QILEGV 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 689 EYLASMSFVHRDLATRNCLVGDTRT---IKIADFGLMR-TSYGSDYYKMLHrswmPVRWMSKEAIEQGRFSEASDVWSFG 764
Cdd:cd14106 122 QYLHERNIVHLDLKPQNILLTSEFPlgdIKLCDFGISRvIGEGEEIREILG----TPDYVAPEILSYEPISLATDMWSIG 197
                       250       260
                ....*....|....*....|.
gi 71980965 765 VTLWEIWSfGRQPYEGASNQQ 785
Cdd:cd14106 198 VLTYVLLT-GHSPFGGDDKQE 217
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
570-770 2.80e-08

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 56.30  E-value: 2.80e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVV----HSGiytSGLFapepmaVAVKKCRH--DATNAERAQLEQEIRAVATFDHPNVIK-------LIGVCYM 636
Cdd:cd13989   1 LGSGGFGYVtlwkHQD---TGEY------VAIKKCRQelSPSDKNRERWCLEVQIMKKLNHPNVVSardvppeLEKLSPN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVfEYMVHGDLHELLKvRVPPAdhdmGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLV--GDTRTI 714
Cdd:cd13989  72 DLPLLAM-EYCSGGDLRKVLN-QPENC----CGLKES--EVRTLLSDISSAISYLHENRIIHRDLKPENIVLqqGGGRVI 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 715 -KIADFGlmrtsygsdYYKMLHRSWM------PVRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd13989 144 yKLIDLG---------YAKELDQGSLctsfvgTLQYLAPELFESKKYTCTVDYWSFGTLAFEC 197
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
551-790 3.01e-08

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: 56.21  E-value: 3.01e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 551 DNSYKVFEItpsqlsvREKIGEGQFG--VVHSGIYTSGLFApepmavaVKKCRHDATNAERAQLEQEIRAVATFDHPNVI 628
Cdd:cd14168   6 EDIKKIFEF-------KEVLGTGAFSevVLAEERATGKLFA-------VKCIPKKALKGKESSIENEIAVLRKIKHENIV 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 629 KLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd14168  72 ALEDIYESPNHLYLVMQLVSGGELFDRIV--------EKGFYTEKDASTL--IRQVLDAVYYLHRMGIVHRDLKPENLLY 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 ---GDTRTIKIADFGLMRTSYGSDyykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQPYEGASNQQ 785
Cdd:cd14168 142 fsqDEESKIMISDFGLSKMEGKGD---VMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPFYDENDSK 217

                ....*
gi 71980965 786 VIELV 790
Cdd:cd14168 218 LFEQI 222
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
570-729 3.49e-08

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


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 56.43  E-value: 3.49e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGI--YTSGLFAPEPMAVAvkkcrhDATNAERA-QLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd05610  12 ISRGAFGKVYLGRkkNNSKLYAVKVVKKA------DMINKNMVhQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEY 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLkvrvppadHDMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSY 726
Cdd:cd05610  86 LIGGDVKSLL--------HIYGYFDEEMAVK-YIS-EVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTL 155

                ...
gi 71980965 727 GSD 729
Cdd:cd05610 156 NRE 158
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
614-787 4.30e-08

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: 55.83  E-value: 4.30e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEIRAVATFDHPNVIKLIGVCYMD-NSLLAVFEYMVHGDLHELLKvrvppaDHDMGGITEANAeflyIATQIALGMEYLA 692
Cdd:cd14040  59 REYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLK------QHKLMSEKEARS----IVMQIVNALRYLN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 693 SMS--FVHRDLATRNCLVGDTRT---IKIADFGLMRT----SYGSDYYKMLHRSWMPVRWMSKEAI----EQGRFSEASD 759
Cdd:cd14040 129 EIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKImdddSYGVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVD 208
                       170       180
                ....*....|....*....|....*...
gi 71980965 760 VWSFGVTLWEIWsFGRQPYEGASNQQVI 787
Cdd:cd14040 209 VWSVGVIFFQCL-YGRKPFGHNQSQQDI 235
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
569-787 4.70e-08

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: 55.01  E-value: 4.70e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSglfapepMAVAVKKCR---HDATNAERAQLEQEIRAVATFDHPNVIKLI----GVCYMDNSLL 641
Cdd:cd14033   8 EIGRGSFKTVYRGLDTE-------TTVEVAWCElqtRKLSKGERQRFSEEVEMLKGLQHPNIVRFYdswkSTVRGHKCII 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKvrvppadhdmgGITEANAEFLY-IATQIALGMEYLASMS--FVHRDLATRNCLV-GDTRTIKIA 717
Cdd:cd14033  81 LVTELMTSGTLKTYLK-----------RFREMKLKLLQrWSRQILKGLHFLHSRCppILHRDLKCDNIFItGPTGSVKIG 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGLMRTSYGSDYYKMLHRSwmpvRWMSKEAIEQgRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVI 787
Cdd:cd14033 150 DLGLATLKRASFAKSVIGTP----EFMAPEMYEE-KYDEAVDVYAFGMCILEM-ATSEYPYSECQNAAQI 213
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
624-720 5.26e-08

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: 55.05  E-value: 5.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 624 HPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVppadhdmggiTEANAEFLYIATQIALGMEYLASMSFVHRDLAT 703
Cdd:cd14093  68 HPNIIELHDVFESPTFIFLVFELCRKGELFDYLTEVV----------TLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKP 137
                        90
                ....*....|....*..
gi 71980965 704 RNCLVGDTRTIKIADFG 720
Cdd:cd14093 138 ENILLDDNLNVKISDFG 154
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
615-788 5.76e-08

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: 55.77  E-value: 5.76e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVATFDHPNVIKLIGVCYMD-NSLLAVFEYMVHGDLHELLKvrvppadhDMGGITEANAEFLyiATQIALGMEYLAS 693
Cdd:cd05615  60 EKRVLALQDKPPFLTQLHSCFQTvDRLYFVMEYVNGGDLMYHIQ--------QVGKFKEPQAVFY--AAEISVGLFFLHK 129
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 694 MSFVHRDLATRNCLVGDTRTIKIADFGL----------MRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWSF 763
Cdd:cd05615 130 KGIIYRDLKLDNVMLDSEGHIKIADFGMckehmvegvtTRTFCGTPDY------------IAPEIIAYQPYGRSVDWWAY 197
                       170       180
                ....*....|....*....|....*
gi 71980965 764 GVTLWEIWSfGRQPYEGASNQQVIE 788
Cdd:cd05615 198 GVLLYEMLA-GQPPFDGEDEDELFQ 221
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
552-770 6.82e-08

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 55.48  E-value: 6.82e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 552 NSYKVFEITPSQLSVREK------IGEGQFGVVHSGiYTSGLfapePMAVAVKKCR---HDATNAERAQleQEIRAVATF 622
Cdd:cd07874   1 NQFYSVEVGDSTFTVLKRyqnlkpIGSGAQGIVCAA-YDAVL----DRNVAIKKLSrpfQNQTHAKRAY--RELVLMKCV 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 623 DHPNVIKLIGVcYMDNSLLAVFE--YMV----HGDLHELLKVRVppaDHDmggiteanaEFLYIATQIALGMEYLASMSF 696
Cdd:cd07874  74 NHKNIISLLNV-FTPQKSLEEFQdvYLVmelmDANLCQVIQMEL---DHE---------RMSYLLYQMLCGIKHLHSAGI 140
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 697 VHRDLATRNCLVGDTRTIKIADFGLMRTSyGSDYykMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd07874 141 IHRDLKPSNIVVKSDCTLKILDFGLARTA-GTSF--MMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEM 211
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
570-785 7.05e-08

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: 55.01  E-value: 7.05e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH-----SGIYTSGLFAPEPM--AVAVKKCR-HDATNAERAQLEQeIRavatfDHPNVIKLIGVCYMDNSLL 641
Cdd:cd05613   8 LGTGAYGKVFlvrkvSGHDAGKLYAMKVLkkATIVQKAKtAEHTRTERQVLEH-IR-----QSPFLVTLHYAFQTDTKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRVPPADHDMGgiteanaefLYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd05613  82 LILDYINGGELFTHLSQRERFTENEVQ---------IYIG-EIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 722 MRtSYGSDYYKMLHRSWMPVRWMSKEAIEQGR--FSEASDVWSFGVTLWEIWSfGRQPY--EGASNQQ 785
Cdd:cd05613 152 SK-EFLLDENERAYSFCGTIEYMAPEIVRGGDsgHDKAVDWWSLGVLMYELLT-GASPFtvDGEKNSQ 217
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
598-790 7.93e-08

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 55.02  E-value: 7.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 598 KKCRHDATNAERA---------QLEQEIRAVATF-DHPNVIKLIGVCYMDNSLLAVFEYMVHGDL-HELLKVRVppadhd 666
Cdd:cd14177  21 KRCIHRATNMEFAvkiidkskrDPSEEIEILMRYgQHPNIITLKDVYDDGRYVYLVTELMKGGELlDRILRQKF------ 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 667 mggITEANA-EFLYIATQIalgMEYLASMSFVHRDLATRNCLV----GDTRTIKIADFGLMRTSYGSDyyKMLHRSWMPV 741
Cdd:cd14177  95 ---FSEREAsAVLYTITKT---VDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQLRGEN--GLLLTPCYTA 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 71980965 742 RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd14177 167 NFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFANGPNDTPEEIL 214
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
615-790 8.26e-08

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 55.05  E-value: 8.26e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDL--HeLLKVRVppadhdmggITEANAEFlYIAtQIALGMEYLA 692
Cdd:cd05571  45 ENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGELffH-LSRERV---------FSEDRTRF-YGA-EIVLALGYLH 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 693 SMSFVHRDLATRNCLVGDTRTIKIADFGL----------MRTSYGSDYYkmlhrswmpvrwMSKEAIEQGRFSEASDVWS 762
Cdd:cd05571 113 SQGIVYRDLKLENLLLDKDGHIKITDFGLckeeisygatTKTFCGTPEY------------LAPEVLEDNDYGRAVDWWG 180
                       170       180
                ....*....|....*....|....*...
gi 71980965 763 FGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd05571 181 LGVVMYEMMC-GRLPFYNRDHEVLFELI 207
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
569-778 1.06e-07

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


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 54.61  E-value: 1.06e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVV------HSGiytsglfapepMAVAVKKCrhDATNAERAQLE-QEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06659  28 KIGEGSTGVVciarekHSG-----------RQVAVKMM--DLRKQQRRELLfNEVVIMRDYQHPNVVEMYKSYLVGEELW 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVrvppadhdmggiTEANAEflYIAT---QIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd06659  95 VLMEYLQGGALTDIVSQ------------TRLNEE--QIATvceAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSD 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGLMrTSYGSDYYKMLHRSWMPVrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd06659 161 FGFC-AQISKDVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIEMVD-GEPPY 217
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
565-829 1.19e-07

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 54.05  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 565 SVREKIGEGQFGVVhsgiYTSGLFAPEPMAVAVKKCRHDATNAERAQLE--QEIRAVAT--------FDHPNVIKLIGVc 634
Cdd:cd08528   3 AVLELLGSGAFGCV----YKVRKKSNGQTLLALKEINMTNPAFGRTEQErdKSVGDIISevniikeqLRHPNIVRYYKT- 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 635 YMDNSLLAVFEYMVHGdlhellkvrVPPADHdMGGITEANAEF-----LYIATQIALGMEYL-ASMSFVHRDLATRNCLV 708
Cdd:cd08528  78 FLENDRLYIVMELIEG---------APLGEH-FSSLKEKNEHFtedriWNIFVQMVLALRYLhKEKQIVHRDLKPNNIML 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 GDTRTIKIADFGLMRTSyGSDYYKMLHRSWMPVRWmSKEAIEQGRFSEASDVWSFGVTLWEIWSFgrQPYEGASNqqvIE 788
Cdd:cd08528 148 GEDDKVTITDFGLAKQK-GPESSKMTSVVGTILYS-CPEIVQNEPYGEKADIWALGCILYQMCTL--QPPFYSTN---ML 220
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 71980965 789 LVANRHLLECPHNCPTNIYSLMVE-----CWHENIERRPTFSEIRS 829
Cdd:cd08528 221 TLATKIVEAEYEPLPEGMYSDDITfvirsCLTPDPEARPDIVEVSS 266
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
596-769 1.27e-07

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: 54.33  E-value: 1.27e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 596 AVKK----CRHDATN--AERAQLEQEIraVATFDHPNVIKLIGVCYM-DNSLLAVFEYMvHGDLHELLKVRVPPADhdmg 668
Cdd:cd14001  32 AVKKinskCDKGQRSlyQERLKEEAKI--LKSLNHPNIVGFRAFTKSeDGSLCLAMEYG-GKSLNDLIEERYEAGL---- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 669 GITEAnAEFLYIATQIALGMEYLAS-MSFVHRDLATRNCLV-GDTRTIKIADFG--------LMRTSYGSDYYkmlhrsw 738
Cdd:cd14001 105 GPFPA-ATILKVALSIARALEYLHNeKKILHGDIKSGNVLIkGDFESVKLCDFGvslpltenLEVDSDPKAQY------- 176
                       170       180       190
                ....*....|....*....|....*....|....*
gi 71980965 739 mpV---RWMSKEAIEQGR-FSEASDVWSFGVTLWE 769
Cdd:cd14001 177 --VgtePWKAKEALEEGGvITDKADIFAYGLVLWE 209
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
599-765 1.58e-07

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: 53.84  E-value: 1.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 599 KCRHDATNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFl 678
Cdd:cd14166  34 KCIKKSPLSRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILER--------GVYTEKDASR- 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 679 yIATQIALGMEYLASMSFVHRDLATRNCLV---GDTRTIKIADFGL--------MRTSYGSDYYkmlhrswmpvrwMSKE 747
Cdd:cd14166 105 -VINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLskmeqngiMSTACGTPGY------------VAPE 171
                       170
                ....*....|....*...
gi 71980965 748 AIEQGRFSEASDVWSFGV 765
Cdd:cd14166 172 VLAQKPYSKAVDCWSIGV 189
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
564-821 1.62e-07

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 54.28  E-value: 1.62e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHS--GIYTSGLFAPEpmavAVKKCRHDATNAERAQLEQEI--RAVATFDHPNVIKLIGVCYMDNS 639
Cdd:cd14223   2 FSVHRIIGRGGFGEVYGcrKADTGKMYAMK----CLDKKRIKMKQGETLALNERImlSLVSTGDCPFIVCMSYAFHTPDK 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 640 LLAVFEYMVHGDLHELLkvrvppADHdmGGITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:cd14223  78 LSFILDLMNGGDLHYHL------SQH--GVFSEAEMRFY--AAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 720 GLmrtsyGSDYYKML-HRSWMPVRWMSKEAIEQG-RFSEASDVWSFGVTLWEIWSfGRQPY--EGASNQQVIELVANRHL 795
Cdd:cd14223 148 GL-----ACDFSKKKpHASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLLR-GHSPFrqHKTKDKHEIDRMTLTMA 221
                       250       260
                ....*....|....*....|....*.
gi 71980965 796 LECPHNCPTNIYSLMVECWHENIERR 821
Cdd:cd14223 222 VELPDSFSPELRSLLEGLLQRDVNRR 247
IgI_3_Robo cd05725
Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
20-101 1.63e-07

Third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the third immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1,Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409390 [Multi-domain]  Cd Length: 83  Bit Score: 49.70  E-value: 1.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  20 NATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTkRVKIRDkENSsrLVITQLDVLDSGYYQCIVSNPAASVNTTSVL 99
Cdd:cd05725   6 NQVVLVDDSAEFQCEVGGDPVPTVRWRKEDGELPKG-RYEILD-DHS--LKIRKVTAGDMGSYTCVAENMVGKIEASATL 81

                ..
gi 71980965 100 RV 101
Cdd:cd05725  82 TV 83
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
623-773 1.66e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 54.50  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  623 DHPNVIKLIGVCYMDNSLLAVFEYMvHGDLHELLKVRVPPADHDMGGIteanaeflyIATQIALGMEYLASMSFVHRDLA 702
Cdd:PHA03209 115 NHPSVIRMKDTLVSGAITCMVLPHY-SSDLYTYLTKRSRPLPIDQALI---------IEKQILEGLRYLHAQRIIHRDVK 184
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965  703 TRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSF 773
Cdd:PHA03209 185 TENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGT---VETNAPEVLARDKYNSKADIWSAGIVLFEMLAY 252
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
643-787 1.76e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 54.88  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  643 VFEYMVHGDLHELLKVRV----PPADHDMGgiteanaeFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:PTZ00283 117 VLDYANAGDLRQEIKSRAktnrTFREHEAG--------LLFI--QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGD 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  719 FGLM------------RTSYGSDYYKmlhrswMPVRWMSKEaieqgrFSEASDVWSFGVTLWEIWSFGRqPYEGASNQQV 786
Cdd:PTZ00283 187 FGFSkmyaatvsddvgRTFCGTPYYV------APEIWRRKP------YSKKADMFSLGVLLYELLTLKR-PFDGENMEEV 253

                 .
gi 71980965  787 I 787
Cdd:PTZ00283 254 M 254
ig pfam00047
Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of ...
19-99 1.78e-07

Immunoglobulin domain; Members of the immunoglobulin superfamily are found in hundreds of proteins of different functions. Examples include antibodies, the giant muscle kinase titin and receptor tyrosine kinases. Immunoglobulin-like domains may be involved in protein-protein and protein-ligand interactions.


Pssm-ID: 395002  Cd Length: 86  Bit Score: 49.50  E-value: 1.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965    19 RNATKSSGDEVRFKCEA-LGTPPLKFIWLKNNG-PVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTT 96
Cdd:pfam00047   4 PTVTVLEGDSATLTCSAsTGSPGPDVTWSKEGGtLIESLKVKHDNGRTTQSSLLISNVTKEDAGTYTCVVNNPGGSATLS 83

                  ...
gi 71980965    97 SVL 99
Cdd:pfam00047  84 TSL 86
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
567-721 1.89e-07

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 53.44  E-value: 1.89e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 567 REKIGEGQFGVVHSGIY--TSGLFAPEPMAVAVKKCRHDATNAERAQLEQEI---RAVAtfDHPNVIKLIGVCYMDNSLL 641
Cdd:cd14181  15 KEVIGRGVSSVVRRCVHrhTGQEFAVKIIEVTAERLSPEQLEEVRSSTLKEIhilRQVS--GHPSIITLIDSYESSTFIF 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLYiatqialgmeYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd14181  93 LVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVS----------YLHANNIVHRDLKPENILLDDQLHIKLSDFGF 162
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
569-787 2.21e-07

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: 53.19  E-value: 2.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSGLfapepmaVAVKKCR---HDATNAERAQLEQEIRAVATFDHPNVIKLI----GVCYMDNSLL 641
Cdd:cd14031  17 ELGRGAFKTVYKGLDTETW-------VEVAWCElqdRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYdsweSVLKGKKCIV 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELL---KVRVPPADHDMggiteanaeflyiATQIALGMEYLASMS--FVHRDLATRNCLV-GDTRTIK 715
Cdd:cd14031  90 LVTELMTSGTLKTYLkrfKVMKPKVLRSW-------------CRQILKGLQFLHTRTppIIHRDLKCDNIFItGPTGSVK 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 716 IADFG---LMRTSYGSDYYKMlhrswmpVRWMSKEAIEQgRFSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVI 787
Cdd:cd14031 157 IGDLGlatLMRTSFAKSVIGT-------PEFMAPEMYEE-HYDESVDVYAFGMCMLEM-ATSEYPYSECQNAAQI 222
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
595-790 2.59e-07

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 53.63  E-value: 2.59e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCR-HDATNAERAQleQEIRAVATFDHPNVIKL--------------IGVCYMDNSLLAVFEYMvHGDLHELLKVR 659
Cdd:cd07854  33 VAVKKIVlTDPQSVKHAL--REIKIIRRLDHDNIVKVyevlgpsgsdltedVGSLTELNSVYIVQEYM-ETDLANVLEQG 109
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 660 VPPADHdmggiteaNAEFLYiatQIALGMEYLASMSFVHRDLATRNCLVG-DTRTIKIADFGLMRTsYGSDYYKMLHRSW 738
Cdd:cd07854 110 PLSEEH--------ARLFMY---QLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLARI-VDPHYSHKGYLSE 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 739 -MPVRWM-SKEAIEQGR-FSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd07854 178 gLVTKWYrSPRLLLSPNnYTKAIDMWAAGCIFAEMLT-GKPLFAGAHELEQMQLI 231
IgI_1_MuSK cd20970
agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of ...
10-90 2.86e-07

agrin-responsive first immunoglobulin-like domains (Ig1) of the MuSK ectodomain; a member of the I-set of IgSF domains; The members here are composed of the first immunoglobulin-like domains (Ig1) of the Muscle-specific kinase (MuSK). MuSK is a receptor tyrosine kinase specifically expressed in skeletal muscle, where it plays a central role in the formation and maintenance of the neuromuscular junction (NMJ). MuSK is activated by agrin, a neuron-derived heparan sulfate proteoglycan. The activation of MUSK in myotubes regulates the formation of NMJs through the regulation of different processes including the specific expression of genes in subsynaptic nuclei, the reorganization of the actin cytoskeleton and the clustering of the acetylcholine receptors (AChR) in the postsynaptic membrane. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the MuSK lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409562 [Multi-domain]  Cd Length: 92  Bit Score: 49.04  E-value: 2.86e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  10 PYIRLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKN-NGPVEKTKRVKIRdkENSSRLVITQLDVLDSGYYQCIVSN 88
Cdd:cd20970   1 PVISTPQPSFTVTAREGENATFMCRAEGSPEPEISWTRNgNLIIEFNTRYIVR--ENGTTLTIRNIRRSDMGIYLCIASN 78

                ..
gi 71980965  89 PA 90
Cdd:cd20970  79 GV 80
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
570-778 2.91e-07

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 53.53  E-value: 2.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH-------SGIYTSGLFAPEPMavaVKKcrhdatnAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd05596  34 IGRGAFGEVQlvrhkstKKVYAMKLLSKFEM---IKR-------SDSAFFWEERDIMAHANSEWIVQLHYAFQDDKYLYM 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLkvrvppADHDmggITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGlm 722
Cdd:cd05596 104 VMDYMPGGDLVNLM------SNYD---VPEKWARF-YTA-EVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFG-- 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 723 rTSYGSDYYKMLhRSWMPV---RWMSKEAIE-QGRFSE---ASDVWSFGVTLWEIWsFGRQPY 778
Cdd:cd05596 171 -TCMKMDKDGLV-RSDTAVgtpDYISPEVLKsQGGDGVygrECDWWSVGVFLYEML-VGDTPF 230
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
570-732 3.07e-07

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 53.48  E-value: 3.07e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVV--HSGIYTSGLFApepMAVAVKKCRHDATNAERAQLEQEIRAVAtfDHPNVIKLIGVCYMDNSLLAVFEYM 647
Cdd:cd05626   9 LGIGAFGEVclACKVDTHALYA---MKTLRKKDVLNRNQVAHVKAERDILAEA--DNEWVVKLYYSFQDKDNLYFVMDYI 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 648 VHGDLHELLkVRvppadhdMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL---MRT 724
Cdd:cd05626  84 PGGDMMSLL-IR-------MEVFPEVLARF-YIA-ELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLctgFRW 153

                ....*...
gi 71980965 725 SYGSDYYK 732
Cdd:cd05626 154 THNSKYYQ 161
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
613-782 3.58e-07

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 53.47  E-value: 3.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 613 EQEIRAVAtfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppADHDmggITEANAEFlYIAtQIALGMEYLA 692
Cdd:cd05622 123 ERDIMAFA--NSPWVVQLFYAFQDDRYLYMVMEYMPGGDLVNLM------SNYD---VPEKWARF-YTA-EVVLALDAIH 189
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 693 SMSFVHRDLATRNCLVGDTRTIKIADF---------GLMR--TSYGSDYYkmlhrswmpvrwMSKEAIEQ----GRFSEA 757
Cdd:cd05622 190 SMGFIHRDVKPDNMLLDKSGHLKLADFgtcmkmnkeGMVRcdTAVGTPDY------------ISPEVLKSqggdGYYGRE 257
                       170       180
                ....*....|....*....|....*
gi 71980965 758 SDVWSFGVTLWEIWsFGRQPYEGAS 782
Cdd:cd05622 258 CDWWSVGVFLYEML-VGDTPFYADS 281
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
614-787 3.82e-07

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 52.88  E-value: 3.82e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEIRAVATFDHPNVIKLIGVCYMDNSL--LAVFEYMVHGDLHELLkvrvppaDHDMGGITEANAEFLYIATQIALGMEYL 691
Cdd:cd13988  40 REFEVLKKLNHKNIVKLFAIEEELTTRhkVLVMELCPCGSLYTVL-------EEPSNAYGLPESEFLIVLRDVVAGMNHL 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 692 ASMSFVHRDLATRNCL--VGD--TRTIKIADFGLMR---------TSYGSDYYkmLHRSWMPVRWMSKEAieQGRFSEAS 758
Cdd:cd13988 113 RENGIVHRDIKPGNIMrvIGEdgQSVYKLTDFGAAReleddeqfvSLYGTEEY--LHPDMYERAVLRKDH--QKKYGATV 188
                       170       180       190
                ....*....|....*....|....*....|...
gi 71980965 759 DVWSFGVTLWEIwSFGR---QPYEGA-SNQQVI 787
Cdd:cd13988 189 DLWSIGVTFYHA-ATGSlpfRPFEGPrRNKEVM 220
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
570-790 4.13e-07

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 53.11  E-value: 4.13e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVV------HSGIYTSGLFAPEPMAVAVKKCRHDATnaeraqleqEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:cd05594  33 LGKGTFGKVilvkekATGRYYAMKILKKEVIVAKDEVAHTLT---------ENRVLQNSRHPFLTALKYSFQTHDRLCFV 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 644 FEYMVHGDLH-ELLKVRVppadhdmggITEANAEFLyiATQIALGMEYL-ASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd05594 104 MEYANGGELFfHLSRERV---------FSEDRARFY--GAEIVSALDYLhSEKNVVYRDLKLENLMLDKDGHIKITDFGL 172
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71980965 722 MRTSYgSDYYKMLHRSWMPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELV 790
Cdd:cd05594 173 CKEGI-KDGATMKTFCGTP-EYLAPEVLEDNDYGRAVDWWGLGVVMYEMMC-GRLPFYNQDHEKLFELI 238
IgC2_3_Dscam cd20957
Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
26-101 4.19e-07

Third immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the Constant 2 (C2)-set of IgSF domains; The members here are composed of the third immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. This group belongs to the C2-set of IgSF domains, having A, B, and E strands in one beta-sheet and A', G, F, C, and C' in the other. Unlike other Ig domain sets, the C2-set lacks the D strand.


Pssm-ID: 409549  Cd Length: 88  Bit Score: 48.68  E-value: 4.19e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965  26 GDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKensSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRV 101
Cdd:cd20957  16 GRTAVFNCSVTGNPIHTVLWMKDGKPLGHSSRVQILSE---DVLVIPSVKREDKGMYQCFVRNDGDSAQATAELKL 88
IgI_4_Dscam cd20956
Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
22-101 4.23e-07

Fourth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the fourth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409548 [Multi-domain]  Cd Length: 96  Bit Score: 48.71  E-value: 4.23e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  22 TKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLV-----ITQLDVLDSGYYQCIVSNPAASVNTT 96
Cdd:cd20956  12 TLQPGPSVSLKCVASGNPLPQITWTLDGFPIPESPRFRVGDYVTSDGDVvsyvnISSVRVEDGGEYTCTATNDVGSVSHS 91

                ....*
gi 71980965  97 SVLRV 101
Cdd:cd20956  92 ARINV 96
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
559-778 4.43e-07

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: 52.76  E-value: 4.43e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 559 ITPSQLSVREKIGEGQFGVVHS--GIYTSGLFAPEpmavAVKKCRHDATNAERAQLEQEI--RAVATFDHPNVIKLIGVC 634
Cdd:cd05633   2 LTMNDFSVHRIIGRGGFGEVYGcrKADTGKMYAMK----CLDKKRIKMKQGETLALNERImlSLVSTGDCPFIVCMTYAF 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 635 YMDNSLLAVFEYMVHGDLHELLkvrvppADHdmGGITEAnaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd05633  78 HTPDKLCFILDLMNGGDLHYHL------SQH--GVFSEK--EMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHV 147
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 715 KIADFGLmrtsyGSDYYKML-HRSWMPVRWMSKEAIEQGR-FSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd05633 148 RISDLGL-----ACDFSKKKpHASVGTHGYMAPEVLQKGTaYDSSADWFSLGCMLFKLLR-GHSPF 207
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
568-832 5.50e-07

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: 52.38  E-value: 5.50e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG---IYTSGLFAPepmaVAVKKCRHDatnaERA--QLEQEIRAVATFDHPNVIKLIGVCYMDNSL-- 640
Cdd:cd14055   1 KLVGKGRFAEVWKAklkQNASGQYET----VAVKIFPYE----EYAswKNEKDIFTDASLKHENILQFLTAEERGVGLdr 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 --LAVFEYMVHGDLHELLKVRVppadhdmggITEAnaEFLYIATQIALGMEYLAS---------MSFVHRDLATRNCLVG 709
Cdd:cd14055  73 qyWLITAYHENGSLQDYLTRHI---------LSWE--DLCKMAGSLARGLAHLHSdrtpcgrpkIPIAHRDLKSSNILVK 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 710 DTRTIKIADFGL-MR--TSYGSDYYKMLHRSWMPvRWMSKEAIEQ-------GRFSEAsDVWSFGVTLWEIWS------- 772
Cdd:cd14055 142 NDGTCVLADFGLaLRldPSLSVDELANSGQVGTA-RYMAPEALESrvnledlESFKQI-DVYSMALVLWEMASrceasge 219
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 773 -------FGRQPYEGASNQQVIELVA-NRHLLECP-----HNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd14055 220 vkpyelpFGSKVRERPCVESMKDLVLrDRGRPEIPdswltHQGMCVLCDTITECWDHDPEARLTASCVAERFN 292
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
569-831 5.63e-07

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: 52.35  E-value: 5.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAEraqlEQEIRAVATFDHPNVIKLIGV----CYMDNSLLAVF 644
Cdd:cd14220   2 QIGKGRYGEVWMGKWRG-----EKVAVKVFFTTEEASWFR----ETEIYQTVLMRHENILGFIAAdikgTGSWTQLYLIT 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 645 EYMVHGDLHELLKVrvppadhdmggITEANAEFLYIATQIALGMEYLASM--------SFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd14220  73 DYHENGSLYDFLKC-----------TTLDTRALLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCI 141
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGLMrTSYGSDYYKM---LHRSWMPVRWMSKEAIEQ----GRFSE--ASDVWSFGVTLWE---------IWSFGRQPY 778
Cdd:cd14220 142 ADLGLA-VKFNSDTNEVdvpLNTRVGTKRYMAPEVLDEslnkNHFQAyiMADIYSFGLIIWEmarrcvtggIVEEYQLPY 220
                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 779 -----EGASNQQVIELVANRHLLECPHN------CPTNIYSLMVECWHENIERRPTFSEIRSRL 831
Cdd:cd14220 221 ydmvpSDPSYEDMREVVCVKRLRPTVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTL 284
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
567-778 6.33e-07

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 51.84  E-value: 6.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 567 REKIGEGQFGVVHSGIytsglFAPEPMAVAVKKCRHDATNAERAQLEQEIRAVATFD---------HPNVIKLIGvCYMD 637
Cdd:cd14182   8 KEILGRGVSSVVRRCI-----HKPTRQEYAVKIIDITGGGSFSPEEVQELREATLKEidilrkvsgHPNIIQLKD-TYET 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLL-AVFEYMVHGDLHELLKVRVPPADHDMGGITEANAEFLyiatqialgmEYLASMSFVHRDLATRNCLVGDTRTIKI 716
Cdd:cd14182  82 NTFFfLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVI----------CALHKLNIVHRDLKPENILLDDDMNIKL 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965 717 ADFGL---------MRTSYGSDYY---KMLHRSWMPvrwmskeaiEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd14182 152 TDFGFscqldpgekLREVCGTPGYlapEIIECSMDD---------NHPGYGKEVDMWSTGVIMYTLLA-GSPPF 215
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
564-832 8.57e-07

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: 51.57  E-value: 8.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 564 LSVREKIGEGQFGVVHSGIYTSglfAPEPMAVAVKKCrHDATNAERAQLEQEI-RAVAtfDHPNVIKLIG--VCYMDNSL 640
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHDVN---TGRRYALKRMYF-NDEEQLRVAIKEIEImKRLC--GHPNIVQYYDsaILSSEGRK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 641 --LAVFEYmVHGDLHELLKVRVPpadhdmGGITEAnaEFLYIATQIALGMEYLASMS--FVHRDLATRNCLVGDTRTIKI 716
Cdd:cd13985  76 evLLLMEY-CPGSLVDILEKSPP------SPLSEE--EVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKL 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 717 ADFGlmrtSYGSDYYKMLHRSWMPvrwMSKEAIEQG-----------------RFSEASDVWSFGVTLWEIwSFGRQPYE 779
Cdd:cd13985 147 CDFG----SATTEHYPLERAEEVN---IIEEEIQKNttpmyrapemidlyskkPIGEKADIWALGCLLYKL-CFFKLPFD 218
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 71980965 780 GASnqqVIELVANRHLLECPHNCPTNIYSLMVECWHENIERRPTFSEIRSRLQ 832
Cdd:cd13985 219 ESS---KLAIVAGKYSIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIIT 268
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
597-778 9.01e-07

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 51.13  E-value: 9.01e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 597 VKKCRHDATN------------AERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkVRvppad 664
Cdd:cd14113  23 VKKCDQRGTKravatkfvnkklMKRDQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEMADQGRLLDYV-VR----- 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 665 hdMGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTR---TIKIADFGlMRTSYGSDYYkmLHRSWMPV 741
Cdd:cd14113  97 --WGNLTEEKIRF-YLR-EILEALQYLHNCRIAHLDLKPENILVDQSLskpTIKLADFG-DAVQLNTTYY--IHQLLGSP 169
                       170       180       190
                ....*....|....*....|....*....|....*..
gi 71980965 742 RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd14113 170 EFAAPEIILGNPVSLTSDLWSIGVLTYVLLS-GVSPF 205
IgI_2_FGFRL1-like cd05856
Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1 ...
26-96 9.79e-07

Second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor_like-1(FGFRL1); member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of fibroblast growth factor (FGF) receptor like-1(FGFRL1). FGFRL1 is comprised of a signal peptide, three extracellular Ig-like modules, a transmembrane segment, and a short intracellular domain. FGFRL1 is expressed preferentially in skeletal tissues. Similar to FGF receptors, the expressed protein interacts specifically with heparin and with FGF2. FGFRL1 does not have a protein tyrosine kinase domain at its C-terminus; neither does its cytoplasmic domain appear to interact with a signaling partner. It has been suggested that FGFRL1 may not have any direct signaling function, but instead acts as a decoy receptor trapping FGFs and preventing them from binding other receptors.


Pssm-ID: 409442  Cd Length: 92  Bit Score: 47.55  E-value: 9.79e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965  26 GDEVRFKCEALGTPPLKFIWLKNNGPVekTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTT 96
Cdd:cd05856  19 GSSVRLKCVASGNPRPDITWLKDNKPL--TPPEIGENKKKKWTLSLKNLKPEDSGKYTCHVSNRAGEINAT 87
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
615-780 9.91e-07

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 51.62  E-value: 9.91e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVATFDHPNVIKLIGVCY--MDNsLLAVFEYMVHGDL-HELLKVrvppadhdmGGITEANAEFLyiATQIALGMEYL 691
Cdd:cd05587  46 EKRVLALSGKPPFLTQLHSCFqtMDR-LYFVMEYVNGGDLmYHIQQV---------GKFKEPVAVFY--AAEIAVGLFFL 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 692 ASMSFVHRDLATRNCLVGDTRTIKIADFGL----------MRTSYGS-DYykmlhrswmpvrwMSKEAIEQGRFSEASDV 760
Cdd:cd05587 114 HSKGIIYRDLKLDNVMLDAEGHIKIADFGMckegifggktTRTFCGTpDY-------------IAPEIIAYQPYGKSVDW 180
                       170       180
                ....*....|....*....|
gi 71980965 761 WSFGVTLWEIWSfGRQPYEG 780
Cdd:cd05587 181 WAYGVLLYEMLA-GQPPFDG 199
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
611-772 1.01e-06

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: 51.58  E-value: 1.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 611 QLEQEIRAVATFDHPNVIKLIGV----CYMDNSLLAVFEYMVHGDLHELLKVRVPPADhdmggiteanaEFLYIATQIAL 686
Cdd:cd14141  35 QNEYEIYSLPGMKHENILQFIGAekrgTNLDVDLWLITAFHEKGSLTDYLKANVVSWN-----------ELCHIAQTMAR 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 687 GMEYLAS----------MSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQG-RFS 755
Cdd:cd14141 104 GLAYLHEdipglkdghkPAIAHRDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTRRYMAPEVLEGAiNFQ 183
                       170       180
                ....*....|....*....|.
gi 71980965 756 EAS----DVWSFGVTLWEIWS 772
Cdd:cd14141 184 RDAflriDMYAMGLVLWELAS 204
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
565-768 1.21e-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: 51.40  E-value: 1.21e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 565 SVREKIGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDA-TNAERAQleQEIRAVATFD--HPNVIKLiGVCYMDNSLL 641
Cdd:cd13977   3 SLIREVGRGSYGVVYEAVVRR-----TGARVAVKKIRCNApENVELAL--REFWALSSIQrqHPNVIQL-EECVLQRDGL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 A-------------------------------------VFEYMVHGDLHELLKVRVPPAdhdmggitEANAEFLyiaTQI 684
Cdd:cd13977  75 AqrmshgssksdlylllvetslkgercfdprsacylwfVMEFCDGGDMNEYLLSRRPDR--------QTNTSFM---LQL 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 685 ALGMEYLASMSFVHRDLATRNCLVGDTR---TIKIADFGLMRTSYGS----DYYKMLHRSWMPVR-----WMSKEAIEqG 752
Cdd:cd13977 144 SSALAFLHRNQIVHRDLKPDNILISHKRgepILKVADFGLSKVCSGSglnpEEPANVNKHFLSSAcgsdfYMAPEVWE-G 222
                       250
                ....*....|....*.
gi 71980965 753 RFSEASDVWSFGVTLW 768
Cdd:cd13977 223 HYTAKADIFALGIIIW 238
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
569-778 1.23e-06

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: 51.19  E-value: 1.23e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVV------HSGiytsglfapepMAVAVKKCrhDATNAERAQLE-QEIRAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd06658  29 KIGEGSTGIVciatekHTG-----------KQVAVKKM--DLRKQQRRELLfNEVVIMRDYHHENVVDMYNSYLVGDELW 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKvrvppadHdmggiTEANAE-FLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFG 720
Cdd:cd06658  96 VVMEFLEGGALTDIVT-------H-----TRMNEEqIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFG 163
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 721 LMrTSYGSDYYKMLHRSWMPVrWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd06658 164 FC-AQVSKEVPKRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIEMID-GEPPY 218
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
638-779 1.25e-06

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: 51.18  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLhellKVRVppadHDMG--GITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIK 715
Cdd:cd05630  73 DALCLVLTLMNGGDL----KFHI----YHMGqaGFPEARAVFY--AAEICCGLEDLHRERIVYRDLKPENILLDDHGHIR 142
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965 716 IADFGL-MRTSYGsdyyKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd05630 143 ISDLGLaVHVPEG----QTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFQ 202
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
570-769 1.34e-06

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 51.08  E-value: 1.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH------SG-IYtsglfapepmavAVKKCRhDATNAERAQLEQeIRA----VATFDHPNVIKLigvcYM-- 636
Cdd:cd05599   9 IGRGAFGEVRlvrkkdTGhVY------------AMKKLR-KSEMLEKEQVAH-VRAerdiLAEADNPWVVKL----YYsf 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 --DNSLLAVFEYMVHGDLHELLkVRvppadHDMggITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTI 714
Cdd:cd05599  71 qdEENLYLIMEFLPGGDMMTLL-MK-----KDT--LTEEETRF-YIA-ETVLAIESIHKLGYIHRDIKPDNLLLDARGHI 140
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965 715 KIADFGLmrtsygSDYYKMLHRSWMPV---RWMSKEAIEQGRFSEASDVWSFGVTLWE 769
Cdd:cd05599 141 KLSDFGL------CTGLKKSHLAYSTVgtpDYIAPEVFLQKGYGKECDWWSLGVIMYE 192
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
595-778 1.45e-06

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 51.14  E-value: 1.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 595 VAVKKCRHDATNAER-AQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppaDHDMGGITEa 673
Cdd:cd08216  28 VAVKKINLESDSKEDlKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGSCRDLLK------THFPEGLPE- 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 674 nAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFglmRTSY----GSDYYKMLHRSwmPVR------W 743
Cdd:cd08216 101 -LAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGL---RYAYsmvkHGKRQRVVHDF--PKSseknlpW 174
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 71980965 744 MSKEAIEQ---GrFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd08216 175 LSPEVLQQnllG-YNEKSDIYSVGITACELAN-GVVPF 210
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
568-770 1.67e-06

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


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 50.60  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHSG--IYTSGLfapepmaVAVKKcrhdatnaERAQLEQE------IRAVATF----DHPNVIKLIGVCY 635
Cdd:cd07837   7 EKIGEGTYGKVYKArdKNTGKL-------VALKK--------TRLEMEEEgvpstaLREVSLLqmlsQSIYIVRLLDVEH 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNS----LLAVFEYMvHGDLHELLKVRVPPADHDMGGITEANaeFLYiatQIALGMEYLASMSFVHRDLATRNCLVGDT 711
Cdd:cd07837  72 VEENgkplLYLVFEYL-DTDLKKFIDSYGRGPHNPLPAKTIQS--FMY---QLCKGVAHCHSHGVMHRDLKPQNLLVDKQ 145
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 712 R-TIKIADFGLMRT------SYGSDYYKMLHRSwmpvrwmSKEAIEQGRFSEASDVWSFGVTLWEI 770
Cdd:cd07837 146 KgLLKIADLGLGRAftipikSYTHEIVTLWYRA-------PEVLLGSTHYSTPVDMWSVGCIFAEM 204
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
588-787 1.67e-06

Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha, stabilized through ATP and MO25, may be needed to activate LKB1. A mutation which results in a truncation of a C-terminal part of the human STRAD-alpha pseudokinase domain and disrupts its association with LKB1, leads to PMSE (polyhydramnios, megalencephaly, symptomatic epilepsy) syndrome. Several splice variants of STRAD-alpha exist which exhibit different effects on the localization and activation of LKB1. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. The STRAD alpha subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173767 [Multi-domain]  Cd Length: 327  Bit Score: 51.10  E-value: 1.67e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 588 FAPEPMAVAVKKCRHDA-TNAERAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppADHD 666
Cdd:cd08227  21 YKPTGEYVTVRRINLEAcTNEMVTFLQGELHVSKLFNHPNIVPYRATFIADNELWVVTSFMAYGSAKDLI------CTHF 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 667 MGGITEanAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF--GLMRTSYGSDyYKMLH----RSWMP 740
Cdd:cd08227  95 MDGMSE--LAIAYILQGVLKALDYIHHMGYVHRSVKASHILISVDGKVYLSGLrsNLSMINHGQR-LRVVHdfpkYSVKV 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 71980965 741 VRWMSKEAIEQGR--FSEASDVWSFGVTLWEIwSFGRQPYEGASNQQVI 787
Cdd:cd08227 172 LPWLSPEVLQQNLqgYDAKSDIYSVGITACEL-ANGHVPFKDMPATQML 219
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
614-799 1.87e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 51.43  E-value: 1.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  614 QEIRAVATFDHPNVIKLIGVCYMDN-SLLAVFEYmvHGDLHELLKVRVPPADHdmggiteanAEFLYIATQIALGMEYLA 692
Cdd:PHA03211 209 HEARLLRRLSHPAVLALLDVRVVGGlTCLVLPKY--RSDLYTYLGARLRPLGL---------AQVTAVARQLLSAIDYIH 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  693 SMSFVHRDLATRNCLVGDTRTIKIADFG---LMRTSYGSDYYKMLHRSwmpVRWMSKEAIEQGRFSEASDVWSFGVTLWE 769
Cdd:PHA03211 278 GEGIIHRDIKTENVLVNGPEDICLGDFGaacFARGSWSTPFHYGIAGT---VDTNAPEVLAGDPYTPSVDIWSAGLVIFE 354
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 71980965  770 -------IWSFGRQPYEGASNQQVIELV--ANRHLLECP 799
Cdd:PHA03211 355 aavhtasLFSASRGDERRPYDAQILRIIrqAQVHVDEFP 393
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
26-98 1.88e-06

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 433563 [Multi-domain]  Cd Length: 76  Bit Score: 46.24  E-value: 1.88e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965    26 GDEVRFKCEALGTPPLKFIWLKNNGPVEKtkrvkirdkenSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSV 98
Cdd:pfam13895  14 GEPVTLTCSAPGNPPASYTWYKGGEALNS-----------SPNFFILAVSAEDSGTYTCVARNGRGGKVSNPV 75
IgI_Titin_like cd05747
Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the ...
13-88 2.05e-06

Immunoglobulin (Ig)-like domain of human titin C terminus and similar proteins; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the fifth immunoglobulin (Ig)-like domain from the C-terminus of human titin x and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is gigantic; depending on isoform composition it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone and appears to function similar to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 143224 [Multi-domain]  Cd Length: 92  Bit Score: 46.58  E-value: 2.05e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965  13 RLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSN 88
Cdd:cd05747   5 TILTKPRSLTVSEGESARFSCDVDGEPAPTVTWMREGQIIVSSQRHQITSTEYKSTFEISKVQMSDEGNYTVVVEN 80
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
557-785 2.05e-06

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 50.32  E-value: 2.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 557 FEITPSQlsvreKIGEGQFGVVHSGIY--TSGLFAPEPMAVAVK--KCR----HDATNAERAQleqeiravatfDHPNVI 628
Cdd:cd14197   9 YSLSPGR-----ELGRGKFAVVRKCVEkdSGKEFAAKFMRKRRKgqDCRmeiiHEIAVLELAQ-----------ANPWVI 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 629 KLIGVCYMDNSLLAVFEYMVHGDLHELLKvrvppADHDMGgITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLV 708
Cdd:cd14197  73 NLHEVYETASEMILVLEYAAGGEIFNQCV-----ADREEA-FKEKDVKRL--MKQILEGVSFLHNNNVVHLDLKPQNILL 144
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 709 ------GDtrtIKIADFGLMRTSYGSDYYKMLHRSwmPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGAS 782
Cdd:cd14197 145 tsesplGD---IKIVDFGLSRILKNSEELREIMGT--P-EYVAPEILSYEPISTATDMWSIGVLAYVMLT-GISPFLGDD 217

                ...
gi 71980965 783 NQQ 785
Cdd:cd14197 218 KQE 220
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
638-793 2.12e-06

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: 50.74  E-value: 2.12e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 638 NSLLAVFEYMVHGDLhellKVRVppadHDMGGITEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05632  75 DALCLVLTIMNGGDL----KFHI----YNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRIS 146
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71980965 718 DFGL-MRTSYGsdyyKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQVIELVANR 793
Cdd:cd05632 147 DLGLaVKIPEG----ESIRGRVGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRGRKEKVKREEVDRR 218
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
615-827 2.22e-06

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 50.08  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 615 EIRAVAT---FDHPNVIKLIGVcyMDNSLLAVFEYMVHG---DLHELLKVRVppadhdmgGITEANAEflYIATQIALGM 688
Cdd:cd14004  55 EIHILDTlnkRSHPNIVKLLDF--FEDDEFYYLVMEKHGsgmDLFDFIERKP--------NMDEKEAK--YIFRQVADAV 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 689 EYLASMSFVHRDLATRNCLVGDTRTIKIADFG---LMRTSYGSDYYKMLHrswmpvrWMSKEAIEQGRF-SEASDVWSFG 764
Cdd:cd14004 123 KHLHDQGIVHRDIKDENVILDGNGTIKLIDFGsaaYIKSGPFDTFVGTID-------YAAPEVLRGNPYgGKEQDIWALG 195
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 765 VTLWEIwSFGRQPYegasnQQVIELVANRhlLECPHNCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd14004 196 VLLYTL-VFKENPF-----YNIEEILEAD--LRIPYAVSEDLIDLISRMLNRDVGDRPTIEEL 250
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
637-778 2.24e-06

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 50.42  E-value: 2.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELLKV---RVPPadhDMggiteanAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd05597  73 ENYLYLVMDYYCGGDLLTLLSKfedRLPE---EM-------ARF-YLA-EMVLAIDSIHQLGYVHRDIKPDNVLLDRNGH 140
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFG----LMR-------TSYGS-DYykmlhrswmpvrwMSKE---AIE--QGRFSEASDVWSFGVTLWEIWsFGRQ 776
Cdd:cd05597 141 IRLADFGsclkLREdgtvqssVAVGTpDY-------------ISPEilqAMEdgKGRYGPECDWWSLGVCMYEML-YGET 206

                ..
gi 71980965 777 PY 778
Cdd:cd05597 207 PF 208
IgI_4_Robo cd05726
Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of ...
19-104 2.41e-06

Fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors; member of the I-set of Ig superfamily (IgSF) domains; Members here are composed the fourth immunoglobulin (Ig)-like domain in Robo (roundabout) receptors. Robo receptors play a role in the development of the central nervous system (CNS), and are receptors of Slit protein. Slit is a repellant secreted by the neural cells in the midline. Slit acts through Robo to prevent most neurons from crossing the midline from either side. Three mammalian Robo homologs (Robo1, Robo2, Robo3), and three mammalian Slit homologs (Slit-1, Slit-2, Slit-3), have been identified. Commissural axons, which cross the midline, express low levels of Robo; longitudinal axons, which avoid the midline, express high levels of Robo. Robo1, Robo2, and Robo3 are expressed by commissural neurons in the vertebrate spinal cord and Slit-1, Slit-2, and Slit-3 are expressed at the ventral midline. Robo-3 is a divergent member of the Robo family which instead of being a positive regulator of Slit responsiveness, antagonizes Slit responsiveness in precrossing axons. The Slit-Robo interaction is mediated by the second leucine-rich repeat (LRR) domain of Slit and the two N-terminal Ig domains of Robo, Ig1 and Ig2. The primary Robo binding site for Slit2 has been shown by surface plasmon resonance experiments and mutational analysis to be the Ig1 domain, while the Ig2 domain has been proposed to harbor a weak secondary binding site. This group belongs to the I-set of IgSF domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409391  Cd Length: 98  Bit Score: 46.87  E-value: 2.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  19 RNATKSSGDEVRFKCEALGTPPLKFIWLKN--------NGPVEKTKRVKIrdkENSSRLVITQLDVLDSGYYQCIVSNPA 90
Cdd:cd05726   7 RDQVVALGRTVTFQCETKGNPQPAIFWQKEgsqnllfpYQPPQPSSRFSV---SPTGDLTITNVQRSDVGYYICQALNVA 83
                        90
                ....*....|....
gi 71980965  91 ASVNTTSVLRVNNV 104
Cdd:cd05726  84 GSILAKAQLEVTDV 97
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
614-787 2.70e-06

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: 50.06  E-value: 2.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 614 QEIRAVATFDHPNVIKLIGVCYMD-NSLLAVFEYMVHGDLHELLKvrvppaDHDMGGITEANAeflyIATQIALGMEYLA 692
Cdd:cd14041  59 REYRIHKELDHPRIVKLYDYFSLDtDSFCTVLEYCEGNDLDFYLK------QHKLMSEKEARS----IIMQIVNALKYLN 128
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 693 SMS--FVHRDLATRNCLVGDTRT---IKIADFGLMRT----SYGS-DYYKMLHRSWMPVRWMSKEAI----EQGRFSEAS 758
Cdd:cd14041 129 EIKppIIHYDLKPGNILLVNGTAcgeIKITDFGLSKImdddSYNSvDGMELTSQGAGTYWYLPPECFvvgkEPPKISNKV 208
                       170       180
                ....*....|....*....|....*....
gi 71980965 759 DVWSFGVTLWEIWsFGRQPYEGASNQQVI 787
Cdd:cd14041 209 DVWSVGVIFYQCL-YGRKPFGHNQSQQDI 236
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
488-803 2.88e-06

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 50.85  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  488 NSAANSAYYRKLNGTSTPIMGRvppHVEMTSLLPSAQhlGPPPypmdqhLQQARRFPSQEPIddNSYKVFEITPSQ---- 563
Cdd:PHA03210  97 SNADLFASAGDGPSGAEDSDAS---HLDFDEAPPDAA--GPVP------LAQAKLKHDDEFL--AHFRVIDDLPAGafgk 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  564 ---LSVREKIGEGQfgvVHSGIYTSGLFAPEPMAVAVKKCRhdATNAERAQLEQEIRAVATFDHPNVIKLIGVC-YMDNS 639
Cdd:PHA03210 164 ifiCALRASTEEAE---ARRGVNSTNQGKPKCERLIAKRVK--AGSRAAIQLENEILALGRLNHENILKIEEILrSEANT 238
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  640 LLA-------VFEYMVHGDLHEllkvrvppADHDMGGITEAnaeflyIATQIALGMEYLASMSFVHRDLATRNCLVGDTR 712
Cdd:PHA03210 239 YMItqkydfdLYSFMYDEAFDW--------KDRPLLKQTRA------IMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDG 304
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  713 TIKIADFGLMRT----SYGSDYykmlhrSWM-PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWSFGRQPYEGAS---NQ 784
Cdd:PHA03210 305 KIVLGDFGTAMPfekeREAFDY------GWVgTVATNSPEILAGDGYCEITDIWSCGLILLDMLSHDFCPIGDGGgkpGK 378
                        330
                 ....*....|....*....
gi 71980965  785 QVIELVanRHLLECPHNCP 803
Cdd:PHA03210 379 QLLKII--DSLSVCDEEFP 395
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
570-792 2.91e-06

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 50.38  E-value: 2.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIY--TSGLFAPEpmavAVKKC----RH--DATNAERAQLEqeirAVATFDHPNVIKLIGVCYMDNSLL 641
Cdd:cd05589   7 LGRGHFGKVLLAEYkpTGELFAIK----ALKKGdiiaRDevESLMCEKRIFE----TVNSARHPFLVNLFACFQTPEHVC 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDL----HEllkvrvppadhDMggITEANAEFlYIATqIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIA 717
Cdd:cd05589  79 FVMEYAAGGDLmmhiHE-----------DV--FSEPRAVF-YAAC-VVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIA 143
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 718 DFGL----M----RTSY--GSdyykmlhrswmPvRWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGASNQQVI 787
Cdd:cd05589 144 DFGLckegMgfgdRTSTfcGT-----------P-EFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFPGDDEEEVF 210

                ....*
gi 71980965 788 ELVAN 792
Cdd:cd05589 211 DSIVN 215
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
639-803 3.66e-06

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 50.04  E-value: 3.66e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 639 SLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFlYIATQIaLGMEYLASMSFVHRDLATRNCLVGDTRTIKIAD 718
Cdd:cd05628  75 NLYLIMEFLPGGDMMTLLMKK--------DTLTEEETQF-YIAETV-LAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSD 144
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 719 FGL---MRTSYGSDYYKMLHRS------------------WMPVR------------WMSKEAIEQGRFSEASDVWSFGV 765
Cdd:cd05628 145 FGLctgLKKAHRTEFYRNLNHSlpsdftfqnmnskrkaetWKRNRrqlafstvgtpdYIAPEVFMQTGYNKLCDWWSLGV 224
                       170       180       190
                ....*....|....*....|....*....|....*....
gi 71980965 766 TLWEIWsFGRQPYEGASNQQVIELVAN-RHLLECPHNCP 803
Cdd:cd05628 225 IMYEML-IGYPPFCSETPQETYKKVMNwKETLIFPPEVP 262
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
593-779 3.80e-06

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


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 50.03  E-value: 3.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 593 MAVAVKKCRHDATNAERAQLEQEIRAVATfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDL-HELLKVRVPPADHdmggit 671
Cdd:cd05618  50 MKVVKKELVNDDEDIDWVQTEKHVFEQAS-NHPFLVGLHSCFQTESRLFFVIEYVNGGDLmFHMQRQRKLPEEH------ 122
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 672 eanAEFlyIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG-SDYYKMLHRSwmpVRWMSKEAIE 750
Cdd:cd05618 123 ---ARF--YSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRpGDTTSTFCGT---PNYIAPEILR 194
                       170       180
                ....*....|....*....|....*....
gi 71980965 751 QGRFSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd05618 195 GEDYGFSVDWWALGVLMFEMMA-GRSPFD 222
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
569-778 3.98e-06

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 49.64  E-value: 3.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 569 KIGEGQFGVVH-SGIYTSGLFapepmaVAVKKCrhDATNAERAQLE-QEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEY 646
Cdd:cd06657  27 KIGEGSTGIVCiATVKSSGKL------VAVKKM--DLRKQQRRELLfNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEF 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKvrvppadHdmggiTEANAEFL-YIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGlmrts 725
Cdd:cd06657  99 LEGGALTDIVT-------H-----TRMNEEQIaAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFG----- 161
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 726 YGSDYYKMLHRSWMPV---RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPY 778
Cdd:cd06657 162 FCAQVSKEVPRRKSLVgtpYWMAPELISRLPYGPEVDIWSLGIMVIEMVD-GEPPY 216
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
570-822 4.58e-06

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


Pssm-ID: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 49.53  E-value: 4.58e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH-----SGIYTSGLFAPEPM--AVAVKKCR-HDATNAERAQLEQeIRavatfDHPNVIKLIGVCYMDNSLL 641
Cdd:cd05614   8 LGTGAYGKVFlvrkvSGHDANKLYAMKVLrkAALVQKAKtVEHTRTERNVLEH-VR-----QSPFLVTLHYAFQTDAKLH 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 642 AVFEYMVHGDLHELLKVRvppaDHdmggITEANAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGL 721
Cdd:cd05614  82 LILDYVSGGELFTHLYQR----DH----FSEDEVRFY--SGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGL 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 722 MRtSYGSDYYKMLHRSWMPVRWMSKEAIE-QGRFSEASDVWSFGVTLWEIWSfGRQPY--EGASNQQVielVANRHLLEC 798
Cdd:cd05614 152 SK-EFLTEEKERTYSFCGTIEYMAPEIIRgKSGHGKAVDWWSLGILMFELLT-GASPFtlEGEKNTQS---EVSRRILKC 226
                       250       260
                ....*....|....*....|....
gi 71980965 799 PHNCPTNIYSLMVECWHENIERRP 822
Cdd:cd05614 227 DPPFPSFIGPVARDLLQKLLCKDP 250
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
570-791 5.34e-06

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


Pssm-ID: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 49.49  E-value: 5.34e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVH-------SGIYTSGLFAPEpmaVAVKKCRHDATNAERAQLEQeiraVATFDHPNVIKLIGVCYMDNSLLA 642
Cdd:cd05586   1 IGKGTFGQVYqvrkkdtRRIYAMKVLSKK---VIVAKKEVAHTIGERNILVR----TALDESPFIVGLKFSFQTPTDLYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 643 VFEYMVHGDLHELLKvrvppadHDmGGITEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLM 722
Cdd:cd05586  74 VTDYMSGGELFWHLQ-------KE-GRFSEDRAKF-YIA-ELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLS 143
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 723 RTSYGSDyyKMLHRSWMPVRWMSKEA-IEQGRFSEASDVWSFGVTLWEI---WSfgrqPYEGASNQQVIELVA 791
Cdd:cd05586 144 KADLTDN--KTTNTFCGTTEYLAPEVlLDEKGYTKMVDFWSLGVLVFEMccgWS----PFYAEDTQQMYRNIA 210
IgI_2_Follistatin_like cd05736
Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; ...
10-101 5.89e-06

Second immunoglobulin (Ig)-like domain of a Follistatin-related protein 5, and similar domains; member of the I-set of Ig superfamily (IgSF) domains; The members here are composed of the second immunoglobulin (Ig)-like domain found in human Follistatin-related protein 5 (FSTL5) and a follistatin-like molecule encoded by the CNS-related Mahya gene. Mahya genes have been retained in certain Bilaterian branches during evolution. They are conserved in Hymenoptera and Deuterostomes, but are absent from other metazoan species such as fruit fly and nematode. Mahya proteins are secretory, with a follistatin-like domain (Kazal-type serine/threonine protease inhibitor domain and EF-hand calcium-binding domain), two Ig-like domains, and a novel C-terminal domain. Mahya may be involved in learning and memory and in processing of sensory information in Hymenoptera and vertebrates. Follistatin is a secreted, multidomain protein that binds activins with high affinity and antagonizes their signaling.


Pssm-ID: 409399 [Multi-domain]  Cd Length: 93  Bit Score: 45.33  E-value: 5.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  10 PYIRLTSqlRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNP 89
Cdd:cd05736   1 PVIRVYP--EFQAKEPGVEASLRCHAEGIPLPRVQWLKNGMDINPKLSKQLTLIANGSELHISNVRYEDTGAYTCIAKNE 78
                        90
                ....*....|..
gi 71980965  90 AASVNTTSVLRV 101
Cdd:cd05736  79 GGVDEDISSLFV 90
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
637-782 6.08e-06

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


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 49.63  E-value: 6.08e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELL---KVRVPpadhdmggitEANAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd05623 144 DNNLYLVMDYYVGGDLLTLLskfEDRLP----------EDMARF-YLA-EMVLAIDSVHQLHYVHRDIKPDNILMDMNGH 211
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 714 IKIADFG----LMRTSYGSDYYKMLHRSWMPVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWsFGRQPYEGAS 782
Cdd:cd05623 212 IRLADFGsclkLMEDGTVQSSVAVGTPDYISPEILQAMEDGKGKYGPECDWWSLGVCMYEML-YGETPFYAES 283
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
593-779 6.24e-06

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 49.25  E-value: 6.24e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 593 MAVAVKKCRHDATNAERAQLEQEIRAVATfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDL-HELLKVRVPPADHdmggit 671
Cdd:cd05617  45 MKVVKKELVHDDEDIDWVQTEKHVFEQAS-SNPFLVGLHSCFQTTSRLFLVIEYVNGGDLmFHMQRQRKLPEEH------ 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 672 eanAEFLyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYG-SDYYKMLHRSwmpVRWMSKEAIE 750
Cdd:cd05617 118 ---ARFY--AAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGpGDTTSTFCGT---PNYIAPEILR 189
                       170       180
                ....*....|....*....|....*....
gi 71980965 751 QGRFSEASDVWSFGVTLWEIWSfGRQPYE 779
Cdd:cd05617 190 GEEYGFSVDWWALGVLMFEMMA-GRSPFD 217
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
683-822 6.94e-06

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: 48.86  E-value: 6.94e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 683 QIALGMEYL-ASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMLHRSWMPVR---------WMSKEAIEQG 752
Cdd:cd14011 122 QISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREYDPNLpplaqpnlnYLAPEYILSK 201
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 753 RFSEASDVWSFGVTLWEIWSFGRQPYEGASNQQ---VIELVANRHLLECPHNCPTNIYSLMVECWHENIERRP 822
Cdd:cd14011 202 TCDPASDMFSLGVLIYAIYNKGKPLFDCVNNLLsykKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRP 274
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
570-768 7.70e-06

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 48.45  E-value: 7.70e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 570 IGEGQFGVVHSGIYTSglfapEPMAVAVKKCRHDATNAERAQ--LEQEIRAVATFDHPNVIKLIGVC-YMDNSLLAVFEY 646
Cdd:cd14163   8 IGEGTYSKVKEAFSKK-----HQRKVAIKIIDKSGGPEEFIQrfLPRELQIVERLDHKNIIHVYEMLeSADGKIYLVMEL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 647 MVHGDLHELLKVRVPPADHdmggitEANAEFLyiatQIALGMEYLASMSFVHRDLATRNCLVgDTRTIKIADFGLMRTSY 726
Cdd:cd14163  83 AEDGDVFDCVLHGGPLPEH------RAKALFR----QLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLP 151
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 71980965 727 GSdyYKMLHRSWMPVRWMSKEAIEQG--RFSEASDVWSFGVTLW 768
Cdd:cd14163 152 KG--GRELSQTFCGSTAYAAPEVLQGvpHDSRKGDIWSMGVVLY 193
IgI_LRIG1-like cd05763
Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like ...
19-101 8.36e-06

Immunoglobulin (Ig)-like ectodomain of the LRIG1 (Leucine-rich Repeats And Immunoglobulin-like Domains Protein 1) and similar proteins; member of the I-set of IgSF domains; The members here are composed of subgroup of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. The ectodomain of LRIG1 has two distinct regions: the proposed 15 LRRs and three Ig-like domains closer to the membrane. LRIG1 has been reported to interact with many receptor tyrosine kinases, GDNF/c-Ret, E-cadherin, JAK/STAT, c-Met, and the EGFR family signaling systems. Immunoglobulin Superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. The structure of the LRIG1 extracellular Ig domain lacks a C" strand and thus is better described as a member of the I-set of IgSF domains.


Pssm-ID: 409420 [Multi-domain]  Cd Length: 91  Bit Score: 44.92  E-value: 8.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  19 RNATKSSGDEVRFKCEALGTPPLKFIWLKNNG---PVEKTKRVKIrdKENSSRLVITQLDVLDSGYYQCIVSNPAASVNT 95
Cdd:cd05763   7 HDITIRAGSTARLECAATGHPTPQIAWQKDGGtdfPAARERRMHV--MPEDDVFFIVDVKIEDTGVYSCTAQNSAGSISA 84

                ....*.
gi 71980965  96 TSVLRV 101
Cdd:cd05763  85 NATLTV 90
CRD_TK_ROR_related cd07469
Cysteine-rich domain of proteins similar to tyrosine kinase-like orphan receptors; The ...
177-308 8.72e-06

Cysteine-rich domain of proteins similar to tyrosine kinase-like orphan receptors; The cysteine-rich domain (CRD) is an essential part of the tyrosine kinase-like orphan receptor (Ror) proteins, a conserved family of tyrosine kinases that function in various processes, including neuronal and skeletal development, cell polarity, and cell movement. Ror proteins are receptors of Wnt proteins, which are key players in a number of fundamental cellular processes in embryogenesis and postnatal development. In different cellular contexts, Ror proteins can either activate or repress transcription of Wnt target genes, and can modulate Wnt signaling by sequestering Wnt ligands.


Pssm-ID: 143578  Cd Length: 147  Bit Score: 46.24  E-value: 8.72e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 177 GDCVQYRGEACRQYLSNKFVMMTN------ESREEMydIDRNLRAAMLfingaPTISQKCRQLSQAVACHHMYKVCESDS 250
Cdd:cd07469   3 GYCATYRGEVCRAYLSNDALVWFNssyadpEGLNEQ--LTTGLWEELI-----KTVSELCRPAAEKLLCNYAFPECHPSG 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 251 NNQI-VSICKHDCDVIQNDECPSELAL--AAQHELVGDTPKALF--PLCSRLSSTSNCIPVMS 308
Cdd:cd07469  76 VGPTpKPLCREDCLAVKELFCYKDWALieENKQRGIYLKSRGHFtlPECESLPSIHADPPACS 138
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
637-782 8.79e-06

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 49.24  E-value: 8.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 637 DNSLLAVFEYMVHGDLHELL---KVRVPpadHDMggiteanAEFlYIAtQIALGMEYLASMSFVHRDLATRNCLVGDTRT 713
Cdd:cd05624 144 ENYLYLVMDYYVGGDLLTLLskfEDKLP---EDM-------ARF-YIG-EMVLAIHSIHQLHYVHRDIKPDNVLLDMNGH 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 714 IKIADFGlmrtsygsDYYKMLH----RSWMPV---RWMSKEAIE-----QGRFSEASDVWSFGVTLWEIWsFGRQPYEGA 781
Cdd:cd05624 212 IRLADFG--------SCLKMNDdgtvQSSVAVgtpDYISPEILQamedgMGKYGPECDWWSLGVCMYEML-YGETPFYAE 282

                .
gi 71980965 782 S 782
Cdd:cd05624 283 S 283
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
597-792 9.42e-06

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 48.28  E-value: 9.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 597 VKKCRHDATNAERAQ-----------LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRVPPADH 665
Cdd:cd14085  19 VYRCRQKGTQKPYAVkklkktvdkkiVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSER 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 666 DmggitEANAeflyiATQIALGMEYLASMSFVHRDLATRNCLVGDTRT---IKIADFGL---------MRTSYGSDYYkm 733
Cdd:cd14085  99 D-----AADA-----VKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLskivdqqvtMKTVCGTPGY-- 166
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 734 lhrswmpvrwMSKEAIEQGRFSEASDVWSFGVTLWeIWSFGRQP-YEGASNQQVIELVAN 792
Cdd:cd14085 167 ----------CAPEILRGCAYGPEVDMWSVGVITY-ILLCGFEPfYDERGDQYMFKRILN 215
pknD PRK13184
serine/threonine-protein kinase PknD;
569-778 9.54e-06

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 49.38  E-value: 9.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  569 KIGEGQFGVVhsgiytsgLFAPEPMA---VAVKKCRHDATNAE--RAQLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAV 643
Cdd:PRK13184   9 LIGKGGMGEV--------YLAYDPVCsrrVALKKIREDLSENPllKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  644 FEYMVHGDLHELLK-VR---VPPADHDMGgitEANAEFLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADF 719
Cdd:PRK13184  81 MPYIEGYTLKSLLKsVWqkeSLSKELAEK---TSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDW 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965  720 GLMRTSYG-------SDYYK---MLHRSWMPVR------WMSKEAIEQGRFSEASDVWSFGVTLWEIWSFgRQPY 778
Cdd:PRK13184 158 GAAIFKKLeeedlldIDVDErniCYSSMTIPGKivgtpdYMAPERLLGVPASESTDIYALGVILYQMLTL-SFPY 231
IgI_6_Dscam cd20959
Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; ...
37-101 1.18e-05

Sixth immunoglobulin domain of the Drosophila melanogaster Dscam protein, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the sixth immunoglobulin domain of the Drosophila melanogaster Down syndrome cell adhesion molecule (DSCAM) protein and similar proteins. Down syndrome cell adhesion molecule (DSCAM) is a cell adhesion molecule that plays critical roles in neural development, including axon guidance and branching, axon target recognition, self-avoidance and synaptic formation. DSCAM belongs to the immunoglobulin superfamily and contributes to defects in the central nervous system in Down syndrome patients. Vertebrate DSCAMs differ from Drosophila Dscam1 in that they lack the extensive alternative splicing that occurs in the insect gene. Drosophila melanogaster Dscam has 38,016 isoforms generated by the alternative splicing of four variable exon clusters, which allows every neuron in the fly to display a distinctive set of Dscam proteins on its cell surface. Drosophila Dscam1 is a cell-surface protein that plays important roles in neural development and axon tiling of neurons. It is shown that thousands of isoforms bind themselves through specific homophilic (self-binding) interactions, a process which mediates cellular self-recognition. Drosophila Dscam2 is also alternatively spliced and plays a key role in the development of two visual system neurons, monopolar cells L1 and L2. This group is a member of the I-set Ig domains, having A-B-E-D strands in one beta-sheet and A'-G-F-C-C' in the other. Like the V-set Ig domains, members of the I-set have a discontinuous A strand but lack a C" strand.


Pssm-ID: 409551  Cd Length: 94  Bit Score: 44.79  E-value: 1.18e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  37 GTPPLKFIWLKNNGPVE-----KTKRVKIRdkenSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRV 101
Cdd:cd20959  29 GDLPLNIRWTLDGQPISddlgiTVSRLGRR----SSILSIDSLEASHAGNYTCHARNSAGSASYTAPLTV 94
IgI_8_hMLCK_like cd05762
Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar ...
25-106 1.30e-05

Eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar protein; member of the I-set of IgSF domains; The members here are composed of the eighth immunoglobulin (Ig)-like domain of human myosin light-chain kinase (MLCK) and similar proteins. Myosin light-chain kinase (MLCK) is a key regulator of different forms of cell motility involving actin and myosin II. Agonist stimulation of smooth muscle cells increases cytosolic Ca2+ which binds calmodulin. This Ca2+-calmodulin complex in turn binds to and activates MLCK. Activated MLCK leads to the phosphorylation of the 20 kDa myosin regulatory light chain (RLC) of myosin II and the stimulation of actin-activated myosin MgATPase activity. MLCK is widely present in vertebrate tissues; it phosphorylates the 20 kDa RLC of both smooth and nonmuscle myosin II. Phosphorylation leads to the activation of the myosin motor domain and altered structural properties of myosin II. In smooth muscle MLCK it is involved in initiating contraction. In nonmuscle cells, MLCK may participate in cell division and cell motility; it has been suggested MLCK plays a role in cardiomyocyte differentiation and contraction through regulation of nonmuscle myosin II.


Pssm-ID: 409419  Cd Length: 99  Bit Score: 44.56  E-value: 1.30e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  25 SGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRVNNV 104
Cdd:cd05762  15 AGESVELFCKVTGTQPITCTWMKFRKQIQEGEGIKIENTENSSKLTITEGQQEHCGCYTLEVENKLGSRQAQVNLTVVDK 94

                ..
gi 71980965 105 PD 106
Cdd:cd05762  95 PD 96
Ig_Titin_like cd05748
Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed ...
28-101 1.34e-05

Immunoglobulin (Ig)-like domain of titin and similar proteins; The members here are composed of the immunoglobulin (Ig)-like domain found in titin-like proteins and similar proteins. Titin (also called connectin) is a fibrous sarcomeric protein specifically found in vertebrate striated muscle. Titin is a giant protein; depending on isoform composition, it ranges from 2970 to 3700 kDa, and is of a length that spans half a sarcomere. Titin largely consists of multiple repeats of Ig-like and fibronectin type 3 (FN-III)-like domains. Titin connects the ends of myosin thick filaments to Z disks and extends along the thick filament to the H zone. It appears to function similarly to an elastic band, keeping the myosin filaments centered in the sarcomere during muscle contraction or stretching. Within the sarcomere, titin is also attached to or is associated with myosin binding protein C (MyBP-C). MyBP-C appears to contribute to the generation of passive tension by titin and like titin has repeated Ig-like and FN-III domains. Also included in this group are worm twitchin and insect projectin, thick filament proteins of invertebrate muscle which also have repeated Ig-like and FN-III domains.


Pssm-ID: 409406 [Multi-domain]  Cd Length: 82  Bit Score: 44.12  E-value: 1.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 71980965  28 EVRFKcealGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRV 101
Cdd:cd05748  13 DIPIK----GRPTPTVTWSKDGQPLKETGRVQIETTASSTSLVIKNAKRSDSGKYTLTLKNSAGEKSATINVKV 82
Ig3_Peroxidasin cd05745
Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the ...
26-101 1.34e-05

Third immunoglobulin (Ig)-like domain of peroxidasin; The members here are composed of the third immunoglobulin (Ig)-like domain in peroxidasin. Peroxidasin has a peroxidase domain and interacting extracellular motifs containing four Ig-like domains. It has been suggested that peroxidasin is secreted and has functions related to the stabilization of the extracellular matrix. It may play a part in various other important processes such as removal and destruction of cells which have undergone programmed cell death and protection of the organism against non-self.


Pssm-ID: 143222 [Multi-domain]  Cd Length: 74  Bit Score: 43.77  E-value: 1.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965  26 GDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRdkeNSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRV 101
Cdd:cd05745   2 GQTVDFLCEAQGYPQPVIAWTKGGSQLSVDRRHLVL---SSGTLRISRVALHDQGQYECQAVNIVGSQRTVAQLTV 74
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
605-785 1.45e-05

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 47.77  E-value: 1.45e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 605 TNAERAQLEQeIRavatfDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLKVRvppadhdmGGITEANAEFlYIAtQI 684
Cdd:cd05583  45 TMTERQVLEA-VR-----QSPFLVTLHYAFQTDAKLHLILDYVNGGELFTHLYQR--------EHFTESEVRI-YIG-EI 108
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 685 ALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGLMRTSYGSDYYKMlHRSWMPVRWMSKEAIEQGR--FSEASDVWS 762
Cdd:cd05583 109 VLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRA-YSFCGTIEYMAPEVVRGGSdgHDKAVDWWS 187
                       170       180
                ....*....|....*....|....*
gi 71980965 763 FGVTLWEIWSfGRQPY--EGASNQQ 785
Cdd:cd05583 188 LGVLTYELLT-GASPFtvDGERNSQ 211
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
612-787 1.46e-05

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 47.51  E-value: 1.46e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 612 LEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDlhELLKVRVPPAdHDMggITEAN-AEFLYiatQIALGMEY 690
Cdd:cd14109  43 LMREVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTI--ELVRDNLLPG-KDY--YTERQvAVFVR---QLLLALKH 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 691 LASMSFVHRDLATRNCLVGDTRtIKIADFGLMR-----TSYGSDYykmlhrsWMPvRWMSKEAIEQGRFSEASDVWSFGV 765
Cdd:cd14109 115 MHDLGIAHLDLRPEDILLQDDK-LKLADFGQSRrllrgKLTTLIY-------GSP-EFVSPEIVNSYPVTLATDMWSVGV 185
                       170       180
                ....*....|....*....|..
gi 71980965 766 TLWEIWSfGRQPYEGASNQQVI 787
Cdd:cd14109 186 LTYVLLG-GISPFLGDNDRETL 206
IgI_2_Titin_Z1z2-like cd20972
Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and ...
13-101 1.57e-05

Second Ig-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk, and similar domains; a member of the I-set of IgSF domains; The members here are composed of the second immunoglobulin (Ig)-like domain of the giant muscle protein titin Z1z2 in the sarcomeric Z-disk and similar proteins. Titin is a key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the titin Z1z2 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409564 [Multi-domain]  Cd Length: 91  Bit Score: 44.11  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  13 RLTSQLRNATKSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAAS 92
Cdd:cd20972   3 QFIQKLRSQEVAEGSKVRLECRVTGNPTPVVRWFCEGKELQNSPDIQIHQEGDLHSLIIAEAFEEDTGRYSCLATNSVGS 82

                ....*....
gi 71980965  93 VNTTSVLRV 101
Cdd:cd20972  83 DTTSAEIFV 91
Ig_C5_MyBP-C cd05894
C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here ...
25-101 1.65e-05

C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C); The members here are composed of the C5 immunoglobulin (Ig) domain of cardiac myosin binding protein C (MyBP-C). MyBP-C consists of repeated domains, Ig and fibronectin type 3, and various linkers. Three isoforms of MYBP-C exist: slow-skeletal (ssMyBP-C), fast-skeletal (fsMyBP-C), and cardiac (cMyBP-C). cMYBP-C has insertions between and inside domains and an additional cardiac-specific Ig domain at the N-terminus. For cMYBP_C an interaction has been demonstrated between this C5 domain and the Ig C8 domain.


Pssm-ID: 409475 [Multi-domain]  Cd Length: 86  Bit Score: 44.06  E-value: 1.65e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 71980965  25 SGDEVRFKCEALGTPPLKFIWLKNNGPVEKTK-RVKIRDKENSSRLVITQLDVLDSGYYQCIVSNPAASVNTTSVLRV 101
Cdd:cd05894   9 AGNKLRLDVPISGEPAPTVTWSRGDKAFTATEgRVRVESYKDLSSFVIEGAEREDEGVYTITVTNPVGEDHASLFVKV 86
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
572-806 1.80e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 48.07  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  572 EGQFGVVHSGIYTSGLFAP--EPMAVAV---KKCRHDATNA-ERAQLEQEIRAVATFDHPNVIKLIGVcYMDNSLLAVFE 645
Cdd:PHA03212  84 EARAGIEKAGFSILETFTPgaEGFAFACidnKTCEHVVIKAgQRGGTATEAHILRAINHPSIIQLKGT-FTYNKFTCLIL 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  646 YMVHGDLHELLKVRVPPADHDMggiteanaefLYIATQIALGMEYLASMSFVHRDLATRNCLVGDTRTIKIADFGlmRTS 725
Cdd:PHA03212 163 PRYKTDLYCYLAAKRNIAICDI----------LAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFG--AAC 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965  726 YGSDYYKMLHRSWM-PVRWMSKEAIEQGRFSEASDVWSFGVTLWEIWS-----FGRQPYEG-ASNQQVIELVANR---HL 795
Cdd:PHA03212 231 FPVDINANKYYGWAgTIATNAPELLARDPYGPAVDIWSAGIVLFEMATchdslFEKDGLDGdCDSDRQIKLIIRRsgtHP 310
                        250
                 ....*....|.
gi 71980965  796 LECPHNCPTNI 806
Cdd:PHA03212 311 NEFPIDAQANL 321
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
597-785 1.97e-05

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


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 46.88  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 597 VKKCRHDATNAERA------------QLEQEIRAVATFDHPNVIKLIGVCYMDNSLLAVFEYMVHGDLHELLkvrvppAD 664
Cdd:cd14115   9 VKKCLHKATRKDVAvkfvskkmkkkeQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLLDYL------MN 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 665 HDMggITEANAEFlYIaTQIALGMEYLASMSFVHRDLATRNCLVG---DTRTIKIADFGlmRTSYGSDYYKMLHRSWMPv 741
Cdd:cd14115  83 HDE--LMEEKVAF-YI-RDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLE--DAVQISGHRHVHHLLGNP- 155
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 71980965 742 RWMSKEAIEQGRFSEASDVWSFGVTLWEIWSfGRQPYEGASNQQ 785
Cdd:cd14115 156 EFAAPEVIQGTPVSLATDIWSIGVLTYVMLS-GVSPFLDESKEE 198
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
563-827 1.97e-05

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


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 47.27  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 563 QLSVREK-IGEGQFG-VVHSGIYtsglfapEPMAVAVKK----CRHDAtnaeraqlEQEIRAVATFD-HPNVIKLIGVCY 635
Cdd:cd13982   1 KLTFSPKvLGYGSEGtIVFRGTF-------DGRPVAVKRllpeFFDFA--------DREVQLLRESDeHPNVIRYFCTEK 65
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 636 MDNsllavFEYMV----HGDLHELLKvrvppaDHDMGGITEANA-EFLYIATQIALGMEYLASMSFVHRDLATRNCLVG- 709
Cdd:cd13982  66 DRQ-----FLYIAlelcAASLQDLVE------SPRESKLFLRPGlEPVRLLRQIASGLAHLHSLNIVHRDLKPQNILISt 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 710 DTRT----IKIADFGL------MRTSYGsdyykmlHRSWMP--VRWMSKEAIEQG---RFSEASDVWSFGVTLWEIWSFG 774
Cdd:cd13982 135 PNAHgnvrAMISDFGLckkldvGRSSFS-------RRSGVAgtSGWIAPEMLSGStkrRQTRAVDIFSLGCVFYYVLSGG 207
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 71980965 775 RQPYeGASNQQVIELVANRHLLECPH---NCPTNIYSLMVECWHENIERRPTFSEI 827
Cdd:cd13982 208 SHPF-GDKLEREANILKGKYSLDKLLslgEHGPEAQDLIERMIDFDPEKRPSAEEV 262
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
568-711 2.37e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The Wee1a subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 46.94  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 568 EKIGEGQFGVVHS------GIYTSGLFAPEPMAVAVkkcrhDATNAERaqleqEIRAVATF-DHPNVIKLIGVCYMDNSL 640
Cdd:cd14138  11 EKIGSGEFGSVFKcvkrldGCIYAIKRSKKPLAGSV-----DEQNALR-----EVYAHAVLgQHSHVVRYYSAWAEDDHM 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71980965 641 LAVFEYMVHGDLHELlkvrVPPADHDMGGITEANAEFLYIatQIALGMEYLASMSFVHRDLATRNCLVGDT 711
Cdd:cd14138  81 LIQNEYCNGGSLADA----ISENYRIMSYFTEPELKDLLL--QVARGLKYIHSMSLVHMDIKPSNIFISRT 145
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
612-779 2.37e-05

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: 46.97  E-value: 2.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 612 LEQEIRAVATFDHPNVIKLIGVCY----MDNSLL--AVFEYMVHGDLHELLKvRVPPADhdmggITEANAeflyIATQIA 685
Cdd:cd14012  45 LEKELESLKKLRHPNLVSYLAFSIerrgRSDGWKvyLLTEYAPGGSLSELLD-SVGSVP-----LDTARR----WTLQLL 114
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 686 LGMEYLASMSFVHRDLATRNCLV----GDTrTIKIADFGLMRT------SYGSDYYKmlhrswmPVRWMSKEAIEQG-RF 754
Cdd:cd14012 115 EALEYLHRNGVVHKSLHAGNVLLdrdaGTG-IVKLTDYSLGKTlldmcsRGSLDEFK-------QTYWLPPELAQGSkSP 186
                       170       180
                ....*....|....*....|....*
gi 71980965 755 SEASDVWSFGVTLWEIwSFGRQPYE 779
Cdd:cd14012 187 TRKTDVWDLGLLFLQM-LFGLDVLE 210
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
556-770 2.77e-05

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


Pssm-ID: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 47.20  E-value: 2.77e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 556 VFEItPSQLSVREKIGEGQFGVVHSGI-YTSGlfapepMAVAVKK-CR--HDATNAERAQleQEIRAVATFDHPNVIKLI 631
Cdd:cd07879  10 VWEL-PERYTSLKQVGSGAYGSVCSAIdKRTG------EKVAIKKlSRpfQSEIFAKRAY--RELTLLKHMQHENVIGLL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71980965 632 GVCYMDNSLLAVFE-YMVHGDLH-ELLKVRVPPADHDmggiteanaEFLYIATQIALGMEYLASMSFVHRDLATRNCLVG 709
Cdd:cd07879  81 DVFTSAVSGDEFQDfYLVMPYMQtDLQKIMGHPLSED---------KVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVN 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71980965 710 DTRTIKIADFGLMRTSYGSdyykmlHRSWMPVRWM-SKEAI-EQGRFSEASDVWSFGVTLWEI 770
Cdd:cd07879 152 EDCELKILDFGLARHADAE------MTGYVVTRWYrAPEVIlNWMHYNQTVDIWSVGCIMAEM 208
IgI_1_Contactin-1 cd05849
First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; ...
23-96 2.89e-05

First immunoglobulin (Ig) domain of contactin-1; member of the I-set of Ig superfamily domains; The members here are composed of the first immunoglobulin (Ig) domain of the neural cell adhesion molecule contactin-1. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-1 is differentially expressed in tumor tissues and may, through a RhoA mechanism, facilitate invasion and metastasis of human lung adenocarcinoma. This group belongs to the I-set of IgSF domains.


Pssm-ID: 409436 [Multi-domain]  Cd Length: 95  Bit Score: 43.40  E-value: 2.89e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71980965  23 KSSGDEVRFKCEALGTPPLKFIWLKNNGPVEKTKRvkiRDKENSSRLVITQLD-VLDSGYYQCIVSNPAASVNTT 96
Cdd:cd05849  16 ESTEGKVSVNCRARANPFPIYKWRKNNLDIDLTND---RYSMVGGNLVINNPDkYKDAGRYVCIVSNIYGKVRSR 87
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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