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Conserved domains on  [gi|1914781966|ref|NP_001374533|]
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focal adhesion kinase 1 isoform 49 [Homo sapiens]

Protein Classification

PTKc_FAK and Focal_AT domain-containing protein( domain architecture ID 10351313)

protein containing domains PH-like, PTKc_FAK, and Focal_AT

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
101-370 0e+00

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: 587.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05056     1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd05056    81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 340
Cdd:cd05056   161 SYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1914781966 341 MTKCWAYDPSRRPRFTELKAQLSTILEEEK 370
Cdd:cd05056   241 MTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
Focal_AT pfam03623
Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in ...
605-734 2.23e-75

Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localising FAK to focal adhesions. The crystal structure of FAT shows it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not.


:

Pssm-ID: 460992  Cd Length: 130  Bit Score: 239.09  E-value: 2.23e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 605 NLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLG 684
Cdd:pfam03623   1 DLDRTNDKVYECVTRVVKAVMQLSQEVQTAKPDEYVDLVKNVGLELRNLLTSVDELLPILPASSHREIEMAQKLLNKDLA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 685 ELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKM 734
Cdd:pfam03623  81 ELINKMKLAQQYSITTLDEEYRKQMLTAAHTLAMDAKNLLDVVDSARLRA 130
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
1-50 3.39e-22

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13190:

Pssm-ID: 473070  Cd Length: 111  Bit Score: 91.92  E-value: 3.39e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966   1 MLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQK 50
Cdd:cd13190    62 LLQLKIAGASEPLSITCSSLATAESLADLIDGYCRLVNQTDSSLIIRPEK 111
 
Name Accession Description Interval E-value
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
101-370 0e+00

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: 587.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05056     1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd05056    81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 340
Cdd:cd05056   161 SYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1914781966 341 MTKCWAYDPSRRPRFTELKAQLSTILEEEK 370
Cdd:cd05056   241 MTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
108-362 1.75e-135

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 399.95  E-value: 1.75e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 185
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLkGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGePLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYK 264
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDiYDDDYYRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:pfam07714 161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQC 240
                         250
                  ....*....|....*...
gi 1914781966 345 WAYDPSRRPRFTELKAQL 362
Cdd:pfam07714 241 WAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
108-362 2.73e-129

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 384.19  E-value: 2.73e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  108 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 185
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEePLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 265
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  266 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 345
Cdd:smart00219 161 RGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCW 240
                          250
                   ....*....|....*..
gi 1914781966  346 AYDPSRRPRFTELKAQL 362
Cdd:smart00219 241 AEDPEDRPTFSELVEIL 257
Focal_AT pfam03623
Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in ...
605-734 2.23e-75

Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localising FAK to focal adhesions. The crystal structure of FAT shows it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not.


Pssm-ID: 460992  Cd Length: 130  Bit Score: 239.09  E-value: 2.23e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 605 NLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLG 684
Cdd:pfam03623   1 DLDRTNDKVYECVTRVVKAVMQLSQEVQTAKPDEYVDLVKNVGLELRNLLTSVDELLPILPASSHREIEMAQKLLNKDLA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 685 ELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKM 734
Cdd:pfam03623  81 ELINKMKLAQQYSITTLDEEYRKQMLTAAHTLAMDAKNLLDVVDSARLRA 130
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
102-412 1.43e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 161.33  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 179
Cdd:COG0515     3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRP---VALKVLRPelAADPEARERFRREARALARLNHPNIVRVYDVGEED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PV-WIIMELCTlGE-LRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 257
Cdd:COG0515    80 GRpYLVMEYVE-GEsLADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKAS--KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPMP---PN 332
Cdd:COG0515   158 GGATLTQTGtvVGTPG--YMAPEQARGEPVDPRSDVYSLGVTLYE-LLTGRPPFDGDSPAELLRAHLREPPPPPSelrPD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRS 411
Cdd:COG0515   235 LPPALDAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 314

                  .
gi 1914781966 412 S 412
Cdd:COG0515   315 A 315
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
1-50 3.39e-22

FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion kinase-related nonkinase; p125FAK/pp125FAK;PTK2/Protein-tyrosine kinase 2 protein tyrosine kinase 2 (PTK2) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. It has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival. The N-terminal region of FAK1 contains a FERM domain, a linker, a kinase domain, and a C-terminal FRNK (FAK-related-non-kinase) domain. Three subdomains of FERM: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), form a cloverleaf fold, similar to those of known FERM structures despite the low sequence conservation. The C-lobe/F3 within the FERM domain is part of the PH domain family. The phosphoinositide-binding site found in ERM family proteins is not present in the FERM domain of FAK1. The adjacent Src SH3 and SH2 binding sites in the linker of FAK1 associates with the F3 and F1 lobes and are thought to be involved in regulation. The FERM domain of FAK1 can inhibit enzymatic activity and repress FAK signaling. In an inactive state of FAK1, the FERM domain is thought to interact with the catalytic domain of FAK1 to repress its activity. Upon activation this interaction is disrupted and its kinase activity restored. The FRNK domain is thought to function as a negative regulator of kinase activity. The C-lobe/F3 is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270011  Cd Length: 111  Bit Score: 91.92  E-value: 3.39e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966   1 MLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQK 50
Cdd:cd13190    62 LLQLKIAGASEPLSITCSSLATAESLADLIDGYCRLVNQTDSSLIIRPEK 111
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
132-402 1.27e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 86.61  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 132 NPALAVAIKTCKNCTSDSVREKFL------------QEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ 198
Cdd:PTZ00267   78 NPTTAAFVATRGSDPKEKVVAKFVmlnderqaayarSELHCLAACDHFGIVKHFDDFkSDDKLLLIMEYGSGGDLNKQIK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 199 VR-KYSLDLAS--LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKW 274
Cdd:PTZ00267  158 QRlKEHLPFQEyeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDvASSFCGTPYY 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 275 MAPESINFRRFTSASDVWMFGVCMWEIL-MHgvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:PTZ00267  238 LAPELWERKRYSKKADMWSLGVILYELLtLH--RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRP 315
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 354 R-----FTELKAQLSTILEE-----EKAQQEERMRMESRRQatvswdsgGSDEAPPKPS 402
Cdd:PTZ00267  316 TtqqllHTEFLKYVANLFQDivrhsETISPHDREEILRQLQ--------ESGERAPPPS 366
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
106-419 2.87e-15

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 79.45  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHqgiymspenpaLA--------VAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGV 175
Cdd:NF033483    7 GRYEIGERIGRGGMAEVY-----------LAkdtrldrdVAVKVLRPdlARDPEFVARFRREAQSAASLSHPNIVSVYDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 ITENPV-WIIMEL---CTLGEL---RSFLQVRKySLDLASLILyayqlsTALAYLESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:NF033483   76 GEDGGIpYIVMEYvdgRTLKDYireHGPLSPEE-AVEIMIQIL------SALEHAHRNGIVHRDIKPQNILITKDGRVKV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDST-----------YYkaskgklpikwMAPE-----SINFRrftsaSDVWMFGVCMWEILMhGVKPFQGv 312
Cdd:NF033483  149 TDFGIARALSSTTmtqtnsvlgtvHY-----------LSPEqarggTVDAR-----SDIYSLGIVLYEMLT-GRPPFDG- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 313 knndvigriEN---------GERLPMP----PNCPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAqQEERMR 378
Cdd:NF033483  211 ---------DSpvsvaykhvQEDPPPPselnPGIPQSLDAVVLKATAKDPDDRYQsAAEMRADLETALSGQRL-NAPKFA 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 379 MESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSP 419
Cdd:NF033483  281 PDSDDDRTKVLPPIPPAPAPTAAEPPEDPDDDGEGGEPADD 321
 
Name Accession Description Interval E-value
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
101-370 0e+00

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: 587.08  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05056     1 YEIQREDITLGRCIGEGQFGDVYQGVYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd05056    81 VWIVMELAPLGELRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 340
Cdd:cd05056   161 SYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMLGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSL 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 1914781966 341 MTKCWAYDPSRRPRFTELKAQLSTILEEEK 370
Cdd:cd05056   241 MTKCWAYDPSKRPRFTELKAQLSDILQEEK 270
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
108-362 1.75e-135

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 399.95  E-value: 1.75e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 185
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLkGEGENTKIKVAVKTLKEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGePLYIVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYK 264
Cdd:pfam07714  81 EYMPGGDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRDiYDDDYYRK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:pfam07714 161 RGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEFLEDGYRLPQPENCPDELYDLMKQC 240
                         250
                  ....*....|....*...
gi 1914781966 345 WAYDPSRRPRFTELKAQL 362
Cdd:pfam07714 241 WAYDPEDRPTFSELVEDL 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
108-362 2.73e-129

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 384.19  E-value: 2.73e-129
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  108 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIM 185
Cdd:smart00219   1 LTLGKKLGEGAFGEVYKGKLkGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEePLYIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 265
Cdd:smart00219  81 EYMEGGDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  266 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 345
Cdd:smart00219 161 RGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGMSNEEVLEYLKNGYRLPQPPNCPPELYDLMLQCW 240
                          250
                   ....*....|....*..
gi 1914781966  346 AYDPSRRPRFTELKAQL 362
Cdd:smart00219 241 AEDPEDRPTFSELVEIL 257
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
108-362 5.98e-128

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: 380.74  E-value: 5.98e-128
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  108 IELGRCIGEGQFGDVHQGIY-MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIM 185
Cdd:smart00221   1 LTLGKKLGEGAFGEVYKGTLkGKGDGKEVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEeEPLMIVM 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  186 ELCTLGELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 264
Cdd:smart00221  81 EYMPGGDLLDYLRKnRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYK 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  265 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:smart00221 161 VKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGMSNAEVLEYLKKGYRLPKPPNCPPELYKLMLQC 240
                          250
                   ....*....|....*...
gi 1914781966  345 WAYDPSRRPRFTELKAQL 362
Cdd:smart00221 241 WAEDPEDRPTFSELVEIL 258
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
112-362 7.11e-127

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: 378.03  E-value: 7.11e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCTL 190
Cdd:cd00192     1 KKLGEGAFGEVYKGKLKGGDGKTVDVAVKTLKEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEeEPLYLVMEYMEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRK--------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd00192    81 GDLLDFLRKSRpvfpspepSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSRDIYDDDY 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 Y-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLM 341
Cdd:cd00192   161 YrKKTGGKLPIRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPGLSNEEVLEYLRKGYRLPKPENCPDELYELM 240
                         250       260
                  ....*....|....*....|.
gi 1914781966 342 TKCWAYDPSRRPRFTELKAQL 362
Cdd:cd00192   241 LSCWQLDPEDRPTFSELVERL 261
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
114-367 1.62e-99

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: 307.35  E-value: 1.62e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 193
Cdd:cd05060     3 LGHGNFGSVRKGVYLMKSGKEVEVAVKTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGVCKGEPLMLVMELAPLGPL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 194 RSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYKA-SKGKLP 271
Cdd:cd05060    83 LKYLKKRR-EIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGaGSDYYRAtTAGRWP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 272 IKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSR 351
Cdd:cd05060   162 LKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGAKPYGEMKGPEVIAMLESGERLPRPEECPQEIYSIMLSCWKYRPED 241
                         250
                  ....*....|....*.
gi 1914781966 352 RPRFTELKAQLSTILE 367
Cdd:cd05060   242 RPTFSELESTFRRDPE 257
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
114-363 1.62e-89

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: 281.15  E-value: 1.62e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLG 191
Cdd:cd05040     3 LGDGSFGVVRRGEWTTPSGKVIQVAVKCLKsdVLSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLMMVTELAPLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM--EDSTYYKASKGK 269
Cdd:cd05040    83 SLLDRLRKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALpqNEDHYVMQEHRK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE-NGERLPMPPNCPPTLYSLMTKCWAYD 348
Cdd:cd05040   163 VPFAWCAPESLKTRKFSHASDVWMFGVTLWEMFTYGEEPWLGLNGSQILEKIDkEGERLERPDDCPQDIYNVMLQCWAHK 242
                         250
                  ....*....|....*
gi 1914781966 349 PSRRPRFTELKAQLS 363
Cdd:cd05040   243 PADRPTFVALRDFLP 257
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
108-363 1.98e-87

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: 276.18  E-value: 1.98e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIME 186
Cdd:cd05033     6 VTIEKVIGGGEFGEVCSGSLKLPGKKEIDVAIKTLKSGYSDKQRLDFLTEASIMGQFDHPNVIRLEGVVTKsRPVMIVTE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-TYYKA 265
Cdd:cd05033    86 YMENGSLDKFLRENDGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSeATYTT 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 345
Cdd:cd05033   166 KGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSYGERPYWDMSNQDVIKAVEDGYRLPPPMDCPSALYQLMLDCW 245
                         250
                  ....*....|....*...
gi 1914781966 346 AYDPSRRPRFTELKAQLS 363
Cdd:cd05033   246 QKDRNERPTFSQIVSTLD 263
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
101-363 8.45e-87

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: 274.99  E-value: 8.45e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-T 177
Cdd:cd05032     1 WELPREKITLIRELGQGSFGMVYEGLAkgVVKGEPETRVAIKTVNENASMRERIEFLNEASVMKEFNCHHVVRLLGVVsT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFL--------QVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:cd05032    81 GQPTLVVMELMAKGDLKSYLrsrrpeaeNNPGLgPPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 327
Cdd:cd05032   161 GDFGMTRDIYETDYYrKGGKGLLPVRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYQGLSNEEVLKFVIDGGHL 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 328 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 363
Cdd:cd05032   241 DLPENCPDKLLELMRMCWQYNPKMRPTFLEIVSSLK 276
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
101-362 4.16e-86

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: 272.74  E-value: 4.16e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVIT-EN 179
Cdd:cd05068     3 WEIDRKSLKLLRKLGSGQFGEVWEGLW----NNTTPVAVKTLKPGTMDP--EDFLREAQIMKKLRHPKLIQLYAVCTlEE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd05068    77 PIYIITELMKHGSLLEYLQGKGRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYYKASKG-KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05068   157 EDEYEAREGaKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIVTYGRIPYPGMTNAEVLQQVERGYRMPCPPNCPPQLY 236
                         250       260
                  ....*....|....*....|....
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05068   237 DIMLECWKADPMERPTFETLQWKL 260
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
114-362 2.21e-84

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: 267.39  E-value: 2.21e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 192
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDN---TEVAVKTCRETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKqPIMIVMELVPGGS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRyMEDSTYYKASKG--KL 270
Cdd:cd05041    80 LLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR-EEEDGEYTVSDGlkQI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPS 350
Cdd:cd05041   159 PIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYPGMSNQQTREQIESGYRMPAPELCPEAVYRLMLQCWAYDPE 238
                         250
                  ....*....|..
gi 1914781966 351 RRPRFTELKAQL 362
Cdd:cd05041   239 NRPSFSEIYNEL 250
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
112-362 2.48e-84

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: 267.23  E-value: 2.48e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTL 190
Cdd:cd05034     1 KKLGAGQFGEVWMGVW----NGTTKVAVKTLKPGTMSP--EAFLQEAQIMKKLRHDKLVQLYAVCSdEEPIYIVTELMSK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd05034    75 GSLLDYLRTgEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAK 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05034   155 FPIKWTAPEAALYGRFTIKSDVWSFGILLYEIVTYGRVPYPGMTNREVLEQVERGYRMPKPPGCPDELYDIMLQCWKKEP 234
                         250
                  ....*....|...
gi 1914781966 350 SRRPRFTELKAQL 362
Cdd:cd05034   235 EERPTFEYLQSFL 247
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
101-365 8.96e-83

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: 263.44  E-value: 8.96e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 179
Cdd:cd05039     1 WAINKKDLKLGELIGKGEFGDVMLGDYRGQK-----VAVKCLKD--DSTAAQAFLAEASVMTTLRHPNLVQLLGVVLEgN 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05039    74 GLYIVTEYMAKGSLVDYLRSRGRAvITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEAS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTyykaSKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05039   154 SNQ----DGGKLPIKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPHVEKGYRMEAPEGCPPEVY 229
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd05039   230 KVMKNCWELDPAKRPTFKQLREKLEHI 256
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
114-362 2.17e-81

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: 260.43  E-value: 2.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGI---YMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCT 189
Cdd:cd05044     3 LGSGAFGEVFEGTakdILGDGSGETKVAVKTLRKGATDQEKAEFLKEAHLMSNFKHPNILKLLGVCLDNdPQYIILELME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYS------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYMED 259
Cdd:cd05044    83 GGDLLSYLRAARPTaftpplLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDyrerVVKIGDFGLARDIYK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05044   163 NDYYrKEGEGLLPVRWMAPESLVDGVFTTQSDVWAFGVLMWEILTLGQQPYPARNNLEVLHFVRAGGRLDQPDNCPDDLY 242
                         250       260
                  ....*....|....*....|....
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05044   243 ELMLRCWSTDPEERPSFARILEQL 266
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
107-366 1.11e-80

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: 258.88  E-value: 1.11e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM 185
Cdd:cd05057     8 ELEKGKVLGSGAFGTVYKGVWIPEgEKVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQLIT 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYK 264
Cdd:cd05057    88 QLMPLGCLLDYVRNHRDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDvDEKEYH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:cd05057   168 AEGGKVPIKWMALESIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLLEKGERLPQPPICTIDVYMVLVKC 247
                         250       260
                  ....*....|....*....|..
gi 1914781966 345 WAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05057   248 WMIDAESRPTFKELANEFSKMA 269
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
111-364 3.38e-79

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: 253.77  E-value: 3.38e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIyMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 189
Cdd:cd05085     1 GELLGKGNFGEVYKGT-LKDKTP---VAVKTCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQrQPIYIVMELVP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd05085    77 GGDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLKQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05085   157 IPIKWTAPEALNYGRYSSESDVWSFGILLWETFSLGVCPYPGMTNQQAREQVEKGYRMSAPQRCPEDIYKIMQRCWDYNP 236
                         250
                  ....*....|....*
gi 1914781966 350 SRRPRFTELKAQLST 364
Cdd:cd05085   237 ENRPKFSELQKELAA 251
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
102-364 9.77e-78

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: 251.14  E-value: 9.77e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-E 178
Cdd:cd05048     1 EIPLSAVRFLEELGEGAFGKVYKGelLGPSSEESAISVAIKTLKENASPKTQQDFRREAELMSDLQHPNIVCLLGVCTkE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQVR---------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 243
Cdd:cd05048    81 QPQCMLFEYMAHGDLHEFLVRHsphsdvgvssdddgtASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 244 DCVKLGDFGLSRYMEDSTYYKA-SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE 322
Cdd:cd05048   161 LTVKISDFGLSRDIYSSDYYRVqSKSLLPVRWMPPEAILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGYSNQEVIEMIR 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 323 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 364
Cdd:cd05048   241 SRQLLPCPEDCPARVYSLMVECWHEIPSRRPRFKEIHTRLRT 282
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
114-362 1.39e-77

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: 249.88  E-value: 1.39e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpALAVAIKTCKNCTSD-SVREKFLQEALTMRQFDHPHIVKLIGvITENPVW-IIMELCTLG 191
Cdd:cd05116     3 LGSGNFGTVKKGYYQMKKV-VKTVAVKILKNEANDpALKDELLREANVMQQLDNPYIVRMIG-ICEAESWmLVMEMAELG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-SKGK 269
Cdd:cd05116    81 PLNKFLQKNRHVTE-KNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALrADENYYKAqTHGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05116   160 WPVKWYAPECMNYYKFSSKSDVWSFGVLMWEAFSYGQKPYKGMKGNEVTQMIEKGERMECPAGCPPEMYDLMKLCWTYDV 239
                         250
                  ....*....|...
gi 1914781966 350 SRRPRFTELKAQL 362
Cdd:cd05116   240 DERPGFAAVELRL 252
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
111-362 1.82e-77

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: 249.46  E-value: 1.82e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 189
Cdd:cd05084     1 GERIGRGNFGEVFSGRLRADNTP---VAVKSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQkQPIYIVMELVQ 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYykASKG- 268
Cdd:cd05084    78 GGDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVY--AATGg 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 --KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 346
Cdd:cd05084   156 mkQIPVKWTAPEALNYGRYSSESDVWSFGILLWETFSLGAVPYANLSNQQTREAVEQGVRLPCPENCPDEVYRLMEQCWE 235
                         250
                  ....*....|....*.
gi 1914781966 347 YDPSRRPRFTELKAQL 362
Cdd:cd05084   236 YDPRKRPSFSTVHQDL 251
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
101-365 2.28e-77

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: 249.65  E-value: 2.28e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVIT-EN 179
Cdd:cd05052     1 WEIERTDITMKHKLGGGQYGEVYEGVW---KKYNLTVAVKTLKEDTMEV--EEFLKEAAVMKEIKHPNLVQLLGVCTrEP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVR-KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05052    76 PFYIITEFMPYGNLLDYLRECnREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05052   156 GDTYTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEIATYGMSPYPGIDLSQVYELLEKGYRMERPEGCPPKVY 235
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd05052   236 ELMRACWQWNPSDRPSFAEIHQALETM 262
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
114-366 3.15e-77

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: 249.99  E-value: 3.15e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT---ENPVWIIMELCT 189
Cdd:cd05038    12 LGEGHFGSVELCRYDPLgDNTGEQVAVKSLQPSGEEQHMSDFKREIEILRTLDHEYIVKYKGVCEspgRRSLRLIMEYLP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-SK 267
Cdd:cd05038    92 SGSLRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLpEDKEYYYVkEP 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHG-------------VKPFQGVKN-NDVIGRIENGERLPMPPNC 333
Cdd:cd05038   172 GESPIFWYAPECLRESRFSSASDVWSFGVTLYELFTYGdpsqsppalflrmIGIAQGQMIvTRLLELLKSGERLPRPPSC 251
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05038   252 PDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
114-379 1.44e-75

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: 244.86  E-value: 1.44e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 193
Cdd:cd05115    12 LGSGNFGCVKKGVY-KMRKKQIDVAIKVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEALMLVMEMASGGPL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 194 RSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-SKGKLP 271
Cdd:cd05115    91 NKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALgADDSYYKArSAGKWP 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 272 IKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSR 351
Cdd:cd05115   171 LKWYAPECINFRKFSSRSDVWSYGVTMWEAFSYGQKPYKKMKGPEVMSFIEQGKRMDCPAECPPEMYALMSDCWIYKWED 250
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 352 RPRFTELkaqlstileeekaqqEERMRM 379
Cdd:cd05115   251 RPNFLTV---------------EQRMRT 263
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
108-366 1.81e-75

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: 244.78  E-value: 1.81e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIME 186
Cdd:cd05065     6 VKIEEVIGAGEFGEVCRGRLKLPGKREIFVAIKTLKSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSrPVMIITE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS----TY 262
Cdd:cd05065    86 FMENGALDSFLRQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDDtsdpTY 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMT 342
Cdd:cd05065   166 TSSLGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWDMSNQDVINAIEQDYRLPPPMDCPTALHQLML 245
                         250       260
                  ....*....|....*....|....
gi 1914781966 343 KCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05065   246 DCWQKDRNLRPKFGQIVNTLDKMI 269
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
103-366 2.04e-75

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: 244.39  E-value: 2.04e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PV 181
Cdd:cd05066     1 IDASCIKIEKVIGAGEFGEVCSGRLKLPGKREIPVAIKTLKAGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTRSkPV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED-- 259
Cdd:cd05066    81 MIVTEYMENGSLDAFLRKHDGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDdp 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYS 339
Cdd:cd05066   161 EAAYTTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVMSYGERPYWEMSNQDVIKAIEEGYRLPAPMDCPAALHQ 240
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 340 LMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05066   241 LMLDCWQKDRNERPKFEQIVSILDKLI 267
Focal_AT pfam03623
Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in ...
605-734 2.23e-75

Focal adhesion targeting region; Focal adhesion kinase (FAK) is a tyrosine kinase found in focal adhesions, intracellular signaling complexes that are formed following engagement of the extracellular matrix by integrins. The C-terminal 'focal adhesion targeting' (FAT) region is necessary and sufficient for localising FAK to focal adhesions. The crystal structure of FAT shows it forms a four-helix bundle that resembles those found in two other proteins involved in cell adhesion, alpha-catenin and vinculin. The binding of FAT to the focal adhesion protein, paxillin, requires the integrity of the helical bundle, whereas binding to another focal adhesion protein, talin, does not.


Pssm-ID: 460992  Cd Length: 130  Bit Score: 239.09  E-value: 2.23e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 605 NLDRSNDKVYENVTGLVKAVIEMSSKIQPAPPEEYVPMVKEVGLALRTLLATVDETIPLLPASTHREIEMAQKLLNSDLG 684
Cdd:pfam03623   1 DLDRTNDKVYECVTRVVKAVMQLSQEVQTAKPDEYVDLVKNVGLELRNLLTSVDELLPILPASSHREIEMAQKLLNKDLA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 685 ELINKMKLAQQYVMTSLQQEYKKQMLTAAHALAVDAKNLLDVIDQARLKM 734
Cdd:pfam03623  81 ELINKMKLAQQYSITTLDEEYRKQMLTAAHTLAMDAKNLLDVVDSARLRA 130
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
101-365 4.24e-74

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: 240.80  E-value: 4.24e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSpenpALAVAIKTCKNcTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN- 179
Cdd:cd05148     1 WERPREEFTLERKLGSGYFGEVWEGLWKN----RVRVAIKILKS-DDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGe 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05148    76 PVYIITELMEKGSLLAFLRSPEgQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKgKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05148   156 EDVYLSSDK-KIPYKWTAPEAASHGTFSTKSDVWSFGILLYEMFTYGQVPYPGMNNHEVYDQITAGYRMPCPAKCPQEIY 234
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd05148   235 KIMLECWAAEPEDRPSFKALREELDNI 261
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
102-367 5.68e-74

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: 241.14  E-value: 5.68e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITE 178
Cdd:cd05036     2 EVPRKNLTLIRALGQGAFGEVYEGTVsgMPGDPSPLQVAVKTLPELCSEQDEMDFLMEALIMSKFNHPNIVRCIGVcFQR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFL-QVRKY-----SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLG 249
Cdd:cd05036    82 LPRFILLELMAGGDLKSFLrENRPRpeqpsSLTMLDLLQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKGpgrVAKIG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 250 DFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLP 328
Cdd:cd05036   162 DFGMARDIYRADYYrKGGKAMLPVKWMPPEAFLDGIFTSKTDVWSFGVLLWEIFSLGYMPYPGKSNQEVMEFVTSGGRMD 241
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1914781966 329 MPPNCPPTLYSLMTKCWAYDPSRRPRFTelkaqlsTILE 367
Cdd:cd05036   242 PPKNCPGPVYRIMTQCWQHIPEDRPNFS-------TILE 273
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
110-362 1.49e-73

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: 239.27  E-value: 1.49e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSpenpALAVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELC 188
Cdd:cd05059     8 FLKELGSGQFGVVHLGKWRG----KIDVAIKMIKEGSMS--EDDFIEEAKVMMKLSHPKLVQLYGVCTKQrPIFIVTEYM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd05059    82 ANGCLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSVGT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYD 348
Cdd:cd05059   162 KFPVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERFSNSEVVEHISQGYRLYRPHLAPTEVYTIMYSCWHEK 241
                         250
                  ....*....|....
gi 1914781966 349 PSRRPRFTELKAQL 362
Cdd:cd05059   242 PEERPTFKILLSQL 255
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
95-366 5.68e-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: 238.86  E-value: 5.68e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  95 MPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENP---ALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIV 170
Cdd:cd05053     1 LPLDPEWELPRDRLTLGKPLGEGAFGQVVKAEAVGLDNKpneVVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHKNII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 171 KLIGVITEN-PVWIIMELCTLGELRSFLQVR-----KYSLD----------LASLILYAYQLSTALAYLESKRFVHRDIA 234
Cdd:cd05053    81 NLLGACTQDgPLYVVVEYASKGNLREFLRARrppgeEASPDdprvpeeqltQKDLVSFAYQVARGMEYLASKKCIHRDLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 235 ARNVLVSSNDCVKLGDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK 313
Cdd:cd05053   161 ARNVLVTEDNVMKIADFGLARDIHHIDYYrKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIP 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 314 NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05053   241 VEELFKLLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDLDRIL 293
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
102-366 8.19e-73

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: 237.56  E-value: 8.19e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NP 180
Cdd:cd05063     1 EIHPSHITKQKVIGAGEFGEVFRGILKMPGRKEVAVAIKTLKPGYTEKQRQDFLSEASIMGQFSHHNIIRLEGVVTKfKP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED- 259
Cdd:cd05063    81 AMIITEYMENGALDKYLRDHDGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDd 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 -STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05063   161 pEGTYTTSGGKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVMSFGERPYWDMSNHEVMKAINDGFRLPAPMDCPSAVY 240
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05063   241 QLMLQCWQQDRARRPRFVDIVNLLDKLL 268
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
100-362 1.62e-71

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: 234.01  E-value: 1.62e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITEN 179
Cdd:cd05067     1 EWEVPRETLKLVERLGAGQFGEVWMGYY----NGHTKVAIKSLKQGSMSP--DAFLAEANLMKQLQHQRLVRLYAVVTQE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05067    75 PIYIITEYMENGSLVDFLKTPSgIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05067   155 DNEYTAREGAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVTHGRIPYPGMTNPEVIQNLERGYRMPRPDNCPEELY 234
                         250       260
                  ....*....|....*....|....
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05067   235 QLMRLCWKERPEDRPTFEYLRSVL 258
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
95-366 1.16e-70

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: 233.70  E-value: 1.16e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  95 MPSTRDYEIQRERIELGRCIGEGQFGDV--HQGIYMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMRQFD-HPHI 169
Cdd:cd05099     1 LPLDPKWEFPRDRLVLGKPLGEGCFGQVvrAEAYGIDKSRPdqTVTVAVKMLKDNATDKDLADLISEMELMKLIGkHKNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 170 VKLIGVIT-ENPVWIIMELCTLGELRSFLQVRK-----YSLDLA----------SLILYAYQLSTALAYLESKRFVHRDI 233
Cdd:cd05099    81 INLLGVCTqEGPLYVIVEYAAKGNLREFLRARRppgpdYTFDITkvpeeqlsfkDLVSCAYQVARGMEYLESRRCIHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 234 AARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGV 312
Cdd:cd05099   161 AARNVLVTEDNVMKIADFGLARGVHDIDYYKkTSNGRLPVKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYPGI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 313 KNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05099   241 PVEELFKLLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
114-358 3.52e-70

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: 229.73  E-value: 3.52e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKT-CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPV-WIIMELCTLG 191
Cdd:cd13999     1 IGSGSFGEVYKGKWRGTD-----VAIKKlKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPlCIVTEYMPGG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK-GKL 270
Cdd:cd13999    76 SLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGVvGTP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 piKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd13999   156 --RWMAPEVLRGEPYTEKADVYSFGIVLWELLT-GEVPFKELSPIQIAaAVVQKGLRPPIPPDCPPELSKLIKRCWNEDP 232

                  ....*....
gi 1914781966 350 SRRPRFTEL 358
Cdd:cd13999   233 EKRPSFSEI 241
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
101-375 4.89e-70

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: 230.31  E-value: 4.89e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSdSVrEKFLQEALTMRQFDHPHIVKLIGVIT-EN 179
Cdd:cd05072     2 WEIPRESIKLVKKLGAGQFGEVWMGYY----NNSTKVAVKTLKPGTM-SV-QAFLEEANLMKTLQHDKLVRLYAVVTkEE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05072    76 PIYIITEYMAKGSLLDFLKSDEGGkVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIE 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05072   156 DNEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIVTYGKIPYPGMSNSDVMSALQRGYRMPRMENCPDELY 235
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQEE 375
Cdd:cd05072   236 DIMKTCWKEKAEERPTFDYLQSVLDDFYTATEGQYQQ 272
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
101-358 5.71e-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: 231.01  E-value: 5.71e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE 178
Cdd:cd05061     1 WEVSREKITLLRELGQGSFGMVYEGNArdIIKGEAETRVAVKTVNESASLRERIEFLNEASVMKGFTCHHVVRLLGVVSK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 -NPVWIIMELCTLGELRSFLQVRKYSLD---------LASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:cd05061    81 gQPTLVVMELMAHGDLKSYLRSLRPEAEnnpgrppptLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 327
Cdd:cd05061   161 GDFGMTRDIYETDYYrKGGKGLLPVRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQGLSNEQVLKFVMDGGYL 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 328 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd05061   241 DQPDNCPERVTDLMRMCWQFNPKMRPTFLEI 271
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
102-358 1.81e-69

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: 229.33  E-value: 1.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE- 178
Cdd:cd05050     1 EYPRNNIEYVRDIGQGAFGRVFQARApgLLPYEPFTMVAVKMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQ----------------VRKYSLD-----LASLILYAYQLSTALAYLESKRFVHRDIAARN 237
Cdd:cd05050    81 KPMCLLFEYMAYGDLNEFLRhrspraqcslshstssARKCGLNplplsCTEQLCIAKQVAAGMAYLSERKFVHRDLATRN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 238 VLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK-LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNND 316
Cdd:cd05050   161 CLVGENMVVKIADFGLSRNIYSADYYKASENDaIPIRWMPPESIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGMAHEE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 317 VIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd05050   241 VIYYVRDGNVLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
102-366 2.47e-69

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: 228.27  E-value: 2.47e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NP 180
Cdd:cd05064     1 ELDNKSIKIERILGTGRFGELCRGCLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEALTLGQFDHSNIVRLEGVITRgNT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGlsRYMED- 259
Cdd:cd05064    81 MMIVTEYMSNGALDSFLRKHEGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFR--RLQEDk 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 -STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05064   159 sEAIYTTMSGKSPVLWAAPEAIQYHHFSSASDVWSFGIVMWEVMSYGERPYWDMSGQDVIKAVEDGFRLPAPRNCPNLLH 238
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05064   239 QLMLDCWQKERGERPRFSQIHSILSKMV 266
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
112-381 3.31e-69

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: 229.91  E-value: 3.31e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTL 190
Cdd:cd05108    13 KVLGSGAFGTVYKGLWIPEgEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPF 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGK 269
Cdd:cd05108    93 GCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLgAEEKEYHAEGGK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05108   173 VPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDA 252
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 350 SRRPRFTELKAQLSTILEEEK----AQQEERMRMES 381
Cdd:cd05108   253 DSRPKFRELIIEFSKMARDPQrylvIQGDERMHLPS 288
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
107-368 6.90e-69

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: 227.58  E-value: 6.90e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIyMSPENPALAVAIKTCKN--CTSDSVrEKFLQEALTMRQFDHPHIVKLIGVITEN----- 179
Cdd:cd05075     1 KLALGKTLGEGEFGSVMEGQ-LNQDDSVLKVAVKTMKIaiCTRSEM-EDFLSEAVCMKEFDHPNVMRLIGVCLQNteseg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 ---PVwIIMELCTLGELRSFLQVRKYS-----LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDF 251
Cdd:cd05075    79 ypsPV-VILPFMKHGDLHSFLLYSRLGdcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 252 GLSRYMEDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMP 330
Cdd:cd05075   158 GLSKKIYNGDYYRQGRiSKMPVKWIAIESLADRVYTTKSDVWSFGVTMWEIATRGQTPYPGVENSEIYDYLRQGNRLKQP 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 331 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEE 368
Cdd:cd05075   238 PDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKD 275
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
112-365 1.02e-68

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: 227.21  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTL 190
Cdd:cd05109    13 KVLGSGAFGTVYKGIWIPDgENVKIPVAIKVLRENTSPKANKEILDEAYVMAGVGSPYVCRLLGICLTSTVQLVTQLMPY 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYKASKGK 269
Cdd:cd05109    93 GCLLDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDiDETEYHADGGK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05109   173 VPIKWMALESILHRRFTHQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLLEKGERLPQPPICTIDVYMIMVKCWMIDS 252
                         250
                  ....*....|....*.
gi 1914781966 350 SRRPRFTELKAQLSTI 365
Cdd:cd05109   253 ECRPRFRELVDEFSRM 268
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
110-366 5.52e-68

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: 225.11  E-value: 5.52e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCK--NCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVITE--------N 179
Cdd:cd05035     3 LGKILGEGEFGSVMEAQLKQDDGSQLKVAVKTMKvdIHTYSEI-EEFLSEAACMKDFDHPNVMRLIGVCFTasdlnkppS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVwIIMELCTLGELRSFLQVRK-----YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd05035    82 PM-VILPFMKHGDLHSYLLYSRlgglpEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYMEDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNC 333
Cdd:cd05035   161 RKIYSGDYYRQGRiSKMPVKWIALESLADNVYTSKSDVWSFGVTMWEIATRGQTPYPGVENHEIYDYLRNGNRLKQPEDC 240
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05035   241 LDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
99-366 8.97e-68

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: 224.80  E-value: 8.97e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  99 RDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCK---NCTSDSvrEKFLQEALTMRQFDHPHIVKLIGV 175
Cdd:cd05074     2 KDVLIQEQQFTLGRMLGKGEFGSVREAQLKSEDGSFQKVAVKMLKadiFSSSDI--EEFLREAACMKEFDHPNVIKLIGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 ITEN------PV-WIIMELCTLGELRSFLQVRK-----YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 243
Cdd:cd05074    80 SLRSrakgrlPIpMVILPFMKHGDLHTFLLMSRigeepFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNEN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 244 DCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE 322
Cdd:cd05074   160 MTVCVADFGLSKKIYSGDYYRqGCASKLPVKWLALESLADNVYTTHSDVWAFGVTMWEIMTRGQTPYAGVENSEIYNYLI 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1914781966 323 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05074   240 KGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELIW 283
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
102-362 1.79e-67

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: 223.88  E-value: 1.79e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 179
Cdd:cd05049     1 HIKRDTIVLKRELGEGAFGKVFLGecYNLEPEQDKMLVAVKTLKDASSPDARKDFEREAELLTNLQHENIVKFYGVCTEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWI-IMELCTLGELRSFLQ-------------VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 245
Cdd:cd05049    81 DPLLmVFEYMEHGDLNKFLRshgpdaaflasedSAPGELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 246 VKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENG 324
Cdd:cd05049   161 VKIGDFGMSRDIYSTDYYRvGGHTMLPIRWMPPESILYRKFTTESDVWSFGVVLWEIFTYGKQPWFQLSNTEVIECITQG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 325 ERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05049   241 RLLQRPRTCPSEVYAVMLGCWKREPQQRLNIKDIHKRL 278
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
112-368 1.82e-67

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: 223.12  E-value: 1.82e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI--TENPVWIIMELCT 189
Cdd:cd05058     1 EVIGKGHFGCVYHGTLIDSDGQKIHCAVKSLNRITDIEEVEQFLKEGIIMKDFSHPNVLSLLGIClpSEGSPLVVLPYMK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK-- 267
Cdd:cd05058    81 HGDLRNFIRSETHNPTVKDLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKEYYSVHNht 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 -GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 346
Cdd:cd05058   161 gAKLPVKWMALESLQTQKFTTKSDVWSFGVLLWELMTRGAPPYPDVDSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWH 240
                         250       260
                  ....*....|....*....|..
gi 1914781966 347 YDPSRRPRFTELKAQLSTILEE 368
Cdd:cd05058   241 PKPEMRPTFSELVSRISQIFST 262
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
106-364 1.54e-66

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: 220.52  E-value: 1.54e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKnCtsDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM 185
Cdd:cd05083     6 QKLTLGEIIGEGEFGAVLQGEYMGQK-----VAVKNIK-C--DVTAQAFLEETAVMTKLQHKNLVRLLGVILHNGLYIVM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymedSTYYK 264
Cdd:cd05083    78 ELMSKGNLVNFLRSRGRALvPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAK----VGSMG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:cd05083   154 VDNSRLPVKWTAPEALKNKKFSSKSDVWSYGVLLWEVFSYGRAPYPKMSVKEVKEAVEKGYRMEPPEGCPPDVYSIMTSC 233
                         250       260
                  ....*....|....*....|
gi 1914781966 345 WAYDPSRRPRFTELKAQLST 364
Cdd:cd05083   234 WEAEPGKRPSFKKLREKLEK 253
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
102-358 5.04e-66

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: 220.67  E-value: 5.04e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVH-------QGI-------YMSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHP 167
Cdd:cd05051     1 EFPREKLEFVEKLGEGQFGEVHlceanglSDLtsddfigNDNKDEPVL-VAVKMLRPDASKNAREDFLKEVKIMSQLKDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGVITENPVW-IIMELCTLGELRSFLQVR-----------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAA 235
Cdd:cd05051    80 NIVRLLGVCTRDEPLcMIVEYMENGDLNQFLQKHeaetqgasatnSKTLSYGTLLYMATQIASGMKYLESLNFVHRDLAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 236 RNVLVSSNDCVKLGDFGLSRYMEDSTYYKAsKGK--LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVK-PFQGV 312
Cdd:cd05051   160 RNCLVGPNYTIKIADFGMSRNLYSGDYYRI-EGRavLPIRWMAWESILLGKFTTKSDVWAFGVTLWEILTLCKEqPYEHL 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 313 KNNDVigrIEN--------GER--LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd05051   239 TDEQV---IENageffrddGMEvyLSRPPNCPKEIYELMLECWRRDEEDRPTFREI 291
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
100-367 8.67e-66

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: 219.42  E-value: 8.67e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE 178
Cdd:cd14204     1 DVMIDRNLLSLGKVLGEGEFGSVMEGELQQPDGTNHKVAVKTMKlDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVCLE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 -------NPVwIIMELCTLGELRSFLQVRKYSLD-----LASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV 246
Cdd:cd14204    81 vgsqripKPM-VILPFMKYGDLHSFLLRSRLGSGpqhvpLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 247 KLGDFGLSRYMEDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14204   160 CVADFGLSKKIYSGDYYRQGRiAKMPVKWIAVESLADRVYTVKSDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYLLHGH 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 326 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14204   240 RLKQPEDCLDELYDIMYSCWRSDPTDRPTFTQLRENLEKLLE 281
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
99-381 1.55e-65

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: 219.55  E-value: 1.55e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  99 RDYEIQRERIelgrcIGEGQFGDVHQGIYMSP-ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT 177
Cdd:cd05110     5 KETELKRVKV-----LGSGAFGTVYKGIWVPEgETVKIPVAIKILNETTGPKANVEFMDEALIMASMDHPHLVRLLGVCL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 257
Cdd:cd05110    80 SPTIQLVTQLMPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 E-DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPT 336
Cdd:cd05110   160 EgDEKEYNADGGKMPIKWMALECIHYRKFTHQSDVWSYGVTIWELMTFGGKPYDGIPTREIPDLLEKGERLPQPPICTID 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 337 LYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEK----AQQEERMRMES 381
Cdd:cd05110   240 VYMVMVKCWMIDADSRPKFKELAAEFSRMARDPQrylvIQGDDRMKLPS 288
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
109-362 2.00e-65

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: 218.73  E-value: 2.00e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCigegQFGDVHQG-IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIME 186
Cdd:cd05090    12 ELGEC----AFGKIYKGhLYLPGMDHAQLVAIKTLKDYNNPQQWNEFQQEASLMTELHHPNIVCLLGVVTqEQPVCMLFE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVR----------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 250
Cdd:cd05090    88 FMNQGDLHEFLIMRsphsdvgcssdedgtvKSSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISD 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 251 FGLSRYMEDSTYYKA-SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPM 329
Cdd:cd05090   168 LGLSREIYSSDYYRVqNKSLLPIRWMPPEAIMYGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSNQEVIEMVRKRQLLPC 247
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1914781966 330 PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05090   248 SEDCPPRMYSLMTECWQEIPSRRPRFKDIHARL 280
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
101-365 3.17e-65

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: 217.16  E-value: 3.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNctsDSVREKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05082     1 WALNMKELKLLQTIGKGEFGDVMLGDYRGNK-----VAVKCIKN---DATAQAFLAEASVMTQLRHSNLVQLLGVIVEEK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 --VWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRym 257
Cdd:cd05082    73 ggLYIVTEYMAKGSLVDYLRSRGRSvLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK-- 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTyyKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTL 337
Cdd:cd05082   151 EASS--TQDTGKLPVKWTAPEALREKKFSTKSDVWSFGILLWEIYSFGRVPYPRIPLKDVVPRVEKGYKMDAPDGCPPAV 228
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd05082   229 YDVMKNCWHLDAAMRPSFLQLREQLEHI 256
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
102-364 3.18e-65

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: 217.96  E-value: 3.18e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-E 178
Cdd:cd05091     2 EINLSAVRFMEELGEDRFGKVYKGhlFGTAPGEQTQAVAIKTLKDKAEGPLREEFRHEAMLRSRLQHPNIVCLLGVVTkE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQVR---------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 243
Cdd:cd05091    82 QPMSMIFSYCSHGDLHEFLVMRsphsdvgstdddktvKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVFDK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 244 DCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIE 322
Cdd:cd05091   162 LNVKISDLGLFREVYAADYYKlMGNSLLPIRWMSPEAIMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVIEMIR 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 323 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 364
Cdd:cd05091   242 NRQVLPCPDDCPAWVYTLMLECWNEFPSRRPRFKDIHSRLRT 283
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
114-362 6.39e-64

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: 213.24  E-value: 6.39e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 193
Cdd:cd14203     3 LGQGCFGEVWMGTW----NGTTKVAIKTLKPGTMSP--EAFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEFMSKGSL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 194 RSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd14203    77 LDFLKDGEgKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 KWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd14203   157 KWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPPGCPESLHELMCQCWRKDPEER 236
                         250
                  ....*....|
gi 1914781966 353 PRFTELKAQL 362
Cdd:cd14203   237 PTFEYLQSFL 246
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
91-358 1.11e-63

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: 214.66  E-value: 1.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  91 DTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHP 167
Cdd:cd05055    20 DPTQLPYDLKWEFPRNNLSFGKTLGAGAFGKVVEATAygLSKSDAVMKVAVKMLKPTAHSSEREALMSELKIMSHLgNHE 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 245
Cdd:cd05055   100 NIVNLLGACTIGgPILVITEYCCYGDLLNFLRRKRESfLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKI 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 246 VKLGDFGLSR-YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIEN 323
Cdd:cd05055   180 VKICDFGLARdIMNDSNYVVKGNARLPVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPGMPvDSKFYKLIKE 259
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1914781966 324 GERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd05055   260 GYRMAQPEHAPAEIYDIMKTCWDADPLKRPTFKQI 294
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
109-360 1.75e-63

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 212.39  E-value: 1.75e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  109 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKL---VAIKVIKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFeDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  188 CTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:smart00220  79 CEGGDLFDLLK-KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFV 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  268 GKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPP---NCPPTLYSLMTKC 344
Cdd:smart00220 158 GTPE--YMAPEVLLGKGYGKAVDIWSLGVILYELLT-GKPPFPGDDQLLELFKKIGKPKPPFPPpewDISPEAKDLIRKL 234
                          250
                   ....*....|....*.
gi 1914781966  345 WAYDPSRRPRFTELKA 360
Cdd:smart00220 235 LVKDPEKRLTAEEALQ 250
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
114-363 1.01e-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: 210.19  E-value: 1.01e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalaVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 192
Cdd:cd05112    12 IGSGQFGLVHLGYWLNKDK----VAIKTIREGAMS--EEDFIEEAEVMMKLSHPKLVQLYGVCLEQaPICLVFEFMEHGC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd05112    86 LSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFPV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 KWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05112   166 KWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERPEDR 245
                         250
                  ....*....|.
gi 1914781966 353 PRFTELKAQLS 363
Cdd:cd05112   246 PSFSLLLRQLA 256
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
101-358 3.83e-62

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: 3.83e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE 178
Cdd:cd05062     1 WEVAREKITMSRELGQGSFGMVYEGIAkgVVKDEPETRVAIKTVNEAASMRERIEFLNEASVMKEFNCHHVVRLLGVVSQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 -NPVWIIMELCTLGELRSFLQVRKYSLD---------LASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:cd05062    81 gQPTLVIMELMTRGDLKSYLRSLRPEMEnnpvqappsLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDSTYY-KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 327
Cdd:cd05062   161 GDFGMTRDIYETDYYrKGGKGLLPVRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVMEGGLL 240
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 328 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd05062   241 DKPDNCPDMLFELMRMCWQYNPKMRPSFLEI 271
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
101-362 2.98e-61

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: 206.80  E-value: 2.98e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVhqgiYMSPENPALAVAIKTCKNCTSdSVrEKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05073     6 WEIPRESLKLEKKLGAGQFGEV----WMATYNKHTKVAVKTMKPGSM-SV-EAFLAEANVMKTLQHDKLVKLHAVVTKEP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd05073    80 IYIITEFMAKGSLLDFLKSDEGSkQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYS 339
Cdd:cd05073   160 NEYTAREGAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYPGMSNPEVIRALERGYRMPRPENCPEELYN 239
                         250       260
                  ....*....|....*....|...
gi 1914781966 340 LMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05073   240 IMMRCWKNRPEERPTFEYIQSVL 262
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
103-362 1.03e-60

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: 205.97  E-value: 1.03e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVH--QGIYMSPENPALAVAIKTCKNCTsDSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 179
Cdd:cd05092     2 IKRRDIVLKWELGEGAFGKVFlaECHNLLPEQDKMLVAVKALKEAT-ESARQDFQREAELLTVLQHQHIVRFYGVCTEgE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQ--------------VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 245
Cdd:cd05092    81 PLIMVFEYMRHGDLNRFLRshgpdakildggegQAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 246 VKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENG 324
Cdd:cd05092   161 VKIGDFGMSRDIYSTDYYRvGGRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIFTYGKQPWYQLSNTEAIECITQG 240
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 325 ERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05092   241 RELERPRTCPPEVYAIMQGCWQREPQQRHSIKDIHSRL 278
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
114-362 1.05e-60

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 203.27  E-value: 1.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 192
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKK---VAVKVIPKEKLKKLLEELLREIEILKKLNHPNIVKLYDVfETENFLYLVMEYCEGGS 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGKLP 271
Cdd:cd00180    78 LKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLdSDDSLLKTTGGTTP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 272 IKWMAPESINFRRFTSASDVWMFGVCMWEIlmhgvkpfqgvknndvigriengerlpmppncpPTLYSLMTKCWAYDPSR 351
Cdd:cd00180   158 PYYAPPELLGGRYYGPKVDIWSLGVILYEL---------------------------------EELKDLIRRMLQYDPKK 204
                         250
                  ....*....|.
gi 1914781966 352 RPRFTELKAQL 362
Cdd:cd00180   205 RPSAKELLEHL 215
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
107-366 2.13e-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: 205.20  E-value: 2.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPA--LAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWI 183
Cdd:cd05045     1 NLVLGKTLGEGEFGKVVKATAFRLKGRAgyTTVAVKMLKENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDgPLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQV-RKY----------------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV 240
Cdd:cd05045    81 IVEYAKYGSLRSFLREsRKVgpsylgsdgnrnssyldnpderALTMGDLISFAWQISRGMQYLAEMKLVHRDLAARNVLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 241 SSNDCVKLGDFGLSR--YMEDStYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVI 318
Cdd:cd05045   161 AEGRKMKISDFGLSRdvYEEDS-YVKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYPGIAPERLF 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1914781966 319 GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05045   240 NLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
93-366 4.37e-60

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: 205.25  E-value: 4.37e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  93 YTMPSTRDYEIQRERIELGRCIGEGQFGDV--HQGIYMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHP 167
Cdd:cd05101    11 YELPEDPKWEFPRDKLTLGKPLGEGCFGQVvmAEAVGIDKDKPkeAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIgKHK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-----YSLDLA----------SLILYAYQLSTALAYLESKRFVHR 231
Cdd:cd05101    91 NIINLLGACTQDgPLYVIVEYASKGNLREYLRARRppgmeYSYDINrvpeeqmtfkDLVSCTYQLARGMEYLASQKCIHR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 232 DIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQ 310
Cdd:cd05101   171 DLAARNVLVTENNVMKIADFGLARDINNIDYYKkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYP 250
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 311 GVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05101   251 GIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIL 306
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
95-373 7.53e-60

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: 204.09  E-value: 7.53e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  95 MPSTRDYEIQRERIELGRCIGEGQFGDV--HQGIYMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHI 169
Cdd:cd05098     2 LPEDPRWELPRDRLVLGKPLGEGCFGQVvlAEAIGLDKDKPnrVTKVAVKMLKSDATEKDLSDLISEMEMMKMIgKHKNI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 170 VKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-----YS----------LDLASLILYAYQLSTALAYLESKRFVHRDI 233
Cdd:cd05098    82 INLLGACTQDgPLYVIVEYASKGNLREYLQARRppgmeYCynpshnpeeqLSSKDLVSCAYQVARGMEYLASKKCIHRDL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 234 AARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGV 312
Cdd:cd05098   162 AARNVLVTEDNVMKIADFGLARDIHHIDYYKkTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGV 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 313 KNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQ 373
Cdd:cd05098   242 PVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQE 302
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
101-374 2.23e-59

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: 202.22  E-value: 2.23e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05071     4 WEIPRESLRLEVKLGQGCFGEVWMGTW----NGTTRVAIKTLKPGTMSP--EAFLQEAQVMKKLRHEKLVQLYAVVSEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFL--QVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05071    78 IYIVTEYMSKGSLLDFLkgEMGKY-LRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05071   157 DNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELTTKGRVPYPGMVNREVLDQVERGYRMPCPPECPESLH 236
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQE 374
Cdd:cd05071   237 DLMCQCWRKEPEERPTFEYLQAFLEDYFTSTEPQYQ 272
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
95-366 3.53e-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: 203.33  E-value: 3.53e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  95 MPSTRDYEIQRERIELGRCIGEGQFGDVHQ----GIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHI 169
Cdd:cd05100     1 LPADPKWELSRTRLTLGKPLGEGCFGQVVMaeaiGIDKDKPNKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIgKHKNI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 170 VKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-----YSLD----------LASLILYAYQLSTALAYLESKRFVHRDI 233
Cdd:cd05100    81 INLLGACTQDgPLYVLVEYASKGNLREYLRARRppgmdYSFDtcklpeeqltFKDLVSCAYQVARGMEYLASQKCIHRDL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 234 AARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGV 312
Cdd:cd05100   161 AARNVLVTEDNVMKIADFGLARDVHNIDYYKkTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGI 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 313 KNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05100   241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVEDLDRVL 294
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
111-363 3.75e-59

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: 201.72  E-value: 3.75e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIYMsPENPALA--VAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELC 188
Cdd:cd05111    12 LKVLGSGVFGTVHKGIWI-PEGDSIKipVAIKVIQDRSGRQSFQAVTDHMLAIGSLDHAYIVRLLGICPGASLQLVTQLL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR--YMEDSTYYkAS 266
Cdd:cd05111    91 PLGSLLDHVRQHRGSLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADllYPDDKKYF-YS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 346
Cdd:cd05111   170 EAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMMTFGAEPYAGMRLAEVPDLLEKGERLAQPQICTIDVYMVMVKCWM 249
                         250
                  ....*....|....*..
gi 1914781966 347 YDPSRRPRFTELKAQLS 363
Cdd:cd05111   250 IDENIRPTFKELANEFT 266
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
101-363 1.35e-58

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: 200.79  E-value: 1.35e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQ----GIYMSPEnpALAVAIKTCKNCTSDSVREKFLQEaltMRQFDH--PH--IVKL 172
Cdd:cd05054     2 WEFPRDRLKLGKPLGRGAFGKVIQasafGIDKSAT--CRTVAVKMLKEGATASEHKALMTE---LKILIHigHHlnVVNL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 173 IGVIT--ENPVWIIMELCTLGELRSFLQVR-------------------------KYSLDLASLILYAYQLSTALAYLES 225
Cdd:cd05054    77 LGACTkpGGPLMVIVEFCKFGNLSNYLRSKreefvpyrdkgardveeeedddelyKEPLTLEDLICYSFQVARGMEFLAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 226 KRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMH 304
Cdd:cd05054   157 RKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGDARLPLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSL 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 305 GVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 363
Cdd:cd05054   237 GASPYPGVQmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDCWHGEPKERPTFSELVEKLG 296
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
114-363 4.74e-58

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: 198.46  E-value: 4.74e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiYMSP---ENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 189
Cdd:cd05046    13 LGRGEFGEVFLA-KAKGieeEGGETLVLVKALQKTKDENLQSEFRRELDMFRKLSHKNVVRLLGLCREaEPHYMILEYTD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLAS--------LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 261
Cdd:cd05046    92 LGDLKQFLRATKSKDEKLKppplstkqKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDVYNSE 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSL 340
Cdd:cd05046   172 YYKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEVFTQGELPFYGLSDEEVLNRLQAGKlELPVPEGCPSRLYKL 251
                         250       260
                  ....*....|....*....|...
gi 1914781966 341 MTKCWAYDPSRRPRFTELKAQLS 363
Cdd:cd05046   252 MTRCWAVNPKDRPSFSELVSALG 274
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
103-366 4.93e-58

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: 197.80  E-value: 4.93e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVHQGIYMSPENpalaVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVIT-ENPV 181
Cdd:cd05113     1 IDPKDLTFLKELGTGQFGVVKYGKWRGQYD----VAIKMIKEGSMS--EDEFIEEAKVMMNLSHEKLVQLYGVCTkQRPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 261
Cdd:cd05113    75 FIITEYMANGCLLNYLREMRKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLM 341
Cdd:cd05113   155 YTSSVGSKFPVRWSPPEVLMYSKFSSKSDVWAFGVLMWEVYSLGKMPYERFTNSETVEHVSQGLRLYRPHLASEKVYTIM 234
                         250       260
                  ....*....|....*....|....*
gi 1914781966 342 TKCWAYDPSRRPRFTELkaqLSTIL 366
Cdd:cd05113   235 YSCWHEKADERPTFKIL---LSNIL 256
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
101-374 5.30e-58

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: 198.37  E-value: 5.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05070     4 WEIPRESLQLIKRLGNGQFGEVWMGTW----NGNTKVAIKTLKPGTMSP--ESFLEEAQIMKKLKHDKLVQLYAVVSEEP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd05070    78 IYIVTEYMSKGSLLDFLKDGEgRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIED 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYS 339
Cdd:cd05070   158 NEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPISLHE 237
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1914781966 340 LMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQE 374
Cdd:cd05070   238 LMIHCWKKDPEERPTFEYLQGFLEDYFTATEPQYQ 272
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
101-374 2.18e-57

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: 196.83  E-value: 2.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSvrEKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd05069     7 WEIPRESLRLDVKLGQGCFGEVWMGTW----NGTTKVAIKTLKPGTMMP--EAFLQEAQIMKKLRHDKLVPLYAVVSEEP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVR--KYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05069    81 IYIVTEFMGKGSLLDFLKEGdgKY-LKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIE 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLY 338
Cdd:cd05069   160 DNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMVNREVLEQVERGYRMPCPQGCPESLH 239
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTILEEEKAQQE 374
Cdd:cd05069   240 ELMKLCWKKDPDERPTFEYIQSFLEDYFTATEPQYQ 275
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
103-363 1.45e-56

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: 194.59  E-value: 1.45e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN--P 180
Cdd:cd05043     3 VSRERVTLSDLLQEGTFGRIFHGILRDEKGKEEEVLVKTVKDHASEIQVTMLLQESSLLYGLSHQNLLPILHVCIEDgeK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKY-------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd05043    83 PMVLYPYMNWGNLKLFLQQCRLseannpqALSTQQLVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNAL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGK-LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPN 332
Cdd:cd05043   163 SRDLFPMDYHCLGDNEnRPIKWMSLESLVNKEYSSASDVWSFGVLLWELMTLGQTPYVEIDPFEMAAYLKDGYRLAQPIN 242
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 363
Cdd:cd05043   243 CPDELFAVMACCWALDPEERPSFQQLVQCLT 273
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
112-367 1.94e-56

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: 193.54  E-value: 1.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSpenpALAVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTL 190
Cdd:cd05114    10 KELGSGLFGVVRLGKWRA----QYKVAIKAIRE--GAMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQkPIYIVTEFMEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 270
Cdd:cd05114    84 GCLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKF 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPS 350
Cdd:cd05114   164 PVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCWHEKPE 243
                         250
                  ....*....|....*..
gi 1914781966 351 RRPRFTELKAQLSTILE 367
Cdd:cd05114   244 GRPTFADLLRTITEIAE 260
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
104-367 1.33e-54

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: 189.34  E-value: 1.33e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 104 QRERIELGRCIGEGQFGDVHQGIYmSPENPALA--VAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE--- 178
Cdd:cd05080     2 HKRYLKKIRDLGEGHFGKVSLYCY-DPTNDGTGemVAVKALKADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEqgg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM- 257
Cdd:cd05080    81 KSLQLIMEYVPLGSLRDYLP--KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVp 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKASK-GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHG-------------VKPFQGVKNN-DVIGRIE 322
Cdd:cd05080   159 EGHEYYRVREdGDSPVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCdssqspptkflemIGIAQGQMTVvRLIELLE 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 323 NGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd05080   239 RGERLPCPDKCPQEVYHLMKNCWETEASFRPTFENLIPILKTVHE 283
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
114-365 3.44e-54

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: 188.30  E-value: 3.44e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmSP--ENPALAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELC 188
Cdd:cd14205    12 LGKGNFGSVEMCRY-DPlqDNTGEVVAVKKLQHSTEEHLRD-FEREIEILKSLQHDNIVKYKGVCysaGRRNLRLIMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASK 267
Cdd:cd14205    90 PYGSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLpQDKEYYKVKE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 -GKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKP------FQGVKNNDVIGR---------IENGERLPMPP 331
Cdd:cd14205   170 pGESPIFWYAPESLTESKFSVASDVWSFGVVLYELFTYIEKSksppaeFMRMIGNDKQGQmivfhlielLKNNGRLPRPD 249
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1914781966 332 NCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14205   250 GCPDEIYMIMTECWNNNVNQRPSFRDLALRVDQI 283
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
103-365 6.50e-54

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: 187.55  E-value: 6.50e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVH--QGIYMSPENPALAVAIKTCKNcTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 179
Cdd:cd05093     2 IKRHNIVLKRELGEGAFGKVFlaECYNLCPEQDKILVAVKTLKD-ASDNARKDFHREAELLTNLQHEHIVKFYGVCVEgD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRK------------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 247
Cdd:cd05093    81 PLIMVFEYMKHGDLNKFLRAHGpdavlmaegnrpAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 248 LGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGER 326
Cdd:cd05093   161 IGDFGMSRDVYSTDYYRvGGHTMLPIRWMPPESIMYRKFTTESDVWSLGVVLWEIFTYGKQPWYQLSNNEVIECITQGRV 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1914781966 327 LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd05093   241 LQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNL 279
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
101-368 1.43e-52

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: 185.57  E-value: 1.43e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQG--IYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVIT 177
Cdd:cd05102     2 WEFPRDRLRLGKVLGHGAFGKVVEAsaFGIDKSSSCETVAVKMLKEGATASEHKALMSELKILIHIgNHLNVVNLLGACT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 E--NPVWIIMELCTLGELRSFL-------------------QVR------------------------------------ 200
Cdd:cd05102    82 KpnGPLMVIVEFCKYGNLSNFLrakregfspyrersprtrsQVRsmveavradrrsrqgsdrvasftestsstnqprqev 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 201 ----KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKGKLPIKWM 275
Cdd:cd05102   162 ddlwQSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGSARLPLKWM 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 276 APESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPR 354
Cdd:cd05102   242 APESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPGVQiNEEFCQRLKDGTRMRAPEYATPEIYRIMLSCWHGDPKERPT 321
                         330
                  ....*....|....
gi 1914781966 355 FTELKAQLSTILEE 368
Cdd:cd05102   322 FSDLVEILGDLLQE 335
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
112-366 1.81e-52

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: 183.59  E-value: 1.81e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYmSPE--NPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE---NPVWIIME 186
Cdd:cd05079    10 RDLGEGHFGKVELCRY-DPEgdNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEdggNGIKLIME 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd05079    89 FLPSGSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTV 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHG-------------VKPFQG-VKNNDVIGRIENGERLPMP 330
Cdd:cd05079   169 KDDLdsPVFWYAPECLIQSKFYIASDVWSFGVTLYELLTYCdsesspmtlflkmIGPTHGqMTVTRLVRVLEEGKRLPRP 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 331 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05079   249 PNCPEEVYQLMRKCWEFQPSKRTTFQNLIEGFEAIL 284
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
102-364 2.25e-52

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: 183.64  E-value: 2.25e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVH--------QGIYMSP----ENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHI 169
Cdd:cd05097     1 EFPRQQLRLKEKLGEGQFGEVHlceaeglaEFLGEGApefdGQPVL-VAVKMLRADVTKTARNDFLKEIKIMSRLKNPNI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 170 VKLIGV-ITENPVWIIMELCTLGELRSFLQVRKY-----------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARN 237
Cdd:cd05097    80 IRLLGVcVSDDPLCMITEYMENGDLNQFLSQREIestfthannipSVSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 238 VLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL-MHGVKPFQGVKNN 315
Cdd:cd05097   160 CLVGNHYTIKIADFGMSRNLYSGDYYRiQGRAVLPIRWMAWESILLGKFTTASDVWAFGVTLWEMFtLCKEQPYSLLSDE 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 316 DVigrIEN-GE---------RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 364
Cdd:cd05097   240 QV---IENtGEffrnqgrqiYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
101-365 3.46e-52

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: 184.44  E-value: 3.46e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQ----GIYMSPEnpALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHP-HIVKLIGV 175
Cdd:cd14207     2 WEFARERLKLGKSLGRGAFGKVVQasafGIKKSPT--CRVVAVKMLKEGATASEYKALMTELKILIHIGHHlNVVNLLGA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 ITEN--PVWIIMELCTLGELRSFLQVR----------------------------------------------------- 200
Cdd:cd14207    80 CTKSggPLMVIVEYCKYGNLSNYLKSKrdffvtnkdtslqeelikekkeaeptggkkkrlesvtssesfassgfqedksl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 201 --------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA 265
Cdd:cd14207   160 sdveeeeedsgdfyKRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIyKNPDYVRK 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:cd14207   240 GDARLPLKWMAPESIFDKIYSTKSDVWSYGVLLWEIFSLGASPYPGVQiDEDFCSKLKEGIRMRAPEFATSEIYQIMLDC 319
                         330       340
                  ....*....|....*....|.
gi 1914781966 345 WAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14207   320 WQGDPNERPRFSELVERLGDL 340
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
103-362 4.70e-51

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: 179.82  E-value: 4.70e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVH--QGIYMSPENPALAVAIKTCKNCTSdSVREKFLQEALTMRQFDHPHIVKLIGVITE-N 179
Cdd:cd05094     2 IKRRDIVLKRELGEGAFGKVFlaECYNLSPTKDKMLVAVKTLKDPTL-AARKDFQREAELLTNLQHDHIVKFYGVCGDgD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVR---------------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND 244
Cdd:cd05094    81 PLIMVFEYMKHGDLNKFLRAHgpdamilvdgqprqaKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 245 CVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIEN 323
Cdd:cd05094   161 LVKIGDFGMSRDVYSTDYYRvGGHTMLPIRWMPPESIMYRKFTTESDVWSFGVILWEIFTYGKQPWFQLSNTEVIECITQ 240
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1914781966 324 GERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05094   241 GRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKIL 279
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
102-363 7.48e-51

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: 179.75  E-value: 7.48e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIYMSPEN-------------PALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPH 168
Cdd:cd05096     1 KFPRGHLLFKEKLGEGQFGEVHLCEVVNPQDlptlqfpfnvrkgRPLLVAVKILRPDANKNARNDFLKEVKILSRLKDPN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 169 IVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKY------------------SLDLASLILYAYQLSTALAYLESKRFV 229
Cdd:cd05096    81 IIRLLGVcVDEDPLCMITEYMENGDLNQFLSSHHLddkeengndavppahclpAISYSSLLHVALQIASGMKYLSSLNFV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS-KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMH-GVK 307
Cdd:cd05096   161 HRDLATRNCLVGENLTIKIADFGMSRNLYAGDYYRIQgRAVLPIRWMAWECILMGKFTTASDVWAFGVTLWEILMLcKEQ 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 308 PFQGVKNNDVI---GRI--ENGER--LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLS 363
Cdd:cd05096   241 PYGELTDEQVIenaGEFfrDQGRQvyLFRPPPCPQGLYELMLQCWSRDCRERPSFSDIHAFLT 303
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
102-362 3.41e-50

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: 177.88  E-value: 3.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVH----QGIY----------MSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHP 167
Cdd:cd05095     1 EFPRKLLTFKEKLGEGQFGEVHlceaEGMEkfmdkdfaleVSENQPVL-VAVKMLRADANKNARNDFLKEIKIMSRLKDP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKYSLDLAS-----------LILYAYQLSTALAYLESKRFVHRDIAA 235
Cdd:cd05095    80 NIIRLLAVcITDDPLCMITEYMENGDLNQFLSRQQPEGQLALpsnaltvsysdLRFMAAQIASGMKYLSSLNFVHRDLAT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 236 RNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL-MHGVKPFQGVK 313
Cdd:cd05095   160 RNCLVGKNYTIKIADFGMSRNLYSGDYYRiQGRAVLPIRWMSWESILLGKFTTASDVWAFGVTLWETLtFCREQPYSQLS 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 314 NNDVigrIEN-GE---------RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05095   240 DEQV---IENtGEffrdqgrqtYLPQPALCPDSVYKLMLSCWRRDTKDRPSFQEIHTLL 295
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
114-362 3.41e-50

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: 177.39  E-value: 3.41e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmSP--ENPALAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELC 188
Cdd:cd05081    12 LGKGNFGSVELCRY-DPlgDNTGALVAVKQLQHSGPDQQRD-FQREIQILKALHSDFIVKYRGVSygpGRRSLRLVMEYL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKA-S 266
Cdd:cd05081    90 PSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpLDKDYYVVrE 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEI----------------LMHGVKPFQGVKNndVIGRIENGERLPMP 330
Cdd:cd05081   170 PGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELftycdkscspsaeflrMMGCERDVPALCR--LLELLEEGQRLPAP 247
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1914781966 331 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd05081   248 PACPAEVHELMKLCWAPSPQDRPSFSALGPQL 279
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
101-367 4.18e-50

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: 179.02  E-value: 4.18e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAL--AVAIKTCKNCTSDSVREKFLQEALTMRQFDHP-HIVKLIGVIT 177
Cdd:cd05103     2 WEFPRDRLKLGKPLGRGAFGQVIEADAFGIDKTATcrTVAVKMLKEGATHSEHRALMSELKILIHIGHHlNVVNLLGACT 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 E--NPVWIIMELCTLGELRSFLQVR------------------------------------------------------- 200
Cdd:cd05103    82 KpgGPLMVIVEFCKFGNLSAYLRSKrsefvpyktkgarfrqgkdyvgdisvdlkrrldsitssqssassgfveekslsdv 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 201 -----------KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDSTYYKASKG 268
Cdd:cd05103   162 eeeeagqedlyKDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIyKDPDYVRKGDA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAY 347
Cdd:cd05103   242 RLPLKWMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKiDEEFCRRLKEGTRMRAPDYTTPEMYQTMLDCWHG 321
                         330       340
                  ....*....|....*....|
gi 1914781966 348 DPSRRPRFTELKAQLSTILE 367
Cdd:cd05103   322 EPSQRPTFSELVEHLGNLLQ 341
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
114-367 3.22e-49

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: 174.07  E-value: 3.22e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIyMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVITENP-VWIIMELCTLG 191
Cdd:cd05047     3 IGEGNFGQVLKAR-IKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLCKLgHHPNIINLLGACEHRGyLYLAIEYAPHG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKY---------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd05047    82 NLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEdsTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPT 336
Cdd:cd05047   162 QE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRLEKPLNCDDE 239
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 337 LYSLMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd05047   240 VYDLMRQCWREKPYERPSFAQILVSLNRMLE 270
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
106-371 5.53e-49

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: 174.42  E-value: 5.53e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIyMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGViTENP--VW 182
Cdd:cd05089     2 EDIKFEDVIGEGNFGQVIKAM-IKKDGLKMNAAIKMLKEFASENDHRDFAGELEVLCKLgHHPNIINLLGA-CENRgyLY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRKY---------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 247
Cdd:cd05089    80 IAIEYAPYGNLLDFLRKSRVletdpafakehgtasTLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 248 LGDFGLSRYMEdsTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERL 327
Cdd:cd05089   160 IADFGLSRGEE--VYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVSLGGTPYCGMTCAELYEKLPQGYRM 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1914781966 328 PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEKA 371
Cdd:cd05089   238 EKPRNCDDEVYELMRQCWRDRPYERPPFSQISVQLSRMLEARKA 281
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
107-358 7.64e-49

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 172.71  E-value: 7.64e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGiyMSPENPALaVAIKT--CKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGV-ITENPVWI 183
Cdd:cd06606     1 RWKKGELLGKGSFGSVYLA--LNLDTGEL-MAVKEveLSGDSEEELEA-LEREIRILSSLKHPNIVRYLGTeRTENTLNI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLqvRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd06606    77 FLEYVPGGSLASLL--KKFgKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASK---GKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN-DVIGRIENGERLP-MPPNCPPTL 337
Cdd:cd06606   155 GEGTKslrGTPY--WMAPEVIRGEGYGRAADIWSLGCTVIEMAT-GKPPWSELGNPvAALFKIGSSGEPPpIPEHLSEEA 231
                         250       260
                  ....*....|....*....|.
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06606   232 KDFLRKCLQRDPKKRPTADEL 252
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
70-369 1.04e-47

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: 173.11  E-value: 1.04e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  70 MRTHAVSVSETDDYAEIideeDTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTS 147
Cdd:cd05106     6 IRWKIIEAAEGNNYTFI----DPTQLPYNEKWEFPRDNLQFGKTLGAGAFGKVVEATAfgLGKEDNVLRVAVKMLKASAH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 148 DSVREKFLQEALTMRQF-DHPHIVKLIGVITEN-PVWIIMELCTLGELRSFLQ--------------------------- 198
Cdd:cd05106    82 TDEREALMSELKILSHLgQHKNIVNLLGACTHGgPVLVITEYCCYGDLLNFLRkkaetflnfvmalpeisetssdyknit 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 199 -----VRKYS-------------------------------------LDLASLILYAYQLSTALAYLESKRFVHRDIAAR 236
Cdd:cd05106   162 lekkyIRSDSgfssqgsdtyvemrpvsssssqssdskdeedtedswpLDLDDLLRFSSQVAQGMDFLASKNCIHRDVAAR 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 237 NVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-N 314
Cdd:cd05106   242 NVLLTDGRVAKICDFGLARdIMNDSNYVVKGNARLPVKWMAPESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGILvN 321
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 315 NDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTelkaQLSTILEEE 369
Cdd:cd05106   322 SKFYKMVKRGYQMSRPDFAPPEIYSIMKMCWNLEPTERPTFS----QISQLIQRQ 372
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
107-364 9.38e-47

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 166.99  E-value: 9.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWI 183
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRP---VAIKVLRpeLAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDgRPYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 263
Cdd:cd14014    78 VMEYVEGGSLADLLR-ERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPMP---PNCPPTLYSL 340
Cdd:cd14014   157 QTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYE-LLTGRPPFDGDSPAAVLAKHLQEAPPPPSplnPDVPPALDAI 235
                         250       260
                  ....*....|....*....|....*
gi 1914781966 341 MTKCWAYDPSRRPR-FTELKAQLST 364
Cdd:cd14014   236 ILRALAKDPEERPQsAAELLAALRA 260
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
91-366 2.89e-46

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: 169.82  E-value: 2.89e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  91 DTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFD-HP 167
Cdd:cd05105    22 DPMQLPYDSRWEFPRDGLVLGRILGSGAFGKVVEGTAygLSRSQPVMKVAVKMLKPTARSSEKQALMSELKIMTHLGpHL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGVITEN-PVWIIMELCTLGELRSFL------------------------------------------------- 197
Cdd:cd05105   102 NIVNLLGACTKSgPIYIITEYCFYGDLVNYLhknrdnflsrhpekpkkdldifginpadestrsyvilsfenkgdymdmk 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 198 --------------QVRKYS--------------------------------LDLASLILYAYQLSTALAYLESKRFVHR 231
Cdd:cd05105   182 qadttqyvpmleikEASKYSdiqrsnydrpasykgsndsevknllsddgsegLTTLDLLSFTYQVARGMEFLASKNCVHR 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 232 DIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQ 310
Cdd:cd05105   262 DLAARNVLLAQGKIVKICDFGLARdIMHDSNYVSKGSTFLPVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYP 341
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 311 G-VKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05105   342 GmIVDSTFYNKIKSGYRMAKPDHATQEVYDIMVKCWNSEPEKRPSFLHLSDIVESLL 398
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
114-367 1.20e-43

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: 157.98  E-value: 1.20e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKnctSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTLGE 192
Cdd:cd14058     1 VGRGSFGVVCKARWRNQI-----VAVKIIE---SESEKKAFEVEVRQLSRVDHPNIIKLYGaCSNQKPVCLVMEYAEGGS 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFL--QVRKYSLDLASLILYAYQLSTALAYLES---KRFVHRDIAARNVLVSSNDCV-KLGDFGLSRYMedSTYYKAS 266
Cdd:cd14058    73 LYNVLhgKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTACDI--STHMTNN 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEIlMHGVKPFQGVKNND--VIGRIENGERLPMPPNCPPTLYSLMTKC 344
Cdd:cd14058   151 KGSAA--WMAPEVFEGSKYSEKCDVFSWGIILWEV-ITRRKPFDHIGGPAfrIMWAVHNGERPPLIKNCPKPIESLMTRC 227
                         250       260
                  ....*....|....*....|...
gi 1914781966 345 WAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14058   228 WSKDPEKRPSMKEIVKIMSHLMQ 250
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
109-360 2.34e-43

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: 157.29  E-value: 2.34e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYmspENPALAVAIKT-CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 186
Cdd:cd14003     3 ELGKTLGEGSFGKVKLARH---KLTGEKVAIKIiDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIeTENKIYLVME 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKY-SLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 265
Cdd:cd14003    80 YASGGELFDYIVNNGRlSEDEARRFFQ--QLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKLPikWMAPESINFRRF-TSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMTKC 344
Cdd:cd14003   158 FCGTPA--YAAPEVLLGRKYdGPKADVWSLGVILY-AMLTGYLPFDDDNDSKLFRKILKGK-YPIPSHLSPDARDLIRRM 233
                         250
                  ....*....|....*.
gi 1914781966 345 WAYDPSRRPRFTELKA 360
Cdd:cd14003   234 LVVDPSKRITIEEILN 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
102-412 1.43e-42

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 161.33  E-value: 1.43e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 179
Cdd:COG0515     3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRP---VALKVLRPelAADPEARERFRREARALARLNHPNIVRVYDVGEED 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PV-WIIMELCTlGE-LRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 257
Cdd:COG0515    80 GRpYLVMEYVE-GEsLADLLR-RRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARAL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKAS--KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPMP---PN 332
Cdd:COG0515   158 GGATLTQTGtvVGTPG--YMAPEQARGEPVDPRSDVYSLGVTLYE-LLTGRPPFDGDSPAELLRAHLREPPPPPSelrPD 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAQQEERMRMESRRQATVSWDSGGSDEAPPKPSRPGYPSPRS 411
Cdd:COG0515   235 LPPALDAIVLRALAKDPEERYQsAAELAAALRAVLRSLAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 314

                  .
gi 1914781966 412 S 412
Cdd:COG0515   315 A 315
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
103-370 4.35e-42

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: 155.16  E-value: 4.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 103 IQRERIELGRCIGEGQFGDVHQGiYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTM-RQFDHPHIVKLIGVITENP- 180
Cdd:cd05088     4 LEWNDIKFQDVIGEGNFGQVLKA-RIKKDGLRMDAAIKRMKEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGy 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKY---------------SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC 245
Cdd:cd05088    83 LYLAIEYAPHGNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 246 VKLGDFGLSRYMEdsTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd05088   163 AKIADFGLSRGQE--VYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYCGMTCAELYEKLPQGY 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 326 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEEK 370
Cdd:cd05088   241 RLEKPLNCDDEVYDLMRQCWREKPYERPSFAQILVSLNRMLEERK 285
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
114-365 5.60e-41

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: 150.62  E-value: 5.60e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKTCK--NCTSDSV-REKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCT 189
Cdd:cd14061     2 IGVGGFGKVYRGIWRGEE-----VAVKAARqdPDEDISVtLENVRQEARLFWMLRHPNIIALRGVCLQPPnLCLVMEYAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS--------SNDCVKLGDFGLSRYME 258
Cdd:cd14061    77 GGALNRVLA--GRKIPPHVLVDWAIQIARGMNYLHNEAPVpiiHRDLKSSNILILeaienedlENKTLKITDFGLAREWH 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE-NGERLPMPPNCPPTL 337
Cdd:cd14061   155 KTTRMSAAG---TYAWMAPEVIKSSTFSKASDVWSYGVLLWELLT-GEVPYKGIDGLAVAYGVAvNKLTLPIPSTCPEPF 230
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14061   231 AQLMKDCWQPDPHDRPSFADILKQLENI 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
109-359 6.71e-41

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: 150.43  E-value: 6.71e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMEL 187
Cdd:cd05122     3 EILEKIGKGGFGVVYKARH---KKTGQIVAIKKINLESKEK-KESILNEIAILKKCKHPNIVKYYGsYLKKDELWIVMEF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd05122    79 CSGGSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRNTFV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQG---------VKNNDVIGriengerLPMPPNCPPTLY 338
Cdd:cd05122   159 GTPY--WMAPEVIQGKPYGFKADIWSLGITAIE-MAEGKPPYSElppmkalflIATNGPPG-------LRNPKKWSKEFK 228
                         250       260
                  ....*....|....*....|.
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELK 359
Cdd:cd05122   229 DFLKKCLQKDPEKRPTAEQLL 249
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
102-365 1.31e-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: 150.19  E-value: 1.31e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDSVR---EKFLQEALTMRQFDHPHIVKLIGVITE 178
Cdd:cd14145     2 EIDFSELVLEEIIGIGGFGKVYRAIWIGDE-----VAVKAARHDPDEDISqtiENVRQEAKLFAMLKHPNIIALRGVCLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NP-VWIIMELCTLGELRSFLQVRKYSLDLasLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS--------SNDCV 246
Cdd:cd14145    77 EPnLCLVMEFARGGPLNRVLSGKRIPPDI--LVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILILekvengdlSNKIL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 247 KLGDFGLSRYMEDSTYYKASKGklpIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGE 325
Cdd:cd14145   155 KITDFGLAREWHRTTKMSAAGT---YAWMAPEVIRSSMFSKGSDVWSYGVLLWELLT-GEVPFRGIDGLAVAyGVAMNKL 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1914781966 326 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14145   231 SLPIPSTCPEPFARLMEDCWNPDPHSRPPFTNILDQLTAI 270
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
110-358 1.54e-40

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 149.30  E-value: 1.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMspeNPALAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:cd06627     4 LGDLIGRGAFGSVYKGLNL---NTGEFVAIKQISlEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVkTKDSLYIILEY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLqvRKYSLDLASLI-LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd06627    81 VENGSLASII--KKFGKFPESLVaVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVATKLNEVEKDENS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWA 346
Cdd:cd06627   159 VVGTP-YWMAPEVIEMSGVTTASDIWSVGCTVIELLT-GNPPYYDLQPMAALFRIVQDDHPPLPENISPELRDFLLQCFQ 236
                         250
                  ....*....|..
gi 1914781966 347 YDPSRRPRFTEL 358
Cdd:cd06627   237 KDPTLRPSAKEL 248
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
91-358 2.64e-40

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: 152.37  E-value: 2.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  91 DTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHP 167
Cdd:cd05104    20 DPTQLPYDHKWEFPRDRLRFGKTLGAGAFGKVVEATAygLAKADSAMTVAVKMLKPSAHSTEREALMSELKVLSYLgNHI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGVIT-ENPVWIIMELCTLGELRSFLQVRKYS------------------------------------------- 203
Cdd:cd05104   100 NIVNLLGACTvGGPTLVITEYCCYGDLLNFLRRKRDSficpkfedlaeaalyrnllhqremacdslneymdmkpsvsyvv 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 204 -------------------------------LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd05104   180 ptkadkrrgvrsgsyvdqdvtseileedelaLDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFG 259
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYME-DSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVK-NNDVIGRIENGERLPMP 330
Cdd:cd05104   260 LARDIRnDSNYVVKGNARLPVKWMAPESIFECVYTFESDVWSYGILLWEIFSLGSSPYPGMPvDSKFYKMIKEGYRMDSP 339
                         330       340
                  ....*....|....*....|....*...
gi 1914781966 331 PNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd05104   340 EFAPSEMYDIMRSCWDADPLKRPTFKQI 367
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
114-362 8.89e-40

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: 8.89e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKtcknctsdSVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELCTLGE 192
Cdd:cd14059     1 LGSGAQGAVFLGKFRGEE-----VAVK--------KVRDEKETDIKHLRKLNHPNIIKFKGVCTQAPCYcILMEYCPYGQ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFL-QVRKYSLDLasLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlp 271
Cdd:cd14059    68 LYEVLrAGREITPSL--LVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGT-- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 272 IKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGERLPMPPNCPPTLYSLMTKCWAYDPS 350
Cdd:cd14059   144 VAWMAPEVIRNEPCSEKVDIWSFGVVLWELLT-GEIPYKDVDSSAIIwGVGSNSLQLPVPSTCPDGFKLLMKQCWNSKPR 222
                         250
                  ....*....|..
gi 1914781966 351 RRPRFTELKAQL 362
Cdd:cd14059   223 NRPSFRQILMHL 234
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
91-366 1.12e-39

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: 151.32  E-value: 1.12e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  91 DTYTMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIY--MSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFD-HP 167
Cdd:cd05107    22 DPMQLPYDSAWEMPRDNLVLGRTLGSGAFGRVVEATAhgLSHSQSTMKVAVKMLKSTARSSEKQALMSELKIMSHLGpHL 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 168 HIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRKYS----------------------------------------LDL 206
Cdd:cd05107   102 NIVNLLGACTKGgPIYIITEYCRYGDLVDYLHRNKHTflqyyldknrddgslisggstplsqrkshvslgsesdggyMDM 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 207 AS---------------------------------------------------------LILYAYQLSTALAYLESKRFV 229
Cdd:cd05107   182 SKdesadyvpmqdmkgtvkyadiessnyespydqylpsapertrrdtlinespalsymdLVGFSYQVANGMEFLASKNCV 261
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKP 308
Cdd:cd05107   262 HRDLAARNVLICEGKLVKICDFGLARdIMRDSNYISKGSTFLPLKWMAPESIFNNLYTTLSDVWSFGILLWEIFTLGGTP 341
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 309 FQGVKNNDVI-GRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd05107   342 YPELPMNEQFyNAIKRGYRMAKPAHASDEIYEIMQKCWEEKFEIRPDFSQLVHLVGDLL 400
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
109-360 5.24e-38

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: 142.23  E-value: 5.24e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHqgiymspenpaLA--------VAIKT------CKNCTSDSVRekflQEALTMRQFDHPHIVKLIG 174
Cdd:cd14007     3 EIGKPLGKGKFGNVY-----------LArekksgfiVALKVisksqlQKSGLEHQLR----REIEIQSHLRHPNILRLYG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 175 V-ITENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd14007    68 YfEDKKRIYLILEYAPNGELYKELKkQKRFDEKEAAK--YIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYMEDS-------TY-YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENG 324
Cdd:cd14007   146 WSVHAPSNrrktfcgTLdY-----------LPPEMVEGKEYDYKVDIWSLGVLCYELL-VGKPPFESKSHQETYKRIQNV 213
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 325 ErLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKA 360
Cdd:cd14007   214 D-IKFPSSVSPEAKDLISKLLQKDPSKRLSLEQVLN 248
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
100-353 2.12e-37

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: 140.68  E-value: 2.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHqgiymspenpaLAVAIKTCKNCT---------SDSVREKFLQEALTMRQFDHPHIV 170
Cdd:cd08215     1 KYEKIRV-------IGKGSFGSAY-----------LVRRKSDGKLYVlkeidlsnmSEKEREEALNEVKLLSKLKHPNIV 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 171 KLIGVITENPV-WIIMELCTLGELRSFLQVRKYSLDL--ASLILYAY-QLSTALAYLESKRFVHRDIAARNVLVSSNDCV 246
Cdd:cd08215    63 KYYESFEENGKlCIVMEYADGGDLAQKIKKQKKKGQPfpEEQILDWFvQICLALKYLHSRKILHRDLKTQNIFLTKDGVV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 247 KLGDFGLSRYMEDST----------YYkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMHgVKPFQGVKNND 316
Cdd:cd08215   143 KLGDFGISKVLESTTdlaktvvgtpYY-----------LSPELCENKPYNYKSDIWALGCVLYELCTL-KHPFEANNLPA 210
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1914781966 317 VIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd08215   211 LVYKIVKGQYPPIPSQYSSELRDLVNSMLQKDPEKRP 247
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
115-365 1.02e-36

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: 138.17  E-value: 1.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 115 GEGQFGDVHQGIYMSPENpalAVAIKtcknctsdsvreKFLQ---EALTMRQFDHPHIVKLIGVITENPVW-IIMELCTL 190
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDK---EVAVK------------KLLKiekEAEILSVLSHRNIIQFYGAILEAPNYgIVTEYASY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESK---RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd14060    67 GSLFDYLNSnESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 kGKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMHGVkPFQGVKNNDVIGRI-ENGERLPMPPNCPPTLYSLMTKCW 345
Cdd:cd14060   147 -GTFP--WMAPEVIQSLPVSETCDTYSYGVVLWEMLTREV-PFKGLEGLQVAWLVvEKNERPTIPSSCPRSFAELMRRCW 222
                         250       260
                  ....*....|....*....|
gi 1914781966 346 AYDPSRRPRFTELKAQLSTI 365
Cdd:cd14060   223 EADVKERPSFKQIIGILESM 242
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
106-365 1.46e-36

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: 138.62  E-value: 1.46e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPenpalAVAIKTCK-------NCTSDSVRekflQEALTMRQFDHPHIVKLIGVITE 178
Cdd:cd14147     3 QELRLEEVIGIGGFGKVYRGSWRGE-----LVAVKAARqdpdediSVTAESVR----QEARLFAMLAHPNIIALKAVCLE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NP-VWIIMELCTLGELRSFLQVRKYSLDLasLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS---SNDC-----V 246
Cdd:cd14147    74 EPnLCLVMEYAAGGPLSRALAGRRVPPHV--LVNWAVQIARGMHYLHCEALVpviHRDLKSNNILLLqpiENDDmehktL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 247 KLGDFGLSRYMEDSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGE 325
Cdd:cd14147   152 KITDFGLAREWHKTTQMSAAG---TYAWMAPEVIKASTFSKGSDVWSFGVLLWELLT-GEVPYRGIDCLAVAyGVAVNKL 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1914781966 326 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14147   228 TLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEAL 267
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
114-363 2.24e-36

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: 138.16  E-value: 2.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVaIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 192
Cdd:cd14206     5 IGNGWFGKVILGEIFSDYTPAQVV-VKELRVSAGPLEQRKFISEAQPYRSLQHPNILQCLGLCTETiPFLLIMEFCQLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRK---------YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR--YMEDsT 261
Cdd:cd14206    84 LKRYLRAQRkadgmtpdlPTRDLRTLQRMAYEITLGLLHLHKNNYIHSDLALRNCLLTSDLTVRIGDYGLSHnnYKED-Y 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKLPIKWMAPESINFRRF-------TSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI--ENGERLPMPPN 332
Cdd:cd14206   163 YLTPDRLWIPLRWVAPELLDELHGnlivvdqSKESNVWSLGVTIWELFEFGAQPYRHLSDEEVLTFVvrEQQMKLAKPRL 242
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1914781966 333 CPP---TLYSLMTKCWaYDPSRRPRFTELKAQLS 363
Cdd:cd14206   243 KLPyadYWYEIMQSCW-LPPSQRPSVEELHLQLS 275
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
108-355 3.44e-36

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: 137.23  E-value: 3.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSD--SVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM 185
Cdd:cd05037     1 ITFHEHLGQGTFTNIYDGILREVGDGRVQEVEVLLKVLDSDhrDISESFFETASLMSQISHKHLVKLYGVCVADENIMVQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC------VKLGDFGLSRymed 259
Cdd:cd05037    81 EYVRYGPLDKYLRRMGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGVPI---- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 sTYYKASKGKLPIKWMAPESI-NFRRFTS-ASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMpPNCPPtL 337
Cdd:cd05037   157 -TVLSREERVDRIPWIAPECLrNLQANLTiAADKWSFGTTLWEICSGGEEPLSALSSQEKLQFYEDQHQLPA-PDCAE-L 233
                         250
                  ....*....|....*...
gi 1914781966 338 YSLMTKCWAYDPSRRPRF 355
Cdd:cd05037   234 AELIMQCWTYEPTKRPSF 251
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
114-365 3.65e-36

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: 137.04  E-value: 3.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKTCK-------NCTSDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIM 185
Cdd:cd14148     2 IGVGGFGKVYKGLWRGEE-----VAVKAARqdpdediAVTAENVR----QEARLFWMLQHPNIIALRGVCLNPPhLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLasLILYAYQLSTALAYLESKRFV---HRDIAARNVLVS--------SNDCVKLGDFGLS 254
Cdd:cd14148    73 EYARGGALNRALAGKKVPPHV--LVNWAVQIARGMNYLHNEAIVpiiHRDLKSSNILILepienddlSGKTLKITDFGLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYMEDSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDV-IGRIENGERLPMPPNC 333
Cdd:cd14148   151 REWHKTTKMSAAG---TYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLT-GEVPYREIDALAVaYGVAMNKLTLPIPSTC 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14148   227 PEPFARLLEECWDPDPHGRPDFGSILKRLEDI 258
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
109-353 3.90e-36

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: 136.84  E-value: 3.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIymSPENPALaVAIKT---CKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd05117     3 ELGKVLGRGSFGVVRLAV--HKKTGEE-YAVKIidkKKLKSED--EEMLRREIEILKRLDHPNIVKLYEVFeDDKNLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELrsF---LQVRKYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRYME 258
Cdd:cd05117    78 MELCTGGEL--FdriVKKGSFSEREAAKIM--KQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIFE 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLY 338
Cdd:cd05117   154 EGEKLKTVCGTP--YYVAPEVLKGKGYGKKCDIWSLGVILY-ILLCGYPPFYGETEQELFEKILKGK-YSFDSPEWKNVS 229
                         250
                  ....*....|....*....
gi 1914781966 339 S----LMTKCWAYDPSRRP 353
Cdd:cd05117   230 EeakdLIKRLLVVDPKKRL 248
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
114-365 7.32e-36

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: 136.71  E-value: 7.32e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKN-------CTSDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIM 185
Cdd:cd14146     2 IGVGGFGKVYRATWKGQE-----VAVKAARQdpdedikATAESVR----QEAKLFSMLRHPNIIKLEGVCLEEPnLCLVM 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLAS--------LILYAYQLSTALAYLESKRFV---HRDIAARNVLVSS--------NDCV 246
Cdd:cd14146    73 EFARGGTLNRALAAANAAPGPRRarripphiLVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLLEkiehddicNKTL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 247 KLGDFGLSRYMEDSTYYKASKgklPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI-GRIENGE 325
Cdd:cd14146   153 KITDFGLAREWHRTTKMSAAG---TYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLT-GEVPYRGIDGLAVAyGVAVNKL 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1914781966 326 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14146   229 TLPIPSTCPEPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
114-359 1.52e-35

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: 135.37  E-value: 1.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCK-------------NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI---T 177
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQL---YAIKIFNksrlrkrregkndRGKIKNALDDVRREIAIMKKLDHPNIVRLYEVIddpE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGEL---RSFLQVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd14008    78 SDKLYLVLEYCEGGPVmelDSGDRVPPLPEETARK--YFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYMEDST-YYKASKGKlPIkWMAPESINFRRFT---SASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLPM 329
Cdd:cd14008   156 EMFEDGNdTLQKTAGT-PA-FLAPELCDGDSKTysgKAADIWALGVTLY-CLVFGRLPFNGDNILELYEAIQNQNdEFPI 232
                         250       260       270
                  ....*....|....*....|....*....|
gi 1914781966 330 PPNCPPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14008   233 PPELSPELKDLLRRMLEKDPEKRITLKEIK 262
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
114-362 4.22e-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: 131.42  E-value: 4.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSV-REKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLG 191
Cdd:cd13978     1 LGSGGFGTVSKARHVSWF---GMVAIKCLHSSPNCIEeRKALLKEAEKMERARHSYVLPLLGVCVERrSLGLVMEYMENG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLE--SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd13978    78 SLKSLLEREIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRRRGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LP----IKWMAPESIN--FRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLPMPPNC-------PP 335
Cdd:cd13978   158 ENlggtPIYMAPEAFDdfNKKPTSKSDVYSFAIVIWAVLT-RKEPFENAINPLLIMQIvSKGDRPSLDDIGrlkqienVQ 236
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 336 TLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd13978   237 ELISLMIRCWDGNPDARPTFLECLDRL 263
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
114-358 2.58e-33

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: 128.49  E-value: 2.58e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKtcknCTSDSVREKFLQEAL-----TMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEV---VAIK----EISRKKLNKKLQENLeseiaILKSIKHPNIVRLYDVQkTEDFIYLVLEY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDSTYYK 264
Cdd:cd14009    74 CAGGDLSQYIRKRG-RLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKIADFGFARSLQPASMAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIE-NGERLPMP------PNCPPTL 337
Cdd:cd14009   153 TLCGS-PL-YMAPEILQFQKYDAKADLWSVGAILFEML-VGKPPFRGSNHVQLLRNIErSDAVIPFPiaaqlsPDCKDLL 229
                         250       260
                  ....*....|....*....|.
gi 1914781966 338 YSLMTKcwayDPSRRPRFTEL 358
Cdd:cd14009   230 RRLLRR----DPAERISFEEF 246
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
114-363 3.55e-33

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: 128.86  E-value: 3.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPAlAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLGE 192
Cdd:cd05042     3 IGNGWFGKVLLGEIYSGTSVA-QVVVKELKASANPKEQDTFLKEGQPYRILQHPNILQCLGQCVEAiPYLLVMEFCDLGD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSL----DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL--SRYMEDsTYYKAS 266
Cdd:cd05042    82 LKAYLRSEREHErgdsDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLahSRYKED-YIETDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESIN--FRRF-----TSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI--ENGERLPMPPNCPP-- 335
Cdd:cd05042   161 KLWFPLRWTAPELVTefHDRLlvvdqTKYSNIWSLGVTLWELFENGAQPYSNLSDLDVLAQVvrEQDTKLPKPQLELPys 240
                         250       260
                  ....*....|....*....|....*....
gi 1914781966 336 -TLYSLMTKCWaYDPSRRPRFTELKAQLS 363
Cdd:cd05042   241 dRWYEVLQFCW-LSPEQRPAAEDVHLLLT 268
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
114-363 1.44e-32

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: 127.03  E-value: 1.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPAlAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCTLGE 192
Cdd:cd05087     5 IGHGWFGKVFLGEVNSGLSST-QVVVKELKASASVQDQMQFLEEAQPYRALQHTNLLQCLAQCAEvTPYLLVMEFCPLGD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLA----SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS--RYMEDsTYYKAS 266
Cdd:cd05087    84 LKGYLRSCRAAESMApdplTLQRMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGLShcKYKED-YFVTAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESIN-------FRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMP-PNCPPTL- 337
Cdd:cd05087   163 QLWVPLRWIAPELVDevhgnllVVDQTKQSNVWSLGVTIWELFELGNQPYRHYSDRQVLTYTVREQQLKLPkPQLKLSLa 242
                         250       260
                  ....*....|....*....|....*....
gi 1914781966 338 ---YSLMTKCWaYDPSRRPRFTELKAQLS 363
Cdd:cd05087   243 erwYEVMQFCW-LQPEQRPTAEEVHLLLS 270
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
100-353 2.54e-32

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: 126.23  E-value: 2.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHQGIyMSPENpaLAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVI 176
Cdd:cd08224     1 NYEIEKK-------IGKGQFSVVYRAR-CLLDG--RLVALKKVQifEMMDAKARQDCLKEIDLLQQLNHPNIIKyLASFI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFL---QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd08224    71 ENNELNIVLELADAGDLSRLIkhfKKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEilMHGVK-PFQGVKNN--DVIGRIENGERLPMP 330
Cdd:cd08224   151 GRFFSSKTTAAHSLVGTPY-YMSPERIREQGYDFKSDIWSLGCLLYE--MAALQsPFYGEKMNlySLCKKIEKCEYPPLP 227
                         250       260
                  ....*....|....*....|....
gi 1914781966 331 PNCPPT-LYSLMTKCWAYDPSRRP 353
Cdd:cd08224   228 ADLYSQeLRDLVAACIQPDPEKRP 251
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
108-358 8.27e-32

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: 124.63  E-value: 8.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYmSPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIME 186
Cdd:cd06623     3 LERVKVLGQGSSGVVYKVRH-KPTG--KIYALKKIHVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAfYKEGEISIVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKY--SLDLASLilyAYQLSTALAYLESKR-FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 263
Cdd:cd06623    80 YMDGGSLADLLKKVGKipEPVLAYI---ARQILKGLDYLHTKRhIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLDQ 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KAS-KGKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE---NGERLPMPPN-CPPTLY 338
Cdd:cd06623   157 CNTfVGTVT--YMSPERIQGESYSYAADIWSLGLTLLECAL-GKFPFLPPGQPSFFELMQaicDGPPPSLPAEeFSPEFR 233
                         250       260
                  ....*....|....*....|
gi 1914781966 339 SLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06623   234 DFISACLQKDPKKRPSAAEL 253
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
111-358 4.05e-31

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: 122.51  E-value: 4.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIymSPENPALaVAIKTCKNCTSDSVREKFL----QEALTMRQFDHPHIVKLIGVIT-ENPVWIIM 185
Cdd:cd06632     5 GQLLGSGSFGSVYEGF--NGDTGDF-FAVKEVSLVDDDKKSRESVkqleQEIALLSKLRHPNIVQYYGTEReEDNLYIFL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQvrKYSLDLASLI-LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 264
Cdd:cd06632    82 EYVPGGSIHKLLQ--RYGAFEEPVIrLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKlPIkWMAPESINFR--RFTSASDVWMFGVCMWEilMHGVKP----FQGVKnndVIGRIENGERLP-MPPNCPPTL 337
Cdd:cd06632   160 SFKGS-PY-WMAPEVIMQKnsGYGLAVDIWSLGCTVLE--MATGKPpwsqYEGVA---AIFKIGNSGELPpIPDHLSPDA 232
                         250       260
                  ....*....|....*....|.
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06632   233 KDFIRLCLQRDPEDRPTASQL 253
Pkinase pfam00069
Protein kinase domain;
109-360 4.95e-31

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 121.20  E-value: 4.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITENP-VWIIME 186
Cdd:pfam00069   2 EVLRKLGSGSFGTVYKAKHRDTGKI---VAIKKIKKEKIKKKKDKnILREIKILKKLNHPNIVRLYDAFEDKDnLYLVLE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYleskrfvhrdiaarnvlvssndcvklgdfGLSRYMEDSTYYkas 266
Cdd:pfam00069  79 YVEGGSLFDLLSEKGA-FSEREAKFIMKQILEGLES-----------------------------GSSLTTFVGTPW--- 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 kgklpikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLPM--PPNCPPTLYSLMTKC 344
Cdd:pfam00069 126 -------YMAPEVLGGNPYGPKVDVWSLGCILYE-LLTGKPPFPGINGNEIYELIIDQPYAFPelPSNLSEEAKDLLKKL 197
                         250
                  ....*....|....*.
gi 1914781966 345 WAYDPSRRPRFTELKA 360
Cdd:pfam00069 198 LKKDPSKRLTATQALQ 213
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
106-358 5.54e-31

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: 122.74  E-value: 5.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWII 184
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQV---VAIKVIDLEEAEDEIEDIQQEIQFLSQCDSPYITKYYGSFLKGsKLWII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 264
Cdd:cd06609    78 MEYCGGGSVLDLLKPGPLDETYIAFILR--EVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQLTSTMSKR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIengerlpmPPNCPPTL----YS- 339
Cdd:cd06609   156 NTFVGTPF-WMAPEVIKQSGYDEKADIWSLGITAIELAK-GEPPLSDLHPMRVLFLI--------PKNNPPSLegnkFSk 225
                         250       260
                  ....*....|....*....|...
gi 1914781966 340 ----LMTKCWAYDPSRRPRFTEL 358
Cdd:cd06609   226 pfkdFVELCLNKDPKERPSAKEL 248
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
109-358 6.32e-31

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: 121.99  E-value: 6.32e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKflqEALTMRQFDHPHIVKLIG-VITENPVWIIMEL 187
Cdd:cd06612     6 DILEKLGEGSYGSVYKAIHKETGQV---VAIKVVPVEEDLQEIIK---EISILKQCDSPYIVKYYGsYFKNTDLWIVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd06612    80 CGAGSVSDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAKRNTV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgerlpMPPNC--PPTLYS-----L 340
Cdd:cd06612   160 IGTPF-WMAPEVIQEIGYNNKADIWSLGITAIE-MAEGKPPYSDIHPMRAIFMIPN-----KPPPTlsDPEKWSpefndF 232
                         250
                  ....*....|....*...
gi 1914781966 341 MTKCWAYDPSRRPRFTEL 358
Cdd:cd06612   233 VKKCLVKDPEERPSAIQL 250
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
114-362 2.28e-30

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: 120.29  E-value: 2.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiYMSPENPALAVaIKTCKNCTSDSvreKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 192
Cdd:cd14065     1 LGKGFFGEVYK--VTHRETGKVMV-MKELKRFDEQR---SFLKEVKLMRRLSHPNILRFIGVcVKDNKLNFITEYVNGGT 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV---SSNDCVKLGDFGLSRYMEDstyYKASKG- 268
Cdd:cd14065    75 LEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLAREMPD---EKTKKPd 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 -KLPIK------WMAPESINFRRFTSASDVWMFGVCMWEILmhGVKPfqgvKNNDVIGRIEN------GERLPMPPNCPP 335
Cdd:cd14065   152 rKKRLTvvgspyWMAPEMLRGESYDEKVDVFSFGIVLCEII--GRVP----ADPDYLPRTMDfgldvrAFRTLYVPDCPP 225
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 336 TLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd14065   226 SFLPLAIRCCQLDPEKRPSFVELEHHL 252
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
114-366 5.46e-30

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: 119.68  E-value: 5.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd14221     1 LGKGCFG---QAIKVTHRETGEVMVMKELIRFDEETQR-TFLKEVKVMRCLEHPNVLKFIGVLyKDKRLNFITEYIKGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd14221    77 LRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQPEGLRSLKK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 K-------------WMAPESINFRRFTSASDVWMFGVCMWEIlmhgvkpfqgvknndvIGRIE-NGERLPM--------- 329
Cdd:cd14221   157 PdrkkrytvvgnpyWMAPEMINGRSYDEKVDVFSFGIVLCEI----------------IGRVNaDPDYLPRtmdfglnvr 220
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1914781966 330 -------PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd14221   221 gfldrycPPNCPPSFFPIAVLCCDLDPEKRPSFSKLEHWLETLR 264
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
107-358 7.22e-30

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: 119.33  E-value: 7.22e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSpENPALAVA-IKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWII 184
Cdd:cd06626     1 RWQRGNKIGEGTFGKVYTAVNLD-TGELMAMKeIRFQDN--DPKTIKEIADEMKVLEGLDHPNLVRYYGVeVHREEVYIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyYK 264
Cdd:cd06626    78 MEYCQEGTLEELLRHGRI-LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNT-TT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKL------PIkWMAPESINFRRFTS---ASDVWMFGVCMWEiLMHGVKPFQGVKNN-DVIGRIENGERLPMPPN-- 332
Cdd:cd06626   156 MAPGEVnslvgtPA-YMAPEVITGNKGEGhgrAADIWSLGCVVLE-MATGKRPWSELDNEwAIMYHVGMGHKPPIPDSlq 233
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06626   234 LSPEGKDFLSRCLESDPKKRPTASEL 259
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
106-353 1.01e-29

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: 119.12  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIElgrCIGEGQFG------DVHQGIYmspenpalaVAIKTCKNCTSD------SVREkflqeALTMRQFDHPHIVKLI 173
Cdd:cd07829     2 EKLE---KLGEGTYGvvykakDKKTGEI---------VALKKIRLDNEEegipstALRE-----ISLLKELKHPNIVKLL 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 174 GVI-TENPVWIIMELCTLgELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd07829    65 DVIhTENKLYLVFEYCDQ-DLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFG 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYMEdstyykaskgkLPIKWMAPESINF-----------RRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGR 320
Cdd:cd07829   144 LARAFG-----------IPLRTYTHEVVTLwyrapeillgsKHYSTAVDIWSVGCIFAELITG--KPlFPGDSEIDQLFK 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 321 I-------------------ENGERLPMPPNCP---------PTLYSLMTKCWAYDPSRRP 353
Cdd:cd07829   211 IfqilgtpteeswpgvtklpDYKPTFPKWPKNDlekvlprldPEGIDLLSKMLQYNPAKRI 271
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
114-362 2.76e-29

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: 117.11  E-value: 2.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPenpalaVAIKTCkNCTS--DSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLG 191
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD------VAVKKL-NVTDptPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYmedSTYYKASKGKL- 270
Cdd:cd14062    74 SLYKHLHVLETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLATV---KTRWSGSQQFEq 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 ---PIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVI----GRienGERLP----MPPNCPPT 336
Cdd:cd14062   151 ptgSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYE-LLTGQLPYSHINNRDQIlfmvGR---GYLRPdlskVRSDTPKA 226
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 337 LYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd14062   227 LRRLMEDCIKFQRDERPLFPQILASL 252
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
106-353 6.18e-29

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: 116.33  E-value: 6.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT----ENPV 181
Cdd:cd13979     3 EPLRLQEPLGSGGFGSVYKATYKGET-----VAVKIVRRRRKNRASRQSFWAELNAARLRHENIVRVLAAETgtdfASLG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS- 260
Cdd:cd13979    78 LIIMEYCGNGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEGn 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 -TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPNCPPT--- 336
Cdd:cd13979   158 eVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLT-RELPYAGLRQHVLYAVVAKDLRPDLSGLEDSEfgq 236
                         250
                  ....*....|....*...
gi 1914781966 337 -LYSLMTKCWAYDPSRRP 353
Cdd:cd13979   237 rLRSLISRCWSAQPAERP 254
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
107-360 1.31e-28

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: 115.19  E-value: 1.31e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKnctsdsvREKFLQEAL---------TMRQFDHPHIVKLIGVI- 176
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGES---VAIKIID-------KEQVAREGMveqikreiaIMKLLRHPNIVELHEVMa 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd14663    71 TKTKIFFVMELVTGGELFSKI-AKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDstyyKASKGKL------PiKWMAPESINFRRFTSA-SDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGErLPM 329
Cdd:cd14663   150 SEQ----FRQDGLLhttcgtP-NYVAPEVLARRGYDGAkADIWSCGVILF-VLLAGYLPFDDENLMALYRKIMKGE-FEY 222
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 330 PPNCPPTLYSLMTKCWAYDPSRRPRFTELKA 360
Cdd:cd14663   223 PRWFSPGAKSLIKRILDPNPSTRITVEQIMA 253
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
106-358 2.15e-28

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: 114.66  E-value: 2.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGiymSPENPALAVAIK-TCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 183
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKG---RRKYTGQVVALKfIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFeTKKEFVV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELcTLGELRSFLQV-RKYSLDLASLIlyAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd14002    78 VTEY-AQGELFQILEDdGTLPEEEVRSI--AKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKAS-KGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFqgVKNN--DVIGRIENGE-RLP--MPPNCPPT 336
Cdd:cd14002   155 VLTSiKGT-PL-YMAPELVQEQPYDHTADLWSLGCILYE-LFVGQPPF--YTNSiyQLVQMIVKDPvKWPsnMSPEFKSF 229
                         250       260
                  ....*....|....*....|..
gi 1914781966 337 LYSLMTKcwayDPSRRPRFTEL 358
Cdd:cd14002   230 LQGLLNK----DPSKRLSWPDL 247
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
161-358 2.35e-28

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: 114.95  E-value: 2.35e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 161 MRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKY---SLDLASLILYAYQLSTALAY-----LESKRFV 229
Cdd:cd08217    53 LRELKHPNIVRYYDRIvdrANTTLYIVMEYCEGGDLAQLIKKCKKenqYIPEEFIWKIFTQLLLALYEchnrsVGGGKIL 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDST----------YYkaskgklpikwMAPESINFRRFTSASDVWMFGVCMW 299
Cdd:cd08217   133 HRDLKPANIFLDSDNNVKLGDFGLARVLSHDSsfaktyvgtpYY-----------MSPELLNEQSYDEKSDIWSLGCLIY 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 300 EILMHGvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd08217   202 ELCALH-PPFQAANQLELAKKIKEGKFPRIPSRYSSELNEVIKSMLNVDPDKRPSVEEL 259
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
137-365 2.79e-28

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: 114.79  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKtcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIM-ELCTLGELRSFLQVRKYSLDLASLILYAYQ 215
Cdd:cd13992    28 VAIK--HITFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVtEYCTRGSLQDVLLNREIKMDWMFKSSFIKD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 216 LSTALAYLESKRF-VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIK--WMAPESIN----FRRFTSA 288
Cdd:cd13992   106 IVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKKllWTAPELLRgsllEVRGTQK 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 289 SDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENGERLPMPPN-------CPPTLYSLMTKCWAYDPSRRPRFTELKAQ 361
Cdd:cd13992   186 GDVYSFAIILYEIL-FRSDPFALEREVAIVEKVISGGNKPFRPElavlldeFPPRLVLLVKQCWAENPEKRPSFKQIKKT 264

                  ....
gi 1914781966 362 LSTI 365
Cdd:cd13992   265 LTEN 268
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
110-367 2.81e-28

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: 114.59  E-value: 2.81e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSPENPALaVAIKTC-KNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVITENP-VWIIME 186
Cdd:cd14080     4 LGKTIGEGSYSKVKLAEYTKSGLKEK-VACKIIdKKKAPKDFLEKFLpRELEILRKLRHPNIIQVYSIFERGSkVFIFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd14080    83 YAEHGDLLEYIQKRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDGDVLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 K---GKLpiKWMAPESINFRRFTS-ASDVWMFGVCMWeILMHGVKPFqgvknNDvigriengerlpmpPNCPPTLYSLMT 342
Cdd:cd14080   162 KtfcGSA--AYAAPEILQGIPYDPkKYDIWSLGVILY-IMLCGSMPF-----DD--------------SNIKKMLKDQQN 219
                         250       260
                  ....*....|....*....|....*
gi 1914781966 343 KCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14080   220 RKVRFPSSVKKLSPECKDLIDQLLE 244
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
100-368 5.28e-28

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: 114.00  E-value: 5.28e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRERIELGRCIGEGQFGDVHQGIYMSPenpalaVAIKTCkNCTSDSVRE--KFLQEALTMRQFDHPHIVKLIGVIT 177
Cdd:cd14151     2 DWEIPDGQITVGQRIGSGSFGTVYKGKWHGD------VAVKML-NVTAPTPQQlqAFKNEVGVLRKTRHVNILLFMGYST 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL---- 253
Cdd:cd14151    75 KPQLAIVTQWCEGSSLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLatvk 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGklpIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNND-VIGRIENGERLP- 328
Cdd:cd14151   155 SRWSGSHQFEQLSGS---ILWMAPEVIRMQDknpYSFQSDVYAFGIVLYE-LMTGQLPYSNINNRDqIIFMVGRGYLSPd 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1914781966 329 ---MPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEE 368
Cdd:cd14151   231 lskVRSNCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
114-353 8.93e-28

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: 113.42  E-value: 8.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQG-IYMspENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLG 191
Cdd:cd05086     5 IGNGWFGKVLLGeIYT--GTSVARVVVKELKASANPKEQDDFLQQGEPYYILQHPNILQCVGQCVEAiPYLLVFEFCDLG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFL--QVRKYSLDLASLIL--YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL--SRYMEDstYYKA 265
Cdd:cd05086    83 DLKTYLanQQEKLRGDSQIMLLqrMACEIAAGLAHMHKHNFLHSDLALRNCYLTSDLTVKVGDYGIgfSRYKED--YIET 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKL-PIKWMAPESINFRR-------FTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI--ENGERLPMPPNCPP 335
Cdd:cd05086   161 DDKKYaPLRWTAPELVTSFQdgllaaeQTKYSNIWSLGVTLWELFENAAQPYSDLSDREVLNHVikERQVKLFKPHLEQP 240
                         250       260
                  ....*....|....*....|.
gi 1914781966 336 ---TLYSLMTKCWaYDPSRRP 353
Cdd:cd05086   241 ysdRWYEVLQFCW-LSPEKRP 260
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
100-358 1.45e-27

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 112.12  E-value: 1.45e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCkNCTSDSVREK--FLQEALTMRQFDHPHIVKLIGVIT 177
Cdd:cd08529     1 DFEILNK-------LGKGSFGVVYKVVRKVDGR---VYALKQI-DISRMSRKMReeAIDEARVLSKLNSPYVIKYYDSFV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 E-NPVWIIMELCTLGELRSFLQV-RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd08529    70 DkGKLNIVMEYAENGDLHSLIKSqRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPNCPP 335
Cdd:cd08529   150 ILSDTTNFAQTIVGTPY-YLSPELCEDKPYNEKSDVWALGCVLYELCT-GKHPFEAQNQGALILKIVRGKYPPISASYSQ 227
                         250       260
                  ....*....|....*....|...
gi 1914781966 336 TLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd08529   228 DLSQLIDSCLTKDYRQRPDTTEL 250
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
114-367 1.68e-27

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: 112.42  E-value: 1.68e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPenpaLAVAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGEL 193
Cdd:cd14150     8 IGTGSFGTVFRGKWHGD----VAVKILKVTEPTPEQL-QAFKNEMQVLRKTRHVNILLFMGFMTRPNFAIITQWCEGSSL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 194 RSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYmeDSTYYKASKGKLP-- 271
Cdd:cd14150    83 YRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATV--KTRWSGSQQVEQPsg 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 272 -IKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNND-VIGRIENGERLP----MPPNCPPTLYSLMT 342
Cdd:cd14150   161 sILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYE-LMSGTLPYSNINNRDqIIFMVGRGYLSPdlskLSSNCPKAMKRLLI 239
                         250       260
                  ....*....|....*....|....*
gi 1914781966 343 KCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14150   240 DCLKFKREERPLFPQILVSIELLQR 264
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
108-359 8.50e-27

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: 110.52  E-value: 8.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYMSpenpalAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 185
Cdd:cd14063     2 LEIKEVIGKGRFGRVHRGRWHG------DVAIKLLNiDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPhLAIVT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVkLGDFGLSRyMEDSTYYKA 265
Cdd:cd14063    76 SLCKGRTLYSLIHERKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENGRVV-ITDFGLFS-LSGLLQPGR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKL--PIKW---MAPE-----SINFRR-----FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERlpMP 330
Cdd:cd14063   154 REDTLviPNGWlcyLAPEiiralSPDLDFeeslpFTKASDVYAFGTVWYE-LLAGRWPFKEQPAESIIWQVGCGKK--QS 230
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1914781966 331 PN---CPPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14063   231 LSqldIGREVKDILMQCWAYDPEKRPTFSDLL 262
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
114-367 1.09e-26

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: 109.89  E-value: 1.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKtCKNCT--SDSVREKFLQEALTMRQFDHPHIVKLIGVITEnPVWIIMELCTLG 191
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKT---WLAIK-CPPSLhvDDSERMELLEEAKKMEMAKFRHILPVYGICSE-PVGLVMEYMETG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYayQLSTALAYLESKR--FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd14025    79 SLEKLLASEPLPWELRFRIIH--ETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHSHDLSRDG 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 L--PIKWMAPESI--NFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKN-NDVIGRIENGER--LPMPPNCPPT----LY 338
Cdd:cd14025   157 LrgTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGILTQK-KPFAGENNiLHIMVKVVKGHRpsLSPIPRQRPSecqqMI 235
                         250       260
                  ....*....|....*....|....*....
gi 1914781966 339 SLMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14025   236 CLMKRCWDQDPRKRPTFQDITSETENLLS 264
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
106-358 1.42e-26

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: 109.57  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPenpALAVAIKTC--KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVW 182
Cdd:cd14099     1 KRYRRGKFLGKGGFAKCYEVTDMST---GKVYAGKVVpkSSLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEdEENVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd14099    78 ILLELCSNGSLMELLKRRKA-LTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKLPiKWMAPESINFRRFTS-ASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSL 340
Cdd:cd14099   157 RKKTLCGTP-NYIAPEVLEKKKGHSfEVDIWSLGVILYTLLV-GKPPFETSDVKETYKRIKKNEySFPSHLSISDEAKDL 234
                         250
                  ....*....|....*...
gi 1914781966 341 MTKCWAYDPSRRPRFTEL 358
Cdd:cd14099   235 IRSMLQPDPTKRPSLDEI 252
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
100-358 1.42e-26

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: 109.75  E-value: 1.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN 179
Cdd:cd06610     2 DYELIEV-------IGSGATAVVYAAYCLPKKE---KVAIKRIDLEKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PV-WIIMELCTLGelrSFLQVRKYS-----LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd06610    72 DElWLVMPLLSGG---SLLDIMKSSyprggLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLPIK---WMAPESIN-FRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgerlpm 329
Cdd:cd06610   149 SASLATGGDRTRKVRKTFVGtpcWMAPEVMEqVRGYDFKADIWSFGITAIE-LATGAAPYSKYPPMKVLMLTLQ------ 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 330 ppNCPPTL--------YS-----LMTKCWAYDPSRRPRFTEL 358
Cdd:cd06610   222 --NDPPSLetgadykkYSksfrkMISLCLQKDPSKRPTAEEL 261
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
114-365 1.50e-26

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: 109.65  E-value: 1.50e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGE 192
Cdd:cd14222     1 LGKGFFG---QAIKVTHKATGKVMVMKELIRCDEET-QKTFLTEVKVMRSLDHPNVLKFIGVLYKDKrLNLLTEFIEGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY---------MEDSTYY 263
Cdd:cd14222    77 LKDFLRADDP-FPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLiveekkkppPDKPTTK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLPIK----------WMAPESINFRRFTSASDVWMFGVCMWEILMhgvkpfQGVKNNDVIGR-IENGERLPM--- 329
Cdd:cd14222   156 KRTLRKNDRKkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEIIG------QVYADPDCLPRtLDFGLNVRLfwe 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1914781966 330 ---PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14222   230 kfvPKDCPPAFFPLAAICCRLEPDSRPAFSKLEDSFEAL 268
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
107-358 1.83e-26

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: 109.28  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHqgiymspenpaLAVAIKTCKNC-------TSDSVREKFL--QEALTMRQFDHPHIVKLIGVIT 177
Cdd:cd08225     1 RYEIIKKIGEGSFGKIY-----------LAKAKSDSEHCvikeidlTKMPVKEKEAskKEVILLAKMKHPNIVTFFASFQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 EN-PVWIIMELCTLGELRSFLQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KLGDFGLS 254
Cdd:cd08225    70 ENgRLFIVMEYCDGGDLMKRINRQRGVLFSEDQILsWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHgvkPFQGVKNNDVIGRIENGERLPMPPN 332
Cdd:cd08225   150 RQLNDSMELAYTCVGTPY-YLSPEICQNRPYNNKTDIWSLGCVLYELctLKH---PFEGNNLHQLVLKICQGYFAPISPN 225
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd08225   226 FSRDLRSLISQLFKVSPRDRPSITSI 251
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-353 2.18e-26

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: 108.48  E-value: 2.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKN---CTSDSVRE-KFLQEaLTMRQfDHPHIVKLIGVIT---ENPVWIIME 186
Cdd:cd05118     7 IGEGAFGTVWLARDKVTGE---KVAIKKIKNdfrHPKAALREiKLLKH-LNDVE-GHPNIVKLLDVFEhrgGNHLCLVFE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LctLGE-LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-VKLGDFGLSRYMEDSTYYK 264
Cdd:cd05118    82 L--MGMnLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGqLKLADFGLARSFTSPPYTP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKgklPIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIEngERLPmppncPPTLYSLMTK 343
Cdd:cd05118   160 YVA---TRWYRAPEVLlGAKPYGSSIDIWSLGCILAELLT-GRPLFPGDSEVDQLAKIV--RLLG-----TPEALDLLSK 228
                         250
                  ....*....|
gi 1914781966 344 CWAYDPSRRP 353
Cdd:cd05118   229 MLKYDPAKRI 238
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-353 2.99e-26

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: 108.96  E-value: 2.99e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTL 190
Cdd:cd08228    10 IGRGQFSEVYRATCLLDRKP---VALKKVQifEMMDAKARQDCVKEIDLLKQLNHPNVIKyLDSFIEDNELNIVLELADA 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLA---SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd08228    87 GDLSQMIKYFKKQKRLIperTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI-LMHgvKPFQGVKNN--DVIGRIENGERLPMP-PNCPPTLYSLMTK 343
Cdd:cd08228   167 VGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMaALQ--SPFYGDKMNlfSLCQKIEQCDYPPLPtEHYSEKLRELVSM 243
                         250
                  ....*....|
gi 1914781966 344 CWAYDPSRRP 353
Cdd:cd08228   244 CIYPDPDQRP 253
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
152-357 5.55e-26

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: 107.97  E-value: 5.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 152 EKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVH 230
Cdd:cd14027    36 EALLEEGKMMNRLRHSRVVKLLGVILEEGKYsLVMEYMEKGNLMHVLK--KVSVPLSVKGRIILEIIEGMAYLHGKGVIH 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 231 RDIAARNVLVSSNDCVKLGDFGLS--------------RYMEDSTYYKASKGKLpiKWMAPESIN--FRRFTSASDVWMF 294
Cdd:cd14027   114 KDLKPENILVDNDFHIKIADLGLAsfkmwskltkeehnEQREVDGTAKKNAGTL--YYMAPEHLNdvNAKPTEKSDVYSF 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 295 GVCMWEILMhGVKPFQGVKNND-VIGRIENGERlP----MPPNCPPTLYSLMTKCWAYDPSRRPRFTE 357
Cdd:cd14027   192 AIVLWAIFA-NKEPYENAINEDqIIMCIKSGNR-PdvddITEYCPREIIDLMKLCWEANPEARPTFPG 257
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
114-365 8.41e-26

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: 107.59  E-value: 8.41e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNCtSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGE 192
Cdd:cd14154     1 LGKGFFG---QAIKVTHRETGEVMVMKELIRF-DEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKkLNLITEYIPGGT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED----STYYKASKG 268
Cdd:cd14154    77 LKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEerlpSGNMSPSET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KLPIK---------------WMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNC 333
Cdd:cd14154   157 LRHLKspdrkkrytvvgnpyWMAPEMLNGRSYDEKVDIFSFGIVLCEIIGRVEADPDYLPRTKDFGLNVDSFREKFCAGC 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14154   237 PPPFFKLAFLCCDLDPEKRPPFETLEEWLEAL 268
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
114-364 1.18e-25

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: 106.84  E-value: 1.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPenpalAVAIKTCKNCT--SDSVREKFLQEALTMRQFDHPHIVKLIGVITENP--VWIIMELCT 189
Cdd:cd14064     1 IGSGSFGKVYKGRCRNK-----IVAIKRYRANTycSKSDVDMFCREVSILCRLNHPCVIQFVGACLDDPsqFAIVTQYVS 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLE--SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd14064    76 GGSLFSLLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSLDEDNMTK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPIKWMAPESIN-FRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE-NGERLPMPPNCPPTLYSLMTKCW 345
Cdd:cd14064   156 QPGNLRWMAPEVFTqCTRYSIKADVFSYALCLWELLT-GEIPFAHLKPAAAAADMAyHHIRPPIGYSIPKPISSLLMRGW 234
                         250
                  ....*....|....*....
gi 1914781966 346 AYDPSRRPRFTELKAQLST 364
Cdd:cd14064   235 NAEPESRPSFVEIVALLEP 253
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
113-357 1.29e-25

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: 106.60  E-value: 1.29e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 113 CIGEGQFGDVHQGiyMSPENPALAVAIKtC--KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCT 189
Cdd:cd14121     2 KLGSGTYATVYKA--YRKSGAREVVAVK-CvsKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQwDEEHIYLIMEYCS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND--CVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd14121    79 GGDLSRFIRSRR-TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYnpVLKLADFGFAQHLKPNDEAHSLR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPN------CPPTLYSLM 341
Cdd:cd14121   158 GS-PL-YMAPEMILKKKYDARVDLWSVGVILYECLF-GRAPFASRSFEELEEKIRSSKPIEIPTRpelsadCRDLLLRLL 234
                         250
                  ....*....|....*.
gi 1914781966 342 TKcwayDPSRRPRFTE 357
Cdd:cd14121   235 QR----DPDRRISFEE 246
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
137-358 2.44e-25

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: 106.22  E-value: 2.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKtcknCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ---------VRKYSLDL 206
Cdd:cd14010    28 VAIK----CVDKSKRPEVLNEVRLTHELKHPNVLKFYEWYeTSNHLWLVVEYCTGGDLETLLRqdgnlpessVRKFGRDL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 207 AslilyayqlsTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-------TYYKASKGKLPIK------ 273
Cdd:cd14010   104 V----------RGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEIlkelfgqFSDEGNVNKVSKKqakrgt 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 274 --WMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLPMPPN--CPPT------LYSLMTK 343
Cdd:cd14010   174 pyYMAPELFQGGVHSFASDLWALGCVLYEMFT-GKPPFVAESFTELVEKILNEDPPPPPPKvsSKPSpdfkslLKGLLEK 252
                         250
                  ....*....|....*
gi 1914781966 344 cwayDPSRRPRFTEL 358
Cdd:cd14010   253 ----DPAKRLSWDEL 263
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
109-325 3.88e-25

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: 105.10  E-value: 3.88e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSP-ENPALAVAIKT-CKNctsdsvREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14095     3 DIGRVIGDGNFAVVKECRDKATdKEYALKIIDKAkCKG------KEHMIEnEVAILRRVKHPNIVQLIEEYdTDTELYLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYMED 259
Cdd:cd14095    77 MELVKGGDLfDAITSSTKFTERDASRMVT--DLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADFGLATEVKE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 260 --------STYykaskgklpikwMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNN--DVIGRIENGE 325
Cdd:cd14095   155 plftvcgtPTY------------VAPEILAETGYGLKVDIWAAGVITY-ILLCGFPPFRSPDRDqeELFDLILAGE 217
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
100-353 8.44e-25

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 104.60  E-value: 8.44e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIqrerielGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKncTSDSVREK----FLQEALTMRQFDHPHIVKLIGv 175
Cdd:cd05581     2 DFKF-------GKPLGEGSYSTVVLAKEKETGKE---YAIKVLD--KRHIIKEKkvkyVTIEKEVLSRLAHPGIVKLYY- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 iT---ENPVWIIMELCTLGELRSFLqvRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDF 251
Cdd:cd05581    69 -TfqdESKLYFVLEYAPNGDLLEYI--RKYgSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 252 GLSRYMEDSTYYKASKGKLPIK----------------WMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNN 315
Cdd:cd05581   146 GTAKVLGPDSSPESTKGDADSQiaynqaraasfvgtaeYVSPELLNEKPAGKSSDLWALG-CIIYQMLTGKPPFRGSNEY 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 316 DVIGRIENGErLPMPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd05581   225 LTFQKIVKLE-YEFPENFPPDAKDLIQKLLVLDPSKRL 261
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
114-358 8.54e-25

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


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 104.82  E-value: 8.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 192
Cdd:cd06611    13 LGDGAFGKVYKAQH---KETGLFAAAKIIQIESEEEL-EDFMVEIDILSECKHPNIVGLYEAyFYENKLWILIEFCDGGA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPi 272
Cdd:cd06611    89 LDSIMLELERGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTLQKRDTFIGTP- 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 KWMAPESINFRRFTSA-----SDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGErlpmppncPPTL---------- 337
Cdd:cd06611   168 YWMAPEVVACETFKDNpydykADIWSLGITLIE-LAQMEPPHHELNPMRVLLKILKSE--------PPTLdqpskwsssf 238
                         250       260
                  ....*....|....*....|.
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06611   239 NDFLKSCLVKDPDDRPTAAEL 259
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
112-361 1.37e-24

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: 103.52  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGdvhQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTL 190
Cdd:cd08219     6 RVVGEGSFG---RALLVQHVNSDQKYAMKEIRLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFeADGHLYIVMEYCDG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd08219    83 GDLMQKIKLQRGKLFPEDTILqWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSPGAYACTYVG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHgvkPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAY 347
Cdd:cd08219   163 TPY-YVPPEIWENMPYNNKSDIWSLGCILYELctLKH---PFQANSWKNLILKVCQGSYKPLPSHYSYELRSLIKQMFKR 238
                         250
                  ....*....|....
gi 1914781966 348 DPSRRPRFTELKAQ 361
Cdd:cd08219   239 NPRSRPSATTILSR 252
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
107-353 1.50e-24

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: 104.51  E-value: 1.50e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKtcknctsdsvreKFLQ-------EALTMRQFDHPHIVKLIG---VI 176
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEV---VAIK------------KVLQdkryknrELQIMRRLKHPNIVKLKYffySS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENP----VWIIMELC--TLGE-LRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KL 248
Cdd:cd14137    70 GEKKdevyLNLVMEYMpeTLYRvIRHYSKNKQT-IPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPETGVlKL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMED---------STYYKaskgklpikwmAPESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNND- 316
Cdd:cd14137   149 CDFGSAKRLVPgepnvsyicSRYYR-----------APELIfGATDYTTAIDIWSAGCVLAELLLG--QPlFPGESSVDq 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 317 ------VIG-----------------RIENGERLPM----PPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd14137   216 lveiikVLGtptreqikamnpnytefKFPQIKPHPWekvfPKRTPPDAIDLLSKILVYNPSKRL 279
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
109-353 1.99e-24

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: 103.77  E-value: 1.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKN-------CTSdsVRE-KFLQeALTmrqfDHPHIVKLIGVITEN- 179
Cdd:cd07830     2 KVIKQLGDGTFGSVYLARNKETGE---LVAIKKMKKkfysweeCMN--LREvKSLR-KLN----EHPNIVKLKEVFRENd 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMEL--CTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 257
Cdd:cd07830    72 ELYFVFEYmeGNLYQLMKDRKGKPFSESVIRSIIY--QILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDS---TYYKASkgklpiKWM-APEsINFRR--FTSASDVWMFGVCMWEILMhgVKP-FQGVKNNDVIGRI--------- 321
Cdd:cd07830   150 RSRppyTDYVST------RWYrAPE-ILLRStsYSSPVDIWALGCIMAELYT--LRPlFPGSSEIDQLYKIcsvlgtptk 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 322 ---ENGERL------------PMP-----PNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd07830   221 qdwPEGYKLasklgfrfpqfaPTSlhqliPNASPEAIDLIKDMLRWDPKKRP 272
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
111-358 3.30e-24

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: 103.00  E-value: 3.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIY-MSPENPAL------AVAIKTCKnctsdsvREKFLQEALT-----MRQFDHPHIVKLIGV-IT 177
Cdd:cd06628     5 GALIGSGSFGSVYLGMNaSSGELMAVkqvelpSVSAENKD-------RKKSMLDALQreialLRELQHENIVQYLGSsSD 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFLQvrKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd06628    78 ANHLNIFLEYVPGGSVATLLN--NYGAFEESLVRnFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDSTYYKASKGKLP-----IKWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPP 331
Cdd:cd06628   156 LEANSLSTKNNGARPslqgsVFWMAPEVVKQTSYTRKADIWSLG-CLVVEMLTGTHPFPDCTQMQAIFKIGENASPTIPS 234
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 332 NCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06628   235 NISSEARDFLEKTFEIDHNKRPTADEL 261
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
114-358 3.95e-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. 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: 103.17  E-value: 3.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL--CT 189
Cdd:cd07833     9 VGEGAYGVVLKC--RNKATGEI-VAIKKFKESEDDEdVKKTALREVKVLRQLRHENIVNLKEAFrRKGRLYLVFEYveRT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELrsfLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-----TYYK 264
Cdd:cd07833    86 LLEL---LEASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARpasplTDYV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASkgklpiKWM-APE----SINFRRftsASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIEN---------------- 323
Cdd:cd07833   163 AT------RWYrAPEllvgDTNYGK---PVDVWAIGCIMAELLD-GEPLFPGDSDIDQLYLIQKclgplppshqelfssn 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 324 ----GERLPMPPN-----------CPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd07833   233 prfaGVAFPEPSQpeslerrypgkVSSPALDFLKACLRMDPKERLTCDEL 282
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
104-353 5.10e-24

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: 102.37  E-value: 5.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 104 QRERIELgRCIGEGQFGDVHQ------GIYMspenpalavAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-I 176
Cdd:cd13996     5 LNDFEEI-ELLGSGGFGSVYKvrnkvdGVTY---------AIKKIRLTEKSSASEKVLREVKALAKLNHPNIVRYYTAwV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQVRKYSLDL-ASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGL 253
Cdd:cd13996    75 EEPPLYIQMELCEGGTLRDWIDRRNSSSKNdRKLALeLFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDDlQVKIGDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLPIK-------------WMAPESINFRRFTSASDVWMFGVCMWEIL------MHGVKPFQGVKN 314
Cdd:cd13996   155 ATSIGNQKRELNNLNNNNNGntsnnsvgigtplYASPEQLDGENYNEKADIYSLGIILFEMLhpfktaMERSTILTDLRN 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 315 ndvigriengerLPMPPNC---PPTLYSLMTKCWAYDPSRRP 353
Cdd:cd13996   235 ------------GILPESFkakHPKEADLIQSLLSKNPEERP 264
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-360 5.57e-24

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: 101.82  E-value: 5.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQ-------GIYmspenpalavAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 183
Cdd:cd05123     1 LGKGSFGKVLLvrkkdtgKLY----------AMKVLRkkEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFqTEEKLYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME---D 259
Cdd:cd05123    71 VLDYVPGGELFSHLSkEGRFPEERARF--YAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSsdgD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STY-------YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPN 332
Cdd:cd05123   149 RTYtfcgtpeY-----------LAPEVLLGKGYGKAVDWWSLGVLLYEMLT-GKPPFYAENRKEIYEKILKSP-LKFPEY 215
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRR---PRFTELKA 360
Cdd:cd05123   216 VSPEAKSLISGLLQKDPTKRlgsGGAEEIKA 246
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
97-365 5.98e-24

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: 102.42  E-value: 5.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  97 STRDYEIQRERIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVI 176
Cdd:cd14149     3 SSYYWEIEASEVMLSTRIGSGSFGTVYKGKW----HGDVAVKILKVVDPTPEQF-QAFRNEVAVLRKTRHVNILLFMGYM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd14149    78 TKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MED-STYYKASKGKLPIKWMAPESINFRR---FTSASDVWMFGVCMWEiLMHGVKPFQGVKNND-VIGRIENGERLP--- 328
Cdd:cd14149   158 KSRwSGSQQVEQPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYE-LMTGELPYSHINNRDqIIFMVGRGYASPdls 236
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 329 -MPPNCPPTLYSLMTKCWAYDPSRRPRFTELkaqLSTI 365
Cdd:cd14149   237 kLYKNCPKAMKRLVADCIKKVKEERPLFPQI---LSSI 271
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
114-325 9.99e-24

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: 100.81  E-value: 9.99e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPenpALAVAIKTCKncTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGE 192
Cdd:cd14006     1 LGRGRFGVVKRCIEKAT---GREFAAKFIP--KRDKKKEAVLREISILNQLQHPRIIQLHEAyESPTELVLILELCSGGE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTYYKASKGKL 270
Cdd:cd14006    76 LLDRL-AERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSpqIKIIDFGLARKLNPGEELKEIFGTP 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 271 piKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14006   155 --EFVAPEIVNGEPVSLATDMWSIGVLTY-VLLSGLSPFLGEDDQETLANISACR 206
PTK_Jak1_rpt1 cd05077
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 1; Jak1 is widely ...
154-355 1.58e-23

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: 100.78  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 154 FLQEALTMRQFDHPHIVKLIGVITENPVWIIME-LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRD 232
Cdd:cd05077    55 FFETASMMRQVSHKHIVLLYGVCVRDVENIMVEeFVEFGPLDLFMHRKSDVLTTPWKFKVAKQLASALSYLEDKDLVHGN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 233 IAARNVLVS----SNDC---VKLGDFGLSrymedSTYYKASKGKLPIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMH 304
Cdd:cd05077   135 VCTKNILLAregiDGECgpfIKLSDPGIP-----ITVLSRQECVERIPWIAPECVeDSKNLSIAADKWSFGTTLWEICYN 209
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 305 GVKPfqgVKNNDVI--GRIENGERLPMPPNCpPTLYSLMTKCWAYDPSRRPRF 355
Cdd:cd05077   210 GEIP---LKDKTLAekERFYEGQCMLVTPSC-KELADLMTHCMNYDPNQRPFF 258
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-356 3.17e-23

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: 100.49  E-value: 3.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTL 190
Cdd:cd08229    32 IGRGQFSEVYRATCLLDGVP---VALKKVQifDLMDAKARADCIKEIDLLKQLNHPNVIKYyASFIEDNELNIVLELADA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDL---ASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd08229   109 GDLSRMIKHFKKQKRLipeKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHSL 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNN--DVIGRIENGERLPMPPN-CPPTLYSLMTKC 344
Cdd:cd08229   189 VGTPY-YMSPERIHENGYNFKSDIWSLGCLLYEMAALQ-SPFYGDKMNlySLCKKIEQCDYPPLPSDhYSEELRQLVNMC 266
                         250
                  ....*....|..
gi 1914781966 345 WAYDPSRRPRFT 356
Cdd:cd08229   267 INPDPEKRPDIT 278
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
108-352 3.61e-23

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: 100.35  E-value: 3.61e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCtsDSVREK----FLQEALTMRQFDHPHIVKLIGVIT-ENPVW 182
Cdd:cd05580     3 FEFLKTLGTGSFGRVRLVKHKDSGKY---YALKILKKA--KIIKLKqvehVLNEKRILSEVRHPFIVNLLGSFQdDRNLY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 261
Cdd:cd05580    78 MVMEYVPGGELFSLLrRSGRFPNDVAKF--YAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 Y-------YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCP 334
Cdd:cd05580   156 YtlcgtpeY-----------LAPEIILSKGHGKAVDWWALGILIYEMLA-GYPPFFDENPMKIYEKILEG-KIRFPSFFD 222
                         250
                  ....*....|....*...
gi 1914781966 335 PTLYSLMTKCWAYDPSRR 352
Cdd:cd05580   223 PDAKDLIKRLLVVDLTKR 240
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
106-353 3.76e-23

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: 99.65  E-value: 3.76e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVhqgiYMSPENPA---LAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPV 181
Cdd:cd14116     5 EDFEIGRPLGKGKFGNV----YLAREKQSkfiLALKVLFKAQLEKAGVEHQLRREVEIQSHLRHPNILRLYGYFHDaTRV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSt 261
Cdd:cd14116    81 YLILEYAPLGTVYRELQ-KLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSS- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 yyKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLM 341
Cdd:cd14116   159 --RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFLV-GKPPFEANTYQETYKRISRVE-FTFPDFVTEGARDLI 234
                         250
                  ....*....|..
gi 1914781966 342 TKCWAYDPSRRP 353
Cdd:cd14116   235 SRLLKHNPSQRP 246
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
110-309 3.88e-23

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: 99.26  E-value: 3.88e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELC 188
Cdd:cd14079     6 LGKTLGVGSFGKVKLAEH-ELTGHKVAVKILNRQKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIeTPTDIFMVMEYV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd14079    85 SGGELFDYI-VQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKTSCG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 269 KlPiKWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd14079   164 S-P-NYAAPEVISGKLYAgPEVDVWSCGVILYALLC-GSLPF 202
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
107-368 4.52e-23

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: 99.13  E-value: 4.52e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPenpALAVAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLT---GREVAIKIIdKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIeTEKTLYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 264
Cdd:cd14072    78 MEYASGGEVFDYLVAHGRMKEKEARAKFR-QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPikWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLP--MPPNCPptlySL 340
Cdd:cd14072   157 TFCGSPP--YAAPELFQGKKYDGPEvDVWSLGVILY-TLVSGSLPFDGQNLKELRERVLRGKyRIPfyMSTDCE----NL 229
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 341 MTKCWAYDPSRRprftelkAQLSTILEE 368
Cdd:cd14072   230 LKKFLVLNPSKR-------GTLEQIMKD 250
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
114-358 6.01e-23

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: 98.82  E-value: 6.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKncTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTLGE 192
Cdd:cd06614     8 IGEGASGEVYKATDRATGK---EVAIKKMR--LRKQNKELIINEILIMKECKHPNIVDYYDsYLVGDELWVVMEYMDGGS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFlqVRKYSLDLA-SLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymedstyyKASKGKL 270
Cdd:cd06614    83 LTDI--ITQNPVRMNeSQIAYvCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAA--------QLTKEKS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PIK-------WMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKP----------FQGVKNNdvIGRIENGERLpmppnc 333
Cdd:cd06614   153 KRNsvvgtpyWMAPEVIKRKDYGPKVDIWSLGIMCIE-MAEGEPPyleepplralFLITTKG--IPPLKNPEKW------ 223
                         250       260
                  ....*....|....*....|....*
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06614   224 SPEFKDFLNKCLVKDPEKRPSAEEL 248
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
114-359 7.74e-23

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: 98.48  E-value: 7.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIymspENPALA-VAIKTCKN-------CTSDSVRekflQEALTMRQFDHPHIVKLIGVITEN---PVW 182
Cdd:cd14119     1 LGEGSYGKVKEVL----DTETLCrRAVKILKKrklrripNGEANVK----REIQILRRLNHRNVIKLVDVLYNEekqKLY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG----LSRYME 258
Cdd:cd14119    73 MVMEYCVGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGvaeaLDLFAE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKaSKGKlPiKWMAPESINFRRFTS--ASDVWMFGVCMWEILMhGVKPFQGvknnDVIGR----IENGErLPMPPN 332
Cdd:cd14119   153 DDTCTT-SQGS-P-AFQPPEIANGQDSFSgfKVDIWSAGVTLYNMTT-GKYPFEG----DNIYKlfenIGKGE-YTIPDD 223
                         250       260
                  ....*....|....*....|....*..
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14119   224 VDPDLQDLLRGMLEKDPEKRFTIEQIR 250
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
146-368 8.56e-23

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: 98.32  E-value: 8.56e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 146 TSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLE 224
Cdd:cd14155    27 TLSSNRANMLREVQLMNRLSHPNILRFMGVcVHQGQLHALTEYINGGNLEQLLDSNEP-LSWTVRVKLALDIARGLSYLH 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 225 SKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDstyYKASKGKLPI----KWMAPESINFRRFTSASDVWMFGVC 297
Cdd:cd14155   106 SKGIFHRDLTSKNCLIKRDEngyTAVVGDFGLAEKIPD---YSDGKEKLAVvgspYWMAPEVLRGEPYNEKADVFSYGII 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 298 MWEIlmhgvkpfqgvknndvIGRIE-NGERLP--------------MPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd14155   183 LCEI----------------IARIQaDPDYLPrtedfgldydafqhMVGDCPPDFLQLAFNCCNMDPKSRPSFHDIVKTL 246

                  ....*.
gi 1914781966 363 STILEE 368
Cdd:cd14155   247 EEILEK 252
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
105-352 1.17e-22

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: 98.10  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVHQgiymSPENPALAVAIKTCKNctsDSVREK-----FLQEALTMRQFDHPHIVKLIGVI-TE 178
Cdd:cd14161     2 KHRYEFLETLGKGTYGRVKK----ARDSSGRLVAIKSIRK---DRIKDEqdllhIRREIEIMSSLNHPHIISVYEVFeNS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd14161    75 SKIVIVMEYASRGDLYDYISERQRLSELEARHFFR-QIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKlPIkWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLPMPPN--CP 334
Cdd:cd14161   154 QDKFLQTYCGS-PL-YASPEIVNGRPYIGPEvDSWSLGVLLY-ILVHGTMPFDGHDYKILVKQISSGAyREPTKPSdaCG 230
                         250
                  ....*....|....*...
gi 1914781966 335 PTLYSLMTkcwayDPSRR 352
Cdd:cd14161   231 LIRWLLMV-----NPERR 243
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
114-358 1.20e-22

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: 98.59  E-value: 1.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELctLGE 192
Cdd:cd06640    12 IGKGSFGEVFKGIDNRTQQ---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKGTKLWIIMEY--LGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06640    87 GSALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPPTLYSLMTK--------C 344
Cdd:cd06640   167 -WMAPEVIQQSAYDSKADIWSLGITAIE-LAKGEPPNSDMHPMRVLFLI--------PKNNPPTLVGDFSKpfkefidaC 236
                         250
                  ....*....|....
gi 1914781966 345 WAYDPSRRPRFTEL 358
Cdd:cd06640   237 LNKDPSFRPTAKEL 250
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
109-353 1.23e-22

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: 97.89  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIktckNCTSDSVREKFL--QEALTMRQFDHPHIV--KLIGVITENPVWII 184
Cdd:cd08223     3 QFLRVIGKGSYGEVWLVRHKRDRKQYVIKKL----NLKNASKRERKAaeQEAKLLSKLKHPNIVsyKESFEGEDGFLYIV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRK-YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 263
Cdd:cd08223    79 MGFCEGGDLYTRLKEQKgVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHGvkpFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLM 341
Cdd:cd08223   159 ATTLIGTPY-YMSPELFSNKPYNHKSDVWALGCCVYEMatLKHA---FNAKDMNSLVYKILEGKLPPMPKQYSPELGELI 234
                         250
                  ....*....|..
gi 1914781966 342 TKCWAYDPSRRP 353
Cdd:cd08223   235 KAMLHQDPEKRP 246
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
106-325 1.65e-22

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: 98.66  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMspENPALAVAIKTCK------NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TE 178
Cdd:cd14096     1 ENYRLINKIGEGAFSNVYKAVPL--RNTGKPVAIKVVRkadlssDNLKGSSRANILKEVQIMKRLSHPNIVKLLDFQeSD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELrsFLQVRKY---SLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSSND----------- 244
Cdd:cd14096    79 EYYYIVLELADGGEI--FHQIVRLtyfSEDLSRHVI--TQVASAVKYLHEIGVVHRDIKPENLLFEPIPfipsivklrka 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 245 ----------------------CVKLGDFGLSRYMEDSTyykaskGKLP---IKWMAPESINFRRFTSASDVWMFGVCMW 299
Cdd:cd14096   155 dddetkvdegefipgvggggigIVKLADFGLSKQVWDSN------TKTPcgtVGYTAPEVVKDERYSKKVDMWALGCVLY 228
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 300 EILMhGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14096   229 TLLC-GFPPFYDESIETLTEKISRGD 253
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
109-358 2.01e-22

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: 98.02  E-value: 2.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-------- 180
Cdd:cd14048     9 EPIQCLGRGGFGVVFEAKNKVDDC---NYAVKRIRLPNNELAREKVLREVRALAKLDHPGIVRYFNAWLERPpegwqekm 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 ----VWIIMELCTLGELRSFLQVRK--YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd14048    86 devyLYIQMQLCRKENLKDWMNRRCtmESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLV 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYM----------EDSTYYKASKGKLPIK-WMAPESINFRRFTSASDVWMFGVCMWEILMhgvkPFQgvKNNDVIGRIEN 323
Cdd:cd14048   166 TAMdqgepeqtvlTPMPAYAKHTGQVGTRlYMSPEQIHGNQYSEKVDIFALGLILFELIY----SFS--TQMERIRTLTD 239
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 324 GERLPMPP---NCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14048   240 VRKLKFPAlftNKYPEERDMVQQMLSPSPSERPEAHEV 277
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
110-358 2.42e-22

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: 97.04  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQgIYMSPENPALAVA-IKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVIT-ENPVWIIME 186
Cdd:cd06625     4 QGKLLGQGAFGQVYL-CYDADTGRELAVKqVEIDPINTEASKEVKALEcEIQLLKNLQHERIVQYYGCLQdEKSLSIFME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSflQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME---DSTY 262
Cdd:cd06625    83 YMPGGSVKD--EIKAYgALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQticSSTG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhgVKP----FQGVKnndVIGRIENGERLP-MPPNCPPTL 337
Cdd:cd06625   161 MKSVTGT-PY-WMSPEVINGEGYGRKADIWSVGCTVVEMLT--TKPpwaeFEPMA---AIFKIATQPTNPqLPPHVSEDA 233
                         250       260
                  ....*....|....*....|.
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06625   234 RDFLSLIFVRNKKQRPSAEEL 254
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
114-358 2.47e-22

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: 97.34  E-value: 2.47e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiYMSPEnpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENpvwiimELCTL--- 190
Cdd:cd14066     1 IGSGGFGTVYKG-VLENG---TVVAVKRLNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYCLES------DEKLLvye 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 ----GELRSFLQVRKYS--LDLASLILYAYQLSTALAYLESKRF---VHRDIAARNVLVSSNDCVKLGDFGLSRYM-EDS 260
Cdd:cd14066    71 ympnGSLEDRLHCHKGSppLPWPQRLKIAKGIARGLEYLHEECPppiIHGDIKSSNILLDEDFEPKLTDFGLARLIpPSE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI---------ENGERL--PM 329
Cdd:cd14066   151 SVSKTSAVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLT-GKPAVDENRENASRKDLvewveskgkEELEDIldKR 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 330 PPNCPP-------TLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14066   230 LVDDDGveeeeveALLRLALLCTRSDPSLRPSMKEV 265
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
149-358 2.80e-22

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: 96.66  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 149 SVREKFLQEALTMRqfdHPHIVKLIGV----ITENPVW---IIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALA 221
Cdd:cd14012    43 QLLEKELESLKKLR---HPNLVSYLAFsierRGRSDGWkvyLLTEYAPGGSLSELLD-SVGSVPLDTARRWTLQLLEALE 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 222 YLESKRFVHRDIAARNVLVSSNDC---VKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINF-RRFTSASDVWMFGVC 297
Cdd:cd14012   119 YLHRNGVVHKSLHAGNVLLDRDAGtgiVKLTDYSLGKTLLDMCSRGSLDEFKQTYWLPPELAQGsKSPTRKTDVWDLGLL 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 298 MWEILmhgvkpfQGVknnDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14012   199 FLQML-------FGL---DVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALEL 249
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
110-353 3.09e-22

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: 96.81  E-value: 3.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMsPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:cd14070     6 IGRKLGEGSFAKVREGLHA-VTGEKVAIKVIDKKKAKKDSyVTKNLRREGRIQQMIRHPNITQLLDILeTENSYYLVMEL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK--A 265
Cdd:cd14070    85 CPGGNLMHRI-YDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDpfS 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN--DVIGRIENGERLPMPPNCPPTLYSLMTK 343
Cdd:cd14070   164 TQCGSP-AYAAPELLARKKYGPKVDVWSIGVNMYAMLT-GTLPFTVEPFSlrALHQKMVDKEMNPLPTDLSPGAISFLRS 241
                         250
                  ....*....|
gi 1914781966 344 CWAYDPSRRP 353
Cdd:cd14070   242 LLEPDPLKRP 251
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
101-334 3.14e-22

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: 97.00  E-value: 3.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIelgrcIGEGQFGDVHQGIYMSPENpaLAVAIKtCKNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVIT-E 178
Cdd:cd14202     2 FEFSRKDL-----IGHGAFAVVFKGRHKEKHD--LEVAVK-CINKKNLAKSQTLLgKEIKILKELKHENIVALYDFQEiA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---------SNDCVKLG 249
Cdd:cd14202    74 NSVYLVMEYCNGGDLADYLHTMR-TLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 250 DFGLSRYMEDSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLpm 329
Cdd:cd14202   153 DFGFARYLQNNMMAATLCGS-PM-YMAPEVIMSQHYDAKADLWSIGTIIYQCLT-GKAPFQASSPQDLRLFYEKNKSL-- 227

                  ....*
gi 1914781966 330 PPNCP 334
Cdd:cd14202   228 SPNIP 232
FERM_C_FAK1 cd13190
FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion ...
1-50 3.39e-22

FERM domain C-lobe of Focal Adhesion Kinase 1 and 2; FAK1 (also called FRNK/Focal adhesion kinase-related nonkinase; p125FAK/pp125FAK;PTK2/Protein-tyrosine kinase 2 protein tyrosine kinase 2 (PTK2) is a non-receptor tyrosine kinase that localizes to focal adhesions in adherent cells. It has been implicated in diverse cellular roles including cell locomotion, mitogen response and cell survival. The N-terminal region of FAK1 contains a FERM domain, a linker, a kinase domain, and a C-terminal FRNK (FAK-related-non-kinase) domain. Three subdomains of FERM: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3), form a cloverleaf fold, similar to those of known FERM structures despite the low sequence conservation. The C-lobe/F3 within the FERM domain is part of the PH domain family. The phosphoinositide-binding site found in ERM family proteins is not present in the FERM domain of FAK1. The adjacent Src SH3 and SH2 binding sites in the linker of FAK1 associates with the F3 and F1 lobes and are thought to be involved in regulation. The FERM domain of FAK1 can inhibit enzymatic activity and repress FAK signaling. In an inactive state of FAK1, the FERM domain is thought to interact with the catalytic domain of FAK1 to repress its activity. Upon activation this interaction is disrupted and its kinase activity restored. The FRNK domain is thought to function as a negative regulator of kinase activity. The C-lobe/F3 is the third structural domain within the FERM domain. The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 270011  Cd Length: 111  Bit Score: 91.92  E-value: 3.39e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966   1 MLQLKIAGAPEPLTVTAPSLTIAENMADLIDGYCRLVNGTSQSFIIRPQK 50
Cdd:cd13190    62 LLQLKIAGASEPLSITCSSLATAESLADLIDGYCRLVNQTDSSLIIRPEK 111
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
111-325 3.56e-22

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: 96.85  E-value: 3.56e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIYMSPENPAlavAIKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWIIMELC 188
Cdd:cd14097     6 GRKLGQGSFGVVIEATHKETQTKW---AIKKINREKAGSSAVKLLErEVDILKHVNHAHIIHLEEVFeTPKRMYLVMELC 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQVRK-YSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLVSSNDC-------VKLGDFGLS--RYME 258
Cdd:cd14097    83 EDGELKELLLRKGfFSENETRHIIQS--LASAVAYLHKNDIVHRDLKLENILVKSSIIdnndklnIKVTDFGLSvqKYGL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 259 DSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14097   161 GEDMLQETCGT-PI-YMAPEVISAHGYSQQCDIWSIGVIMY-MLLCGEPPFVAKSEEKLFEEIRKGD 224
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
114-358 4.73e-22

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: 96.66  E-value: 4.73e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELctLGE 192
Cdd:cd06642    12 IGKGSFGEVYKGIDNRTKE---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYYGsYLKGTKLWIIMEY--LGG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06642    87 GSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPPTLYSLMTK--------C 344
Cdd:cd06642   167 -WMAPEVIKQSAYDFKADIWSLGITAIE-LAKGEPPNSDLHPMRVLFLI--------PKNSPPTLEGQHSKpfkefveaC 236
                         250
                  ....*....|....
gi 1914781966 345 WAYDPSRRPRFTEL 358
Cdd:cd06642   237 LNKDPRFRPTAKEL 250
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
108-360 5.98e-22

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: 96.67  E-value: 5.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRcIGEGQFGDVHQgiyMSPENPALAVAIKTCKnCTSDSVREK-FLQEA-LTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd06616     9 KDLGE-IGRGAFGTVNK---MLHKPSGTIMAVKRIR-STVDEKEQKrLLMDLdVVMRSSDCPYIVKFYGALfREGDCWIC 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLgelrsflqvrkySLDLASLILYAYQLST---------------ALAYL-ESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:cd06616    84 MELMDI------------SLDKFYKYVYEVLDSVipeeilgkiavatvkALNYLkEELKIIHRDVKPSNILLDRNGNIKL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDSTYYKASKGKLPikWMAPESINFRRFTSA----SDVWMFGVCMWEiLMHGVKPFQGVKNN-DVIGRIEN 323
Cdd:cd06616   152 CDFGISGQLVDSIAKTRDAGCRP--YMAPERIDPSASRDGydvrSDVWSLGITLYE-VATGKFPYPKWNSVfDQLTQVVK 228
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 324 GErlpmPPNCPPTL---YSLMTK-----CWAYDPSRRPRFTELKA 360
Cdd:cd06616   229 GD----PPILSNSEereFSPSFVnfvnlCLIKDESKRPKYKELLK 269
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
107-368 6.25e-22

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: 96.58  E-value: 6.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 185
Cdd:cd14152     1 QIELGELIGQGRWGKVHRGRW----HGEVAIRLLEIDGNNQDHLK-LFKKEVMNYRQTRHENVVLFMGACMHPPhLAIIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV--KLGDFGLSRYMEDSTyy 263
Cdd:cd14152    76 SFCKGRTLYSFVRDPKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYDNGKVVitDFGLFGISGVVQEGR-- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLPIKW---MAPESI---------NFRRFTSASDVWMFGVcMWEILMHGVKPFQGVKNNDVIGRIENGE---RLP 328
Cdd:cd14152   154 RENELKLPHDWlcyLAPEIVremtpgkdeDCLPFSKAADVYAFGT-IWYELQARDWPLKNQPAEALIWQIGSGEgmkQVL 232
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1914781966 329 MPPNCPPTLYSLMTKCWAYDPSRRPRFTelkaQLSTILEE 368
Cdd:cd14152   233 TTISLGKEVTEILSACWAFDLEERPSFT----LLMDMLEK 268
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
100-358 7.23e-22

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: 95.84  E-value: 7.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGV-ITE 178
Cdd:cd06613     1 DYELIQR-------IGSGTYGDVYKARNIATGE---LAAVKVIKLEPGDDFEI-IQQEISMLKECRHPNIVAYFGSyLRR 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQVrkysLDLASLILYAY---QLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd06613    70 DKLWIVMEYCGGGSLQDIYQV----TGPLSELQIAYvcrETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVSA 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDSTyykaSKGKLPIK---WMAPESINFRR---FTSASDVWMFGVC---MWEIL--MHGVKP----FQGVKNNDVIGR 320
Cdd:cd06613   146 QLTATI----AKRKSFIGtpyWMAPEVAAVERkggYDGKCDIWALGITaieLAELQppMFDLHPmralFLIPKSNFDPPK 221
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 321 IENGERLpmppncPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06613   222 LKDKEKW------SPDFHDFIKKCLTKNPKKRPTATKL 253
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
114-358 7.29e-22

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: 96.29  E-value: 7.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTLGE 192
Cdd:cd06641    12 IGKGSFGEVFKGIDNRTQK---VVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYVTKYYGsYLKDTKLWIIMEYLGGGS 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06641    89 ALDLLE--PGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDTQIKRN*FVGTPF 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPPTL---YS-----LMTKC 344
Cdd:cd06641   167 -WMAPEVIKQSAYDSKADIWSLGITAIE-LARGEPPHSELHPMKVLFLI--------PKNNPPTLegnYSkplkeFVEAC 236
                         250
                  ....*....|....
gi 1914781966 345 WAYDPSRRPRFTEL 358
Cdd:cd06641   237 LNKEPSFRPTAKEL 250
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
107-352 9.82e-22

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: 95.15  E-value: 9.82e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKNC--TSDSVREKFLQEALTMRQFDHPHIVKLIGVItEN--PVW 182
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGR---EVAIKSIKKDkiEDEQDMVRIRREIEIMSSLNHPHIIRIYEVF-ENkdKIV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd14073    78 IVMEYASGGELYDYISERR-RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKlPIkWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGERlpMPPNCPPTLYSLM 341
Cdd:cd14073   157 LQTFCGS-PL-YASPEIVNGTPYQGPEvDCWSLGVLLY-TLVYGTMPFDGSDFKRLVKQISSGDY--REPTQPSDASGLI 231
                         250
                  ....*....|.
gi 1914781966 342 TKCWAYDPSRR 352
Cdd:cd14073   232 RWMLTVNPKRR 242
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
107-358 1.10e-21

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: 95.62  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELgrcIGEGQFGDVHQGIYMSPENpalAVAIK-----TCKNCTSDSVRE-KFLQEaltMRQFDHPHIVKLIGVITENP 180
Cdd:cd06917     5 RLEL---VGRGSYGAVYRGYHVKTGR---VVALKvlnldTDDDDVSDIQKEvALLSQ---LKLGQPKNIIKYYGSYLKGP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 -VWIIMELCTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd06917    76 sLWIIMDYCEGGSIRTLMRAGPIAERYIAVIMR--EVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYYKASKGKLPIkWMAPESI-NFRRFTSASDVWMFGVCMWEIlMHGVKPFQGVKNNDVIGRIENGErlpmPPNCPPTLY 338
Cdd:cd06917   154 NSSKRSTFVGTPY-WMAPEVItEGKYYDTKADIWSLGITTYEM-ATGNPPYSDVDALRAVMLIPKSK----PPRLEGNGY 227
                         250       260
                  ....*....|....*....|....*
gi 1914781966 339 SLMTK-----CWAYDPSRRPRFTEL 358
Cdd:cd06917   228 SPLLKefvaaCLDEEPKDRLSADEL 252
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
112-358 2.45e-21

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: 94.77  E-value: 2.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENpalAVAIKTCK-----NCTSDSVRE--KFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 183
Cdd:cd14084    12 RTLGSGACGEVKLAYDKSTCK---KVAIKIINkrkftIGSRREINKprNIETEIEILKKLSHPCIIKIEDFFdAEDDYYI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDS 260
Cdd:cd14084    89 VLELMEGGELFDRV-VSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSKILGET 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKlpIKWMAPESINF---RRFTSASDVWMFGVCMWeILMHGVKPFQG-VKNNDVIGRIENGERLPMPP---NC 333
Cdd:cd14084   168 SLMKTLCGT--PTYLAPEVLRSfgtEGYTRAVDCWSLGVILF-ICLSGYPPFSEeYTQMSLKEQILSGKYTFIPKawkNV 244
                         250       260
                  ....*....|....*....|....*
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14084   245 SEEAKDLVKKMLVVDPSRRPSIEEA 269
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
113-365 2.75e-21

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: 94.81  E-value: 2.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 113 CIGEGQFGDVHQGIYMspeNPALAVAIKTCKNCTSdSVREKFLQEALTMRqfdHPHIVKLI-----GVITENPVWIIMEL 187
Cdd:cd13998     2 VIGKGRFGEVWKASLK---NEPVAVKIFSSRDKQS-WFREKEIYRTPMLK---HENILQFIaaderDTALRTELWLVTAF 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRF---------VHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd13998    75 HPNGSL*DYL--SLHTIDWVSLCRLALSVARGLAHLHSEIPgctqgkpaiAHRDLKSKNILVKNDGTCCIADFGLAVRLS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYY--KASKGKL-PIKWMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK----------PFQG-VKNNDVI 318
Cdd:cd13998   153 PSTGEedNANNGQVgTKRYMAPEvlegAINLRDFESfkRVDIYAMGLVLWEMASRCTDlfgiveeykpPFYSeVPNHPSF 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 319 GRI-ENGERLPMPPNCPP---------TLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd13998   233 EDMqEVVVRDKQRPNIPNrwlshpglqSLAETIEECWDHDAEARLTAQCIEERLSEF 289
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
114-364 3.31e-21

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: 94.11  E-value: 3.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiYMSPENPALAVAIKTCkNCTS-----------DSVREKFLQEALTMRQFDHPHIVKLIGVITENP-V 181
Cdd:cd08528     8 LGSGAFGCVYK--VRKKSNGQTLLALKEI-NMTNpafgrteqerdKSVGDIISEVNIIKEQLRHPNIVRYYKTFLENDrL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMEL---CTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYL-ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY- 256
Cdd:cd08528    85 YIVMELiegAPLGEHFSSLKEKNEHFTEDRIWNIFVQMVLALRYLhKEKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQk 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPMPPNcppt 336
Cdd:cd08528   165 GPESSKMTSVVGT--ILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQ-PPFYSTNMLTLATKIVEAEYEPLPEG---- 237
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1914781966 337 LYS-----LMTKCWAYDPSRRPRFTELKAQLST 364
Cdd:cd08528   238 MYSdditfVIRSCLTPDPEARPDIVEVSSMISD 270
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
154-363 3.50e-21

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: 94.22  E-value: 3.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 154 FLQEALTMRQFDHPHIVKLIGvITENPVWIIMELCTLGELRSFLQvrKYSLDLASLILY-----AYQLSTALAYLESKRF 228
Cdd:cd14000    57 LRQELTVLSHLHHPSIVYLLG-IGIHPLMLVLELAPLGSLDHLLQ--QDSRSFASLGRTlqqriALQVADGLRYLHSAMI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDC-----VKLGDFGLSRYmedsTYYKASKGKLPIK-WMAPESINFR-RFTSASDVWMFGVCMWEI 301
Cdd:cd14000   134 IYRDLKSHNVLVWTLYPnsaiiIKIADYGISRQ----CCRMGAKGSEGTPgFRAPEIARGNvIYNEKVDVFSFGMLLYEI 209
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 302 LmHGVKPFQGVKNNDVIGRIENGERLPM-PPNC--PPTLYSLMTKCWAYDPSRRPRFTELKAQLS 363
Cdd:cd14000   210 L-SGGAPMVGHLKFPNEFDIHGGLRPPLkQYECapWPEVEVLMKKCWKENPQQRPTAVTVVSILN 273
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
155-358 3.54e-21

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: 93.64  E-value: 3.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQ-VRKYSLDLA-SLIL-YAYQLSTALAYLESKRFVH 230
Cdd:cd08222    50 NREAKLLSKLDHPAIVKFHDSFVEKEsFCIVTEYCEGGDLDDKISeYKKSGTTIDeNQILdWFIQLLLAVQYMHERRILH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 231 RDIAARNVLVsSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEI--LMHGvkp 308
Cdd:cd08222   130 RDLKAKNIFL-KNNVIKVGDFGISRILMGTSDLATTFTGTPY-YMSPEVLKHEGYNSKSDIWSLGCILYEMccLKHA--- 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 309 FQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd08222   205 FDGQNLLSVMYKIVEGETPSLPDKYSKELNAIYSRMLNKDPALRPSAAEI 254
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
107-353 4.80e-21

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: 94.18  E-value: 4.80e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTS---------DSVRE-KFLQEaltmrqFDHPHIVKLIGVI 176
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRI---VAIKKIKLGERkeakdginfTALREiKLLQE------LKHPNIIGLLDVF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENP-VWIIMELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd07841    72 GHKSnINLVFEFME-TDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDST----------YYKaskgklpikwmAPESInF--RRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-- 321
Cdd:cd07841   151 SFGSPNrkmthqvvtrWYR-----------APELL-FgaRHYGVGVDMWSVGCIFAE-LLLRVPFLPGDSDIDQLGKIfe 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 322 --------------------ENGERLPMP-----PNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd07841   218 algtpteenwpgvtslpdyvEFKPFPPTPlkqifPAASDDALDLLQRLLTLNPNKRI 274
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
114-358 5.49e-21

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: 93.18  E-value: 5.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVhQGIYMSPENPALAVaiKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGe 192
Cdd:cd06605     9 LGEGNGGVV-SKVRHRPSGQIMAV--KVIRLEIDEALQKQILRELDVLHKCNSPYIVGFYGAfYSEGDISICMEYMDGG- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 lrSFLQVRKYSLDLASLIL--YAYQLSTALAYLESKR-FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyYKASKGK 269
Cdd:cd06605    85 --SLDKILKEVGRIPERILgkIAVAVVKGLIYLHEKHkIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSL-AKTFVGT 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIE------NGErlpmPPNCP-----PTLY 338
Cdd:cd06605   162 RS--YMAPERISGGKYTVKSDIWSLGLSLVE-LATGRFPYPPPNAKPSMMIFEllsyivDEP----PPLLPsgkfsPDFQ 234
                         250       260
                  ....*....|....*....|
gi 1914781966 339 SLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06605   235 DFVSQCLQKDPTERPSYKEL 254
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
112-352 7.45e-21

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: 94.00  E-value: 7.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCT---SDSVREKFLQEALTmrQFDHPHIVKL-IGVITENPVWIIMEL 187
Cdd:cd05582     1 KVLGQGSFGKVFLVRKITGPDAGTLYAMKVLKKATlkvRDRVRTKMERDILA--DVNHPFIVKLhYAFQTEGKLYLILDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTyyKAS 266
Cdd:cd05582    79 LRGGDLFTRLS-KEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEK--KAY 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCWA 346
Cdd:cd05582   156 SFCGTVEYMAPEVVNRRGHTQSADWWSFGVLMFEMLT-GSLPFQGKDRKETMTMILKA-KLGMPQFLSPEAQSLLRALFK 233

                  ....*.
gi 1914781966 347 YDPSRR 352
Cdd:cd05582   234 RNPANR 239
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
110-360 8.31e-21

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: 92.78  E-value: 8.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSPENpALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIGVITENPV-WIIMELC 188
Cdd:cd14069     5 LVQTLGEGAFGEVFLAVNRNTEE-AVAVKFVDMKRAPGDC-PENIKKEVCIQKMLSHKNVVRFYGHRREGEFqYLFLEYA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELrsFLQVR-KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS---RYMEDSTYYK 264
Cdd:cd14069    83 SGGEL--FDKIEpDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLAtvfRYKGKERLLN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPikWMAPESINFRRF-TSASDVWMFGVCMWEILMhGVKPFQGVKNNDV--IGRIENGERLPMP-PNCPPTLYSL 340
Cdd:cd14069   161 KMCGTLP--YVAPELLAKKKYrAEPVDVWSCGIVLFAMLA-GELPWDQPSDSCQeySDWKENKKTYLTPwKKIDTAALSL 237
                         250       260
                  ....*....|....*....|
gi 1914781966 341 MTKCWAYDPSRRPRFTELKA 360
Cdd:cd14069   238 LRKILTENPNKRITIEDIKK 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
106-360 8.34e-21

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: 93.14  E-value: 8.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMspeNPALAVAIKTCKNcTSDSvREKFLQEALTMRQF-DHPHIVKLIGV-------IT 177
Cdd:cd06608     6 GIFELVEVIGEGTYGKVYKARHK---KTGQLAAIKIMDI-IEDE-EEEIKLEINILRKFsNHPNIATFYGAfikkdppGG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLG---ELRSFLQVRKYSL--DLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd06608    81 DDQLWLVMEYCGGGsvtDLVKGLRKKGKRLkeEWIAYILR--ETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYMeDSTYYK--ASKGKlPIkWMAPESINF-----RRFTSASDVWMFGVCMWEiLMHGVKPFqgvknndvigrienGE 325
Cdd:cd06608   159 VSAQL-DSTLGRrnTFIGT-PY-WMAPEVIACdqqpdASYDARCDVWSLGITAIE-LADGKPPL--------------CD 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 326 RLPM------PPNCPPTLYS----------LMTKCWAYDPSRRPRFTELKA 360
Cdd:cd06608   221 MHPMralfkiPRNPPPTLKSpekwskefndFISECLIKNYEQRPFTEELLE 271
PTK_Jak3_rpt1 cd14208
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 3; Jak3 is ...
108-355 8.51e-21

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: 92.66  E-value: 8.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYMSPENPA-------LAVAIKTCKNCTsdsvrEKFLQEALTMRQFDHPHIVKLIGVITENP 180
Cdd:cd14208     1 LTFMESLGKGSFTKIYRGLRTDEEDDErcetevlLKVMDPTHGNCQ-----ESFLEAASIMSQISHKHLVLLHGVCVGKD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASL--ILYAYQLSTALAYLESKRFVHRDIAARNVLVS------SNDCVKLGDFG 252
Cdd:cd14208    76 SIMVQEFVCHGALDLYLKKQQQKGPVAISwkLQVVKQLAYALNYLEDKQLVHGNVSAKKVLLSregdkgSPPFIKLSDPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYMEDSTYYKASkgklpIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPP 331
Cdd:cd14208   156 VSIKVLDEELLAER-----IPWVAPECLsDPQNLALEADKWGFGATLWEIFSGGHMPLSALDPSKKLQFYNDRKQLPAPH 230
                         250       260
                  ....*....|....*....|....
gi 1914781966 332 NCppTLYSLMTKCWAYDPSRRPRF 355
Cdd:cd14208   231 WI--ELASLIQQCMSYNPLLRPSF 252
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
114-358 9.84e-21

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


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 93.17  E-value: 9.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiyMSPENPALAVA--IKTckncTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTL 190
Cdd:cd06644    20 LGDGAFGKVYKA--KNKETGALAAAkvIET----KSEEELEDYMVEIEILATCNHPYIVKLLGAFYwDGKLWIMIEFCPG 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 270
Cdd:cd06644    94 GAVDAIMLELDRGLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVKTLQRRDSFIGT 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PIkWMAPESINFRRFTSA-----SDVWMFGVCMWEILM-----HGVKPFQgvknndVIGRIENGE--RLPMPPNCPPTLY 338
Cdd:cd06644   174 PY-WMAPEVVMCETMKDTpydykADIWSLGITLIEMAQiepphHELNPMR------VLLKIAKSEppTLSQPSKWSMEFR 246
                         250       260
                  ....*....|....*....|
gi 1914781966 339 SLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06644   247 DFLKTALDKHPETRPSAAQL 266
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
109-352 1.00e-20

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: 92.46  E-value: 1.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 186
Cdd:cd14071     3 DIERTIGKGNFAVVKLARHRITKT---EVAIKIIdKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMeTKDMLYLVTE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFL-QVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKA 265
Cdd:cd14071    80 YASNGEIFDYLaQHGRMSEKEARKKFW--QILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKLPikWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE-RLP--MPPNCPptlySLM 341
Cdd:cd14071   158 WCGSPP--YAAPEVFEGKEYEGPQlDIWSLGVVLY-VLVCGALPFDGSTLQTLRDRVLSGRfRIPffMSTDCE----HLI 230
                         250
                  ....*....|.
gi 1914781966 342 TKCWAYDPSRR 352
Cdd:cd14071   231 RRMLVLDPSKR 241
PTK_Jak2_rpt1 cd05078
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Janus kinase 2; Jak2 is widely ...
117-355 1.12e-20

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: 92.32  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 117 GQFGDVHQGIYMspenpaLAVAIKTCKNCTsdsvrEKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGELRS 195
Cdd:cd05078    24 GDYGQLHETEVL------LKVLDKAHRNYS-----ESFFEAASMMSQLSHKHLVLNYGVcVCGDENILVQEYVKFGSLDT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 196 FLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND--------CVKLGDFGLSRYMEDSTYYKASk 267
Cdd:cd05078    93 YLKKNKNCINILWKLEVAKQLAWAMHFLEEKTLVHGNVCAKNILLIREEdrktgnppFIKLSDPGISITVLPKDILLER- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 gklpIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPPNCppTLYSLMTKCWA 346
Cdd:cd05078   172 ----IPWVPPECIeNPKNLSLATDKWSFGTTLWEICSGGDKPLSALDSQRKLQFYEDRHQLPAPKWT--ELANLINNCMD 245

                  ....*....
gi 1914781966 347 YDPSRRPRF 355
Cdd:cd05078   246 YEPDHRPSF 254
PTK_Tyk2_rpt1 cd05076
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; Tyk2 is ...
154-355 1.22e-20

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: 92.67  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 154 FLQEALTMRQFDHPHIVKLIGVITENPVWIIM-ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRD 232
Cdd:cd05076    62 FFETASLMSQVSHTHLVFVHGVCVRGSENIMVeEFVEHGPLDVWLRKEKGHVPMAWKFVVARQLASALSYLENKNLVHGN 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 233 IAARNVLVS-------SNDCVKLGDFG-----LSRymEDSTYYkaskgklpIKWMAPESI-NFRRFTSASDVWMFGVCMW 299
Cdd:cd05076   142 VCAKNILLArlgleegTSPFIKLSDPGvglgvLSR--EERVER--------IPWIAPECVpGGNSLSTAADKWGFGATLL 211
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 300 EILMHGVKPFQGVKNNDVIGRIENGERLPmPPNCpPTLYSLMTKCWAYDPSRRPRF 355
Cdd:cd05076   212 EICFNGEAPLQSRTPSEKERFYQRQHRLP-EPSC-PELATLISQCLTYEPTQRPSF 265
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
114-353 1.24e-20

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: 92.72  E-value: 1.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQF-DHPHIVKLIGVITENP---VWIIMELCT 189
Cdd:cd07831     7 IGEGTFSEVLKAQSRKTGK---YYAIKCMKKHFKSLEQVNNLREIQALRRLsPHPNILRLIEVLFDRKtgrLALVFELMD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LgELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSNDCVKLGDFGLSRymedSTYykaskGK 269
Cdd:cd07831    84 M-NLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILI-KDDILKLADFGSCR----GIY-----SK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LP------IKWM-APESI-NFRRFTSASDVWMFGVCMWEILmhGVKP-FQGVKNNDVIGRIENGERLPMP---------- 330
Cdd:cd07831   153 PPyteyisTRWYrAPECLlTDGYYGPKMDIWAVGCVFFEIL--SLFPlFPGTNELDQIAKIHDVLGTPDAevlkkfrksr 230
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 331 ------------------PNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd07831   231 hmnynfpskkgtglrkllPNASAEGLDLLKKLLAYDPDERI 271
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
113-353 1.75e-20

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: 92.34  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 113 CIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-------GVITEnpVWII 184
Cdd:cd14056     2 TIGKGRYGEVWLGKYRGEK-----VAVKIFSSRDEDSwFRETEIYQTVMLR---HENILGFIaadikstGSWTQ--LWLI 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDFGLS-R 255
Cdd:cd14056    72 TEYHEHGSLYDYLQ--RNTLDTEEALRLAYSAASGLAHLHTEIVgtqgkpaiAHRDLKSKNILVKRDGTCCIADLGLAvR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDStyykaSKGKLPI-------KWMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK---------PFQGVK 313
Cdd:cd14056   150 YDSDT-----NTIDIPPnprvgtkRYMAPEvlddSINPKSFESfkMADIYSFGLVLWEIARRCEIggiaeeyqlPYFGMV 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 314 NND---------VIGRienGERLPMPP---NCP--PTLYSLMTKCWAYDPSRRP 353
Cdd:cd14056   225 PSDpsfeemrkvVCVE---KLRPPIPNrwkSDPvlRSMVKLMQECWSENPHARL 275
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
114-344 2.10e-20

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 92.01  E-value: 2.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiyMSPENPALAVAiKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGE 192
Cdd:cd06643    13 LGDGAFGKVYKA--QNKETGILAAA-KVIDTKSEEEL-EDYMVEIDILASCDHPNIVKLLDAFYyENNLWILIEFCAGGA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06643    89 VDAVMLELERPLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTRTLQRRDSFIGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 kWMAPESI-----NFRRFTSASDVWMFGVCMWEILM-----HGVKPFQgvknndVIGRIENGE--RLPMPPNCPPTLYSL 340
Cdd:cd06643   169 -WMAPEVVmcetsKDRPYDYKADVWSLGVTLIEMAQiepphHELNPMR------VLLKIAKSEppTLAQPSRWSPEFKDF 241

                  ....
gi 1914781966 341 MTKC 344
Cdd:cd06643   242 LRKC 245
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
161-358 2.39e-20

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 92.05  E-value: 2.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 161 MRQFDHPHIVKLIGV-ITENPVWIIMEL---CtLGELRSFLQvRKYSLDLASLILYAyqLSTALAYLESKRFV-HRDIAA 235
Cdd:cd06618    68 LKSHDCPYIVKCYGYfITDSDVFICMELmstC-LDKLLKRIQ-GPIPEDILGKMTVS--IVKALHYLKEKHGViHRDVKP 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 236 RNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPikWMAPESI---NFRRFTSASDVWMFGVCMWEiLMHGVKPFQGV 312
Cdd:cd06618   144 SNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAA--YMAPERIdppDNPKYDIRADVWSLGISLVE-LATGQFPYRNC 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 313 KNN-DVIGRIENGE--RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06618   221 KTEfEVLTKILNEEppSLPPNEGFSPDFCSFVDLCLTKDHRYRPKYREL 269
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
105-358 2.51e-20

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: 91.53  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVHQGIYM-SPENPALAVAIKTCknCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VW 182
Cdd:cd14187     6 RRRYVRGRFLGKGGFAKCYEITDAdTKEVFAGKIVPKSL--LLKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDfVY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCtlgELRSFLQV--RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd14187    84 VVLELC---RRRSLLELhkRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSL 340
Cdd:cd14187   161 GERKKTLCGTP-NYIAPEVLSKKGHSFEVDIWSIGCIMYTLLV-GKPPFETSCLKETYLRIKKNE-YSIPKHINPVAASL 237
                         250
                  ....*....|....*...
gi 1914781966 341 MTKCWAYDPSRRPRFTEL 358
Cdd:cd14187   238 IQKMLQTDPTARPTINEL 255
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
137-360 3.26e-20

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: 91.12  E-value: 3.26e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKTCKNctSDSVREKFLQEALTMR----QFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFLqvRKY-SLDLASLI 210
Cdd:cd05579    21 YAIKVIKK--RDMIRKNQVDSVLAERnilsQAQNPFVVKLYySFQGKKNLYLVMEYLPGGDLYSLL--ENVgALDEDVAR 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 211 LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKASKGKLPIK-------------WMA 276
Cdd:cd05579    97 IYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVgLVRRQIKLSIQKKSNGApekedrrivgtpdYLA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 277 PESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMP--PNCPPTLYSLMTKCWAYDPSRRP- 353
Cdd:cd05579   177 PEILLGQGHGKTVDWWSLGVILYEFLV-GIPPFHAETPEEIFQNILNG-KIEWPedPEVSDEAKDLISKLLTPDPEKRLg 254

                  ....*....
gi 1914781966 354 --RFTELKA 360
Cdd:cd05579   255 akGIEEIKN 263
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
111-358 3.37e-20

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: 90.95  E-value: 3.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFG------DVHQGIYMspenpalAVA-IKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVITENPV 181
Cdd:cd06630     5 GPLLGTGAFSscyqarDVKTGTLM-------AVKqVSFCRNSSSEQeeVVEAIREEIRMMARLNHPNIVRMLGATQHKSH 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 W-IIMELCTLGELRSFLQvrKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV-SSNDCVKLGDFG-LSRYM 257
Cdd:cd06630    78 FnIFVEWMAGGSVASLLS--KYgAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVdSTGQRLRIADFGaAARLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKASKGKL--PIKWMAPESINFRRFTSASDVWMFGVCMweILMHGVKPFQGVKNND----VIGRIENGERLP-MP 330
Cdd:cd06630   156 SKGTGAGEFQGQLlgTIAFMAPEVLRGEQYGRSCDVWSVGCVI--IEMATAKPPWNAEKISnhlaLIFKIASATTPPpIP 233
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 331 PNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06630   234 EHLSPGLRDVTLRCLELQPEDRPPAREL 261
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
100-358 3.45e-20

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: 90.93  E-value: 3.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRERIELGRcigeGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREkfLQEALTM-RQFDHPHIVKLIGVITE 178
Cdd:cd06624     6 EYDESGERVVLGK----GTFGVVYAARDLSTQ---VRIAIKEIPERDSREVQP--LHEEIALhSRLSHKNIVQYLGSVSE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVW-IIMELCTLGELRSFLQVRKYSL--DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS-NDCVKLGDFGLS 254
Cdd:cd06624    77 DGFFkIFMEQVPGGSLSALLRSKWGPLkdNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGTS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 -RYMEDSTYYKASKGKLpiKWMAPESIN--FRRFTSASDVWMFGVCMWEiLMHGVKPFqgvknndvigrIENGE------ 325
Cdd:cd06624   157 kRLAGINPCTETFTGTL--QYMAPEVIDkgQRGYGPPADIWSLGCTIIE-MATGKPPF-----------IELGEpqaamf 222
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1914781966 326 ---RLPMPPNCPPTLY----SLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06624   223 kvgMFKIHPEIPESLSeeakSFILRCFEPDPDKRATASDL 262
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
100-352 3.77e-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: 91.24  E-value: 3.77e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIqrerieLGRcIGEGQFGDVHQGIYM-SPENPALA-VAIKTCKNCTSDS-VRE-KFLQEALtmrqfDHPHIVKLIGV 175
Cdd:cd07832     1 RYKI------LGR-IGEGAHGIVFKAKDReTGETVALKkVALRKLEGGIPNQaLREiKALQACQ-----GHPYVVKLRDV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 ITENP-VWIIMELcTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd07832    69 FPHGTgFVLVFEY-MLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYM--EDSTYYKASKGKlpiKW-MAPESI-NFRRFTSASDVWMFGVCMWEILmHGVKPFQGvkNND------VI------ 318
Cdd:cd07832   148 RLFseEDPRLYSHQVAT---RWyRAPELLyGSRKYDEGVDLWAVGCIFAELL-NGSPLFPG--ENDieqlaiVLrtlgtp 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 319 --------------GRIENGERLPMP-----PNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd07832   222 nektwpeltslpdyNKITFPESKGIRleeifPDCSPEAIDLLKGLLVYNPKKR 274
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
108-353 3.81e-20

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: 91.33  E-value: 3.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRcIGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP---VWII 184
Cdd:cd06621     4 VELSS-LGEGAGGSVTKCRL---RNTKTIFALKTITTDPNPDVQKQILRELEINKSCASPYIVKYYGAFLDEQdssIGIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFL-QVRKYSLDLASLIL--YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS- 260
Cdd:cd06621    80 MEYCEGGSLDSIYkKVKKKGGRIGEKVLgkIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSl 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 -------TYYkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEIlMHGVKPF--QGVKNNDVIGRIENGERLPMP- 330
Cdd:cd06621   160 agtftgtSYY-----------MAPERIQGGPYSITSDVWSLGLTLLEV-AQNRFPFppEGEPPLGPIELLSYIVNMPNPe 227
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 331 -PNCPP-------TLYSLMTKCWAYDPSRRP 353
Cdd:cd06621   228 lKDEPEngikwseSFKDFIEKCLEKDGTRRP 258
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
149-358 5.14e-20

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


Pssm-ID: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 90.96  E-value: 5.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 149 SVREKFLQEALTMRQFDHPHIVKLIGV-ITENP-VWIIMELCTLGELRSFLQVRK-YSLDLASLIlyAYQLSTALAYLES 225
Cdd:cd06620    45 SVRKQILRELQILHECHSPYIVSFYGAfLNENNnIIICMEYMDCGSLDKILKKKGpFPEEVLGKI--AVAVLEGLTYLYN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 226 K-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS---TYYKASkgklpiKWMAPESINFRRFTSASDVWMFGVCMWEI 301
Cdd:cd06620   123 VhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSiadTFVGTS------TYMSPERIQGGKYSVKSDVWSLGLSIIEL 196
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 302 LMHGVkPFQGVKNN-----------DVIGRIENGE--RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06620   197 ALGEF-PFAGSNDDddgyngpmgilDLLQRIVNEPppRLPKDRIFPKDLRDFVDRCLLKDPRERPSPQLL 265
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
114-359 5.58e-20

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: 90.09  E-value: 5.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIY-MSPENpalaVAIKTCKNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTL 190
Cdd:cd14075    10 LGSGNFSQVKLGIHqLTKEK----VAIKILDKTKLDQKTQRLLsREISSMEKLHHPNIIRLYEVVeTLSKLHLVMEYASG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 270
Cdd:cd14075    86 GELYTKISTEGKLSESEAKPLFA-QIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTFCGSP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PikWMAPEsinfrRFTSAS------DVWMFGVcMWEILMHGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKC 344
Cdd:cd14075   165 P--YAAPE-----LFKDEHyigiyvDIWALGV-LLYFMVTGVMPFRAETVAKLKKCILEG-TYTIPSYVSEPCQELIRGI 235
                         250
                  ....*....|....*
gi 1914781966 345 WAYDPSRRPRFTELK 359
Cdd:cd14075   236 LQPVPSDRYSIDEIK 250
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
114-310 6.09e-20

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: 90.08  E-value: 6.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCKnctSDSVREK-FLQE-ALTMRQFDHPHIVKLIGVITENPVWII--MELCT 189
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTK---MALKFVP---KPSTKLKdFLREyNISLELSVHPHIIKTYDVAFETEDYYVfaQEYAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRyMEDSTyYKASK 267
Cdd:cd13987    75 YGDLFSIIPPQV-GLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCrrVKLCDFGLTR-RVGST-VKRVS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 268 GKLPikWMAPESINFRRFTS-----ASDVWMFGV---CM------WEILMHGVKPFQ 310
Cdd:cd13987   152 GTIP--YTAPEVCEAKKNEGfvvdpSIDVWAFGVllfCCltgnfpWEKADSDDQFYE 206
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
109-311 8.98e-20

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: 89.85  E-value: 8.98e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKT--CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 185
Cdd:cd14105     8 DIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKrrSKASRRGVSREDIEREVSILRQVLHPNIITLHDVFENKTdVVLIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC----VKLGDFGLSRYMEDST 261
Cdd:cd14105    88 ELVAGGELFDFL-AEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNVpiprIKLIDFGLAHKIEDGN 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQG 311
Cdd:cd14105   167 EFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLG 213
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
100-341 1.07e-19

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: 89.68  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRERIelgrcIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekFLQEALTMRQFDHPHIVKLIGVI-TE 178
Cdd:cd14201     5 DFEYSRKDL-----VGHGAFAVVFKGRHRKKTDWEVAIKSINKKNLSKSQIL--LGKEIKILKELQHENIVALYDVQeMP 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLQVrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---------SNDCVKLG 249
Cdd:cd14201    78 NSVFLVMEYCNGGDLADYLQA-KGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 250 DFGLSRYMEdSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERL-- 327
Cdd:cd14201   157 DFGFARYLQ-SNMMAATLCGSPM-YMAPEVIMSQHYDAKADLWSIGTVIYQCLV-GKPPFQANSPQDLRMFYEKNKNLqp 233
                         250
                  ....*....|....
gi 1914781966 328 PMPPNCPPTLYSLM 341
Cdd:cd14201   234 SIPRETSPYLADLL 247
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
109-352 1.18e-19

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: 89.24  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:cd14185     3 EIGRTIGDGNFAVVKE---CRHWNENQEYAMKIIDKSKLKGKEDMIESEILIIKSLSHPNIVKLFEVYeTEKEIYLILEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYMEDSTY 262
Cdd:cd14185    80 VRGGDLfDAIIESVKFTEHDAALMII--DLCEALVYIHSKHIVHRDLKPENLLVQHNPdkstTLKLADFGLAKYVTGPIF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNN--DVIGRIENGERLPMPP---NCPPTL 337
Cdd:cd14185   158 TVCGTP----TYVAPEILSEKGYGLEVDMWAAGVILY-ILLCGFPPFRSPERDqeELFQIIQLGHYEFLPPywdNISEAA 232
                         250
                  ....*....|....*
gi 1914781966 338 YSLMTKCWAYDPSRR 352
Cdd:cd14185   233 KDLISRLLVVDPEKR 247
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
148-352 1.24e-19

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: 89.24  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 148 DSVReKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESK 226
Cdd:cd05578    42 DSVR-NVLNELEILQELEHPFLVNLWYSFQdEEDMYMVVDLLLGGDLRYHLQ-QKVKFSEETVKFYICEIVLALDYLHSK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 227 RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPikWMAPESINFRRFTSASDVWMFGVCMWEILMhGV 306
Cdd:cd05578   120 NIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSGTKP--YMAPEVFMRAGYSFAVDWWSLGVTAYEMLR-GK 196
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1914781966 307 KPFQG--VKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05578   197 RPYEIhsRTSIEEIRAKFETASVLYPAGWSEEAIDLINKLLERDPQKR 244
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
106-311 1.54e-19

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: 89.28  E-value: 1.54e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSpenPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERS---TGREYALKIINKSKCRGKEHMIQNEVSILRRVKHPNIVLLIEEMdMPTELYLV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGEL-RSFLQVRKYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMED 259
Cdd:cd14183    83 MELVKGGDLfDAITSTNKYTERDASGML--YNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDG 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 260 STYYKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQG 311
Cdd:cd14183   161 PLYTVCGTP----TYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRG 207
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
147-361 1.79e-19

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: 88.60  E-value: 1.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 147 SDSVREKFLQEALTMRQFDHPHIVK-----LIGviteNPVWIIMELCTLGELRSFLQVRKYSLDL--ASLIL-YAYQLST 218
Cdd:cd08530    39 SQKEREDSVNEIRLLASVNHPNIIRykeafLDG----NRLCIVMEYAPFGDLSKLISKRKKKRRLfpEDDIWrIFIQMLR 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 219 ALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLpikWMAPESINFRRFTSASDVWMFGVCM 298
Cdd:cd08530   115 GLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKNLAKTQIGTPL---YAAPEVWKGRPYDYKSDIWSLGCLL 191
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 299 WEiLMHGVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ 361
Cdd:cd08530   192 YE-MATFRPPFEARTMQELRYKVCRGKFPPIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
109-359 2.04e-19

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: 88.62  E-value: 2.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPenpALAVAIKTCKNCTSDSV-REKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 186
Cdd:cd14074     6 DLEETLGRGHFAVVKLARHVFT---GEKVAVKVIDKTKLDDVsKAHLFQEVRCMKLVQHPNVVRLYEVIdTQTKLYLILE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-SNDCVKLGDFGLSRYMEDSTYYKA 265
Cdd:cd14074    83 LGDGGDMYDYIMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFeKQGLVKLTDFGFSNKFQPGEKLET 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKLpiKWMAPESINFRRFTS-ASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKC 344
Cdd:cd14074   163 SCGSL--AYSAPEILLGDEYDApAVDIWSLGVILY-MLVCGQPPFQEANDSETLTMIMDC-KYTVPAHVSPECKDLIRRM 238
                         250
                  ....*....|....*
gi 1914781966 345 WAYDPSRRPRFTELK 359
Cdd:cd14074   239 LIRDPKKRASLEEIE 253
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
114-358 2.46e-19

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: 88.21  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiYMSPENpALAVAIKTCKN-CTSDSVREKFLQEALTMRQF-DHPHIVKLIGVITENP-VWIIMELCTL 190
Cdd:cd13997     8 IGSGSFSEVFK--VRSKVD-GCLYAVKKSKKpFRGPKERARALREVEAHAALgQHPNIVRYYSSWEEGGhLYIQMELCEN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFL--QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd13997    85 GSLQDALeeLSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEGDS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 klpiKWMAPESIN-FRRFTSASDVWMFGVCMWEILMHGVKPfqgvKNNDVIGRIENGeRLPMPPNCPPT--LYSLMTKCW 345
Cdd:cd13997   165 ----RYLAPELLNeNYTHLPKADIFSLGVTVYEAATGEPLP----RNGQQWQQLRQG-KLPLPPGLVLSqeLTRLLKVML 235
                         250
                  ....*....|...
gi 1914781966 346 AYDPSRRPRFTEL 358
Cdd:cd13997   236 DPDPTRRPTADQL 248
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
109-352 2.91e-19

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: 88.08  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVItENP--VWIIME 186
Cdd:cd14081     4 RLGKTLGKGQTGLVKLAKH-CVTGQKVAIKIVNKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVY-ENKkyLYLVLE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd14081    82 YVSGGELFDYL-VKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLETS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLpiKWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCW 345
Cdd:cd14081   161 CGSP--HYACPEVIKGEKYDgRKADIWSCGVILYALLV-GALPFDDDNLRQLLEKVKRG-VFHIPHFISPDAQDLLRRML 236

                  ....*..
gi 1914781966 346 AYDPSRR 352
Cdd:cd14081   237 EVNPEKR 243
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
109-321 3.15e-19

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 88.47  E-value: 3.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDS-----VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVW 182
Cdd:cd14196     8 DIGEELGSGQFAIVKK---CREKSTGLEYAAKFIKKRQSRAsrrgvSREEIEREVSILRQVLHPNIITLHDVYeNRTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC----VKLGDFGLSRYME 258
Cdd:cd14196    85 LILELVSGGELFDFL-AQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIpiphIKLIDFGLAHEIE 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 259 DSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd14196   164 DGVEFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANI 223
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
114-352 3.23e-19

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: 88.05  E-value: 3.23e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENP-ALAVAIKtcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLG 191
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTfALKCVKK--RHIVQTRQQEHIFSEKEILEECNSPFIVKLYRTFKDKKyLYMLMEYCLGG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS--TY------- 262
Cdd:cd05572    79 ELWTILRDRG-LFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGrkTWtfcgtpe 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YkaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNND--VIGRIENG-ERLPMPPNCPPTLYS 339
Cdd:cd05572   158 Y-----------VAPEIILNKGYDFSVDYWSLGILLYE-LLTGRPPFGGDDEDPmkIYNIILKGiDKIEFPKYIDKNAKN 225
                         250
                  ....*....|...
gi 1914781966 340 LMTKCWAYDPSRR 352
Cdd:cd05572   226 LIKQLLRRNPEER 238
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
151-367 3.31e-19

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 87.96  E-value: 3.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFV 229
Cdd:cd14156    32 QHKIVREISLLQKLSHPNIVRYLGIcVKDEKLHPILEYVSGGCLEELLAREELPLSWREKVELACDISRGMVYLHSKNIY 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSNDCVK---LGDFGLSRYMEDSTYYKASKgKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd14156   112 HRDLNSKNCLIRVTPRGReavVTDFGLAREVGEMPANDPER-KLSLVgsafWMAPEMLRGEPYDRKVDVFSFGIVLCEIL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 303 mhgvkpfqgvknndviGRI-ENGERLP--------------MPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14156   191 ----------------ARIpADPEVLPrtgdfgldvqafkeMVPGCPEPFLDLAASCCRMDAFKRPSFAELLDELEDIAE 254
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
108-328 3.35e-19

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: 88.12  E-value: 3.35e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIYmspENPALAVAIK-TCKNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14162     2 YIVGKTLGHGSYAVVKKAYS---TKHKCKVAIKiVSKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEAIeTTSRVYII 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRKYSLDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymedsTYYK 264
Cdd:cd14162    79 MELAENGDLLDYIRKNGALPEPQARRWF-RQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR-----GVMK 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 265 ASKGKLPIK--------WMAPESINFRRFTS-ASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGERLP 328
Cdd:cd14162   153 TKDGKPKLSetycgsyaYASPEILRGIPYDPfLSDIWSMGVVLYT-MVYGRLPFDDSNLKVLLKQVQRRVVFP 224
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
151-361 4.26e-19

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: 87.48  E-value: 4.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFLQVRKYSL-DLASLILYAYQLSTALAYLESKRF 228
Cdd:cd08220    43 RQAALNEVKVLSMLHHPNIIEYYeSFLEDKALMIVMEYAPGGTLFEYIQQRKGSLlSEEEILHFFVQILLALHHVHSKQI 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSN-DCVKLGDFGLSRYMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvK 307
Cdd:cd08220   123 LHRDLKTQNILLNKKrTVVKIGDFGISKIL--SSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASLK-R 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 308 PFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ 361
Cdd:cd08220   200 AFEAANLPALVLKIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQ 253
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
114-362 4.72e-19

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


Pssm-ID: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 87.55  E-value: 4.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREkflQEALTmrQFDHPHIVKLIG-----------------VI 176
Cdd:cd14047    14 IGSGGFGQVFKAKHRIDGK---TYAIKRVKLNNEKAERE---VKALA--KLDHPNIVRYNGcwdgfdydpetsssnssRS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQVRKYS--LDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd14047    86 KTKCLFIQMEFCEKGTLESWIEKRNGEklDKVLALEIF-EQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYMEDstYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVcMWEILMHGVKpfQGVKNNDVIGRIENGErlpMPPN-- 332
Cdd:cd14047   165 TSLKN--DGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGL-ILFELLHVCD--SAFEKSKFWTDLRNGI---LPDIfd 236
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 333 -CPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd14047   237 kRYKIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
107-353 6.02e-19

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: 88.74  E-value: 6.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVIT------EN 179
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRK---VAIKKISNVFDDLIDAKrILREIKILRHLKHENIIGLLDILRppspeeFN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELctlgelrsflqvrkYSLDLASLI------------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 247
Cdd:cd07834    78 DVYIVTEL--------------METDLHKVIkspqpltddhiqYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 248 LGDFGLSRYMEDS------TYYKASkgklpiKWM-APESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQG------- 311
Cdd:cd07834   144 ICDFGLARGVDPDedkgflTEYVVT------RWYrAPELLlSSKKYTKAIDIWSVGCIFAELLTR--KPlFPGrdyidql 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 312 --------VKNNDVIGRIENGE------RLP---------MPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd07834   216 nlivevlgTPSEEDLKFISSEKarnylkSLPkkpkkplseVFPGASPEAIDLLEKMLVFNPKKRI 280
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
114-353 6.07e-19

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: 87.17  E-value: 6.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGdvhQGIYMSPENPALAVAIKTCKNC-TSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWIIMELCTLG 191
Cdd:cd08218     8 IGEGSFG---KALLVKSKEDGKQYVIKEINISkMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENgNLYIVMDYCDGG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeDSTYYKASKGKL 270
Cdd:cd08218    85 DLYKRINAQRGVLFPEDQILdWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVL-NSTVELARTCIG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PIKWMAPESINFRRFTSASDVWMFGVCMWEI--LMHgvkPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYD 348
Cdd:cd08218   164 TPYYLSPEICENKPYNNKSDIWALGCVLYEMctLKH---AFEAGNMKNLVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRN 240

                  ....*
gi 1914781966 349 PSRRP 353
Cdd:cd08218   241 PRDRP 245
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
111-358 6.45e-19

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 87.11  E-value: 6.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIymspENPALAVAIKTCKNCTSDSVR-----EKFLQEALTMRQFDHPHIVKLIGV-ITENPVWII 184
Cdd:cd06631     6 GNVLGKGAYGTVYCGL----TSTGQLIAVKQVELDTSDKEKaekeyEKLQEEVDLLKTLKHVNIVGYLGTcLEDNVVSIF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-------YM 257
Cdd:cd06631    82 MEFVPGGSIASILA-RFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAKrlcinlsSG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLP--MPPNCPP 335
Cdd:cd06631   161 SQSQLLKSMRGT-PY-WMAPEVINETGHGRKSDIWSIGCTVFEMAT-GKPPWADMNPMAAIFAIGSGRKPVprLPDKFSP 237
                         250       260
                  ....*....|....*....|...
gi 1914781966 336 TLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06631   238 EARDFVHACLTRDQDERPSAEQL 260
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
106-330 7.59e-19

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: 87.01  E-value: 7.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREkflQEALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKEHLIE---NEVSILRRVKHPNIIMLIEEMdTPAELYLV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMED 259
Cdd:cd14184    78 MELVKGGDLfDAITSSTKYTERDASAMVY--NLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 260 STYYKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKN--NDVIGRIENGE-RLPMP 330
Cdd:cd14184   156 PLYTVCGTP----TYVAPEIIAETGYGLKVDIWAAGVITY-ILLCGFPPFRSENNlqEDLFDQILLGKlEFPSP 224
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
112-358 1.10e-18

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: 86.35  E-value: 1.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHqgiYMSPENPALAVAIK----TCKNCT---SDSVRE-KFLqealtmRQFDHPHIVKLIGV-ITENPVW 182
Cdd:cd06607     7 REIGHGSFGAVY---YARNKRTSEVVAIKkmsySGKQSTekwQDIIKEvKFL------RQLRHPNTIEYKGCyLREHTAW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCtLGELRSFLQVRKYSL---DLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd06607    78 LVMEYC-LGSASDIVEVHKKPLqevEIAAICHGALQ---GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLVCP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 STYYKASkgklPIkWMAPESI---NFRRFTSASDVWMFGV-CmweilmhgvkpfqgvknndvigrIENGERLP------- 328
Cdd:cd06607   154 ANSFVGT----PY-WMAPEVIlamDEGQYDGKVDVWSLGItC-----------------------IELAERKPplfnmna 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 329 ------MPPNCPPTL---------YSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06607   206 msalyhIAQNDSPTLssgewsddfRNFVDSCLQKIPQDRPSAEDL 250
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
114-353 1.11e-18

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: 86.16  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDSVrekFLQEALTMRQFDHPHIVKLIGVITEnPVWIIMELCTLGEL 193
Cdd:cd14068     2 LGDGGFGSVYRAVYRGED-----VAVKIFNKHTSFRL---LRQELVVLSHLHHPSLVALLAAGTA-PRMLVMELAPKGSL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 194 RSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS--NDC---VKLGDFGLSRYMeDSTYYKASKG 268
Cdd:cd14068    73 DALLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTlyPNCaiiAKIADYGIAQYC-CRMGIKTSEG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KLPIKwmAPESINFR-RFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERLPMPP---NCP--PTLYSLMT 342
Cdd:cd14068   152 TPGFR--APEVARGNvIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDELAIQGKLPDPVkeyGCApwPGVEALIK 229
                         250
                  ....*....|.
gi 1914781966 343 KCWAYDPSRRP 353
Cdd:cd14068   230 DCLKENPQCRP 240
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
114-309 1.22e-18

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


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 87.12  E-value: 1.22e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDV----HQGIymspenpALAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGV--------ITEN 179
Cdd:cd13989     1 LGSGGFGYVtlwkHQDT-------GEYVAIKKCRqeLSPSDKNRERWCLEVQIMKKLNHPNVVSARDVppeleklsPNDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVwIIMELCTLGELRSFL-QVRKYS----LDLASLIlyaYQLSTALAYLESKRFVHRDIAARN-VLVSSNDCV--KLGDF 251
Cdd:cd13989    74 PL-LAMEYCSGGDLRKVLnQPENCCglkeSEVRTLL---SDISSAISYLHENRIIHRDLKPENiVLQQGGGRViyKLIDL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 252 GLSRYMEDSTYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd13989   150 GYAKELDQGSLCTSFVGTL--QYLAPELFESKKYTCTVDYWSFGTLAFECIT-GYRPF 204
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
104-358 1.31e-18

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: 86.34  E-value: 1.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 104 QRERIELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVW 182
Cdd:cd06648     5 PRSDLDNFVKIGEGSTGIVCIATDKSTGR---QVAVKK-MDLRKQQRRELLFNEVVIMRDYQHPNIVEMYSsYLVGDELW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 261
Cdd:cd06648    81 VVMEFLEGGALTDIVtHTRMNEEQIATVCRAVLK---ALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGE--RLPMPPNCPPTLYS 339
Cdd:cd06648   158 PRRKSLVGTPY-WMAPEVISRLPYGTEVDIWSLGIMVIE-MVDGEPPYFNEPPLQAMKRIRDNEppKLKNLHKVSPRLRS 235
                         250
                  ....*....|....*....
gi 1914781966 340 LMTKCWAYDPSRRPRFTEL 358
Cdd:cd06648   236 FLDRMLVRDPAQRATAAEL 254
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
110-353 1.35e-18

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: 86.07  E-value: 1.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSPENPaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI--TENPVWIIMEL 187
Cdd:cd14164     4 LGTTIGEGSFSKVKLATSQKYCCK-VAIKIVDRRRASPDFVQKFLPRELSILRRVNHPNIVQMFECIevANGRLYIVMEA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGLSRYMED----STY 262
Cdd:cd14164    83 AATDLLQKIQEVHHIPKDLARDMFA--QMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDypelSTT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGklpikWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGvknnDVIGRIENGERlpmPPNCPPTLySLM 341
Cdd:cd14164   161 FCGSRA-----YTPPEVILGTPYDPKKyDVWSLGVVLY-VMVTGTMPFDE----TNVRRLRLQQR---GVLYPSGV-ALE 226
                         250
                  ....*....|....*....
gi 1914781966 342 TKCWA-------YDPSRRP 353
Cdd:cd14164   227 EPCRAlirtllqFNPSTRP 245
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
107-358 1.41e-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: 86.25  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFG------DVHQGIYmspenpalaVAIKTCKNCTSDSVREKFLQEALTMRQFD-------HPHIVKLI 173
Cdd:cd13993     1 RYQLISPIGEGAYGvvylavDLRTGRK---------YAIKCLYKSGPNSKDGNDFQKLPQLREIDlhrrvsrHPNIITLH 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 174 GVI-TENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAY-QLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGD 250
Cdd:cd13993    72 DVFeTEVAIYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFlQLIDAVKHCHSLGIYHRDIKPENILLSQDEgTVKLCD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 251 FGLSryMEDSTYYKASKGKLpiKWMAPESI--NFRRF----TSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENG 324
Cdd:cd13993   152 FGLA--TTEKISMDFGVGSE--FYMAPECFdeVGRSLkgypCAAGDIWSLGIILLNLTF-GRNPWKIASESDPIFYDYYL 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 325 ER-------LPMPPNCpptlYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd13993   227 NSpnlfdviLPMSDDF----YNLLRQIFTVNPNNRILLPEL 263
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
125-365 1.79e-18

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: 86.07  E-value: 1.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 125 GIYmspENPALAVAIKTCKNCT-SDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQVRKY 202
Cdd:cd14045    26 GIY---DGRTVAIKKIAKKSFTlSKRIR----KEVKQVRELDHPNLCKFIGGCIEVPnVAIITEYCPKGSLNDVLLNEDI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 203 SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS--KGKLPIKWMAPE-- 278
Cdd:cd14045    99 PLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASgyQQRLMQVYLPPEnh 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 279 SINFRRFTSASDVWMFGVCMWEIlmhgvkpfqgVKNNDVIGR----IENGERLPMPP--------NCP-PTLY-SLMTKC 344
Cdd:cd14045   179 SNTDTEPTQATDVYSYAIILLEI----------ATRNDPVPEddysLDEAWCPPLPElisgktenSCPcPADYvELIRRC 248
                         250       260
                  ....*....|....*....|.
gi 1914781966 345 WAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14045   249 RKNNPAQRPTFEQIKKTLHKI 269
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
105-368 1.90e-18

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 86.03  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRC---IGEGQFGDVHQgiyMSPENPALAVAIKTCKnctsdsVREKFLQEALTMRQFDHPHIVKLIGVITENP- 180
Cdd:cd13991     2 REEVHWATHqlrIGRGSFGEVHR---MEDKQTGFQCAVKKVR------LEVFRAEELMACAGLTSPRVVPLYGAVREGPw 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVR-KYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSnDCVK--LGDFGLSRYM 257
Cdd:cd13991    73 VNIFMDLKEGGSLGQLIKEQgCLPEDRA--LHYLGQALEGLEYLHSRKILHGDVKADNVLLSS-DGSDafLCDFGHAECL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKA--SKGKLP--IKWMAPESINFRRFTSASDVWMfGVCMWEILMHGVKPFQGVKNNDVIGRIENgERLPM---P 330
Cdd:cd13991   150 DPDGLGKSlfTGDYIPgtETHMAPEVVLGKPCDAKVDVWS-SCCMMLHMLNGCHPWTQYYSGPLCLKIAN-EPPPLreiP 227
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1914781966 331 PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEE 368
Cdd:cd13991   228 PSCAPLTAQAIQAGLRKEPVHRASAAELRRKTNRALQE 265
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
114-317 2.33e-18

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: 85.36  E-value: 2.33e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVAIKtcknCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKFIK----CRKAKDREDVRNEIEIMNQLRHPRLLQLYDAFeTPREMVLVMEYVAGGE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LrsFLQV--RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd14103    77 L--FERVvdDDFELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGnqIKIIDFGLARKYDPDKKLKVLFG 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 269 KlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGvkNNDV 317
Cdd:cd14103   155 T-P-EFVAPEVVNYEPISYATDMWSVGVICY-VLLSGLSPFMG--DNDA 198
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
109-358 2.63e-18

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: 85.94  E-value: 2.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRcigeGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDSVREKFLQEA-LTMRQFDHPHIVKLIGVI-TENPVWIIME 186
Cdd:cd06617     8 ELGR----GAYGVVDK---MRHVPTGTIMAVKRIRATVNSQEQKRLLMDLdISMRSVDCPYTVTFYGALfREGDVWICME 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDLASLILYAYQLS--TALAYLESK-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 263
Cdd:cd06617    81 VMDTSLDKFYKKVYDKGLTIPEDILGKIAVSivKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVAK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLPikWMAPESIN----FRRFTSASDVWMFGVCMWEILMHGV------KPFQGVKNndVIGriENGERLPMPPnC 333
Cdd:cd06617   161 TIDAGCKP--YMAPERINpelnQKGYDVKSDVWSLGITMIELATGRFpydswkTPFQQLKQ--VVE--EPSPQLPAEK-F 233
                         250       260
                  ....*....|....*....|....*
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06617   234 SPEFQDFVNKCLKKNYKERPNYPEL 258
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
114-303 3.10e-18

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: 85.88  E-value: 3.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMspENPalaVAIKT----CKNCTsdsVREKFLQEALTMRqfdHPHIVKLIGV---ITENPVW---I 183
Cdd:cd14054     3 IGQGRYGTVWKGSLD--ERP---VAVKVfparHRQNF---QNEKDIYELPLME---HSNILRFIGAderPTADGRMeylL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKR---------FVHRDIAARNVLVSSN-DCVkLGDFGL 253
Cdd:cd14054    72 VLEYAPKGSLCSYL--RENTLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADgSCV-ICDFGL 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 254 SRYMEDSTYYK----ASKGKLP-----IKWMAPE----SINFRRFTSA---SDVWMFGVCMWEILM 303
Cdd:cd14054   149 AMVLRGSSLVRgrpgAAENASIsevgtLRYMAPEvlegAVNLRDCESAlkqVDVYALGLVLWEIAM 214
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
111-310 3.19e-18

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 84.98  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCT 189
Cdd:cd14189     6 GRLLGKGGFARCYEMTDLA-TNKTYAVKVIPHSRVAKPHQREKIVNEIELHRDLHHKHVVKFSHHFEDaENIYIFLELCS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd14189    85 RKSLAHIWKARHTLLE-PEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKKTICG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 270 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQ 310
Cdd:cd14189   164 TP-NYLAPEVLLRQGHGPESDVWSLGCVMYTLLC-GNPPFE 202
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
109-352 4.52e-18

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: 84.92  E-value: 4.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVhqgiYMSPENP-----ALAVAIKTckNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VW 182
Cdd:cd14117     9 DIGRPLGKGKFGNV----YLAREKQskfivALKVLFKS--QIEKEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKrIY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdSTY 262
Cdd:cd14117    83 LILEYAPRGELYKELQ-KHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAP-SLR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMT 342
Cdd:cd14117   161 RRTMCGTL--DYLPPEMIEGRTHDEKVDLWCIGVLCYELLV-GMPPFESASHTETYRRIVKVD-LKFPPFLSDGSRDLIS 236
                         250
                  ....*....|
gi 1914781966 343 KCWAYDPSRR 352
Cdd:cd14117   237 KLLRYHPSER 246
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
114-357 4.80e-18

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: 84.34  E-value: 4.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMspENPALAVAIK--TCKNCT-SDSVREKflqEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCT 189
Cdd:cd14120     1 IGHGAFAVVFKGRHR--KKPDLPVAIKciTKKNLSkSQNLLGK---EIKILKELSHENVVALLDCqETSSSVYLVMEYCN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-SNDC--------VKLGDFGLSRYMEDS 260
Cdd:cd14120    76 GGDLADYLQA-KGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLShNSGRkpspndirLKIADFGFARFLQDG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE-NGERLP-MPPNCPPTLY 338
Cdd:cd14120   155 MMAATLCGS-PM-YMAPEVIMSLQYDAKADLWSIGTIVYQCLT-GKAPFQAQTPQELKAFYEkNANLRPnIPSGTSPALK 231
                         250
                  ....*....|....*....
gi 1914781966 339 SLMTKCWAYDPSRRPRFTE 357
Cdd:cd14120   232 DLLLGLLKRNPKDRIDFED 250
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
101-311 8.79e-18

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: 84.54  E-value: 8.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRErielgrcIGEGQFGDVHQGIYMSPENPalaVAIKTCKNctsDSVREKF----LQEALTMRQFDHPHIVKLIGVI 176
Cdd:cd07840     1 YEKIAQ-------IGEGTYGQVYKARNKKTGEL---VALKKIRM---ENEKEGFpitaIREIKLLQKLDHPNVVRLKEIV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENP-------VWIIMELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLG 249
Cdd:cd07840    68 TSKGsakykgsIYMVFEYMD-HDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLA 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 250 DFGLSRYMEdstyyKASKGKLPIK----WMAPESINF--RRFTSASDVWMFGVCMWEILmHGVKPFQG 311
Cdd:cd07840   147 DFGLARPYT-----KENNADYTNRvitlWYRPPELLLgaTRYGPEVDMWSVGCILAELF-TGKPIFQG 208
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
152-361 8.80e-18

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: 84.25  E-value: 8.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 152 EKFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKYSLDLASLilYAYQLSTALAYLESKRF 228
Cdd:cd14199    70 ERVYQEIAILKKLDHPNVVKLVEVLddpSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARF--YFQDLIKGIEYLHYQKI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESINFRR--FT-SASDVWMFGVCMWeILMHG 305
Cdd:cd14199   148 IHRDVKPSNLLVGEDGHIKIADFGVSNEFEGSDALLTNTVGTP-AFMAPETLSETRkiFSgKALDVWAMGVTLY-CFVFG 225
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 306 VKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ 361
Cdd:cd14199   226 QCPFMDERILSLHSKIKTQPlEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLH 282
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
109-358 9.72e-18

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: 84.29  E-value: 9.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQgIYMSPENPALAVAIKTCKNCTSDSVREKF-LQEALTmrqfDHPHIVKLIG------VITENPV 181
Cdd:cd06638    21 EIIETIGKGTYGKVFK-VLNKKNGSKAAVKILDPIHDIDEEIEAEYnILKALS----DHPNVVKFYGmyykkdVKNGDQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTAL---AYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd06638    96 WLVLELCNGGSVTDLVKGFLKRGERMEEPIIAYILHEALmglQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNC 333
Cdd:cd06638   176 STRLRRNTSVGTPF-WMAPEVIACEQqldstYDARCDVWSLGITAIE-LGDGDPPLADLHPMRALFKI--------PRNP 245
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1914781966 334 PPTLYS----------LMTKCWAYDPSRRPRFTEL 358
Cdd:cd06638   246 PPTLHQpelwsnefndFIRKCLTKDYEKRPTVSDL 280
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
110-359 1.07e-17

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: 83.69  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSPENPALA--VAIKTCKNCT-SDSVRE-KFLQEALTMRQFDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14076     5 LGRTLGEGEFGKVKLGWPLPKANHRSGvqVAIKLIRRDTqQENCQTsKIMREINILKGLTHPNIVRLLDVLkTKKYIGIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST--Y 262
Cdd:cd14076    85 LEFVSGGELFDYILARRRLKDSVACRLFA-QLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFDHFNgdL 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKlPIkWMAPESINFRRFTSAS--DVWMFGVCMWEILMhGVKPFQGVKNN---DVIGR----IENGErLPMPPNC 333
Cdd:cd14076   164 MSTSCGS-PC-YAAPELVVSDSMYAGRkaDIWSCGVILYAMLA-GYLPFDDDPHNpngDNVPRlyryICNTP-LIFPEYV 239
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 334 PPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14076   240 TPKARDLLRRILVPNPRKRIRLSAIM 265
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
114-311 1.16e-17

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: 83.43  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd14190    12 LGGGKFGKVHT---CTEKRTGLKLAAKVINKQNSKD-KEMVLLEIQVMNQLNHRNLIQLYEAIeTPNEIVLFMEYVEGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSNDCVKLGDFGLSRYMEDSTYYKASKGKl 270
Cdd:cd14190    88 LFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLARRYNPREKLKVNFGT- 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 271 PiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQG 311
Cdd:cd14190   167 P-EFLSPEVVNYDQVSFPTDMWSMGVITY-MLLSGLSPFLG 205
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
132-402 1.27e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 86.61  E-value: 1.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 132 NPALAVAIKTCKNCTSDSVREKFL------------QEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ 198
Cdd:PTZ00267   78 NPTTAAFVATRGSDPKEKVVAKFVmlnderqaayarSELHCLAACDHFGIVKHFDDFkSDDKLLLIMEYGSGGDLNKQIK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 199 VR-KYSLDLAS--LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK-ASKGKLPIKW 274
Cdd:PTZ00267  158 QRlKEHLPFQEyeVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDvASSFCGTPYY 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 275 MAPESINFRRFTSASDVWMFGVCMWEIL-MHgvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:PTZ00267  238 LAPELWERKRYSKKADMWSLGVILYELLtLH--RPFKGPSQREIMQQVLYGKYDPFPCPVSSGMKALLDPLLSKNPALRP 315
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 354 R-----FTELKAQLSTILEE-----EKAQQEERMRMESRRQatvswdsgGSDEAPPKPS 402
Cdd:PTZ00267  316 TtqqllHTEFLKYVANLFQDivrhsETISPHDREEILRQLQ--------ESGERAPPPS 366
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
111-358 1.50e-17

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: 83.14  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCT 189
Cdd:cd14188     6 GKVLGKGGFAKCYEMTDLT-TNKVYAAKIIPHSRVSKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKEnIYILLEYCS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDlASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd14188    85 RRSMAHILKARKVLTE-PEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEPLEHRRRTICG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd14188   164 TP-NYLSPEVLNKQGHGCESDIWALGCVMYTMLL-GRPPFETTNLKETYRCIREA-RYSLPSSLLAPAKHLIASMLSKNP 240

                  ....*....
gi 1914781966 350 SRRPRFTEL 358
Cdd:cd14188   241 EDRPSLDEI 249
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
114-387 1.64e-17

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: 83.63  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd14086     9 LGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARD--HQKLEREARICRLLKHPNIVRLHDSIsEEGFHYLVFDLVTGGE 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRK-YSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd14086    87 LFEDIVAREfYSEADASHCI--QQILESVNHCHQNGIVHRDLKPENLLLASkskGAAVKLADFGLAIEVQGDQQAWFGFA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGeRLPMPPN----CPPTLYSLMTKC 344
Cdd:cd14086   165 GTP-GYLSPEVLRKDPYGKPVDIWACGVILY-ILLVGYPPFWDEDQHRLYAQIKAG-AYDYPSPewdtVTPEAKDLINQM 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1914781966 345 WAYDPSRRPRFTELkaqlstiLEEEKAQQEERMRMESRRQATV 387
Cdd:cd14086   242 LTVNPAKRITAAEA-------LKHPWICQRDRVASMVHRQETV 277
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
137-357 2.62e-17

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


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 83.76  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKTC----KNCTsDS---VRE-KFLQEaLTmrqfDHPHIVKLIGVI-TEN--PVWIIMElctlgelrsFLQVrkyslD 205
Cdd:cd07852    35 VALKKIfdafRNAT-DAqrtFREiMFLQE-LN----DHPNIIKLLNVIrAENdkDIYLVFE---------YMET-----D 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 206 LASLI----------LY-AYQLSTALAYLESKRFVHRDIAARNVLVSSnDC-VKLGDFGLSRY---MEDS------TYYK 264
Cdd:cd07852    95 LHAVIraniledihkQYiMYQLLKALKYLHSGGVIHRDLKPSNILLNS-DCrVKLADFGLARSlsqLEEDdenpvlTDYV 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASkgklpiKWM-APE----SinfRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGRIENG-------------- 324
Cdd:cd07852   174 AT------RWYrAPEillgS---TRYTKGVDMWSVGCILGEMLLG--KPlFPGTSTLNQLEKIIEVigrpsaediesiqs 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 325 -------ERLP---------MPPNCPPTLYSLMTKCWAYDPSRRPRFTE 357
Cdd:cd07852   243 pfaatmlESLPpsrpksldeLFPKASPDALDLLKKLLVFNPNKRLTAEE 291
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
114-321 2.90e-17

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: 82.36  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekflQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGE 192
Cdd:cd14191    10 LGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIR----QEISIMNCLHHPKLVQCVDAFEEKAnIVMVLEMVSGGE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSNDCVKLGDFGLSRYMEDSTYYKASKGKl 270
Cdd:cd14191    86 LFERIIDEDFELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCvnKTGTKIKLIDFGLARRLENAGSLKVLFGT- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 271 PiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd14191   165 P-EFVAPEVINYEPIGYATDMWSIGVICY-ILVSGLSPFMGDNDNETLANV 213
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
111-359 3.08e-17

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: 82.43  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGIYMspeNPALAVAIKTCKNCTSDSVREKFLQ---------EALTMRQFDHPHIVKLIGV-ITENP 180
Cdd:cd06629     6 GELIGKGTYGRVYLAMNA---TTGEMLAVKQVELPKTSSDRADSRQktvvdalksEIDTLKDLDHPNIVQYLGFeETEDY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQ-VRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd06629    83 FSIFLEYVPGGSIGSCLRkYGKFEEDLVRFFTR--QILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKKSDD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 StyYKASKG---KLPIKWMAPESI-NFRRFTSAS-DVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERL-PMPP-- 331
Cdd:cd06629   161 I--YGNNGAtsmQGSVFWMAPEVIhSQGQGYSAKvDIWSLGCVVLEMLA-GRRPWSDDEAIAAMFKLGNKRSApPVPEdv 237
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 332 NCPPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd06629   238 NLSPEALDFLNACFAIDPRDRPTAAELL 265
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
90-309 3.09e-17

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 83.71  E-value: 3.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  90 EDTYTMPSTRDYEIQRerIELGRCIGEGQFGDVH------QGIYMspenpalavAIKTCKNctSDSVREK----FLQEAL 159
Cdd:PTZ00263    4 AYMFTKPDTSSWKLSD--FEMGETLGTGSFGRVRiakhkgTGEYY---------AIKCLKK--REILKMKqvqhVAQEKS 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 160 TMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARN 237
Cdd:PTZ00263   71 ILMELSHPFIVNMMcSFQDENRVYFLLEFVVGGELFTHLRkAGRFPNDVAKF--YHAELVLAFEYLHSKDIIYRDLKPEN 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 238 VLVSSNDCVKLGDFGLSRYMEDSTYYKASKgklPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:PTZ00263  149 LLLDNKGHVKVTDFGFAKKVPDRTFTLCGT---P-EYLAPEVIQSKGHGKAVDWWTMGVLLYEFIA-GYPPF 215
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
114-301 3.20e-17

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: 83.16  E-value: 3.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCtLGE 192
Cdd:cd06633    29 IGHGSFGAVYFATN-SHTNEVVAIKKMSYSGKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCyLKDHTAWLVMEYC-LGS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKgklpi 272
Cdd:cd06633   107 ASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTP----- 181
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1914781966 273 KWMAPESI---NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd06633   182 YWMAPEVIlamDEGQYDGKVDIWSLGITCIEL 213
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
106-357 3.69e-17

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: 82.97  E-value: 3.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYmSPENPALAVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVW 182
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIH-RETGQQFAVKIVDVAKFTSSPglSTEDLKREASICHMLKHPHIVELLETYsSDGMLY 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELrSFLQVRK------YSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC---VKLGDFGL 253
Cdd:cd14094    82 MVFEFMDGADL-CFEIVKRadagfvYSEAVASH--YMRQILEALRYCHDNNIIHRDVKPHCVLLASKENsapVKLGGFGV 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKnNDVIGRIENGeRLPMPPNC 333
Cdd:cd14094   159 AIQLGESGLVAGGRVGTP-HFMAPEVVKREPYGKPVDVWGCGVILF-ILLSGCLPFYGTK-ERLFEGIIKG-KYKMNPRQ 234
                         250       260
                  ....*....|....*....|....*...
gi 1914781966 334 PPTLYS----LMTKCWAYDPSRRPRFTE 357
Cdd:cd14094   235 WSHISEsakdLVRRMLMLDPAERITVYE 262
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
114-312 3.79e-17

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: 82.47  E-value: 3.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiYMSPENPALAVAIKTCKNCTSD-SVREKFLQEALTMRQFD---HPHIVKLIGVITENP-VWIIMELC 188
Cdd:cd14052     8 IGSGEFSQVYK--VSERVPTGKVYAVKKLKPNYAGaKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGhLYIQTELC 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFL--QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG------LSRYME-- 258
Cdd:cd14052    86 ENGSLDVFLseLGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGmatvwpLIRGIEre 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 259 -DSTYykaskgklpikwMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPFQGV 312
Cdd:cd14052   166 gDREY------------IAPEILSEHMYDKPADIFSLGLILLEAAANVVLPDNGD 208
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
114-358 3.94e-17

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: 82.37  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEAL----TMRQFDHPHIVKLIGV--ITENPVWIIMEL 187
Cdd:cd13990     8 LGKGGFSEVYKAFDLV-EQRYVACKIHQLNKDWSEEKKQNYIKHALreyeIHKSLDHPRIVKLYDVfeIDTDSFCTVLEY 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFL-QVRKYSLDLASLILYayQLSTALAYLESKR--FVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDST 261
Cdd:cd13990    87 CDGNDLDFYLkQHKSIPEREARSIIM--QVVSALKYLNEIKppIIHYDLKPGNILLHSGNvsgEIKITDFGLSKIMDDES 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYK-----ASKGKLPIKWMAPESI----NFRRFTSASDVWMFGVCMWEILmHGVKPF------QGVKNNDVIGRIENGEr 326
Cdd:cd13990   165 YNSdgmelTSQGAGTYWYLPPECFvvgkTPPKISSKVDVWSVGVIFYQML-YGRKPFghnqsqEAILEENTILKATEVE- 242
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1914781966 327 LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd13990   243 FPSKPVVSSEAKDFIRRCLTYRKEDRPDVLQL 274
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
161-362 4.37e-17

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: 82.26  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 161 MRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQVRKYSLD---LASLIlyaYQLSTALAYLESKrfvhrDIAAR 236
Cdd:cd14042    56 MRDLQHDNLTRFIGACVDPPnICILTEYCPKGSLQDILENEDIKLDwmfRYSLI---HDIVKGMHYLHDS-----EIKSH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 237 NVLVSSNdCV-------KLGDFGLSRYMEDSTY----YKASKGKLpikWMAPE--SINFR--RFTSASDVWMFGVCMWEI 301
Cdd:cd14042   128 GNLKSSN-CVvdsrfvlKITDFGLHSFRSGQEPpddsHAYYAKLL---WTAPEllRDPNPppPGTQKGDVYSFGIILQEI 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 302 lMHGVKPFqGVKNND------VIGRIENGERLPMPPN-----CPPTLYSLMTKCWAYDPSRRPRFTELKAQL 362
Cdd:cd14042   204 -ATRQGPF-YEEGPDlspkeiIKKKVRNGEKPPFRPSldeleCPDEVLSLMQRCWAEDPEERPDFSTLRNKL 273
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
112-366 4.79e-17

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: 82.27  E-value: 4.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCT--SDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELC 188
Cdd:cd14026     3 RYLSRGAFGTVSRARHADWRVT---VAIKCLKLDSpvGDSERNCLLKEAEILHKARFSYILPILGICNEPEFLgIVTEYM 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQVRKYSLDLASLILYA--YQLSTALAYLE--SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 264
Cdd:cd14026    80 TNGSLNELLHEKDIYPDVAWPLRLRilYEIALGVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQLSISQS 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLP----IKWMAPESINFRRFTSAS---DVWMFGVCMWEILMHGVkPFQGVKNN-DVIGRIENGER-------LPM 329
Cdd:cd14026   160 RSSKSAPeggtIIYMPPEEYEPSQKRRASvkhDIYSYAIIMWEVLSRKI-PFEEVTNPlQIMYSVSQGHRpdtgedsLPV 238
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1914781966 330 PPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd14026   239 DIPHRATLINLIESGWAQNPDERPSFLKCLIELEPVL 275
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
114-358 5.02e-17

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: 82.35  E-value: 5.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiyMSPENPALAVAIKTCkNCTSDsVREKFLQEALTMRQF-DHPHIVKLIGVITE------NPVWIIME 186
Cdd:cd06639    30 IGKGTYGKVYK---VTNKKDGSLAAVKIL-DPISD-VDEEIEAEYNILRSLpNHPNVVKFYGMFYKadqyvgGQLWLVLE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLG---ELRSFLQVRKYSLD--LASLILYAYQLstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 261
Cdd:cd06639   105 LCNGGsvtELVKGLLKCGQRLDeaMISYILYGALL--GLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEIL--------MHGVKPFqgvknndvigriengerLP 328
Cdd:cd06639   183 LRRNTSVGTPF-WMAPEVIACEQqydysYDARCDVWSLGITAIELAdgdpplfdMHPVKAL-----------------FK 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1914781966 329 MPPNCPPTLYS----------LMTKCWAYDPSRRPRFTEL 358
Cdd:cd06639   245 IPRNPPPTLLNpekwcrgfshFISQCLIKDFEKRPSVTHL 284
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
114-353 5.83e-17

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: 81.93  E-value: 5.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDV-HQGIYMSPENPALAVAIKTCKNCTS-------------DSVRE--KFLQEALTMRQFDHPHIVKLIGvIT 177
Cdd:cd14067     1 LGQGGSGTViYRARYQGQPVAVKRFHIKKCKKRTDgsadtmlkhlraaDAMKNfsEFRQEASMLHSLQHPCIVYLIG-IS 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFLQVRKYS---LDLASLILY--AYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-----VK 247
Cdd:cd14067    80 IHPLCFALELAPLGSLNTVLEENHKGssfMPLGHMLTFkiAYQIAAGLAYLHKKNIIFCDLKSDNILVWSLDVqehinIK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 248 LGDFGLSR--YMEDSTYYKASKGklpikWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14067   160 LSDYGISRqsFHEGALGVEGTPG-----YQAPEIRPRIVYDEKVDMFSYGMVLYE-LLSGQRPSLGHHQLQIAKKLSKGI 233
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 326 R--LPMPPNCP-PTLYSLMTKCWAYDPSRRP 353
Cdd:cd14067   234 RpvLGQPEEVQfFRLQALMMECWDTKPEKRP 264
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
107-365 6.74e-17

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: 81.59  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYmspeNPALAVAIKTCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIM 185
Cdd:cd14153     1 QLEIGELIGKGRFGQVYHGRW----HGEVAIRLIDIERDNEEQLK-AFKREVMAYRQTRHENVVLFMGACMSPPhLAIIT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVsSNDCVKLGDFGL---SRYMEDSTy 262
Cdd:cd14153    76 SLCKGRTLYSVVRDAKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGKVVITDFGLftiSGVLQAGR- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 yKASKGKLPIKW---MAPESI---------NFRRFTSASDVWMFGVCMWEilMHGVK-PFQGVKNNDVIGRIENGerlpM 329
Cdd:cd14153   154 -REDKLRIQSGWlchLAPEIIrqlspeteeDKLPFSKHSDVFAFGTIWYE--LHAREwPFKTQPAEAIIWQVGSG----M 226
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 330 PPNCP-----PTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14153   227 KPNLSqigmgKEISDILLFCWAYEQEERPTFSKLMEMLEKL 267
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
114-352 6.79e-17

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: 81.37  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVH------QGIYMspenpalavAIKTCKNCTSDS---VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 183
Cdd:cd05611     4 ISKGAFGSVYlakkrsTGDYF---------AIKVLKKSDMIAknqVTNVKAERAIMMIQGESPYVAKLYYSFqSKDYLYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 263
Cdd:cd05611    75 VMEYLNGGDCASLIKTLGG-LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPN----CPPTLYS 339
Cdd:cd05611   154 KKFVGT-P-DYLAPETILGVGDDKMSDWWSLGCVIFEFLF-GYPPFHAETPDAVFDNILSR-RINWPEEvkefCSPEAVD 229
                         250
                  ....*....|...
gi 1914781966 340 LMTKCWAYDPSRR 352
Cdd:cd05611   230 LINRLLCMDPAKR 242
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
110-358 7.42e-17

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: 80.98  E-value: 7.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVhQGIYMSPENPALAVAIKTCKNCTSDSVrEKFL-QEALTMRQFDHPHIVKL--IGVITENPVWIIME 186
Cdd:cd14165     5 LGINLGEGSYAKV-KSAYSERLKCNVAIKIIDKKKAPDDFV-EKFLpRELEILARLNHKSIIKTyeIFETSDGKVYIVME 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdstyyKAS 266
Cdd:cd14165    83 LGVQGDLLEFIKLRG-ALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRCL-----RDE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIK--------WMAPESINFRRFT-SASDVWMFGVCMWeILMHGVKPFQGvKNNDVIGRIENGERLPMPPNCPPT- 336
Cdd:cd14165   157 NGRIVLSktfcgsaaYAAPEVLQGIPYDpRIYDIWSLGVILY-IMVCGSMPYDD-SNVKKMLKIQKEHRVRFPRSKNLTs 234
                         250       260
                  ....*....|....*....|...
gi 1914781966 337 -LYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14165   235 eCKDLIYRLLQPDVSQRLCIDEV 257
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
117-357 8.86e-17

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: 81.61  E-value: 8.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 117 GQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREkflQEALTMRQFDHPHIVKLIGV--ITENPV---WIIMELCTL 190
Cdd:cd14053     6 GRFGAVWKAQYLNRL-----VAVKIFPLQEKQSwLTE---REIYSLPGMKHENILQFIGAekHGESLEaeyWLITEFHER 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRkySLDLASLILYAYQLSTALAYLESKR----------FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd14053    78 GSLCDYLKGN--VISWNELCKIAESMARGLAYLHEDIpatngghkpsIAHRDFKSKNVLLKSDLTACIADFGLALKFEPG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIK-WMAPE----SINFRR--FTsASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIENGERlpmppnc 333
Cdd:cd14053   156 KSCGDTHGQVGTRrYMAPEvlegAINFTRdaFL-RIDMYAMGLVLWELLSRCSVHDGPVDEYQLPFEEEVGQH------- 227
                         250       260
                  ....*....|....*....|....
gi 1914781966 334 pPTLySLMTKCWAyDPSRRPRFTE 357
Cdd:cd14053   228 -PTL-EDMQECVV-HKKLRPQIRD 248
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
109-321 9.11e-17

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: 81.20  E-value: 9.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 185
Cdd:cd14195     8 EMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSSRRgvSREEIEREVNILREIQHPNIITLHDIFeNKTDVVLIL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMEDST 261
Cdd:cd14195    88 ELVSGGELFDFL-AEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLldknVPNPRIKLIDFGIAHKIEAGN 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd14195   167 EFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGETKQETLTNI 223
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
109-352 9.14e-17

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: 80.95  E-value: 9.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQG----------IYMSPENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVI- 176
Cdd:cd14077     4 EFVKTIGAGSMGKVKLAkhirtgekcaIKIIPRASNAGLKKEREKRLEKEISRDIrTIREAALSSLLNHPHICRLRDFLr 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd14077    84 TPNHYYMLFEYVDGGQLLDYI-ISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLSNL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDSTYYKASKGKLpiKWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGeRLPMPPNCPP 335
Cdd:cd14077   163 YDPRRLLRTFCGSL--YFAAPELLQAQPYTGPEvDVWSFGVVLY-VLVCGKVPFDDENMPALHAKIKKG-KVEYPSYLSS 238
                         250
                  ....*....|....*..
gi 1914781966 336 TLYSLMTKCWAYDPSRR 352
Cdd:cd14077   239 ECKSLISRMLVVDPKKR 255
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
112-358 9.89e-17

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: 80.55  E-value: 9.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVhqGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG-VITENPVWIIMELCTL 190
Cdd:cd08221     6 RVLGRGAFGEA--VLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNhFLDGESLFIEMEYCNG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSL-DLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeDSTYYKASKGK 269
Cdd:cd08221    84 GNLHDKIAQQKNQLfPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVL-DSESSMAESIV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd08221   163 GTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLK-RTFDATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDP 241

                  ....*....
gi 1914781966 350 SRRPRFTEL 358
Cdd:cd08221   242 EDRPTAEEL 250
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
106-358 1.18e-16

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 82.18  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN-PVWII 184
Cdd:PLN00034   74 SELERVNRIGSGAGGTVYKVIHRPTGRL---YALKVIYGNHEDTVRRQICREIEILRDVNHPNVVKCHDMFDHNgEIQVL 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSflqvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeDSTYYK 264
Cdd:PLN00034  151 LEFMDGGSLEG-----THIADEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL-AQTMDP 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIKWMAPESINF-----RRFTSASDVWMFGVCMWEILMhGVKPFQGVKNND---VIGRIENGERLPMPPNCPPT 336
Cdd:PLN00034  225 CNSSVGTIAYMSPERINTdlnhgAYDGYAGDIWSLGVSILEFYL-GRFPFGVGRQGDwasLMCAICMSQPPEAPATASRE 303
                         250       260
                  ....*....|....*....|..
gi 1914781966 337 LYSLMTKCWAYDPSRRPRFTEL 358
Cdd:PLN00034  304 FRHFISCCLQREPAKRWSAMQL 325
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
114-323 1.19e-16

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: 80.39  E-value: 1.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPALAVAIKTckncTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd14192    12 LGGGRFGQVHKCTELSTGLTLAAKIIKV----KGAKEREEVKNEINIMNQLNHVNLIQLYDAFeSKTNLTLIMEYVDGGE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV--SSNDCVKLGDFGLSRYMEDSTYYKASKGKl 270
Cdd:cd14192    88 LFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCvnSTGNQIKIIDFGLARRYKPREKLKVNFGT- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 271 PiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIEN 323
Cdd:cd14192   167 P-EFLAPEVVNYDFVSFPTDMWSVGVITY-MLLSGLSPFLGETDAETMNNIVN 217
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
114-358 1.33e-16

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: 80.36  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCkNCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTLGE 192
Cdd:cd06647    15 IGQGASGTVYTAIDVATGQ---EVAIKQM-NLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06647    91 LTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-ENGE-RLPMPPNCPPTLYSLMTKCWAYDPS 350
Cdd:cd06647   169 -WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIaTNGTpELQNPEKLSAIFRDFLNRCLEMDVE 246

                  ....*...
gi 1914781966 351 RRPRFTEL 358
Cdd:cd06647   247 KRGSAKEL 254
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
106-321 1.94e-16

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: 80.06  E-value: 1.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVW 182
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSSRRgvSREDIEREVSILKEIQHPNVITLHEVYeNKTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC----VKLGDFGLSRYME 258
Cdd:cd14194    85 LILELVAGGELFDFL-AEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVpkprIKIIDFGLAHKID 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 259 DSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd14194   164 FGNEFKNIFGT-P-EFVAPEIVNYEPLGLEADMWSIGVITY-ILLSGASPFLGDTKQETLANV 223
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
101-321 2.46e-16

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 79.57  E-value: 2.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIelgrcIGEGQFGDVHQGIYMSPenpALAVAIKTCKnCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TEN 179
Cdd:cd14193     4 YNVNKEEI-----LGGGRFGQVHKCEEKSS---GLKLAAKIIK-ARSQKEKEEVKNEIEVMNQLNHANLIQLYDAFeSRN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYM 257
Cdd:cd14193    75 DIVLVMEYVDGGELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREAnqVKIIDFGLARRY 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 258 EDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd14193   155 KPREKLRVNFGT-P-EFLAPEVVNYEFVSFPTDMWSLGVIAY-MLLSGLSPFLGEDDNETLNNI 215
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
105-365 3.27e-16

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: 79.85  E-value: 3.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVHQGiYMSPENPALAVAIKTCKNCTSDsVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-I 183
Cdd:cd14158    14 RPISVGGNKLGEGGFGVVFKG-YINDKNVAVKKLAAMVDISTED-LTKQFEQEIQVMAKCQHENLVELLGYSCDGPQLcL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQVRKYSLDLA--SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DS 260
Cdd:cd14158    92 VYTYMPNGSLLDRLACLNDTPPLSwhMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEkFS 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIKWMAPESINfRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN----DVIGRIENGERL--------- 327
Cdd:cd14158   172 QTIMTERIVGTTAYMAPEALR-GEITPKSDIFSFGVVLLEIIT-GLPPVDENRDPqlllDIKEEIEDEEKTiedyvdkkm 249
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1914781966 328 -PMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14158   250 gDWDSTSIEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
114-309 3.42e-16

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: 79.62  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVhqgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVK-------LIGVITENPVWIIME 186
Cdd:cd14038     2 LGTGGFGNV---LRWINQETGEQVAIKQCRQELSPKNRERWCLEIQIMKRLNHPNVVAardvpegLQKLAPNDLPLLAME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDL--ASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDST 261
Cdd:cd14038    79 YCQGGDLRKYLNQFENCCGLreGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEqrlIHKIIDLGYAKELDQGS 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1914781966 262 YYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd14038   159 LCTSFVGTL--QYLAPELLEQQKYTVTVDYWSFGTLAFECIT-GFRPF 203
PHA02988 PHA02988
hypothetical protein; Provisional
86-364 3.59e-16

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 79.40  E-value: 3.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  86 IIDEEDTYTMPSTRDYEIQRERIELgrcIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS--VREKFLQEALTMRQ 163
Cdd:PHA02988    3 IITRSYINDIKCIESDDIDKYTSVL---IKENDQNSIYKGIFNNKE-----VIIRTFKKFHKGHkvLIDITENEIKNLRR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 164 FDHPHIVKLIGVITENP-----VWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESK-RFVHRDIAARN 237
Cdd:PHA02988   75 IDSNNILKIYGFIIDIVddlprLSLILEYCTRGYLREVLDKEK-DLSFKTKLDMAIDCCKGLYNLYKYtNKPYKNLTSVS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 238 VLVSSNDCVKLGDFGLSRYMEDSTYYKaskgklpIKWMAPESIN-----FRRFTSASDVWMFGVCMWEILMhGVKPFQGV 312
Cdd:PHA02988  154 FLVTENYKLKIICHGLEKILSSPPFKN-------VNFMVYFSYKmlndiFSEYTIKDDIYSLGVVLWEIFT-GKIPFENL 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 313 KNNDVIGRI--ENGErLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLST 364
Cdd:PHA02988  226 TTKEIYDLIinKNNS-LKLPLDCPLEIKCIVEACTSHDSIKRPNIKEILYNLSL 278
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
107-352 3.92e-16

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: 80.14  E-value: 3.92e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQF-DHPHIVKLIG--VITE---N 179
Cdd:cd07857     1 RYELIKELGQGAYGIVCSARNAE-TSEEETVAIKKITNVFSKKILAKrALRELKLLRHFrGHKNITCLYDmdIVFPgnfN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMEL--CTLGE-LRSFLQvrkysLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR- 255
Cdd:cd07857    80 ELYLYEELmeADLHQiIRSGQP-----LTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARg 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDS-------TYYKASkgklpiKWM-APE-SINFRRFTSASDVWMFGVCMWEILmhGVKPF----------------Q 310
Cdd:cd07857   155 FSENPgenagfmTEYVAT------RWYrAPEiMLSFQSYTKAIDVWSVGCILAELL--GRKPVfkgkdyvdqlnqilqvL 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 311 GVKNNDVIGRI------ENGERLPMPPNCP-PTLY--------SLMTKCWAYDPSRR 352
Cdd:cd07857   227 GTPDEETLSRIgspkaqNYIRSLPNIPKKPfESIFpnanplalDLLEKLLAFDPTKR 283
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
155-352 4.20e-16

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: 79.97  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQVRK---YSLDLASLilYAYQLSTALAYLESKRFVH 230
Cdd:cd05574    49 LTEREILATLDHPFLPTLYASFqTSTHLCFVMDYCPGGELFRLLQKQPgkrLPEEVARF--YAAEVLLALEYLHLLGFVY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 231 RDIAARNVLVSSNDCVKLGDFGLS------------RYMEDSTYYKASKGKLPIK----------------WMAPESINF 282
Cdd:cd05574   127 RDLKPENILLHESGHIMLTDFDLSkqssvtpppvrkSLRKGSRRSSVKSIEKETFvaepsarsnsfvgteeYIAPEVIKG 206
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 283 RRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05574   207 DGHGSAVDWWTLGILLYEML-YGTTPFKGSNRDETFSNILKKElTFPESPPVSSEAKDLIRKLLVKDPSKR 276
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
109-360 4.28e-16

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 79.06  E-value: 4.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGvITENP--VWIIME 186
Cdd:cd14098     3 QIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDKNLQLFQREINILKSLEHPGIVRLID-WYEDDqhIYLVME 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND--CVKLGDFGLSRYMEDSTYYK 264
Cdd:cd14098    82 YVEGGDLMDFI-MAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGLAKVIHTGTFLV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLpiKWMAPESINFRR------FTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIENGeRLPMPP----NCP 334
Cdd:cd14098   161 TFCGTM--AYLAPEILMSKEqnlqggYSNLVDMWSVG-CLVYVMLTGALPFDGSSQLPVEKRIRKG-RYTQPPlvdfNIS 236
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 335 PTLYSLMTKCWAYDPSRRPrfTELKA 360
Cdd:cd14098   237 EEAIDFILRLLDVDPEKRM--TAAQA 260
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
151-358 4.70e-16

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: 78.81  E-value: 4.70e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLIGV---ITENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR 227
Cdd:cd13983    44 RQRFKQEIEILKSLKHPNIIKFYDSwesKSKKEVIFITELMTSGTLKQYLK-RFKRLKLKVIKSWCRQILEGLNYLHTRD 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 228 --FVHRDIAARNVLVSSND-CVKLGDFGLSRYMedstyyKASKGKLPI---KWMAPEsINFRRFTSASDVWMFGVCMWEi 301
Cdd:cd13983   123 ppIIHRDLKCDNIFINGNTgEVKIGDLGLATLL------RQSFAKSVIgtpEFMAPE-MYEEHYDEKVDIYAFGMCLLE- 194
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 302 LMHGVKPFQGVKNN-DVIGRIENGErlpmPPNC-----PPTLYSLMTKCWAyDPSRRPRFTEL 358
Cdd:cd13983   195 MATGEYPYSECTNAaQIYKKVTSGI----KPESlskvkDPELKDFIEKCLK-PPDERPSAREL 252
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
106-309 5.29e-16

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: 78.58  E-value: 5.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIY-MSPENpalaVAIKTC--KNCTSDSVREKFLQEAltMRQFDHPHIVKLIGVI-TENPV 181
Cdd:cd14078     3 KYYELHETIGSGGFAKVKLATHiLTGEK----VAIKIMdkKALGDDLPRVKTEIEA--LKNLSHQHICRLYHVIeTDNKI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDST 261
Cdd:cd14078    77 FMVLEYCPGGELFDYI-VAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGM 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 262 YYKASKGKLPIKWMAPESINFRRFT-SASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14078   156 DHHLETCCGSPAYAAPELIQGKPYIgSEADVWSMGVLLY-ALLCGFLPF 203
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
105-301 7.33e-16

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: 78.55  E-value: 7.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekflQEALTMRQFDHPHIVKLIG-VITENPVWI 183
Cdd:cd06645    10 QEDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQ----QEIIMMKDCKHSNIVAYFGsYLRRDKLWI 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYY 263
Cdd:cd06645    86 CMEFCGGGSLQDIYHVTG-PLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIAK 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 264 KASKGKLPIkWMAPESINFRR---FTSASDVWMFGVCMWEI 301
Cdd:cd06645   165 RKSFIGTPY-WMAPEVAAVERkggYNQLCDIWAVGITAIEL 204
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
114-358 8.47e-16

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: 77.73  E-value: 8.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiYMSPENPALaVAIKTCKNC-TSDSVREKFLQEALTMRQF-DHPHIVKLIGVITE-NPVWIIMELCTL 190
Cdd:cd14050     9 LGEGSFGEVFK--VRSREDGKL-YAVKRSRSRfRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWEEkGILYIQTELCDT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 gelrSFLQ--VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd14050    86 ----SLQQycEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KlpIKWMAPESINfRRFTSASDVWMFGVCMWEI-----LMHGVKPFQGVKNNDVIGRIENGerlpMPPNCPPTLYSLMTK 343
Cdd:cd14050   162 D--PRYMAPELLQ-GSFTKAADIFSLGITILELacnleLPSGGDGWHQLRQGYLPEEFTAG----LSPELRSIIKLMMDP 234
                         250
                  ....*....|....*
gi 1914781966 344 cwayDPSRRPRFTEL 358
Cdd:cd14050   235 ----DPERRPTAEDL 245
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
165-352 1.05e-15

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: 78.80  E-value: 1.05e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 165 DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSS 242
Cdd:cd05570    54 RHPFLTGLHACFqTEDRLYFVMEYVNGGDLMFHIQrARRFTEERA--RFYAAEICLALQFLHERGIIYRDLKLDNVLLDA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 243 NDCVKLGDFGLSRymEDSTYYKASK---GKLpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIG 319
Cdd:cd05570   132 EGHIKIADFGMCK--EGIWGGNTTStfcGTP--DYIAPEILREQDYGFSVDWWALGVLLYEMLA-GQSPFEGDDEDELFE 206
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1914781966 320 RIENGE-RLP--MPPNCPPTLYSLMTKcwayDPSRR 352
Cdd:cd05570   207 AILNDEvLYPrwLSREAVSILKGLLTK----DPARR 238
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
215-367 1.35e-15

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 80.30  E-value: 1.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 215 QLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKG--KLPIkWMAPESINFRRFTSASDVW 292
Cdd:PTZ00283  151 QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTfcGTPY-YVAPEIWRRKPYSKKADMF 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 293 MFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL------KAQLSTIL 366
Cdd:PTZ00283  230 SLGVLLYELLTLK-RPFDGENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPSSSKLlnmpicKLFISGLL 308

                  .
gi 1914781966 367 E 367
Cdd:PTZ00283  309 E 309
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
112-301 1.41e-15

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: 78.14  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELCtL 190
Cdd:cd06634    21 REIGHGSFGAVYFARDVR-NNEVVAIKKMSYSGKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCyLREHTAWLVMEYC-L 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKgkl 270
Cdd:cd06634    99 GSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPANSFVGTP--- 175
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1914781966 271 piKWMAPESI---NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd06634   176 --YWMAPEVIlamDEGQYDGKVDVWSLGITCIEL 207
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
106-310 1.59e-15

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: 77.21  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMspeNPALAVAIKTC--KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVW 182
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSL---HTGLEVAIKMIdkKAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFEDsNYVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRK--YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd14186    78 LVLEMCHNGEMSRYLKNRKkpFTEDEARHFMH--QIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMP 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQ 310
Cdd:cd14186   156 HEKHFTMCGTP-NYISPEIATRSAHGLESDVWSLG-CMFYTLLVGRPPFD 203
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
136-353 1.59e-15

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: 77.31  E-value: 1.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 136 AVAIK-TCKNCTSDSVRE-KFLQEAltmrqFDHPHIVKLIGV-ITENPVWIIMELC--TLGEL----RSFLQVRKYSLDL 206
Cdd:cd13982    27 PVAVKrLLPEFFDFADREvQLLRES-----DEHPNVIRYFCTeKDRQFLYIALELCaaSLQDLvespRESKLFLRPGLEP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 207 ASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-----VKLGDFGLSRYMED--STYYKASKGKLPIKWMAPES 279
Cdd:cd13982   102 VRLL---RQIASGLAHLHSLNIVHRDLKPQNILISTPNAhgnvrAMISDFGLCKKLDVgrSSFSRRSGVAGTSGWIAPEM 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 280 IN---FRRFTSASDVWMFGVCMWEILMHGVKPFQG--VKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd13982   179 LSgstKRRQTRAVDIFSLGCVFYYVLSGGSHPFGDklEREANILKGKYSLDKLLSLGEHGPEAQDLIERMIDFDPEKRP 257
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
105-309 1.79e-15

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: 77.03  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKtCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGvITENP--V 181
Cdd:cd14083     2 RDKYEFKEVLGTGAFSEV---VLAEDKATGKLVAIK-CIDKKALKGKEDSLEnEIAVLRKIKHPNIVQLLD-IYESKshL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRyM 257
Cdd:cd14083    77 YLVMELVTGGELfDRIVEKGSYTEKDASHLIR--QVLEAVDYLHSLGIVHRDLKPENLLYYSPDedsKIMISDFGLSK-M 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 258 EDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14083   154 EDSGVMSTACGT-P-GYVAPEVLAQKPYGKAVDCWSIGVISY-ILLCGYPPF 202
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
114-358 2.07e-15

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: 77.20  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgIYMSPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGE 192
Cdd:cd06622     9 LGKGNYGSVYK-VLHRPTG--VTMAMKEIRLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFiEGAVYMCMEYMDAGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFL--QVRKYSLDLASLILYAYQLSTALAYL-ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdstyykASKGK 269
Cdd:cd06622    86 LDKLYagGVATEGIPEDVLRRITYAVVKGLKFLkEEHNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLV------ASLAK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPI---KWMAPESINFR------RFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGR---IENGERLPMPPNCPPTL 337
Cdd:cd06622   160 TNIgcqSYMAPERIKSGgpnqnpTYTVQSDVWSLGLSILEMAL-GRYPYPPETYANIFAQlsaIVDGDPPTLPSGYSDDA 238
                         250       260
                  ....*....|....*....|.
gi 1914781966 338 YSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06622   239 QDFVAKCLNKIPNRRPTYAQL 259
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
114-354 2.55e-15

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: 76.58  E-value: 2.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHqgIYMSPENPALAV-AIKTCKNCTSDSVREKF----LQEALTMRQFDHPHIVKLIGV-ITENPVW-IIME 186
Cdd:cd13994     1 IGKGATSVVR--IVTKKNPRSGVLyAVKEYRRRDDESKRKDYvkrlTSEYIISSKLHHPNIVKVLDLcQDLHGKWcLVME 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS---RYMEDST-- 261
Cdd:cd13994    79 YCPGGDLFTLI-EKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAevfGMPAEKEsp 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKLPikWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLPMPPNCPPTLYS 339
Cdd:cd13994   158 MSAGLCGSEP--YMAPEVFTSGSYDgRAVDVWSCGIVLFALFT-GRFPWRSAKKSDSAYKAyEKSGDFTNGPYEPIENLL 234
                         250       260
                  ....*....|....*....|.
gi 1914781966 340 LMT-KCWAY-----DPSRRPR 354
Cdd:cd13994   235 PSEcRRLIYrmlhpDPEKRIT 255
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
106-419 2.87e-15

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 79.45  E-value: 2.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHqgiymspenpaLA--------VAIKTCKN--CTSDSVREKFLQEALTMRQFDHPHIVKLIGV 175
Cdd:NF033483    7 GRYEIGERIGRGGMAEVY-----------LAkdtrldrdVAVKVLRPdlARDPEFVARFRREAQSAASLSHPNIVSVYDV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 ITENPV-WIIMEL---CTLGEL---RSFLQVRKySLDLASLILyayqlsTALAYLESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:NF033483   76 GEDGGIpYIVMEYvdgRTLKDYireHGPLSPEE-AVEIMIQIL------SALEHAHRNGIVHRDIKPQNILITKDGRVKV 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDST-----------YYkaskgklpikwMAPE-----SINFRrftsaSDVWMFGVCMWEILMhGVKPFQGv 312
Cdd:NF033483  149 TDFGIARALSSTTmtqtnsvlgtvHY-----------LSPEqarggTVDAR-----SDIYSLGIVLYEMLT-GRPPFDG- 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 313 knndvigriEN---------GERLPMP----PNCPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILEEEKAqQEERMR 378
Cdd:NF033483  211 ---------DSpvsvaykhvQEDPPPPselnPGIPQSLDAVVLKATAKDPDDRYQsAAEMRADLETALSGQRL-NAPKFA 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 379 MESRRQATVSWDSGGSDEAPPKPSRPGYPSPRSSEGFYPSP 419
Cdd:NF033483  281 PDSDDDRTKVLPPIPPAPAPTAAEPPEDPDDDGEGGEPADD 321
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
114-359 3.07e-15

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: 77.03  E-value: 3.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQG---IYMSPENPALAVAIKTCKNCTSDSvREKflqEALTMRQFDHPHIVKLI-----GVITENPVWIIM 185
Cdd:cd14055     3 VGKGRFAEVWKAklkQNASGQYETVAVKIFPYEEYASWK-NEK---DIFTDASLKHENILQFLtaeerGVGLDRQYWLIT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRF---------VHRDIAARNVLVSSN-DCVkLGDFGLSR 255
Cdd:cd14055    79 AYHENGSLQDYL--TRHILSWEDLCKMAGSLARGLAHLHSDRTpcgrpkipiAHRDLKSSNILVKNDgTCV-LADFGLAL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDSTYYK--ASKGKL-PIKWMAPES----INFRRFTS--ASDVWMFGVCMWEI-----LMHGVKPFQ----------- 310
Cdd:cd14055   156 RLDPSLSVDelANSGQVgTARYMAPEAlesrVNLEDLESfkQIDVYSMALVLWEMasrceASGEVKPYElpfgskvrerp 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 311 ---GVKNNDVIGRiengERLPMPP--NCPPTLYSL---MTKCWAYDPSRR-------PRFTELK 359
Cdd:cd14055   236 cveSMKDLVLRDR----GRPEIPDswLTHQGMCVLcdtITECWDHDPEARltascvaERFNELK 295
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
100-354 3.52e-15

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: 76.90  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHQGIYMSpENPALAVAI--KTCKNCtSDSVrekflqEALtMRQFDHPHIVKLIGV-I 176
Cdd:cd14091     1 EYEIKEE-------IGKGSYSVCKRCIHKA-TGKEYAVKIidKSKRDP-SEEI------EIL-LRYGQHPNIITLRDVyD 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRS-FLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLVSSN----DCVKLGDF 251
Cdd:cd14091    65 DGNSVYLVTELLRGGELLDrILRQKFFSEREASAVMKT--LTKTVEYLHSQGVVHRDLKPSNILYADEsgdpESLRICDF 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 252 GLSRYMedstyyKASKGKL--PI---KWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKN---NDVIGRIEN 323
Cdd:cd14091   143 GFAKQL------RAENGLLmtPCytaNFVAPEVLKKQGYDAACDIWSLGVLLY-TMLAGYTPFASGPNdtpEVILARIGS 215
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1914781966 324 GeRLPMP-PN---CPPTLYSLMTKCWAYDPSRRPR 354
Cdd:cd14091   216 G-KIDLSgGNwdhVSDSAKDLVRKMLHVDPSQRPT 249
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
107-386 3.58e-15

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


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 77.51  E-value: 3.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFG------DVHQGiymspenpaLAVAIKTCKNC---TSDSVRekFLQEALTMRQFDHPHIVKLIGVI- 176
Cdd:cd07859     1 RYKIQEVIGKGSYGvvcsaiDTHTG---------EKVAIKKINDVfehVSDATR--ILREIKLLRLLRHPDIVEIKHIMl 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 -----TENPVWIIMELctlgeLRSFL-QVRKYSLDLAS--LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKL 248
Cdd:cd07859    70 ppsrrEFKDIYVVFEL-----MESDLhQVIKANDDLTPehHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRYMEDS-------TYYKASkgklpiKWM-APESIN--FRRFTSASDVWMFGvCMWEILMHGvKP---------- 308
Cdd:cd07859   145 CDFGLARVAFNDtptaifwTDYVAT------RWYrAPELCGsfFSKYTPAIDIWSIG-CIFAEVLTG-KPlfpgknvvhq 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 309 ------FQGVKNNDVIGRIENGE----------RLPMP-----PNCPPTLYSLMTKCWAYDPSRRPRFTELKAQ-----L 362
Cdd:cd07859   217 ldlitdLLGTPSPETISRVRNEKarrylssmrkKQPVPfsqkfPNADPLALRLLERLLAFDPKDRPTAEEALADpyfkgL 296
                         330       340
                  ....*....|....*....|....*
gi 1914781966 363 STILEEEKAQQEERMRME-SRRQAT 386
Cdd:cd07859   297 AKVEREPSAQPITKLEFEfERRRLT 321
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
119-365 4.91e-15

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: 75.91  E-value: 4.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 119 FGDVHQGIYMSPENPALAVA-------IKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPVW-IIMELCTL 190
Cdd:cd14043     1 PSSPSSTSSVNATSSNTGVAyegdwvwLKKFPGGSHTELRPSTKNVFSKLRELRHENVNLFLGLFVDCGILaIVSEHCSR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDL---ASLILyayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd14043    81 GSLEDLLRNDDMKLDWmfkSSLLL---DLIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGYNEILEAQNLPLPEP 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPIKWMAPESIN----FRRFTSASDVWMFGVCMWEILMHGvKPF--QGVKNNDVIGRIengeRLPmPPNC-------- 333
Cdd:cd14043   158 APEELLWTAPELLRdprlERRGTFPGDVFSFAIIMQEVIVRG-APYcmLGLSPEEIIEKV----RSP-PPLCrpsvsmdq 231
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1914781966 334 -PPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14043   232 aPLECIQLMKQCWSEAPERRPTFDQIFDQFKSI 264
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
114-358 6.71e-15

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: 75.91  E-value: 6.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPenpALAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTLGE 192
Cdd:cd06656    27 IGQGASGTVYTAIDIAT---GQEVAIKQ-MNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGS 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06656   103 LTDV--VTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 273 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-ENGE-RLPMPPNCPPTLYSLMTKCWAYDPS 350
Cdd:cd06656   181 -WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIaTNGTpELQNPERLSAVFRDFLNRCLEMDVD 258

                  ....*...
gi 1914781966 351 RRPRFTEL 358
Cdd:cd06656   259 RRGSAKEL 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
149-311 6.80e-15

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: 75.47  E-value: 6.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 149 SVREKFLQE-ALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESK 226
Cdd:cd14106    49 DCRNEILHEiAVLELCKDCPRVVNLHEVYeTRSELILILELAAGGELQTLL-DEEECLTEADVRRLMRQILEGVQYLHER 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 227 RFVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDSTYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWeILM 303
Cdd:cd14106   128 NIVHLDLKPQNILLTSefpLGDIKLCDFGISRVIGEGEEIREILGTP--DYVAPEILSYEPISLATDMWSIGVLTY-VLL 204

                  ....*...
gi 1914781966 304 HGVKPFQG 311
Cdd:cd14106   205 TGHSPFGG 212
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
152-359 7.15e-15

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: 75.76  E-value: 7.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 152 EKFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKYSLDLASLilYAYQLSTALAYLESKRF 228
Cdd:cd14200    68 ERVYQEIAILKKLDHVNIVKLIEVLddpAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARL--YFRDIVLGIEYLHYQKI 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESI--NFRRFT-SASDVWMFGVCMWeILMHG 305
Cdd:cd14200   146 VHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDALLSSTAGTP-AFMAPETLsdSGQSFSgKALDVWAMGVTLY-CFVYG 223
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 306 VKPFQGVKNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14200   224 KCPFIDEFILALHNKIKNKPvEFPEEPEISEELKDLILKMLDKNPETRITVPEIK 278
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
112-365 7.84e-15

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 75.59  E-value: 7.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSpENPALAVAIKTCKnctSDSVREKFLQEALTMRqfdHPHIVKLIGV-ITENPVW----IIME 186
Cdd:cd14144     1 RSVGKGRYGEVWKGKWRG-EKVAVKIFFTTEE---ASWFRETEIYQTVLMR---HENILGFIAAdIKGTGSWtqlyLITD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRkySLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDFGLS-RYM 257
Cdd:cd14144    74 YHENGSLYDFLRGN--TLDTQSMLKLAYSAACGLAHLHTEIFgtqgkpaiAHRDIKSKNILVKKNGTCCIADLGLAvKFI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTYYKASKG-KLPIK-WMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK---------PFQGVKNND---- 316
Cdd:cd14144   152 SETNEVDLPPNtRVGTKrYMAPEvldeSLNRNHFDAykMADMYSFGLVLWEIARRCISggiveeyqlPYYDAVPSDpsye 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 317 VIGRIENGERL-PMPPN------CPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14144   232 DMRRVVCVERRrPSIPNrwssdeVLRTMSKLMSECWAHNPAARLTALRVKKTLGKL 287
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
114-332 7.91e-15

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: 75.14  E-value: 7.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLG 191
Cdd:cd14082    11 LGSGQFGIVYGGKH---RKTGRDVAIKVIDKLRFPTKQESQLRnEVAILQQLSHPGVVNLECMFeTPERVFVVMEKLHGD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC---VKLGDFGLSRYMEDSTYYKASKG 268
Cdd:cd14082    88 MLEMILSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARIIGEKSFRRSVVG 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 269 KlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQgvKNNDVIGRIENGERLpMPPN 332
Cdd:cd14082   168 T-P-AYLAPEVLRNKGYNRSLDMWSVGVIIY-VSLSGTFPFN--EDEDINDQIQNAAFM-YPPN 225
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
106-366 9.83e-15

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 75.55  E-value: 9.83e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSpENpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLIG--VITENP-- 180
Cdd:cd14142     5 RQITLVECIGKGRYGEVWRGQWQG-ES----VAVKIFSSRDEKSwFRETEIYNTVLLR---HENILGFIAsdMTSRNSct 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 -VWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDF 251
Cdd:cd14142    77 qLWLITHYHENGSLYDYLQ--RTTLDHQEMLRLALSAASGLVHLHTEIFgtqgkpaiAHRDLKSKNILVKSNGQCCIADL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 252 GLsrymedSTYYKASKGKLPI---------KWMAP----ESINFRRFTS--ASDVWMFGVCMWEI----LMHGV-----K 307
Cdd:cd14142   155 GL------AVTHSQETNQLDVgnnprvgtkRYMAPevldETINTDCFESykRVDIYAFGLVLWEVarrcVSGGIveeykP 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 308 PFQGVKNND--------VIgrIENGERlPMPPN---CPPTLYS---LMTKCWAYDPSRRPRFTELKAQLSTIL 366
Cdd:cd14142   229 PFYDVVPSDpsfedmrkVV--CVDQQR-PNIPNrwsSDPTLTAmakLMKECWYQNPSARLTALRIKKTLLKIL 298
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
60-386 1.04e-14

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 77.00  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  60 PKLANSEKQGMRTHAVSVSETDDYAEIIDEEDTYTmpSTRDYEiqrerieLGRCIGEGQFGDVHQGIYMspeNPALAVAI 139
Cdd:PTZ00036   29 EMNDKKLDEEERSHNNNAGEDEDEEKMIDNDINRS--PNKSYK-------LGNIIGNGSFGVVYEAICI---DTSEKVAI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 140 KtcknctsdsvreKFLQ-------EALTMRQFDHPHIVKLIGVI-------TENPVW--IIMELC--TLGELRSFLQVRK 201
Cdd:PTZ00036   97 K------------KVLQdpqyknrELLIMKNLNHINIIFLKDYYytecfkkNEKNIFlnVVMEFIpqTVHKYMKHYARNN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 202 YSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGLSRYM---EDSTYYKASKgklpiKWMAP 277
Cdd:PTZ00036  165 HALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNThTLKLCDFGSAKNLlagQRSVSYICSR-----FYRAP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 278 E-SINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLP-------MPPN----------------- 332
Cdd:PTZ00036  240 ElMLGATNYTTHIDLWSLGCIIAEMIL-GYPIFSGQSSVDQLVRIIQVLGTPtedqlkeMNPNyadikfpdvkpkdlkkv 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 333 ----CPPTLYSLMTKCWAYDPSRR---------PRFTELK----------AQLSTILEEEKAQQEErMRMESRRQAT 386
Cdd:PTZ00036  319 fpkgTPDDAINFISQFLKYEPLKRlnpiealadPFFDDLRdpciklpkyiDKLPDLFNFCDAEIKE-MSDACRRKII 394
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
151-324 1.13e-14

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: 74.47  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLIGVITENP--VWIIMELCTLGELRSFLQVRKYSLDLASLI-LYAYQLSTALAYLESKR 227
Cdd:cd14109    40 DPFLMREVDIHNSLDHPNIVQMHDAYDDEKlaVTVIDNLASTIELVRDNLLPGKDYYTERQVaVFVRQLLLALKHMHDLG 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 228 FVHRDIAARNVLVSsNDCVKLGDFGLSRYMEDSTYYKASKGkLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVK 307
Cdd:cd14109   120 IAHLDLRPEDILLQ-DDKLKLADFGQSRRLLRGKLTTLIYG-SP-EFVSPEIVNSYPVTLATDMWSVGVLTY-VLLGGIS 195
                         170
                  ....*....|....*..
gi 1914781966 308 PFQGVKNNDVIGRIENG 324
Cdd:cd14109   196 PFLGDNDRETLTNVRSG 212
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
109-352 1.17e-14

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: 75.16  E-value: 1.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIY-MSPENPALAV-AIktcknctSDSVREKFLQ----EALTMRQFDHPHIVKLIGVI-TENPV 181
Cdd:cd05612     4 ERIKTIGTGTFGRVHLVRDrISEHYYALKVmAI-------PEVIRLKQEQhvhnEKRVLKEVSHPFIIRLFWTEhDQRFL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd05612    77 YMLMEYVPGGELFSYLRnSGRFSNSTG--LFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKgklPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGeRLPMPPNCPPTLYSL 340
Cdd:cd05612   155 TWTLCGT---P-EYLAPEVIQSKGHNKAVDWWALGILIYEMLV-GYPPFFDDNPFGIYEKILAG-KLEFPRHLDLYAKDL 228
                         250
                  ....*....|..
gi 1914781966 341 MTKCWAYDPSRR 352
Cdd:cd05612   229 IKKLLVVDRTRR 240
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
114-321 1.24e-14

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: 74.85  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiymSPENPALAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlG 191
Cdd:cd07860     8 IGEGTYGVVYKA---RNKLTGEVVALKKIRlDTETEGVPSTAIREISLLKELNHPNIVKLLDVIhTENKLYLVFEFLH-Q 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY--MEDSTYykaSKG 268
Cdd:cd07860    84 DLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAfgVPVRTY---THE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 269 KLPIKWMAPES-INFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd07860   161 VVTLWYRAPEIlLGCKYYSTAVDIWSLG-CIFAEMVTRRALFPGDSEIDQLFRI 213
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
94-309 1.29e-14

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 75.79  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  94 TMPSTRDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAlaVAIKTCKNCTSdsVREKFLQEALTMRQF----DHPHI 169
Cdd:PTZ00426   18 TKEPKRKNKMKYEDFNFIRTLGTGSFGRVILATYKNEDFPP--VAIKRFEKSKI--IKQKQVDHVFSERKIlnyiNHPFC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 170 VKLIGVIT-ENPVWIIMELCTLGELRSFLQVRK-YSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 247
Cdd:PTZ00426   94 VNLYGSFKdESYLYLVLEFVIGGEFFTFLRRNKrFPNDVGCF--YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIK 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 248 LGDFGLSRYMEDSTYYKASKGklpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:PTZ00426  172 MTDFGFAKVVDTRTYTLCGTP----EYIAPEILLNVGHGKAADWWTLGIFIYEILV-GCPPF 228
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
110-358 1.33e-14

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: 74.68  E-value: 1.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQgIYMSPENPALAVA-IKTCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI---TENPVWII 184
Cdd:cd06653     6 LGKLLGRGAFGEVYL-CYDADTGRELAVKqVPFDPDSQETSKEVNALEcEIQLLKNLRHDRIVQYYGCLrdpEEKKLSIF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSflQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEdsTYY 263
Cdd:cd06653    85 VEYMPGGSVKD--QLKAYgALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQ--TIC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGERLPM-PPNCPPTLY 338
Cdd:cd06653   161 MSGTGIKSVTgtpyWMSPEVISGEGYGRKADVWSVACTVVEMLTEK-PPWAEYEAMAAIFKIATQPTKPQlPDGVSDACR 239
                         250       260
                  ....*....|....*....|
gi 1914781966 339 SLMTKCWaYDPSRRPRFTEL 358
Cdd:cd06653   240 DFLRQIF-VEEKRRPTAEFL 258
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
114-321 1.34e-14

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: 74.95  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNctsDSVREKF----LQEALTMRQFDHPHIVKLIGVI---TENPVWIIME 186
Cdd:cd07843    13 IEEGTYGVVYRARDKKTGE---IVALKKLKM---EKEKEGFpitsLREINILLKLQHPNIVTVKEVVvgsNLDKIYMVME 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 lCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDstyykas 266
Cdd:cd07843    87 -YVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLAREYGS------- 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 267 kgklPIKWM----------APESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGRI 321
Cdd:cd07843   159 ----PLKPYtqlvvtlwyrAPELLlGAKEYSTAIDMWSVGCIFAELLTK--KPlFPGKSEIDQLNKI 219
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
114-358 1.44e-14

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: 74.77  E-value: 1.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiyMSPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVITENPVWII----MELC 188
Cdd:cd07846     9 VGEGSYGMVMK---CRHKETGQIVAIKKFLESEDDKmVKKIAMREIKMLKQLRHENLVNLIEVFRRKKRWYLvfefVDHT 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFlqvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM----EDSTYYK 264
Cdd:cd07846    86 VLDDLEKY----PNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLaapgEVYTDYV 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASkgklpiKWM-APE-SINFRRFTSASDVWMFGVCMWEILM---------------HGVK-----------------PFQ 310
Cdd:cd07846   162 AT------RWYrAPElLVGDTKYGKAVDVWAVGCLVTEMLTgeplfpgdsdidqlyHIIKclgnliprhqelfqknpLFA 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1914781966 311 GVKNNDViGRIENGERLpmPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd07846   236 GVRLPEV-KEVEPLERR--YPKLSGVVIDLAKKCLHIDPDKRPSCSEL 280
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
151-352 1.48e-14

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: 74.35  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQF-----DHPHIVKL-IGVITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLE 224
Cdd:cd05583    38 KAKTAEHTMTERQVleavrQSPFLVTLhYAFQTDAKLHLILDYVNGGELFTHLYQREH-FTESEVRIYIGEIVLALEHLH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 225 SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRR--FTSASDVWMFGVCMWEIL 302
Cdd:cd05583   117 KLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYSFCGTIEYMAPEVVRGGSdgHDKAVDWWSLGVLTYELL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 303 MhGVKPF--QGVKNN--DVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05583   197 T-GASPFtvDGERNSqsEISKRILK-SHPPIPKTFSAEAKDFILKLLEKDPKKR 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
114-323 1.48e-14

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 74.45  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmsPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI---TENP-VWIIMELCT 189
Cdd:cd14664     1 IGRGGAGTVYKGVM--PNG--TLVAVKRLKGEGTQGGDHGFQAEIQTLGMIRHRNIVRLRGYCsnpTTNLlVYEYMPNGS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLILYAYQLSTALAYLE---SKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd14664    77 LGELLHSRPESQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMDDKDSHVMS 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQ---GVKNNDVIGRIEN 323
Cdd:cd14664   157 SVAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLE-LITGKRPFDeafLDDGVDIVDWVRG 215
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
101-321 1.55e-14

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 74.89  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQR---ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNctsdsVRE-KFLQEALTMRQF-DHPHIVKLIGV 175
Cdd:cd14132    10 LNVEWgsqDDYEIIRKIGRGKYSEVFEGINIGNNEK---VVIKVLKP-----VKKkKIKREIKILQNLrGGPNIVKLLDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 176 I----TENPVwIIMEL--CTlgelrSFLQVRkYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLV-SSNDCVKL 248
Cdd:cd14132    82 VkdpqSKTPS-LIFEYvnNT-----DFKTLY-PTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIdHEKRKLRL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 249 GDFGLSRY---MED------STYYKaskgklpikwmAPES-INFRRFTSASDVWMFGvCMWEILMHGVKP-FQGVKNNDV 317
Cdd:cd14132   155 IDWGLAEFyhpGQEynvrvaSRYYK-----------GPELlVDYQYYDYSLDMWSLG-CMLASMIFRKEPfFHGHDNYDQ 222

                  ....
gi 1914781966 318 IGRI 321
Cdd:cd14132   223 LVKI 226
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
152-359 1.66e-14

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: 74.32  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 152 EKFLQEALTMRQFDHPHIVKLIGVI---TENPVWIIMELCTLGELRSFLQVRKYSLDLASLilYAYQLSTALAYLESKRF 228
Cdd:cd14118    59 DRVYREIAILKKLDHPNVVKLVEVLddpNEDNLYMVFELVDKGAVMEVPTDNPLSEETARS--YFRDIVLGIEYLHYQKI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESI-NFRRFTS--ASDVWMFGVCMWeILMHG 305
Cdd:cd14118   137 IHRDIKPSNLLLGDDGHVKIADFGVSNEFEGDDALLSSTAGTP-AFMAPEALsESRKKFSgkALDIWAMGVTLY-CFVFG 214
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 306 VKPFQgvkNNDVIG---RIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14118   215 RCPFE---DDHILGlheKIKTDPvVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIK 269
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
148-352 2.25e-14

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: 73.93  E-value: 2.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 148 DSVREKFLQEALTMRQFD-HPHIVKLIGVItENPVWI--IMELCTLGELRSFL-QVRKYSLDLASLILYayQLSTALAYL 223
Cdd:cd14093    49 EELREATRREIEILRQVSgHPNIIELHDVF-ESPTFIflVFELCRKGELFDYLtEVVTLSEKKTRRIMR--QLFEAVEFL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 224 ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRRFTSAS------DVWMFGVC 297
Cdd:cd14093   126 HSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEKLRELCGT-P-GYLAPEVLKCSMYDNAPgygkevDMWACGVI 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 298 MWEILMhGVKPFQGVKNNDVIGRIENGE---RLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd14093   204 MYTLLA-GCPPFWHRKQMVMLRNIMEGKyefGSPEWDDISDTAKDLISKLLVVDPKKR 260
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
106-358 2.33e-14

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


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 73.79  E-value: 2.33e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIElgrCIGEGQFGDVHQgiYMSPENPALAVAiKTCKNCTSDSVREKFLQE-ALTMRQFDHPHIVKLIGV-ITENP--V 181
Cdd:cd14131     4 EILK---QLGKGGSSKVYK--VLNPKKKIYALK-RVDLEGADEQTLQSYKNEiELLKKLKGSDRIIQLYDYeVTDEDdyL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELctlGE--LRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARN-VLVSSNdcVKLGDFGLSRYM 257
Cdd:cd14131    78 YMVMEC---GEidLATILKKKRPKpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANfLLVKGR--LKLIDFGIAKAI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 -EDST-YYKASK-GKLpiKWMAPESINFRRFTS----------ASDVWMFGvCMWEILMHGVKPFQGVKN-NDVIGRIEN 323
Cdd:cd14131   153 qNDTTsIVRDSQvGTL--NYMSPEAIKDTSASGegkpkskigrPSDVWSLG-CILYQMVYGKTPFQHITNpIAKLQAIID 229
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 324 -GERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14131   230 pNHEIEFPDIPNPDLIDVMKRCLQRDPKKRPSIPEL 265
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
165-367 2.47e-14

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: 73.68  E-value: 2.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 165 DHPHIVKLIGVITEN--------PVWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAAR 236
Cdd:cd13975    56 KHERIVSLHGSVIDYsygggssiAVLLIMERLH----RDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLK 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 237 NVLVSSNDCVKLGDFGlsrYMEDSTYYKASKGKLPIKwMAPESINfRRFTSASDVWMFGVCMWEILMHGVK---PFQGVK 313
Cdd:cd13975   132 NVLLDKKNRAKITDLG---FCKPEAMMSGSIVGTPIH-MAPELFS-GKYDNSVDVYAFGILFWYLCAGHVKlpeAFEQCA 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 314 NNDVIGR-IENGERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd13975   207 SKDHLWNnVRKGVRPERLPVFDEECWNLMEACWSGDPSQRPLLGIVQPKLQGIMD 261
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
159-358 2.51e-14

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 73.86  E-value: 2.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 159 LTMRQFDHPHIVKLIGVItENPV------WIIMELCTLGELRSFLQVR---KYSLDLASLILYayQLSTALAYLESKRFV 229
Cdd:cd14089    46 LHWRASGCPHIVRIIDVY-ENTYqgrkclLVVMECMEGGELFSRIQERadsAFTEREAAEIMR--QIGSAVAHLHSMNIA 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSN--DCV-KLGDFGLSRYMEDST---------YYkaskgklpikwMAPESINFRRFTSASDVWMFGVC 297
Cdd:cd14089   123 HRDLKPENLLYSSKgpNAIlKLTDFGFAKETTTKKslqtpcytpYY-----------VAPEVLGPEKYDKSCDMWSLGVI 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 298 MWeILMHGVKPF---------QGVKNndvigRIENGE-RLPMP--PNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14089   192 MY-ILLCGYPPFysnhglaisPGMKK-----RIRNGQyEFPNPewSNVSEEAKDLIRGLLKTDPSERLTIEEV 258
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
114-309 2.80e-14

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: 73.99  E-value: 2.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPenpALAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVK-LIGVITENPVWIIMELCTLGE 192
Cdd:cd06654    28 IGQGASGTVYTAMDVAT---GQEVAIRQ-MNLQQQPKKELIINEILVMRENKNPNIVNyLDSYLVGDELWVVMEYLAGGS 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI 272
Cdd:cd06654   104 LTDV--VTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSKRSTMVGTPY 181
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1914781966 273 kWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPF 309
Cdd:cd06654   182 -WMAPEVVTRKAYGPKVDIWSLGIMAIE-MIEGEPPY 216
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
114-321 2.93e-14

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: 73.84  E-value: 2.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSD------SVREKFLQEALtmRQFDHPHIVKLIGVIT------ENPV 181
Cdd:cd07863     8 IGVGAYGTVYKA--RDPHSGHF-VALKSVRVQTNEdglplsTVREVALLKRL--EAFDHPNIVRLMDVCAtsrtdrETKV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTlGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMeds 260
Cdd:cd07863    83 TLVFEHVD-QDLRTYLdKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIY--- 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 261 TYYKASKGKLPIKWM-APESINFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRI 321
Cdd:cd07863   159 SCQMALTPVVVTLWYrAPEVLLQSTYATPVDMWSVGCIFAE--MFRRKPlFCGNSEADQLGKI 219
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
114-334 3.20e-14

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 73.91  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMspENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQ---FDHPHIVKLIGVIT------ENPVWI 183
Cdd:cd07862     9 IGEGAYGKVFKARDL--KNGGRFVALKRVRVQTGEEgMPLSTIREVAVLRHletFEHPNVVRLFDVCTvsrtdrETKLTL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTlGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMedsTY 262
Cdd:cd07862    87 VFEHVD-QDLTTYLdKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIY---SF 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 263 YKASKGKLPIKWM-APESINFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRIENGERLPMPPNCP 334
Cdd:cd07862   163 QMALTSVVVTLWYrAPEVLLQSSYATPVDLWSVGCIFAE--MFRRKPlFRGSSDVDQLGKILDVIGLPGEEDWP 234
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
114-352 3.49e-14

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: 73.80  E-value: 3.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHqgIYMSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE-----NPVWII-MEL 187
Cdd:cd14039     1 LGTGGFGNVC--LYQNQETGEK-IAIKSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEmnflvNDVPLLaMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQVRKYSLDL--ASLILYAYQLSTALAYLESKRFVHRDIAARNVL---VSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd14039    78 CSGGDLRKLLNKPENCCGLkeSQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVlqeINGKIVHKIIDLGYAKDLDQGSL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEIL------MHGVKPFQ---GVKNND---------VIGRIENG 324
Cdd:cd14039   158 CTSFVGTL--QYLAPELFENKSYTVTVDYWSFGTMVFECIagfrpfLHNLQPFTwheKIKKKDpkhifaveeMNGEVRFS 235
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1914781966 325 ERLPMPPNCPPTLYSLMtKCW-----AYDPSRR 352
Cdd:cd14039   236 THLPQPNNLCSLIVEPM-EGWlqlmlNWDPVQR 267
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
112-301 4.21e-14

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


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 73.93  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNCTSDSVR--EKFLQEALTMRQFDHPHIVKLIGV-ITENPVWIIMELC 188
Cdd:cd06635    31 REIGHGSFGAVY---FARDVRTSEVVAIKKMSYSGKQSNEkwQDIIKEVKFLQRIKHPNSIEYKGCyLREHTAWLVMEYC 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 tLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKg 268
Cdd:cd06635   108 -LGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPANSFVGTP- 185
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1914781966 269 klpiKWMAPESI---NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd06635   186 ----YWMAPEVIlamDEGQYDGKVDVWSLGITCIEL 217
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
101-316 4.55e-14

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: 73.00  E-value: 4.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRErielgrcIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVRekflQEALTMRQFDHPHIVKLIGVITE-N 179
Cdd:cd14114     4 YDILEE-------LGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVR----KEIQIMNQLHHPKLINLHDAFEDdN 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS--SNDCVKLGDFGLSRYM 257
Cdd:cd14114    73 EMVLILEFLSGGELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHL 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 258 EDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGvKNND 316
Cdd:cd14114   153 DPKESVKVTTGT--AEFAAPEIVEREPVGFYTDMWAVGVLSY-VLLSGLSPFAG-ENDD 207
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
99-301 5.64e-14

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: 72.75  E-value: 5.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  99 RDYE-IQRerielgrcIGEGQFGDVHQGIYMSPENPAlavAIKTCKNCTSDSVrEKFLQEALTMRQFDHPHIVKLIG-VI 176
Cdd:cd06646     9 HDYElIQR--------VGSGTYGDVYKARNLHTGELA---AVKIIKLEPGDDF-SLIQQEIFMVKECKHCNIVAYFGsYL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQVRK--YSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd06646    77 SREKLWICMEYCGGGSLQDIYHVTGplSELQIAYVCRETLQ---GLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVA 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 255 RYMEDSTYYKASKGKLPIkWMAPESINFRR---FTSASDVWMFGVCMWEI 301
Cdd:cd06646   154 AKITATIAKRKSFIGTPY-WMAPEVAAVEKnggYNQLCDIWAVGITAIEL 202
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
108-338 7.17e-14

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 73.64  E-value: 7.17e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVHQGIymsPENPALAVAIKTCKNCTSDSVREKF-------------LQEALTMRQFDHPHIVKLIG 174
Cdd:PTZ00024   11 IQKGAHLGEGTYGKVEKAY---DTLTGKIVAIKKVKIIEISNDVTKDrqlvgmcgihfttLRELKIMNEIKHENIMGLVD 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 175 VITE----NPVWIIMElctlGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 250
Cdd:PTZ00024   88 VYVEgdfiNLVMDIMA----SDLKKVVD-RKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIAD 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 251 FGLSR------YMEDSTYYKASKGKLPIK------WM-APESI-NFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNN 315
Cdd:PTZ00024  163 FGLARrygyppYSDTLSKDETMQRREEMTskvvtlWYrAPELLmGAEKYHFAVDMWSVGCIFAELLTG--KPlFPGENEI 240
                         250       260
                  ....*....|....*....|...
gi 1914781966 316 DVIGRIENGERLPMPPNCPPTLY 338
Cdd:PTZ00024  241 DQLGRIFELLGTPNEDNWPQAKK 263
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
100-358 7.31e-14

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: 72.03  E-value: 7.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 100 DYEIQRErielgrcIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEA-------LTMRQFDHPHIVKL 172
Cdd:cd14004     1 DYTILKE-------MGEGAYGQVNLAIYKSKGKEVVIKFIFKERILVDTWVRDRKLGTVpleihilDTLNKRSHPNIVKL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 173 IGVItENPV--WIIMELCTLG-ELRSFLQvRKYSLD--LASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK 247
Cdd:cd14004    74 LDFF-EDDEfyYLVMEKHGSGmDLFDFIE-RKPNMDekEAKYIFR--QVADAVKHLHDQGIVHRDIKDENVILDGNGTIK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 248 LGDFGLSRYMEDSTYYKASKgklPIKWMAPESINFRRFTSAS-DVWMFGVCMWeILMHGVKPFQGVKNndvigrIENGEr 326
Cdd:cd14004   150 LIDFGSAAYIKSGPFDTFVG---TIDYAAPEVLRGNPYGGKEqDIWALGVLLY-TLVFKENPFYNIEE------ILEAD- 218
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1914781966 327 LPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14004   219 LRIPYAVSEDLIDLISRMLNRDVGDRPTIEEL 250
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
114-358 7.53e-14

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: 72.83  E-value: 7.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVhqgiyMSPENPALA--VAIKTCkNCTSDSVREKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTL 190
Cdd:cd06655    27 IGQGASGTV-----FTAIDVATGqeVAIKQI-NLQKQPKKELIINEILVMKELKNPNIVNFLdSFLVGDELFVVMEYLAG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFlqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKL 270
Cdd:cd06655   101 GSLTDV--VTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSKRSTMVGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 271 PIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI-ENGE-RLPMPPNCPPTLYSLMTKCWAYD 348
Cdd:cd06655   179 PY-WMAPEVVTRKAYGPKVDIWSLGIMAIE-MVEGEPPYLNENPLRALYLIaTNGTpELQNPEKLSPIFRDFLNRCLEMD 256
                         250
                  ....*....|
gi 1914781966 349 PSRRPRFTEL 358
Cdd:cd06655   257 VEKRGSAKEL 266
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
114-321 8.01e-14

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: 72.51  E-value: 8.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlGE 192
Cdd:cd07836     8 LGEGTYATVYKG--RNRTTGEI-VALKEIHLDAEEGTPSTAIREISLMKELKHENIVRLHDVIhTENKLMLVFEYMD-KD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVR--KYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY--MEDSTYykaSKG 268
Cdd:cd07836    84 LKKYMDTHgvRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAfgIPVNTF---SNE 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 269 KLPIKWMAPESI-NFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI 321
Cdd:cd07836   161 VVTLWYRAPDVLlGSRTYSTSIDIWSVGCIMAEMIT-GRPLFPGTNNEDQLLKI 213
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
114-355 8.12e-14

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: 72.14  E-value: 8.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREkFLQEALTMRQFDHPHIVKLIGVITE--NPVwIIMELCTLG 191
Cdd:cd14057     3 INETHSGELWKGRWQGND---IVAKILKVRDVTTRISRD-FNEEYPRLRIFSHPNVLPVLGACNSppNLV-VISQYMPYG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFL-QVRKYSLDLASLILYAYQLSTALAYLES-KRFVHR-DIAARNVLVSSNDCVKLGdfglsryMEDSTYYKASKG 268
Cdd:cd14057    78 SLYNVLhEGTGVVVDQSQAVKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARIN-------MADVKFSFQEPG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KL-PIKWMAPES-------INFRrftsASDVWMFGVCMWEILMHGVkPFQGVKNNDVIGRIE-NGERLPMPPNCPPTLYS 339
Cdd:cd14057   151 KMyNPAWMAPEAlqkkpedINRR----SADMWSFAILLWELVTREV-PFADLSNMEIGMKIAlEGLRVTIPPGISPHMCK 225
                         250
                  ....*....|....*.
gi 1914781966 340 LMTKCWAYDPSRRPRF 355
Cdd:cd14057   226 LMKICMNEDPGKRPKF 241
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
107-359 9.95e-14

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: 71.94  E-value: 9.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 185
Cdd:cd14665     1 RYELVKDIGSGNFGVAR---LMRDKQTKELVAVKYIER--GEKIDENVQREIINHRSLRHPNIVRFKEVIlTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGEL-RSFLQVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTY 262
Cdd:cd14665    76 EYAAGGELfERICNAGRFSEDEARF--FFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKlPiKWMAPESINFRRFTSA-SDVWMFGVCMWEILMhGVKPFQGVKN----NDVIGRIENGE-RLPMPPNCPPT 336
Cdd:cd14665   154 PKSTVGT-P-AYIAPEVLLKKEYDGKiADVWSCGVTLYVMLV-GAYPFEDPEEprnfRKTIQRILSVQySIPDYVHISPE 230
                         250       260
                  ....*....|....*....|...
gi 1914781966 337 LYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14665   231 CRHLISRIFVADPATRITIPEIR 253
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
93-311 1.03e-13

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: 72.73  E-value: 1.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  93 YTMPSTRDYEIqrerieLGRcIGEGQFGDVHQGIYMSPENpalAVAIKtckNCTSDSVREKF----LQEALTMRQFDHPH 168
Cdd:cd07866     2 YGCSKLRDYEI------LGK-LGEGTFGEVYKARQIKTGR---VVALK---KILMHNEKDGFpitaLREIKILKKLKHPN 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 169 IVKLIGVITENPVwiimelCTLGELRSFLQVRKY-SLDLASLI-------------LYAYQLSTALAYLESKRFVHRDIA 234
Cdd:cd07866    69 VVPLIDMAVERPD------KSKRKRGSVYMVTPYmDHDLSGLLenpsvkltesqikCYMLQLLEGINYLHENHILHRDIK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 235 ARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKLPIK--------WM-APESI-NFRRFTSASDVWMFGVCMWEilM 303
Cdd:cd07866   143 AANILIDNQGILKIADFGLARpYDGPPPNPKGGGGGGTRKytnlvvtrWYrPPELLlGERRYTTAVDIWGIGCVFAE--M 220

                  ....*....
gi 1914781966 304 HGVKP-FQG 311
Cdd:cd07866   221 FTRRPiLQG 229
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
110-302 1.22e-13

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: 71.61  E-value: 1.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVH-------------QGIYMSPENPalavaiKTCKNCTSDSVREKFLQEALtmrqfdHPHIVKLIGVI 176
Cdd:cd06652     6 LGKLLGQGAFGRVYlcydadtgrelavKQVQFDPESP------ETSKEVNALECEIQLLKNLL------HERIVQYYGCL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENP---VWIIMELCTLGELRSflQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd06652    74 RDPQertLSIFMEYMPGGSIKD--QLKSYgALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 253 LSRYME----DSTYYKASKGKlPIkWMAPESINFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd06652   152 ASKRLQticlSGTGMKSVTGT-PY-WMSPEVISGEGYGRKADIWSVGCTVVEML 203
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
109-310 1.41e-13

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: 72.33  E-value: 1.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFgdVHQGIYmSPENPALAVAIKTCKNCTSDSVreKFLQ-EALTMRQFDHPHIVKLIGVITEN-PVWIIME 186
Cdd:cd08216     5 EIGKCFKGGGV--VHLAKH-KPTNTLVAVKKINLESDSKEDL--KFLQqEILTSRQLQHPNILPYVTSFVVDnDLYVVTP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQvRKYSLDLASLILyAYQLS---TALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFglsRYMedstYY 263
Cdd:cd08216    80 LMAYGSCRDLLK-THFPEGLPELAI-AFILRdvlNALEYIHSKGYIHRSVKASHILISGDGKVVLSGL---RYA----YS 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 264 KASKGK-------LPI------KWMAPESI--NFRRFTSASDVWMFGVCMWEiLMHGVKPFQ 310
Cdd:cd08216   151 MVKHGKrqrvvhdFPKsseknlPWLSPEVLqqNLLGYNEKSDIYSVGITACE-LANGVVPFS 211
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
112-352 1.48e-13

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: 72.35  E-value: 1.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVhqgIYMSPENPALAVAIKTCKN---CTSDSVREKfLQEALTMRQFDHPHIVKL-IGVITENPVWIIMEL 187
Cdd:cd05595     1 KLLGKGTFGKV---ILVREKATGRYYAMKILRKeviIAKDEVAHT-VTESRVLQNTRHPFLTALkYAFQTHDRLCFVMEY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKA 265
Cdd:cd05595    77 ANGGELFFHLsRERVFTEDRARF--YGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgITDGATMKT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCW 345
Cdd:cd05595   155 FCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPFYNQDHERLFELILM-EEIRFPRTLSPEAKSLLAGLL 230

                  ....*..
gi 1914781966 346 AYDPSRR 352
Cdd:cd05595   231 KKDPKQR 237
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
109-346 1.68e-13

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: 71.58  E-value: 1.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPAlavAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGV-ITENP------V 181
Cdd:cd06636    19 ELVEVVGNGTYGQVYKGRHVKTGQLA---AIKV-MDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAfIKKSPpghddqL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQVRKYSLDLASLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd06636    95 WLVMEFCGAGSVTDLVKNTKGNALKEDWIAYiCREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPIkWMAPESINFRR-----FTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIengerlpmPPNCPP 335
Cdd:cd06636   175 VGRRNTFIGTPY-WMAPEVIACDEnpdatYDYRSDIWSLGITAIE-MAEGAPPLCDMHPMRALFLI--------PRNPPP 244
                         250
                  ....*....|.
gi 1914781966 336 TLYSlmtKCWA 346
Cdd:cd06636   245 KLKS---KKWS 252
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
112-358 1.91e-13

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: 71.21  E-value: 1.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGiymSPENPALAVAIKTCKNCTSDSVREkFLQEALTMRQF-DHPHIVKLIG--VITENP---VWIIM 185
Cdd:cd13985     6 KQLGEGGFSYVYLA---HDVNTGRRYALKRMYFNDEEQLRV-AIKEIEIMKRLcGHPNIVQYYDsaILSSEGrkeVLLLM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTlGELRSFLQVRKYS-LDLASLILYAYQLSTALAYL--ESKRFVHRDIAARNVLVSSNDCVKLGDFGlSRYMEDSTY 262
Cdd:cd13985    82 EYCP-GSLVDILEKSPPSpLSEEEVLRIFYQICQAVGHLhsQSPPIIHRDIKIENILFSNTGRFKLCDFG-SATTEHYPL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKLPIKWM---------APESIN-FRRF--TSASDVWMFGvCMWEILMHGVKPFQGvknnDVIGRIENGE-RLPM 329
Cdd:cd13985   160 ERAEEVNIIEEEIqknttpmyrAPEMIDlYSKKpiGEKADIWALG-CLLYKLCFFKLPFDE----SSKLAIVAGKySIPE 234
                         250       260
                  ....*....|....*....|....*....
gi 1914781966 330 PPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd13985   235 QPRYSPELHDLIRHMLTPDPAERPDIFQV 263
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
166-352 1.99e-13

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: 72.05  E-value: 1.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 166 HPHIVKLIGVI-TENPVWIIMELCTLGELrsFLQVRKYSL---DLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVS 241
Cdd:cd05584    59 HPFIVDLHYAFqTGGKLYLILEYLSGGEL--FMHLEREGIfmeDTACF--YLAEITLALGHLHSLGIIYRDLKPENILLD 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 242 SNDCVKLGDFGLSR-YMEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGR 320
Cdd:cd05584   135 AQGHVKLTDFGLCKeSIHDGTVTHTFCGT--IEYMAPEILTRSGHGKAVDWWSLGALMYDMLT-GAPPFTAENRKKTIDK 211
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1914781966 321 IENGeRLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05584   212 ILKG-KLNLPPYLTNEARDLLKKLLKRNVSSR 242
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
152-365 2.67e-13

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: 71.28  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 152 EKFLQEALTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFV 229
Cdd:cd14209    46 EHTLNEKRILQAINFPFLVKLEYSFKDNSnLYMVMEYVPGGEMFSHLRrIGRFSEPHARF--YAAQIVLAFEYLHSLDLI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKgklPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPF 309
Cdd:cd14209   124 YRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCGT---P-EYLAPEIILSKGYNKAVDWWALGVLIYE-MAAGYPPF 198
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 310 QGVKNNDVIGRIENGeRLPMPPNCPPTLYSLMTKCWAYDPSRrpRFTELKAQLSTI 365
Cdd:cd14209   199 FADQPIQIYEKIVSG-KVRFPSHFSSDLKDLLRNLLQVDLTK--RFGNLKNGVNDI 251
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
155-302 3.43e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 71.83  E-value: 3.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIA 234
Cdd:PHA03209  105 LIEAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVK 184
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 235 ARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEIL 302
Cdd:PHA03209  185 TENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGT--VETNAPEVLARDKYNSKADIWSAGIVLFEML 250
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
114-301 3.55e-13

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: 70.42  E-value: 3.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIymspeNPALAVAIKTCKNCT---SDSVREKFLQEALTMRQFDHPHIVKLIG-----VITENPVWIIM 185
Cdd:cd14033     9 IGRGSFKTVYRGL-----DTETTVEVAWCELQTrklSKGERQRFSEEVEMLKGLQHPNIVRFYDswkstVRGHKCIILVT 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS-NDCVKLGDFGLSrymedsTY 262
Cdd:cd14033    84 ELMTSGTLKTYLK-RFREMKLKLLQRWSRQILKGLHFLHSRCppILHRDLKCDNIFITGpTGSVKIGDLGLA------TL 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1914781966 263 YKASKGKLPI---KWMAPESINfRRFTSASDVWMFGVCMWEI 301
Cdd:cd14033   157 KRASFAKSVIgtpEFMAPEMYE-EKYDEAVDVYAFGMCILEM 197
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
137-302 3.74e-13

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: 71.35  E-value: 3.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKtcKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKY-SLDLASLI---- 210
Cdd:cd07854    33 VAVK--KIVLTDPQSVKhALREIKIIRRLDHDNIVKVYEVLGPSGSDLTEDVGSLTELNSVYIVQEYmETDLANVLeqgp 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 211 -------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KLGDFGLSRYMeDSTYykASKGKLP----IKWM-AP 277
Cdd:cd07854   111 lseeharLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARIV-DPHY--SHKGYLSeglvTKWYrSP 187
                         170       180
                  ....*....|....*....|....*.
gi 1914781966 278 ESI-NFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd07854   188 RLLlSPNNYTKAIDMWAAGCIFAEML 213
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
114-352 3.83e-13

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: 70.53  E-value: 3.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmspENPALAVAIKTCK------NCTSDSVREKFLqealtMRQFDHPHIVKLIGVI-TENPVWIIME 186
Cdd:cd07861     8 IGEGTYGVVYKGRN---KKTGQIVAMKKIRleseeeGVPSTAIREISL-----LKELQHPNIVCLEDVLmQENRLYLVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLgELRSFLQ---VRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMedstyy 263
Cdd:cd07861    80 FLSM-DLKKYLDslpKGKY-MDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAF------ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 kaskgKLPIK----------WMAPESI-NFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRI---------- 321
Cdd:cd07861   152 -----GIPVRvythevvtlwYRAPEVLlGSPRYSTPVDIWSIGTIFAE--MATKKPlFHGDSEIDQLFRIfrilgtpted 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 322 --ENGERLP----------------MPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd07861   225 iwPGVTSLPdykntfpkwkkgslrtAVKNLDEDGLDLLEKMLIYDPAKR 273
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
113-353 4.22e-13

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: 70.78  E-value: 4.22e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 113 CIGEGQFGDVHQGiYMSPENPALAVAIKTCK--NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP---VWIIMEL 187
Cdd:cd07842     7 CIGRGTYGRVYKA-KRKNGKDGKEYAIKKFKgdKEQYTGISQSACREIALLRELKHENVVSLVEVFLEHAdksVYLLFDY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CT--LGEL----RSFLQVRKYSLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSND----CVKLGDFGLSRYm 257
Cdd:cd07842    86 AEhdLWQIikfhRQAKRVSIPPSMVKSLL---WQILNGIHYLHSNWVLHRDLKPANILVMGEGpergVVKIGDLGLARL- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 edstYYKASKGKL-------PIKWMAPESI-NFRRFTSASDVWMFGVCMWEIL-----MHG-------VKPFQgvknNDV 317
Cdd:cd07842   162 ----FNAPLKPLAdldpvvvTIWYRAPELLlGARHYTKAIDIWAIGCIFAELLtlepiFKGreakikkSNPFQ----RDQ 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 318 IGRIENGERLP----------MP--------------PNC------------PPTLYSLMTKCWAYDPSRRP 353
Cdd:cd07842   234 LERIFEVLGTPtekdwpdikkMPeydtlksdtkastyPNSllakwmhkhkkpDSQGFDLLRKLLEYDPTKRI 305
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
109-309 4.36e-13

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: 70.52  E-value: 4.36e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPAlavAIKTcKNCTSDSvREKFLQEALTMRQFDH-PHIVKLIGV-ITENP------ 180
Cdd:cd06637     9 ELVELVGNGTYGQVYKGRHVKTGQLA---AIKV-MDVTGDE-EEEIKQEINMLKKYSHhRNIATYYGAfIKKNPpgmddq 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRSFLQVRKYSLDLASLILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd06637    84 LWLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYiCREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDR 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 260 STYYKASKGKLPIkWMAPESINFRRFTSA-----SDVWMFGVCMWEiLMHGVKPF 309
Cdd:cd06637   164 TVGRRNTFIGTPY-WMAPEVIACDENPDAtydfkSDLWSLGITAIE-MAEGAPPL 216
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
109-316 4.45e-13

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: 69.95  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRcigeGQFGDVHQGIYMSPENPALAVAIKT---CKNCTSDSVREKFLQEALTmrqfDHPHIVKLIGVI-TENPVWII 184
Cdd:cd14198    15 ELGR----GKFAVVRQCISKSTGQEYAAKFLKKrrrGQDCRAEILHEIAVLELAK----SNPRVVNLHEVYeTTSEIILI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSF----LQVRKYSLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSS----NDcVKLGDFGLSRY 256
Cdd:cd14198    87 LEYAAGGEIFNLcvpdLAEMVSENDIIRLI---RQILEGVYYLHQNNIVHLDLKPQNILLSSiyplGD-IKIVDFGMSRK 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNND 316
Cdd:cd14198   163 IGHACELREIMGT--PEYLAPEILNYDPITTATDMWNIGVIAY-MLLTHESPFVGEDNQE 219
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
109-352 4.51e-13

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: 71.10  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQ-FDH----PHIVKL-IGVITENPVW 182
Cdd:cd05614     3 ELLKVLGTGAYGKVFLVRKVSGHDANKLYAMKVLRKAALVQ-KAKTVEHTRTERNvLEHvrqsPFLVTLhYAFQTDAKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM----E 258
Cdd:cd05614    82 LILDYVSGGELFTHLYQRDH-FSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFlteeK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKgklpIKWMAPESINFRR-FTSASDVWMFGVCMWEILMhGVKPF--QGVKNN--DVIGRIENGERlPMPPNC 333
Cdd:cd05614   161 ERTYSFCGT----IEYMAPEIIRGKSgHGKAVDWWSLGILMFELLT-GASPFtlEGEKNTqsEVSRRILKCDP-PFPSFI 234
                         250
                  ....*....|....*....
gi 1914781966 334 PPTLYSLMTKCWAYDPSRR 352
Cdd:cd05614   235 GPVARDLLQKLLCKDPKKR 253
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
105-309 4.61e-13

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: 70.06  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 183
Cdd:cd14167     2 RDIYDFREVLGTGAFSEV---VLAEEKRTQKLVAIKCIAKKALEGKETSIENEIAVLHKIKHPNIVALDDIYeSGGHLYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGEL------RSFLQVRkyslDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLS 254
Cdd:cd14167    79 IMQLVSGGELfdriveKGFYTER----DASKLI---FQILDAVKYLHDMGIVHRDLKPENLLYYSLDedsKIMISDFGLS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 255 RyMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14167   152 K-IEGSGSVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 203
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
112-362 5.14e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 70.82  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENpALAVAIKTCKNCTSDSVREKFLQEA-LTMRQFDHPHIVKL-IGVITENPVWIIMELCT 189
Cdd:cd05602    13 KVIGKGSFGKVLLARHKSDEK-FYAVKVLQKKAILKKKEEKHIMSERnVLLKNVKHPFLVGLhFSFQTTDKLYFVLDYIN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd05602    92 GGELFYHLQRERCFLEPRAR-FYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIEPNGTTSTFCG 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05602   171 TP-EYLAPEVLHKQPYDRTVDWWCLGAVLYEML-YGLPPFYSRNTAEMYDNILN-KPLQLKPNITNSARHLLEGLLQKDR 247
                         250
                  ....*....|....*..
gi 1914781966 350 SRR----PRFTELKAQL 362
Cdd:cd05602   248 TKRlgakDDFTEIKNHI 264
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
112-352 6.12e-13

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


Pssm-ID: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 70.38  E-value: 6.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVhqgIYMSPENPALAVAIKTC-KNCTSDSVREKFL--QEALTMRQFDHPHIVKL-IGVITENPVWIIMEL 187
Cdd:cd05604     2 KVIGKGSFGKV---LLAKRKRDGKYYAVKVLqKKVILNRKEQKHImaERNVLLKNVKHPFLVGLhYSFQTTDKLYFVLDF 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQVRKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd05604    79 VNGGELFFHLQRERSFPEPRAR-FYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGISNSDTTTTF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQgvkNNDVIGRIEN--GERLPMPPNCPPTLYSLMTKCW 345
Cdd:cd05604   158 CGTP-EYLAPEVIRKQPYDNTVDWWCLGSVLYEML-YGLPPFY---CRDTAEMYENilHKPLVLRPGISLTAWSILEELL 232

                  ....*..
gi 1914781966 346 AYDPSRR 352
Cdd:cd05604   233 EKDRQLR 239
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
114-353 6.82e-13

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: 70.00  E-value: 6.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDS------VREKFLQEALTmrQFDHPHIVKLIGVI------TENPV 181
Cdd:cd07838     7 IGEGAYGTVYKARDLQDGR---FVALKKVRVPLSEEgiplstIREIALLKQLE--SFEHPNVVRLLDVChgprtdRELKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTlGELRSFLQ-VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMED 259
Cdd:cd07838    82 TLVFEHVD-QDLATYLDkCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARiYSFE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 ST--------YYKaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEilMHGVKP-FQGVKNNDVIGRI--------- 321
Cdd:cd07838   161 MAltsvvvtlWYR-----------APEVLLQSSYATPVDMWSVGCIFAE--LFNRRPlFRGSSEADQLGKIfdviglpse 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 322 --------------ENGERLPM----PPNCPPTLySLMTKCWAYDPSRRP 353
Cdd:cd07838   228 eewprnsalprssfPSYTPRPFksfvPEIDEEGL-DLLKKMLTFNPHKRI 276
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
114-352 7.10e-13

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


Pssm-ID: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 70.29  E-value: 7.10e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQgiyMSPENPALAVAIKTCKNC--TSDSVREKFLQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTL 190
Cdd:cd05585     2 IGKGSFGKVMQ---VRKKDTSRIYALKTIRKAhiVSRSEVTHTLAERTVLAQVDCPFIVPLkFSFQSPEKLYLVLAFING 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKASKGK 269
Cdd:cd05585    79 GELFHHLQ-REGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLnMKDDDKTNTFCGT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 lPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05585   158 -P-EYLAPELLLGHGYTKAVDWWTLGVLLYEMLT-GLPPFYDENTNEMYRKILQ-EPLRFPDGFDRDAKDLLIGLLNRDP 233

                  ...
gi 1914781966 350 SRR 352
Cdd:cd05585   234 TKR 236
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
151-309 7.58e-13

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: 70.01  E-value: 7.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRF 228
Cdd:cd06659    62 RELLFNEVVIMRDYQHPNVVEMYkSYLVGEELWVLMEYLQGGALTDIVsQTRLNEEQIATVCEAVLQ---ALAYLHSQGV 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKP 308
Cdd:cd06659   139 IHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPKRKSLVGTPY-WMAPEVISRCPYGTEVDIWSLGIMVIE-MVDGEPP 216

                  .
gi 1914781966 309 F 309
Cdd:cd06659   217 Y 217
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
112-352 8.96e-13

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: 69.97  E-value: 8.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGiYMSPENPALAV-AIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCT 189
Cdd:cd05620     1 KVLGKGSFGKVLLA-ELKGKGEYFAVkALKKDVVLIDDDVECTMVEKRVLALAWENPFLTHLYCTFqTKEHLFFVMEFLN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR---YMEDstyyKAS 266
Cdd:cd05620    80 GGDLMFHIQ-DKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKenvFGDN----RAS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErlpmpPNCPPTLY----SLMT 342
Cdd:cd05620   155 TFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEMLI-GQSPFHGDDEDELFESIRVDT-----PHYPRWITkeskDILE 228
                         250
                  ....*....|
gi 1914781966 343 KCWAYDPSRR 352
Cdd:cd05620   229 KLFERDPTRR 238
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
114-302 9.44e-13

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 69.47  E-value: 9.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTS---DSVREKFLQEALTMRQFDHPHIVKLIGVITENP----VWIIME 186
Cdd:cd14159     1 IGEGGFGCVYQAVMRNTE-----YAVKRLKEDSEldwSVVKNSFLTEVEKLSRFRHPNIVDLAGYSAQQGnyclIYVYLP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLgELRSFLQVRKYSLDLASLILYAYQLSTALAYL--ESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM------- 257
Cdd:cd14159    76 NGSL-EDRLHCQVSCPCLSWSQRLHVLLGTARAIQYLhsDSPSLIHGDVKSSNILLDAALNPKLGDFGLARFSrrpkqpg 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 258 EDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd14159   155 MSSTLARTQTVRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELL 199
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
114-314 9.71e-13

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: 69.22  E-value: 9.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIymSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLgE 192
Cdd:cd07870     8 LGEGSYATVYKGI--SRINGQL-VALKVISMKTEEGVPFTAIREASLLKGLKHANIVLLHDIIhTKETLTFVFEYMHT-D 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME-DSTYYKASKGKLp 271
Cdd:cd07870    84 LAQYMIQHPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSiPSQTYSSEVVTL- 162
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 272 ikWMAPESI--NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKN 314
Cdd:cd07870   163 --WYRPPDVllGATDYSSALDIWGAG-CIFIEMLQGQPAFPGVSD 204
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
109-325 1.06e-12

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: 69.12  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRcigeGQFGDVHQGIYMSPENPALAVAIKtCKncTSDSVREKflQEALTMRQFDHPHIVKLIGVItENPVWIIM--E 186
Cdd:cd14104     7 ELGR----GQFGIVHRCVETSSKKTYMAKFVK-VK--GADQVLVK--KEISILNIARHRNILRLHESF-ESHEELVMifE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL----VSSNdcVKLGDFGLSRYMEDSTY 262
Cdd:cd14104    77 FISGVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIyctrRGSY--IKIIEFGQSRQLKPGDK 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 263 YKASKgkLPIKWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14104   155 FRLQY--TSAEFYAPEVHQHESVSTATDMWSLG-CLVYVLLSGINPFEAETNQQTIENIRNAE 214
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
109-352 1.13e-12

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 69.26  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSvREKFLQEALTMRQ-FDH----PHIVKL-IGVITENPVW 182
Cdd:cd05613     3 ELLKVLGTGAYGKVFLVRKVSGHDAGKLYAMKVLKKATIVQ-KAKTAEHTRTERQvLEHirqsPFLVTLhYAFQTDTKLH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTY 262
Cdd:cd05613    82 LILDYINGGELFTHLSQRE-RFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDEN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKLPIKWMAPESINF--RRFTSASDVWMFGVCMWEILMhGVKPF--QGVKNN--DVIGRIENGERlPMPPNCPPT 336
Cdd:cd05613   161 ERAYSFCGTIEYMAPEIVRGgdSGHDKAVDWWSLGVLMYELLT-GASPFtvDGEKNSqaEISRRILKSEP-PYPQEMSAL 238
                         250
                  ....*....|....*.
gi 1914781966 337 LYSLMTKCWAYDPSRR 352
Cdd:cd05613   239 AKDIIQRLLMKDPKKR 254
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
110-309 1.29e-12

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: 69.32  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRcIGEGQFGDVHQGIYMSPENpalAVAIKTCK-NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN---PVWIIM 185
Cdd:cd07845    12 LNR-IGEGTYGIVYRARDTTSGE---IVALKKVRmDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKhldSIFLVM 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDStyYKA 265
Cdd:cd07845    88 EYCE-QDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLARTYGLP--AKP 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1914781966 266 SKGKLPIKWM-APESI-NFRRFTSASDVWMFGVCMWEILMHgvKPF 309
Cdd:cd07845   165 MTPKVVTLWYrAPELLlGCTTYTTAIDMWAVGCILAELLAH--KPL 208
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
106-352 1.83e-12

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: 68.47  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELgrcIGEGQFGDVHQGIYMSPENpalAVAIKTCK------NCTSDSVRE-KFLQEaltMRqfdHPHIVKLIGVI-T 177
Cdd:cd07835     2 QKLEK---IGEGTYGVVYKARDKLTGE---IVALKKIRletedeGVPSTAIREiSLLKE---LN---HPNIVRLLDVVhS 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLgELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd07835    70 ENKLYLVFEFLDL-DLKKYMdSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MedstyykaskgKLPIK---------WM-APES-INFRRFTSASDVWMFGVCMWEILMHgvKP-FQGVKNNDVIGRI--- 321
Cdd:cd07835   149 F-----------GVPVRtythevvtlWYrAPEIlLGSKHYSTPVDIWSVGCIFAEMVTR--RPlFPGDSEIDQLFRIfrt 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 322 ----------------------ENGERLPMP---PNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd07835   216 lgtpdedvwpgvtslpdykptfPKWARQDLSkvvPSLDEDGLDLLSQMLVYDPAKR 271
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
114-348 1.96e-12

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: 69.06  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYmspENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE----NPVwIIMELCT 189
Cdd:cd13988     1 LGQGATANVFRGRH---KKTGDLYAVKVFNNLSFMRPLDVQMREFEVLKKLNHKNIVKLFAIEEElttrHKV-LVMELCP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQ--VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND---CV-KLGDFGLSRYMEDSTYY 263
Cdd:cd13988    77 CGSLYTVLEepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEdgqSVyKLTDFGAARELEDDEQF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKLpiKWMAP---ESINFRR-----FTSASDVWMFGVCMWEILMhGVKPFQ----GVKNNDVIGRI---------- 321
Cdd:cd13988   157 VSLYGTE--EYLHPdmyERAVLRKdhqkkYGATVDLWSIGVTFYHAAT-GSLPFRpfegPRRNKEVMYKIitgkpsgais 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 322 -----ENGE---RLPMPPNCPPT--LYSLMT------------KCWAYD 348
Cdd:cd13988   234 gvqksENGPiewSGELPVSCSLSqgLQTLLTpvlanileadqeKCWGFD 282
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
137-365 2.22e-12

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: 67.99  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKTCKNcTSDSVREKFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELCTLGELRSFLQvRKYS------LDLASL 209
Cdd:cd14044    34 VILKDLKN-NEGNFTEKQKIELNKLLQIDYYNLTKFYGTVKlDTMIFGVIEYCERGSLRDVLN-DKISypdgtfMDWEFK 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 210 ILYAYQLSTALAYLE-SKRFVHRDIAARNVLVSSNDCVKLGDFGlsrymedstyykaSKGKLPIK---WMAPESINFRRF 285
Cdd:cd14044   112 ISVMYDIAKGMSYLHsSKTEVHGRLKSTNCVVDSRMVVKITDFG-------------CNSILPPSkdlWTAPEHLRQAGT 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 286 TSASDVWMFGVCMWEILMHGVKPF--QGVKNNDVIGRIENGERL-PMPPNC--------PPTLYSLMTKCWAYDPSRRPR 354
Cdd:cd14044   179 SQKGDVYSYGIIAQEIILRKETFYtaACSDRKEKIYRVQNPKGMkPFRPDLnlesagerEREVYGLVKNCWEEDPEKRPD 258
                         250
                  ....*....|.
gi 1914781966 355 FTELKAQLSTI 365
Cdd:cd14044   259 FKKIENTLAKI 269
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
114-353 2.97e-12

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: 67.98  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd06619     9 LGHGNGGTVYKAYHLLTRR---ILAVKVIPLDITVELQKQIMSELEILYKCDSPYIIGFYGAFfVENRISICTEFMDGGS 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLAslilyAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS---TYYKASkgk 269
Cdd:cd06619    86 LDVYRKIPEHVLGRI-----AVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSiakTYVGTN--- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 lpiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNdvigrieNGERLPM----------PPNCPPTLYS 339
Cdd:cd06619   158 ---AYMAPERISGEQYGIHSDVWSLGISFMELAL-GRFPYPQIQKN-------QGSLMPLqllqcivdedPPVLPVGQFS 226
                         250
                  ....*....|....*....
gi 1914781966 340 -----LMTKCWAYDPSRRP 353
Cdd:cd06619   227 ekfvhFITQCMRKQPKERP 245
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
110-352 3.03e-12

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: 68.41  E-value: 3.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 110 LGRCIGEGQFGDVHQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELC 188
Cdd:cd05619     9 LHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHLFCTFqTKENLFFVMEYL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymeDSTYYKASKG 268
Cdd:cd05619    89 NGGDLMFHIQ-SCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK---ENMLGDAKTS 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErlPMPPN-CPPTLYSLMTKCW 345
Cdd:cd05619   165 TFcgTPDYIAPEILLGQKYNTSVDWWSFGVLLYEMLI-GQSPFHGQDEEELFQSIRMDN--PFYPRwLEKEAKDILVKLF 241

                  ....*..
gi 1914781966 346 AYDPSRR 352
Cdd:cd05619   242 VREPERR 248
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
214-353 3.20e-12

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: 67.73  E-value: 3.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 214 YQLSTALAYL-ESKRFVHRDIAARNVLVSSNDCVKLGDFGlsrYMEDST-------YYKASKGKLPI------KWMAPES 279
Cdd:cd14011   121 LQISEALSFLhNDVKLVHGNICPESVVINSNGEWKLAGFD---FCISSEqatdqfpYFREYDPNLPPlaqpnlNYLAPEY 197
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 280 INFRRFTSASDVWMFGVCMWEILMHGVKPFQGVKN---NDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd14011   198 ILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVNNllsYKKNSNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEVRP 274
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
151-309 3.31e-12

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: 67.31  E-value: 3.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFV 229
Cdd:cd14113    47 RDQVTHELGVLQSLQHPQLVGLLDTFeTPTSYILVLEMADQGRLLDYV-VRWGNLTEEKIRFYLREILEALQYLHNCRIA 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLV---SSNDCVKLGDFGLSRYMeDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGV 306
Cdd:cd14113   126 HLDLKPENILVdqsLSKPTIKLADFGDAVQL-NTTYYIHQLLGSP-EFAAPEIILGNPVSLTSDLWSIGVLTY-VLLSGV 202

                  ...
gi 1914781966 307 KPF 309
Cdd:cd14113   203 SPF 205
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
112-352 3.67e-12

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: 67.74  E-value: 3.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVhqgiymspenpaLAVAIKT------CKNCTSDSVREK-----FLQEALTMRQFDHPHIVKLI-GVITEN 179
Cdd:cd05630     6 RVLGKGGFGEV------------CACQVRAtgkmyaCKKLEKKRIKKRkgeamALNEKQILEKVNSRFVVSLAyAYETKD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05630    74 ALCLVLTLMNGGDLKFHIyHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNdvIGRiENGERL------PMPPN 332
Cdd:cd05630   154 EGQTIKGRVGT--VGYMAPEVVKNERYTFSPDWWALGCLLYE-MIAGQSPFQQRKKK--IKR-EEVERLvkevpeEYSEK 227
                         250       260
                  ....*....|....*....|
gi 1914781966 333 CPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05630   228 FSPQARSLCSMLLCKDPAER 247
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
105-325 3.75e-12

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 67.71  E-value: 3.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNctSDSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVW 182
Cdd:cd14166     2 RETFIFMEVLGSGAFSEVY---LVKQRSTGKLYALKCIKK--SPLSRDSSLEnEIAVLKRIKHENIVTLEDIYeSTTHYY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGEL-RSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRyME 258
Cdd:cd14166    77 LVMQLVSGGELfDRILERGVYTEKDASRVIN--QVLSAVKYLHENGIVHRDLKPENLLYLTpdeNSKIMITDFGLSK-ME 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 259 DSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGVKNNDVIGRIENGE 325
Cdd:cd14166   154 QNGIMSTACGT-P-GYVAPEVLAQKPYSKAVDCWSIGVITY-ILLCGYPPFYEETESRLFEKIKEGY 217
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
99-330 4.10e-12

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: 68.88  E-value: 4.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  99 RDYEIQRERIELGRCIGEGQFGDVHQgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKL-IGVIT 177
Cdd:cd05624    65 KEMQLHRDDFEIIKVIGRGAFGEVAV-VKMKNTERIYAMKILNKWEMLKRAETACFREERNVLVNGDCQWITTLhYAFQD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFLQVRKYSL--DLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd05624   144 ENYLYLVMDYYVGGDLLTLLSKFEDKLpeDMARF--YIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCL 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YMEDSTYYKASKGKLPIKWMAPESIN-----FRRFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIENG-ERLPM 329
Cdd:cd05624   222 KMNDDGTVQSSVAVGTPDYISPEILQamedgMGKYGPECDWWSLGVCMYEML-YGETPFYAESLVETYGKIMNHeERFQF 300

                  .
gi 1914781966 330 P 330
Cdd:cd05624   301 P 301
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
177-352 5.29e-12

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: 67.72  E-value: 5.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd05616    72 TMDRLYFVMEYVNGGDLMYHIQqVGRFKEPHA--VFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 Y-MEDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLP--MPP 331
Cdd:cd05616   150 EnIWDGVTTKTFCGT-P-DYIAPEIIAYQPYGKSVDWWAFGVLLYEMLA-GQAPFEGEDEDELFQSImEHNVAYPksMSK 226
                         170       180
                  ....*....|....*....|.
gi 1914781966 332 NCPPTLYSLMTKcwayDPSRR 352
Cdd:cd05616   227 EAVAICKGLMTK----HPGKR 243
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
166-325 6.27e-12

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: 67.33  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 166 HPHIVKLIGVIT-ENPVWIIMELCTLGELrsFLQVRK---YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVS 241
Cdd:cd14092    58 HPNIVKLHEVFQdELHTYLVMELLRGGEL--LERIRKkkrFTESEASRIMR--QLVSAVSFMHSKGVVHRDLKPENLLFT 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 242 SND---CVKLGDFGLSRYMEDSTYYKASKGKLPikWMAPE----SINFRRFTSASDVWMFGVCMWEILmHGVKPFQGVKN 314
Cdd:cd14092   134 DEDddaEIKIVDFGFARLKPENQPLKTPCFTLP--YAAPEvlkqALSTQGYDESCDLWSLGVILYTML-SGQVPFQSPSR 210
                         170
                  ....*....|....*
gi 1914781966 315 N----DVIGRIENGE 325
Cdd:cd14092   211 NesaaEIMKRIKSGD 225
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
114-321 6.62e-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: 66.69  E-value: 6.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiymSPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlG 191
Cdd:cd07839     8 IGEGTYGTVFKA---KNRETHEIVALKRVRLDDDDEgVPSSALREICLLKELKHKNIVRLYDVLhSDKKLTLVFEYCD-Q 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASKGKL 270
Cdd:cd07839    84 DLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARaFGIPVRCYSAEVVTL 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 271 pikWMAPESINF--RRFTSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRI 321
Cdd:cd07839   164 ---WYRPPDVLFgaKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRI 213
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
113-352 6.86e-12

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: 67.40  E-value: 6.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 113 CIGEGQFGdvhqgIYMSPENPAL--AVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITE------NPVWI 183
Cdd:cd07858    12 PIGRGAYG-----IVCSAKNSETneKVAIKKIANAFDNRIDAKrTLREIKLLRHLDHENVIAIKDIMPPphreafNDVYI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELctlgelrsflqvrkYSLDLASLI------------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDF 251
Cdd:cd07858    87 VYEL--------------MDTDLHQIIrssqtlsddhcqYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 252 GLSRYMEDS----TYYKASKgklpiKWMAPESI-NFRRFTSASDVWMFGVCMWEILmhGVKP-FQ--------------- 310
Cdd:cd07858   153 GLARTTSEKgdfmTEYVVTR-----WYRAPELLlNCSEYTTAIDVWSVGCIFAELL--GRKPlFPgkdyvhqlklitell 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 311 GVKNNDVIGRIENG------ERLP---------MPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd07858   226 GSPSEEDLGFIRNEkarryiRSLPytprqsfarLFPHANPLAIDLLEKMLVFDPSKR 282
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
96-360 7.22e-12

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: 67.60  E-value: 7.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  96 PSTRDYEIQRErielgrcIGEGQFGDVHQGiymSPENPALAVAIKTCKNctSDSVREKFLQEALTMRQF----DHPHIVK 171
Cdd:cd05610     1 PSIEEFVIVKP-------ISRGAFGKVYLG---RKKNNSKLYAVKVVKK--ADMINKNMVHQVQAERDAlalsKSPFIVH 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 172 LI-GVITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 250
Cdd:cd05610    69 LYySLQSANNVYLVMEYLIGGDVKSLLHIYGY-FDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 251 FGLSRY-------MED--------------------------------STYYKASK----GKLPIK---------WMAPE 278
Cdd:cd05610   148 FGLSKVtlnrelnMMDilttpsmakpkndysrtpgqvlslisslgfntPTPYRTPKsvrrGAARVEgerilgtpdYLAPE 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 279 SINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGErLPMPP-------NCPPTLYSLMTkcwaYDPSR 351
Cdd:cd05610   228 LLLGKPHGPAVDWWALGVCLFEFLT-GIPPFNDETPQQVFQNILNRD-IPWPEgeeelsvNAQNAIEILLT----MDPTK 301

                  ....*....
gi 1914781966 352 RPRFTELKA 360
Cdd:cd05610   302 RAGLKELKQ 310
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
106-360 8.88e-12

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: 67.31  E-value: 8.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTCKNCtsDSVREK----FLQEALTMRQFDHPHIVKLigVIT---E 178
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQV---YAMKILRKS--DMLKREqiahVRAERDILADADSPWIVRL--HYAfqdE 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05573    74 DHLYLVMEYMPGGDLMNLL-IKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGLCTKMN 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DS--TYYKASKGKLPIK--------------------------WMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPFQ 310
Cdd:cd05573   153 KSgdRESYLNDSVNTLFqdnvlarrrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEML-YGFPPFY 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 311 GVKNNDVIGRIENGE---RLPMPPNCPPTLYSLMTKCWAyDPSRR-PRFTELKA 360
Cdd:cd05573   232 SDSLVETYSKIMNWKeslVFPDDPDVSPEAIDLIRRLLC-DPEDRlGSAEEIKA 284
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
114-309 8.90e-12

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: 66.60  E-value: 8.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVhqgIYMSPENPALAVAIKTcKNCTSDSVREKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGE 192
Cdd:cd06658    30 IGEGSTGIV---CIATEKHTGKQVAVKK-MDLRKQQRRELLFNEVVIMRDYHHENVVDMYnSYLVGDELWVVMEFLEGGA 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLP 271
Cdd:cd06658   106 LTDIVtHTRMNEEQIATVCLSVLR---ALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSLVGTP 182
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1914781966 272 IkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPF 309
Cdd:cd06658   183 Y-WMAPEVISRLPYGTEVDIWSLGIMVIE-MIDGEPPY 218
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
114-334 9.68e-12

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


Pssm-ID: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 66.75  E-value: 9.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIymsPENPALAVAIKTCKnctSDSVREKF----LQEALTMRQFDHPHIVKLIGVITENpvwiIMELCT 189
Cdd:cd07864    15 IGEGTYGQVYKAK---DKDTGELVALKKVR---LDNEKEGFpitaIREIKILRQLNHRSVVNLKEIVTDK----QDALDF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKY-SLDLASLI-------------LYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd07864    85 KKDKGAFYLVFEYmDHDLMGLLesglvhfsedhikSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGLAR 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 YM--EDSTYYkasKGKLPIKWMAPESINF--RRFTSASDVWMFGVCMWEILMHgvKP-FQGvknNDVIGRIENGERL--- 327
Cdd:cd07864   165 LYnsEESRPY---TNKVITLWYRPPELLLgeERYGPAIDVWSCGCILGELFTK--KPiFQA---NQELAQLELISRLcgs 236

                  ....*..
gi 1914781966 328 PMPPNCP 334
Cdd:cd07864   237 PCPAVWP 243
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
118-325 1.09e-11

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: 66.19  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 118 QFGDVhqgiYMSPENPALAvAIKTCKNCT-------------SDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-VWI 183
Cdd:cd14177     1 QFTDV----YELKEDIGVG-SYSVCKRCIhratnmefavkiiDKSKRDPSEEIEILMRYGQHPNIITLKDVYDDGRyVYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLV----SSNDCVKLGDFGLSRYMe 258
Cdd:cd14177    76 VTELMKGGELlDRILRQKFFSEREASAVLYT--ITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRICDFGFAKQL- 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 259 dstyyKASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNN---DVIGRIENGE 325
Cdd:cd14177   153 -----RGENGLLltpcyTANFVAPEVLMRQGYDAACDIWSLGVLLYTMLA-GYTPFANGPNDtpeEILLRIGSGK 221
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
151-324 1.10e-11

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


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 65.71  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLSTALAYLESKRFV 229
Cdd:cd14110    43 KQLVLREYQVLRRLSHPRIAQLHSAYlSPRHLVLIEELCSGPELLYNLAERN-SYSEAEVTDYLWQILSAVDYLHSRRIL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 230 HRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14110   122 HLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTDKKGDYVETMAPELLEGQGAGPQTDIWAIGVTAF-IMLSADYPV 200
                         170
                  ....*....|....*
gi 1914781966 310 QGVKNNDVIGRIENG 324
Cdd:cd14110   201 SSDLNWERDRNIRKG 215
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
114-310 1.43e-11

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 65.25  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCKncTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGE 192
Cdd:cd14087     9 IGRGSFSRVVRVEHRVTRQP---YAIKMIE--TKCRGREVCESELNVLRRVRHTNIIQLIEVFeTKERVYMVMELATGGE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVR-KYSLDLASLILyaYQLSTALAYLESKRFVHRDIAARNVLV--SSNDC-VKLGDFGLS--RYMEDSTYYKAS 266
Cdd:cd14087    84 LFDRIIAKgSFTERDATRVL--QMVLDGVKYLHGLGITHRDLKPENLLYyhPGPDSkIMITDFGLAstRKKGPNCLMKTT 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1914781966 267 KGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQ 310
Cdd:cd14087   162 CGT-P-EYIAPEILLRKPYTQSVDMWAVGVIAY-ILLSGTMPFD 202
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
151-358 1.44e-11

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 65.81  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 151 REKFLQEALTMRQFDHPHIVKLI-GVITENPVWIIMELCTLGELRSFL-QVRKYSLDLASLILYAYQlstALAYLESKRF 228
Cdd:cd06657    61 RELLFNEVVIMRDYQHENVVEMYnSYLVGDELWVVMEFLEGGALTDIVtHTRMNEEQIAAVCLAVLK---ALSVLHAQGV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKP 308
Cdd:cd06657   138 IHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPY-WMAPELISRLPYGPEVDIWSLGIMVIE-MVDGEPP 215
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 309 FQGVKNNDVIGRIENG--ERLPMPPNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd06657   216 YFNEPPLKAMKMIRDNlpPKLKNLHKVSPSLKGFLDRLLVRDPAQRATAAEL 267
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
114-361 1.52e-11

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: 65.63  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHqGIYMSPENPALAvaiktCKNCTSDSVREK-----FLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:cd05577     1 LGRGGFGEVC-ACQVKATGKMYA-----CKKLDKKRIKKKkgetmALNEKIILEKVSSPFIVSLAYAFeTKDKLCLVLTL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFL-QVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKAS 266
Cdd:cd05577    75 MNGGDLKYHIyNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKlpIKWMAPESI-NFRRFTSASDVWMFGVCMWEiLMHGVKPFQ----GVKNNDVIGRIENGErLPMPPNCPPTLYSLM 341
Cdd:cd05577   155 VGT--HGYMAPEVLqKEVAYDFSVDWFALGCMLYE-MIAGRSPFRqrkeKVDKEELKRRTLEMA-VEYPDSFSPEARSLC 230
                         250       260
                  ....*....|....*....|
gi 1914781966 342 TKCWAYDPSRRPRFTELKAQ 361
Cdd:cd05577   231 EGLLQKDPERRLGCRGGSAD 250
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
114-354 1.61e-11

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: 65.37  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTS---DSVRE-KFLQEALTMRQFDHPHIVKLIGVIT-ENPVWIIMELc 188
Cdd:cd14133     7 LGKGTFGQVVKCYDLLTGE---EVALKIIKNNKDyldQSLDEiRLLELLNKKDKADKYHIVRLKDVFYfKNHLCIVFEL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 tLGE-LRSFLQVRKYS-LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSND-C-VKLGDFGLSRYMED----- 259
Cdd:cd14133    83 -LSQnLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSrCqIKIIDFGSSCFLTQrlysy 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 260 --STYYKaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIE------NGERLPMPP 331
Cdd:cd14133   162 iqSRYYR-----------APEVILGLPYDEKIDMWSLGCILAELYT-GEPLFPGASEVDQLARIIgtigipPAHMLDQGK 229
                         250       260
                  ....*....|....*....|...
gi 1914781966 332 NCPPTLYSLMTKCWAYDPSRRPR 354
Cdd:cd14133   230 ADDELFVDFLKKLLEIDPKERPT 252
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
109-367 1.84e-11

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: 64.95  E-value: 1.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMspeNPALAVAIK-TCKNCTSDSVR----EKFLQE-ALTMR--QFDHPHIVKLIG--VITE 178
Cdd:cd14005     3 EVGDLLGKGGFGTVYSGVRI---RDGLPVAVKfVPKSRVTEWAMingpVPVPLEiALLLKasKPGVPGVIRLLDwyERPD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVwIIME---LCTlgELRSFLQVR-KYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGL 253
Cdd:cd14005    80 GFL-LIMErpePCQ--DLFDFITERgALSENLARIIFR--QVVEAVRHCHQRGVLHRDIKDENLLINLRTgEVKLIDFGC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLpikWMAPESINFRRF--TSASdVWMFGVCMWEiLMHGVKPFqgvkNNDvIGRIENgeRLPMPP 331
Cdd:cd14005   155 GALLKDSVYTDFDGTRV---YSPPEWIRHGRYhgRPAT-VWSLGILLYD-MLCGDIPF----END-EQILRG--NVLFRP 222
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 332 NCPPTLYSLMTKCWAYDPSRRPrftelkaQLSTILE 367
Cdd:cd14005   223 RLSKECCDLISRCLQFDPSKRP-------SLEQILS 251
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
112-352 2.75e-11

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: 65.87  E-value: 2.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVhqgIYMSPENPALAVAIKTCKN---CTSDSVREKfLQEALTMRQFDHPHIVKL-IGVITENPVWIIMEL 187
Cdd:cd05593    21 KLLGKGTFGKV---ILVREKASGKYYAMKILKKeviIAKDEVAHT-LTESRVLKNTRHPFLTSLkYSFQTKDRLCFVMEY 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKA 265
Cdd:cd05593    97 VNGGELFFHLsRERVFSEDRTRF--YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKT 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGvKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCW 345
Cdd:cd05593   175 FCGT--PEYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPFYN-QDHEKLFELILMEDIKFPRTLSADAKSLLSGLL 250

                  ....*..
gi 1914781966 346 AYDPSRR 352
Cdd:cd05593   251 IKDPNKR 257
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
78-301 2.87e-11

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 65.07  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  78 SETDDYAEIIDEEDTYTMPSTRDYEIQRERIELGRcigeGQFGDVHQGIymspeNPALAVAIKTCK---NCTSDSVREKF 154
Cdd:cd14030     1 EERNKQQDEIEELETKAVG*SPDGRFLKFDIEIGR----GSFKTVYKGL-----DTETTVEVAWCElqdRKLSKSERQRF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKLIG-----VITENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR-- 227
Cdd:cd14030    72 KEEAGMLKGLQHPNIVRFYDswestVKGKKCIVLVTELMTSGTLKTYLK-RFKVMKIKVLRSWCRQILKGLQFLHTRTpp 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 228 FVHRDIAARNVLVSS-NDCVKLGDFGLSRyMEDSTYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWEI 301
Cdd:cd14030   151 IIHRDLKCDNIFITGpTGSVKIGDLGLAT-LKRASFAKSVIGT--PEFMAPEMYE-EKYDESVDVYAFGMCMLEM 221
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
99-330 2.89e-11

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: 66.19  E-value: 2.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  99 RDYEIQRERIELGRCIGEGQFGDVHQgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKL-IGVIT 177
Cdd:cd05623    65 KQMRLHKEDFEILKVIGRGAFGEVAV-VKLKNADKVFAMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLhYAFQD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 178 ENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS-RY 256
Cdd:cd05623   144 DNNLYLVMDYYVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSClKL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDSTYYKASKGKLPiKWMAPESINFR-----RFTSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIEN-GERLPMP 330
Cdd:cd05623   224 MEDGTVQSSVAVGTP-DYISPEILQAMedgkgKYGPECDWWSLGVCMYEML-YGETPFYAESLVETYGKIMNhKERFQFP 301
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
106-369 3.04e-11

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


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 65.07  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-----GVITEN 179
Cdd:cd14219     5 KQIQMVKQIGKGRYGEVWMGKWRGEK-----VAVKVFFTTEEASwFRETEIYQTVLMR---HENILGFIaadikGTGSWT 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDF 251
Cdd:cd14219    77 QLYLITDYHENGSLYDYL--KSTTLDTKAMLKLAYSSVSGLCHLHTEIFstqgkpaiAHRDLKSKNILVKKNGTCCIADL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 252 GLS-RYMEDStyykaSKGKLPI-------KWMAPE----SINFRRFTS--ASDVWMFGVCMWEILMHGVK---------P 308
Cdd:cd14219   155 GLAvKFISDT-----NEVDIPPntrvgtkRYMPPEvldeSLNRNHFQSyiMADMYSFGLILWEVARRCVSggiveeyqlP 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 309 FQGVKNND----------VIGRIEngerlPMPPN------CPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTILEEE 369
Cdd:cd14219   230 YHDLVPSDpsyedmreivCIKRLR-----PSFPNrwssdeCLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQ 301
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
142-310 3.09e-11

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: 65.06  E-value: 3.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 142 CKNCTSDSVREKFL-------QEALTMRQF-------DHPHIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-YSLD 205
Cdd:cd14179    23 CRKCLHKKTNQEYAvkivskrMEANTQREIaalklceGHPNIVKLHEVYHDQlHTFLVMELLKGGELLERIKKKQhFSET 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 206 LASLILYayQLSTALAYLESKRFVHRDIAARNVLV---SSNDCVKLGDFGLSRYME-DSTYYKASKgkLPIKWMAPESIN 281
Cdd:cd14179   103 EASHIMR--KLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKPpDNQPLKTPC--FTLHYAAPELLN 178
                         170       180
                  ....*....|....*....|....*....
gi 1914781966 282 FRRFTSASDVWMFGVCMWEILmHGVKPFQ 310
Cdd:cd14179   179 YNGYDESCDLWSLGVILYTML-SGQVPFQ 206
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
109-309 3.23e-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: 3.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVhqgIYMSPENPALAVAIKtCKNCTSDSVREKFLQ-EALTMRQFDHPHIVKLIGvITENP--VWIIM 185
Cdd:cd14169     6 ELKEKLGEGAFSEV---VLAQERGSQRLVALK-CIPKKALRGKEAMVEnEIAVLRRINHENIVSLED-IYESPthLYLAM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRKY--SLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRyMEDS 260
Cdd:cd14169    81 ELVTGGELFDRIIERGSytEKDASQLI---GQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSK-IEAQ 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 261 TYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14169   157 GMLSTACGT-P-GYVAPELLEQKPYGKAVDVWAIGVISY-ILLCGYPPF 202
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
106-352 3.53e-11

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: 65.08  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQEAL----TMRQFDHPHIVKLIGVIT--EN 179
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLT-EQRYVAVKIHQLNKNWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSldTD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKY--SLDLASLILyayQLSTALAYLESKR--FVHRDIAARNVL-VSSNDC--VKLGDFG 252
Cdd:cd14041    85 SFCTVLEYCEGNDLDFYLKQHKLmsEKEARSIIM---QIVNALKYLNEIKppIIHYDLKPGNILlVNGTACgeIKITDFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYMEDSTYYK------ASKGKLPIKWMAPESINF----RRFTSASDVWMFGVCMWEILmHGVKPFQG-------VKNN 315
Cdd:cd14041   162 LSKIMDDDSYNSvdgmelTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFYQCL-YGRKPFGHnqsqqdiLQEN 240
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1914781966 316 DVIGRIEngERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd14041   241 TILKATE--VQFPPKPVVTPEAKAFIRRCLAYRKEDR 275
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
107-261 3.82e-11

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 64.40  E-value: 3.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKT-CKNCTSDSVRekflQEALTMRQF-DHPHIVKLIGVITENPV-WI 183
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEE---VAIKIeKKDSKHPQLE----YEAKVYKLLqGGPGIPRLYWFGQEGDYnVM 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMEL--CTLGELRSFLQvRKYSLDLASLIlyAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVK---LGDFGLS-RYM 257
Cdd:cd14016    74 VMDLlgPSLEDLFNKCG-RKFSLKTVLML--ADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAkKYR 150

                  ....
gi 1914781966 258 EDST 261
Cdd:cd14016   151 DPRT 154
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
106-316 4.12e-11

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: 65.43  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQfgdvhQGIYMSPENPALAVAI---KTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP-- 180
Cdd:cd07876    21 KRYQQLKPIGSGA-----QGIVCAAFDTVLGINVavkKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKsl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 -----VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd07876    96 eefqdVYLVMELMD----ANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 256 YMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNND 316
Cdd:cd07876   172 TA--CTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGE-LVKGSVIFQGTDHID 229
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
114-301 4.12e-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: 64.64  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlGE 192
Cdd:cd07873    10 LGEGTYATVYKGRSKLTDN---LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIhTEKSLTLVFEYLD-KD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyyKASKGKLPI 272
Cdd:cd07873    86 LKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSIPT--KTYSNEVVT 163
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1914781966 273 KWMAPESI--NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd07873   164 LWYRPPDIllGSTDYSTQIDMWGVGCIFYEM 194
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
140-301 4.16e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 65.40  E-value: 4.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 140 KTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKySLDLASLILYAYQLST 218
Cdd:PHA03212  115 KTCEHVVIKAgQRGGTATEAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKTDLYCYLAAKR-NIAICDILAIERSVLR 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 219 ALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCM 298
Cdd:PHA03212  194 AIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVDINANKYYGWAGTIATNAPELLARDPYGPAVDIWSAGIVL 273

                  ...
gi 1914781966 299 WEI 301
Cdd:PHA03212  274 FEM 276
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
114-342 4.38e-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: 65.06  E-value: 4.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIymsPENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQFDHPHIVKLIGVITE-------NPVWIIM 185
Cdd:cd07877    25 VGSGAYGSVCAAF---DTKTGLRVAVKKLSRPFQSIIHAKrTYRELRLLKHMKHENVIGLLDVFTParsleefNDVYLVT 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTlGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyyka 265
Cdd:cd07877   102 HLMG-ADLNNIVKCQKLTDDHVQFLIY--QILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEM---- 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 266 sKGKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEILMhGVKPFQGvknNDVIGRIENGERLPMPPncPPTLYSLMT 342
Cdd:cd07877   175 -TGYVATRWYrAPEiMLNWMHYNQTVDIWSVGCIMAELLT-GRTLFPG---TDHIDQLKLILRLVGTP--GAELLKKIS 246
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
114-305 5.28e-11

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: 64.31  E-value: 5.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKnctSDSVREKF----LQEALTMRQFDHPHIVKLIGVITENP--------- 180
Cdd:cd07865    20 IGQGTFGEVFKARHRKTGQ---IVALKKVL---MENEKEGFpitaLREIKILQLLKHENVVNLIEICRTKAtpynrykgs 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd07865    94 IYLVFEFCE-HDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARAFSLA 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 261 TYYKASK--GKLPIKWM-APES-INFRRFTSASDVWMFGVCMWEI-----LMHG 305
Cdd:cd07865   173 KNSQPNRytNRVVTLWYrPPELlLGERDYGPPIDMWGAGCIMAEMwtrspIMQG 226
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
106-309 5.39e-11

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 63.89  E-value: 5.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDvhqgIYMSPENPALAvaIKTCKNCTSD---SVREKFLQEALTMRQFDHPHIVKLIGV-ITENPV 181
Cdd:cd14088     1 DRYDLGQVIKTEEFCE----IFRAKDKTTGK--LYTCKKFLKRdgrKVRKAAKNEINILKMVKHPNILQLVDVfETRKEY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 182 WIIMELCTLGELRSFLQVRKY--SLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRY 256
Cdd:cd14088    75 FIFLELATGREVFDWILDQGYysERDTSNVI---RQVLEAVAYLHSLKIVHRNLKLENLVYYNrlkNSKIVISDFHLAKL 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 257 meDSTYYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14088   152 --ENGLIKEPCGT-P-EYLAPEVVGRQRYGRPVDCWAIGVIMY-ILLSGNPPF 199
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
111-302 6.82e-11

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: 63.56  E-value: 6.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVH-------------QGIYMSPENPALAVAIKTCKnCtsdsvrekflqEALTMRQFDHPHIVKLIGVI- 176
Cdd:cd06651    12 GKLLGQGAFGRVYlcydvdtgrelaaKQVQFDPESPETSKEVSALE-C-----------EIQLLKNLQHERIVQYYGCLr 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 --TENPVWIIMELCTLGELRSflQVRKYSLDLASLIL-YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd06651    80 drAEKTLTIFMEYMPGGSVKD--QLKAYGALTESVTRkYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 254 SRYMEdsTYYKASKGKLPIK----WMAPESINFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd06651   158 SKRLQ--TICMSGTGIRSVTgtpyWMSPEVISGEGYGRKADVWSLGCTVVEML 208
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
114-301 8.13e-11

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: 63.62  E-value: 8.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSdSVREKFLQEALTMRqfdHPHIVKLI-------GVITEnpVWIIME 186
Cdd:cd14143     3 IGKGRFGEVWRGRWRGED---VAVKIFSSREERS-WFREAEIYQTVMLR---HENILGFIaadnkdnGTWTQ--LWLVSD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESK--------RFVHRDIAARNVLVSSNDCVKLGDFGLS-RY- 256
Cdd:cd14143    74 YHEHGSLFDYLN--RYTVTVEGMIKLALSIASGLAHLHMEivgtqgkpAIAHRDLKSKNILVKKNGTCCIADLGLAvRHd 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 257 MEDSTYYKASKGKLPIK-WMAPE----SINFRRFTS--ASDVWMFGVCMWEI 301
Cdd:cd14143   152 SATDTIDIAPNHRVGTKrYMAPEvlddTINMKHFESfkRADIYALGLVFWEI 203
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
159-325 9.19e-11

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


Pssm-ID: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 63.49  E-value: 9.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 159 LTMRQFDHPHIVKLIGVITENP-VWIIMELCTLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAAR 236
Cdd:cd14178    49 ILLRYGQHPNIITLKDVYDDGKfVYLVMELMRGGELlDRILRQKCFSEREASAVLCT--ITKTVEYLHSQGVVHRDLKPS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 237 NVL----VSSNDCVKLGDFGLSRYMedstyyKASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVK 307
Cdd:cd14178   127 NILymdeSGNPESIRICDFGFAKQL------RAENGLLmtpcyTANFVAPEVLKRQGYDAACDIWSLGILLYTMLA-GFT 199
                         170       180
                  ....*....|....*....|.
gi 1914781966 308 PFQGVKNN---DVIGRIENGE 325
Cdd:cd14178   200 PFANGPDDtpeEILARIGSGK 220
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
149-360 9.97e-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: 63.61  E-value: 9.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 149 SVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLILYAyqLSTALAYLESK 226
Cdd:cd06615    41 AIRNQIIRELKVLHECNSPYIVGFYGAFySDGEISICMEHMDGGSLDQVLKkAGRIPENILGKISIA--VLRGLTYLREK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 227 R-FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyykASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEIL--- 302
Cdd:cd06615   119 HkIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM---ANSFVGTRSYMSPERLQGTHYTVQSDIWSLGLSLVEMAigr 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 303 -------------MHGVKPFQGVKNNDVIGRIENG--ERLPM-------------PPNCPPTLYS-----LMTKCWAYDP 349
Cdd:cd06615   196 ypipppdakeleaMFGRPVSEGEAKESHRPVSGHPpdSPRPMaifelldyivnepPPKLPSGAFSdefqdFVDKCLKKNP 275
                         250
                  ....*....|.
gi 1914781966 350 SRRPRFTELKA 360
Cdd:cd06615   276 KERADLKELTK 286
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
106-302 1.01e-10

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: 63.92  E-value: 1.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIymsPENPALAVAIKTCKNcTSDSVR--EKFLQEALTMRQFDHPHIVKLIGVITEN---- 179
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAI---DTKSGQKVAIKKIPN-AFDVVTtaKRTLRELKILRHFKHDNIIAIRDILRPKvpya 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 ---PVWIIMELctlgeLRSFLQVRKYS---LDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd07855    81 dfkDVYVVLDL-----MESDLHHIIHSdqpLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGM 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 254 SRYM----EDSTYYKASkgKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd07855   156 ARGLctspEEHKYFMTE--YVATRWYrAPElMLSLPEYTQAIDMWSVGCIFAEML 208
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
114-321 1.35e-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: 63.17  E-value: 1.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGiyMSPENPALaVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLgE 192
Cdd:cd07869    13 LGEGSYATVYKG--KSKVNGKL-VALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIhTKETLTLVFEYVHT-D 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKASKGKLPI 272
Cdd:cd07869    89 LCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAR--AKSVPSHTYSNEVVT 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 273 KWMAPESI--NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKN-NDVIGRI 321
Cdd:cd07869   167 LWYRPPDVllGSTEYSTCLDMWGVG-CIFVEMIQGVAAFPGMKDiQDQLERI 217
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
105-353 1.40e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 62.91  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRcIGEGQFGDVHQ------GIYMspenpalavAIK--TCKNCTSDSVReKFLQEALTMRQFDHPHIVKLIGVI 176
Cdd:cd14049     6 NEFEEIAR-LGKGGYGKVYKvrnkldGQYY---------AIKkiLIKKVTKRDCM-KVLREVKVLAGLQHPNIVGYHTAW 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TEN---PVWIIMELCTLgELRSFLQVRK---------------YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNV 238
Cdd:cd14049    75 MEHvqlMLYIQMQLCEL-SLWDWIVERNkrpceeefksapytpVDVDVTTKILQ--QLLEGVTYIHSMGIVHRDLKPRNI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 239 LVSSNDC-VKLGDFGL-----------SRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILmhgv 306
Cdd:cd14049   152 FLHGSDIhVRIGDFGLacpdilqdgndSTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYDFKSDMYSIGVILLELF---- 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 307 KPFQG-VKNNDVIGRIENGErlpMPPN---CPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd14049   228 QPFGTeMERAEVLTQLRNGQ---IPKSlckRWPVQAKYIKLLTSTEPSERP 275
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
184-309 1.49e-10

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: 63.49  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLqVRK--YSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS---RYME 258
Cdd:cd05598    79 VMDYIPGGDLMSLL-IKKgiFEEDLARF--YIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfRWTH 155
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 259 DSTYYKA-SKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd05598   156 DSKYYLAhSLVGTP-NYIAPEVLLRTGYTQLCDWWSVGVILYEMLV-GQPPF 205
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
112-365 1.61e-10

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: 62.75  E-value: 1.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPEnpalaVAIKTCKNCTSDS-VREKFLQEALTMRqfdHPHIVKLI-----GVITENPVWIIM 185
Cdd:cd14220     1 RQIGKGRYGEVWMGKWRGEK-----VAVKVFFTTEEASwFRETEIYQTVLMR---HENILGFIaadikGTGSWTQLYLIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLQVRkySLDLASLILYAYQLSTALAYLESKRF--------VHRDIAARNVLVSSNDCVKLGDFGLSRYM 257
Cdd:cd14220    73 DYHENGSLYDFLKCT--TLDTRALLKLAYSAACGLCHLHTEIYgtqgkpaiAHRDLKSKNILIKKNGTCCIADLGLAVKF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 258 EDSTyykaSKGKLPI-------KWMAP----ESINFRRFTS--ASDVWMFGVCMWEILMHGVK---------PFQGVKNN 315
Cdd:cd14220   151 NSDT----NEVDVPLntrvgtkRYMAPevldESLNKNHFQAyiMADIYSFGLIIWEMARRCVTggiveeyqlPYYDMVPS 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 316 DV----IGRIENGERL-PMPPN------CPPTLYSLMTKCWAYDPSRRPRFTELKAQLSTI 365
Cdd:cd14220   227 DPsyedMREVVCVKRLrPTVSNrwnsdeCLRAVLKLMSECWAHNPASRLTALRIKKTLAKM 287
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
114-358 1.84e-10

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 61.95  E-value: 1.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHqgiymspenpaLAVAIKTCKNCTSDSVR-EKFLQEALTMRQ-FDHPHIVKLIG-VITENPVWIIMEL--- 187
Cdd:cd13995    12 IPRGAFGKVY-----------LAQDTKTKKRMACKLIPvEQFKPSDVEIQAcFRHENIAELYGaLLWEETVHLFMEAgeg 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 -CTLGELRSFLQVRKYSLdlaslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVkLGDFGLSRYMEDSTYYKAS 266
Cdd:cd13995    81 gSVLEKLESCGPMREFEI-----IWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAV-LVDFGLSVQMTEDVYVPKD 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 267 KGKLPIkWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFqgVKNNDVIG-----RIENGERLPM---PPNCPPTLY 338
Cdd:cd13995   155 LRGTEI-YMSPEVILCRGHNTKADIYSLGATIIH-MQTGSPPW--VRRYPRSAypsylYIIHKQAPPLediAQDCSPAMR 230
                         250       260
                  ....*....|....*....|
gi 1914781966 339 SLMTKCWAYDPSRRPRFTEL 358
Cdd:cd13995   231 ELLEAALERNPNHRSSAAEL 250
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
166-352 1.86e-10

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: 62.79  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 166 HPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 243
Cdd:cd05592    55 HPFLTHLFCTFqTESHLFFVMEYLNGGDLMFHIQqSGRFDEDRARF--YGAEIICGLQFLHSRGIIYRDLKLDNVLLDRE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 244 DCVKLGDFGLS-----RYMEDSTYYKASKgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVI 318
Cdd:cd05592   133 GHIKIADFGMCkeniyGENKASTFCGTPD------YIAPEILKGQKYNQSVDWWSFGVLLYEMLI-GQSPFHGEDEDELF 205
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1914781966 319 GRIENgERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05592   206 WSICN-DTPHYPRWLTKEAASCLSLLLERNPEKR 238
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
95-329 1.91e-10

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 64.37  E-value: 1.91e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966   95 MPST-RDYEIQRERIELGRCIGEGQFGDVHQGIYMSPENPAL--AVAIKTCKNctsdsvREK--FLQEALTMRQFDHPHI 169
Cdd:PTZ00266     1 MPGKyDDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCwkAISYRGLKE------REKsqLVIEVNVMRELKHKNI 74
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  170 VKLIGVI---TENPVWIIMELCTLGELRSFLQvRKYSL----DLASLILYAYQLSTALAYLES-------KRFVHRDIAA 235
Cdd:PTZ00266    75 VRYIDRFlnkANQKLYILMEFCDAGDLSRNIQ-KCYKMfgkiEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKP 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  236 RNVLVSSN-----------------DCVKLGDFGLSRYMEDSTYYKASKGKlPIKWmAPESI--NFRRFTSASDVWMFGV 296
Cdd:PTZ00266   154 QNIFLSTGirhigkitaqannlngrPIAKIGDFGLSKNIGIESMAHSCVGT-PYYW-SPELLlhETKSYDDKSDMWALGC 231
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1914781966  297 CMWEiLMHGVKPFQGVKN-NDVIGRIENGERLPM 329
Cdd:PTZ00266   232 IIYE-LCSGKTPFHKANNfSQLISELKRGPDLPI 264
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
112-313 2.05e-10

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 62.23  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVhqgiymspenpaLAVAIKT------CKNCTSDSVREK-----FLQEALTMRQFDHPHIVKLIGVI-TEN 179
Cdd:cd05607     8 RVLGKGGFGEV------------CAVQVKNtgqmyaCKKLDKKRLKKKsgekmALLEKEILEKVNSPFIVSLAYAFeTKT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELR-SFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05607    76 HLCLVMSLMNGGDLKyHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 259 DS---TYYKASKGklpikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVK 313
Cdd:cd05607   156 EGkpiTQRAGTNG-----YMAPEILKEESYSYPVDWFAMGCSIYEMVA-GRTPFRDHK 207
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
112-352 2.21e-10

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 62.62  E-value: 2.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSPENpalAVAIKTCKN---CTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMEL 187
Cdd:cd05590     1 RVLGKGSFGKVMLARLKESGR---LYAVKVLKKdviLQDDDVECTMTEKRILSLARNHPFLTQLYCCFqTPDRLFFVMEF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 188 CTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASK 267
Cdd:cd05590    78 VNGGDLMFHIQ-KSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGKTTSTF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 268 GKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGERLP---MPPNCPPTLYSLMTKc 344
Cdd:cd05590   157 CGTP-DYIAPEILQEMLYGPSVDWWAMGVLLYEMLC-GHAPFEAENEDDLFEAILNDEVVYptwLSQDAVDILKAFMTK- 233

                  ....*...
gi 1914781966 345 wayDPSRR 352
Cdd:cd05590   234 ---NPTMR 238
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
108-302 2.37e-10

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


Pssm-ID: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 62.84  E-value: 2.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRCIGEGQFGDVhqgiyMSPENP--ALAVAIKTCKNCTSDSVREKFLQEALTMR-QFDHPHIVKLIGVITENPVWII 184
Cdd:cd07853     2 VEPDRPIGYGAFGVV-----WSVTDPrdGKRVALKKMPNVFQNLVSCKRVFRELKMLcFFKHDNVLSALDILQPPHIDPF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGEL-RSFLQ---VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS 260
Cdd:cd07853    77 EEIYVVTELmQSDLHkiiVSPQPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPD 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1914781966 261 TYYKASKGKLPIKWMAPESI-NFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd07853   157 ESKHMTQEVVTQYYRAPEILmGSRHYTSAVDIWSVGCIFAELL 199
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
106-352 2.44e-10

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: 62.38  E-value: 2.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPAlAVAIKTCKNCTSDSVREKFLQEAL----TMRQFDHPHIVKLIGVIT--EN 179
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYA-AVKIHQLNKSWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSldTD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKY--SLDLASLILyayQLSTALAYLESKR--FVHRDIAARNVL-VSSNDC--VKLGDFG 252
Cdd:cd14040    85 TFCTVLEYCEGNDLDFYLKQHKLmsEKEARSIVM---QIVNALRYLNEIKppIIHYDLKPGNILlVDGTACgeIKITDFG 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 253 LSRYMEDSTYYK-----ASKGKLPIKWMAPESINF----RRFTSASDVWMFGVCMWEILmHGVKPFQG-------VKNND 316
Cdd:cd14040   162 LSKIMDDDSYGVdgmdlTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFGHnqsqqdiLQENT 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1914781966 317 VIGRIEngERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd14040   241 ILKATE--VQFPVKPVVSNEAKAFIRRCLAYRKEDR 274
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
138-309 2.66e-10

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


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 62.15  E-value: 2.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 138 AIKTCKNctsdSVREKFLQ-EALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQVRKY--SLDLASLIlya 213
Cdd:cd14085    32 AVKKLKK----TVDKKIVRtEIGVLLRLSHPNIIKLKEIFeTPTEISLVLELVTGGELFDRIVEKGYysERDAADAV--- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 214 YQLSTALAYLESKRFVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRRFTSASD 290
Cdd:cd14085   105 KQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKIVDQQVTMKTVCGT-P-GYCAPEILRGCAYGPEVD 182
                         170
                  ....*....|....*....
gi 1914781966 291 VWMFGVCMWeILMHGVKPF 309
Cdd:cd14085   183 MWSVGVITY-ILLCGFEPF 200
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
106-321 2.68e-10

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: 62.76  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGiYMSPENPALAVAiKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE------- 178
Cdd:cd07878    15 ERYQNLTPVGSGAYGSVCSA-YDTRLRQKVAVK-KLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPatsienf 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTlGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSnDC-VKLGDFGLSRYM 257
Cdd:cd07878    93 NEVYLVTNLMG-ADLNNIVKCQKLSDEHVQFLIY--QLLRGLKYIHSAGIIHRDLKPSNVAVNE-DCeLRILDFGLARQA 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 258 EDSTyykasKGKLPIKWM-APE-SINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI 321
Cdd:cd07878   169 DDEM-----TGYVATRWYrAPEiMLNWMHYNQTVDIWSVGCIMAE-LLKGKALFPGNDYIDQLKRI 228
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
167-309 2.81e-10

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 62.36  E-value: 2.81e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 167 PHIVKLIGVI-----TENPVWIIMELCTLGELRSFLQVR---KYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNV 238
Cdd:cd14170    55 PHIVRIVDVYenlyaGRKCLLIVMECLDGGELFSRIQDRgdqAFTEREASEIMKS--IGEAIQYLHSINIAHRDVKPENL 132
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 239 LVSS---NDCVKLGDFGLSRymEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14170   133 LYTSkrpNAILKLTDFGFAK--ETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGYPPF 203
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
114-321 2.98e-10

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: 62.32  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKN---CTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCT 189
Cdd:cd05615    18 LGKGSFGKVMLAERKGSDE---LYAIKILKKdvvIQDDDVECTMVEKRVLALQDKPPFLTQLHSCFqTVDRLYFVMEYVN 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR-YMEDSTYYKASK 267
Cdd:cd05615    95 GGDLMYHIQqVGKFKEPQA--VFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKeHMVEGVTTRTFC 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 268 GKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI 321
Cdd:cd05615   173 GT-P-DYIAPEIIAYQPYGRSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSI 223
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
106-358 3.24e-10

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: 61.62  E-value: 3.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIE-LGRcIGEGQFGDVHQgiYMSPENPALaVAIKTCKNCTSDSVREKF-LQEALTMRQFDHPHIVKLIGVITEN-PVW 182
Cdd:cd07847     1 EKYEkLSK-IGEGSYGVVFK--CRNRETGQI-VAIKKFVESEDDPVIKKIaLREIRMLKQLKHPNLVNLIEVFRRKrKLH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELCTLGELRSfLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYM----E 258
Cdd:cd07847    77 LVFEYCDHTVLNE-LEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILtgpgD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 259 DSTYYKASkgklpiKWM-APESI-NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIE-------------- 322
Cdd:cd07847   156 DYTDYVAT------RWYrAPELLvGDTQYGPPVDVWAIG-CVFAELLTGQPLWPGKSDVDQLYLIRktlgdliprhqqif 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 323 ------NGERLPMP----------PNCPPTLYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd07847   229 stnqffKGLSIPEPetrepleskfPNISSPALSFLKGCLQMDPTERLSCEEL 280
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
156-306 3.48e-10

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


Pssm-ID: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 62.05  E-value: 3.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 156 QEALTMRQFDHPHIVKLIGVITENP-------VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRF 228
Cdd:cd07850    48 RELVLMKLVNHKNIIGLLNVFTPQKsleefqdVYLVMELMD----ANLCQVIQMDLDHERMSYLLYQMLCGIKHLHSAGI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSnDCV-KLGDFGLSRYMEDST---------YYKaskgklpikwmAPESINFRRFTSASDVWMFGVCM 298
Cdd:cd07850   124 IHRDLKPSNIVVKS-DCTlKILDFGLARTAGTSFmmtpyvvtrYYR-----------APEVILGMGYKENVDIWSVGCIM 191

                  ....*...
gi 1914781966 299 WEILMHGV 306
Cdd:cd07850   192 GEMIRGTV 199
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
114-325 3.75e-10

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


Pssm-ID: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 61.58  E-value: 3.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGD----VHQGIYMSpenpalaVAIKTCKNCTSDSVREKflqeALTMRQFDHPHIVKLIGVITE-NPVWIIMELC 188
Cdd:cd14175     9 IGVGSYSVckrcVHKATNME-------YAVKVIDKSKRDPSEEI----EILLRYGQHPNIITLKDVYDDgKHVYLVTELM 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 189 TLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLV---SSN-DCVKLGDFGLSRYMedstyy 263
Cdd:cd14175    78 RGGELlDKILRQKFFSEREASSVLHT--ICKTVEYLHSQGVVHRDLKPSNILYvdeSGNpESLRICDFGFAKQL------ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 264 KASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF-QGVKNN--DVIGRIENGE 325
Cdd:cd14175   150 RAENGLLmtpcyTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLA-GYTPFaNGPSDTpeEILTRIGSGK 218
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
155-353 3.89e-10

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: 60.99  E-value: 3.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTLGELRSFLQVR-KYSLDlaSLILYAYQLSTALAYLESKRFVHRD 232
Cdd:cd14111    47 LQEYEILKSLHHERIMALhEAYITPRYLVLIAEFCSGKELLHSLIDRfRYSED--DVVGYLVQILQGLEYLHGRRVLHLD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 233 IAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQGV 312
Cdd:cd14111   125 IKPDNIMVTNLNAIKIVDFGSAQSFNPLSLRQLGRRTGTLEYMAPEMVKGEPVGPPADIWSIGVLTY-IMLSGRSPFEDQ 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1914781966 313 KNNDVIGRIENGERLP--MPPNCPPTLYSLMTKCWAYDPSRRP 353
Cdd:cd14111   204 DPQETEAKILVAKFDAfkLYPNVSQSASLFLKKVLSSYPWSRP 246
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
155-352 3.97e-10

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: 61.99  E-value: 3.97e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKL-IGVITENPVWIIMELCTLGELrsFLQV---RKYSLDLASLilYAYQLSTALAYLESKRFVH 230
Cdd:cd05571    43 LTENRVLQNTRHPFLTSLkYSFQTNDRLCFVMEYVNGGEL--FFHLsreRVFSEDRTRF--YGAEIVLALGYLHSQGIVY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 231 RDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKASK---GKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVK 307
Cdd:cd05571   119 RDLKLENLLLDKDGHIKITDFGLCK--EEISYGATTKtfcGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRL 193
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 308 PFQGvKNNDVIGRIENGERLPMPPNCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd05571   194 PFYN-RDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKDPKKR 237
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
94-301 4.37e-10

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: 61.28  E-value: 4.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  94 TMPSTRDYEIQrerIELGRcigeGQFGDVHQGIymspeNPALAVAIKTCK---NCTSDSVREKFLQEALTMRQFDHPHIV 170
Cdd:cd14031     5 TSPGGRFLKFD---IELGR----GAFKTVYKGL-----DTETWVEVAWCElqdRKLTKAEQQRFKEEAEMLKGLQHPNIV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 171 KLIG-----VITENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS- 242
Cdd:cd14031    73 RFYDswesvLKGKKCIVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGp 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 243 NDCVKLGDFGLSRYMEDStYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWEI 301
Cdd:cd14031   152 TGSVKIGDLGLATLMRTS-FAKSVIGT--PEFMAPEMYE-EHYDESVDVYAFGMCMLEM 206
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
156-309 4.45e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 62.60  E-value: 4.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 156 QEALTMRQFDHPHIVKLIGVITENPVWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAA 235
Cdd:PHA03211  209 HEARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRSDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKT 288
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 236 RNVLVSSNDCVKLGDFG---LSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKPF 309
Cdd:PHA03211  289 ENVLVNGPEDICLGDFGaacFARGSWSTPFHYGIAGT--VDTNAPEVLAGDPYTPSVDIWSAGLVIFEAAVHTASLF 363
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
108-301 5.41e-10

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: 61.18  E-value: 5.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRcIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIME 186
Cdd:cd07871     8 VKLDK-LGEGTYATVFKGRSKLTEN---LVALKEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIhTERCLTLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKAS 266
Cdd:cd07871    84 YLD-SDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLAR--AKSVPTKTY 160
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1914781966 267 KGKLPIKWMAPESI--NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd07871   161 SNEVVTLWYRPPDVllGSTEYSTPIDMWGVGCILYEM 197
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
101-254 5.59e-10

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


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 60.85  E-value: 5.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRERIELgrcIGEGQFGDVHQ------GIYMspenpalavAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG 174
Cdd:cd14046     4 YLTDFEELQV---LGKGAFGQVVKvrnkldGRYY---------AIKKIKLRSESKNNSRILREVMLLSRLNHQHVVRYYQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 175 V-ITENPVWIIMELCTLGELRSFLQVRKYsLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd14046    72 AwIERANLYIQMEYCEKSTLRDLIDSGLF-QDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGL 150

                  .
gi 1914781966 254 S 254
Cdd:cd14046   151 A 151
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
106-302 5.68e-10

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: 61.55  E-value: 5.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIymspENPA-LAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI------TE 178
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAV----HKPTgQKVAIKKISPFEHQTYCLRTLREIKILLRFKHENIIGILDIQrpptfeSF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NPVWIIMELCTLgELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd07849    81 KDVYIVQELMET-DLYKLIKTQHLSNDHIQYFLY--QILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIAD 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 259 DS-------TYYKASkgklpiKWM-APE-SINFRRFTSASDVWMFGVCMWEIL 302
Cdd:cd07849   158 PEhdhtgflTEYVAT------RWYrAPEiMLNSKGYTKAIDIWSVGCILAEML 204
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
114-252 6.51e-10

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: 57.84  E-value: 6.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMsPENPALAVAIKTCKNctsDSVREKFLQEALTMRQFD--HPHIVKLIGV-ITENPVWIIMELCTL 190
Cdd:cd13968     1 MGEGASAKVFWAEGE-CTTIGVAVKIGDDVN---NEEGEDLESEMDILRRLKglELNIPKVLVTeDVDGPNILLMELVKG 76
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 191 GELRSFLQVRkySLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd13968    77 GTLIAYTQEE--ELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
114-352 6.63e-10

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 60.31  E-value: 6.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDV------HQGIYMSPENPAlaVAIKtCKNCTSDSVRekFLQE-ALTMRQFDHPHIVKLIGVI-TENPVWIIM 185
Cdd:cd14019     9 IGEGTFSSVykaedkLHDLYDRNKGRL--VALK-HIYPTSSPSR--ILNElECLERLGGSNNVSGLITAFrNEDQVVAVL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGELRSFLqvrkYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSndcvKLG-----DFGLSRYMEDS 260
Cdd:cd14019    84 PYIEHDDFRDFY----RKMSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNR----ETGkgvlvDFGLAQREEDR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 261 TYYKASKGKLPiKWMAPESInFRRF--TSASDVWMFGVCMWEILMHGVKPFQGVKNNDVIGRIEN--GERLpmppncppt 336
Cdd:cd14019   156 PEQRAPRAGTR-GFRAPEVL-FKCPhqTTAIDIWSAGVILLSILSGRFPFFFSSDDIDALAEIATifGSDE--------- 224
                         250
                  ....*....|....*.
gi 1914781966 337 LYSLMTKCWAYDPSRR 352
Cdd:cd14019   225 AYDLLDKLLELDPSKR 240
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
112-309 6.68e-10

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


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 61.14  E-value: 6.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCIGEGQFGDVHQGIYMSpENPALAVAIKTCKNCTSDSVREKFLQE-ALTMRQFDHPHIVKL-IGVITENPVWIIMELCT 189
Cdd:cd05603     1 KVIGKGSFGKVLLAKRKC-DGKFYAVKVLQKKTILKKKEQNHIMAErNVLLKNLKHPFLVGLhYSFQTSEKLYFVLDYVN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGK 269
Cdd:cd05603    80 GGELFFHLQ-RERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKEGMEPEETTSTFCG 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1914781966 270 LPiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVKPF 309
Cdd:cd05603   159 TP-EYLAPEVLRKEPYDRTVDWWCLGAVLYEML-YGLPPF 196
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
210-325 6.75e-10

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


Pssm-ID: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 60.78  E-value: 6.75e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 210 ILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSAS 289
Cdd:cd05631   105 IFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGT--VGYMAPEVINNEKYTFSP 182
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1914781966 290 DVWMFGVCMWEiLMHGVKPF----QGVKNNDVIGRIENGE 325
Cdd:cd05631   183 DWWGLGCLIYE-MIQGQSPFrkrkERVKREEVDRRVKEDQ 221
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
109-352 6.80e-10

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: 61.58  E-value: 6.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCKN---CTSDSVREKfLQEALTMRQFDHPHIVKL-IGVITENPVWII 184
Cdd:cd05594    28 EYLKLLGKGTFGKV---ILVKEKATGRYYAMKILKKeviVAKDEVAHT-LTENRVLQNSRHPFLTALkYSFQTHDRLCFV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFL-QVRKYSLDLASLilYAYQLSTALAYLESKR-FVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDST 261
Cdd:cd05594   104 MEYANGGELFFHLsRERVFSEDRARF--YGAEIVSALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDGA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 YYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGvKNNDVIGRIENGERLPMPPNCPPTLYSLM 341
Cdd:cd05594   182 TMKTFCGT-P-EYLAPEVLEDNDYGRAVDWWGLGVVMYE-MMCGRLPFYN-QDHEKLFELILMEEIRFPRTLSPEAKSLL 257
                         250
                  ....*....|.
gi 1914781966 342 TKCWAYDPSRR 352
Cdd:cd05594   258 SGLLKKDPKQR 268
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
167-309 7.21e-10

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 60.39  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 167 PHIVKLIGVItENP------VWIIMELCTLGELRSFLQVR---KYSLDLASLILYayQLSTALAYLESKRFVHRDIAARN 237
Cdd:cd14172    57 PHIVHILDVY-ENMhhgkrcLLIIMECMEGGELFSRIQERgdqAFTEREASEIMR--DIGTAIQYLHSMNIAHRDVKPEN 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 238 VLVSS---NDCVKLGDFGLSRymEDSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14172   134 LLYTSkekDAVLKLTDFGFAK--ETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMY-ILLCGFPPF 205
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
149-343 7.23e-10

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: 61.22  E-value: 7.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 149 SVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTLGELRsflQVRKYSLDLASLILYAYQLST--ALAYLES 225
Cdd:cd06650    45 AIRNQIIRELQVLHECNSPYIVGFYGAFySDGEISICMEHMDGGSLD---QVLKKAGRIPEQILGKVSIAVikGLTYLRE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 226 K-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyykASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMH 304
Cdd:cd06650   122 KhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSM---ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEMAVG 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1914781966 305 -------GVKPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTK 343
Cdd:cd06650   199 rypipppDAKELELMFGCQVEGDAAETPPRPRTPGRPLSSYGMDSR 244
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
107-311 9.02e-10

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


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 60.64  E-value: 9.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDV-----HQgiymSPENpalaVAIKTCKNctsdsvREKFLQEALT-------MRQFD---HPHIVK 171
Cdd:cd14210    14 RYEVLSVLGKGSFGQVvkcldHK----TGQL----VAIKIIRN------KKRFHQQALVevkilkhLNDNDpddKHNIVR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 172 LIGVIT-ENPVWIIMELctLG-ELRSFLQVRKY---SLDLASLIlyAYQLSTALAYLESKRFVHRDIAARNVLVSSND-- 244
Cdd:cd14210    80 YKDSFIfRGHLCIVFEL--LSiNLYELLKSNNFqglSLSLIRKF--AKQILQALQFLHKLNIIHCDLKPENILLKQPSks 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 245 CVKLGDFGLS--------RYMEdSTYYKaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQG 311
Cdd:cd14210   156 SIKVIDFGSScfegekvyTYIQ-SRFYR-----------APEVILGLPYDTAIDMWSLGCILAE-LYTGYPLFPG 217
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
107-302 1.03e-09

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: 60.65  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYmspENPALAVAIKTCKnCTSDSVREKFLQE--ALTMRQFDHPHIVK------------- 171
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVV---RRTGARVAVKKIR-CNAPENVELALREfwALSSIQRQHPNVIQleecvlqrdglaq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 172 -------------------LIGVITENP-----VWIIMELCTLGELRSFLQVRKYSLDL-ASLILyayQLSTALAYLESK 226
Cdd:cd13977    77 rmshgssksdlylllvetsLKGERCFDPrsacyLWFVMEFCDGGDMNEYLLSRRPDRQTnTSFML---QLSSALAFLHRN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 227 RFVHRDIAARNVLVSSND---CVKLGDFGLSRYMEDStyykASKGKLPIK--------------WMAPEsINFRRFTSAS 289
Cdd:cd13977   154 QIVHRDLKPDNILISHKRgepILKVADFGLSKVCSGS----GLNPEEPANvnkhflssacgsdfYMAPE-VWEGHYTAKA 228
                         250
                  ....*....|...
gi 1914781966 290 DVWMFGVCMWEIL 302
Cdd:cd13977   229 DIFALGIIIWAMV 241
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
109-323 1.08e-09

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: 60.79  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVH-------QGIYmspenpalavAIKTCKNCTSDSVREK--FLQEALTMRQFDHPHIVKLIGVITEN 179
Cdd:cd05601     4 EVKNVIGRGHFGEVQvvkekatGDIY----------AMKVLKKSETLAQEEVsfFEEERDIMAKANSPWITKLQYAFQDS 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 P-VWIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYME 258
Cdd:cd05601    74 EnLYLVMEYHPGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLS 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 259 DStyyKASKGKLPI---KWMAPE---SINfRRFTSASDV----WMFGVCMWEiLMHGVKPFQGVKNNDVIGRIEN 323
Cdd:cd05601   154 SD---KTVTSKMPVgtpDYIAPEvltSMN-GGSKGTYGVecdwWSLGIVAYE-MLYGKTPFTEDTVIKTYSNIMN 223
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
157-359 1.09e-09

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


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 60.27  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 157 EALTMRQF-------DHPHIVKLIGVITEN-PVWIIMELCTLGELRSFLQVRK-YSLDLASLILYAyqLSTALAYLESKR 227
Cdd:cd14180    44 EANTQREVaalrlcqSHPNIVALHEVLHDQyHTYLVMELLRGGELLDRIKKKArFSESEASQLMRS--LVSAVSFMHEAG 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 228 FVHRDIAARNVLVSS---NDCVKLGDFGLSRYMEDStyykASKGKLP---IKWMAPESINFRRFTSASDVWMFGVCMWEI 301
Cdd:cd14180   122 VVHRDLKPENILYADesdGAVLKVIDFGFARLRPQG----SRPLQTPcftLQYAAPELFSNQGYDESCDLWSLGVILYTM 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 302 LmHGVKPFQGVKNN-------DVIGRIENGErlpmppncpptlYSLMTKCW---------------AYDPSRRPRFTELK 359
Cdd:cd14180   198 L-SGQVPFQSKRGKmfhnhaaDIMHKIKEGD------------FSLEGEAWkgvseeakdlvrgllTVDPAKRLKLSELR 264
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
165-325 1.19e-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: 60.11  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 165 DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSS 242
Cdd:cd05609    58 ENPFVVSMYCSFeTKRHLCMVMEYVEGGDCATLLKnIGPLPVDMARM--YFAETVLALEYLHSYGIVHRDLKPDNLLITS 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 243 NDCVKLGDFGLSR-------------YMEDSTYYKASKGKL--PiKWMAPESINFRRFTSASDVWMFGVCMWEILmHGVK 307
Cdd:cd05609   136 MGHIKLTDFGLSKiglmslttnlyegHIEKDTREFLDKQVCgtP-EYIAPEVILRQGYGKPVDWWAMGIILYEFL-VGCV 213
                         170
                  ....*....|....*...
gi 1914781966 308 PFQGVKNNDVIGRIENGE 325
Cdd:cd05609   214 PFFGDTPEELFGQVISDE 231
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
86-325 1.20e-09

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: 60.42  E-value: 1.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  86 IIDEEDTYTMPSTRDYEIQRErielgrcIGEGQFGDVHQGIYMSPEnpaLAVAIKTCKNCTSDSVREKflqeALTMRQFD 165
Cdd:cd14176     6 IVQQLHRNSIQFTDGYEVKED-------IGVGSYSVCKRCIHKATN---MEFAVKIIDKSKRDPTEEI----EILLRYGQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 166 HPHIVKLIGVITENP-VWIIMELCTLGEL-RSFLQVRKYSLDLASLILYAyqLSTALAYLESKRFVHRDIAARNVLV--- 240
Cdd:cd14176    72 HPNIITLKDVYDDGKyVYVVTELMKGGELlDKILRQKFFSEREASAVLFT--ITKTVEYLHAQGVVHRDLKPSNILYvde 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 241 SSN-DCVKLGDFGLSRYMedstyyKASKGKL-----PIKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKN 314
Cdd:cd14176   150 SGNpESIRICDFGFAKQL------RAENGLLmtpcyTANFVAPEVLERQGYDAACDIWSLGVLLYTMLT-GYTPFANGPD 222
                         250
                  ....*....|....
gi 1914781966 315 N---DVIGRIENGE 325
Cdd:cd14176   223 DtpeEILARIGSGK 236
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
107-339 1.31e-09

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: 60.01  E-value: 1.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTCKNCT-SDSVREKFLQEALTMRQFDHPHIVKLIGVITE-NPVWII 184
Cdd:cd07848     2 KFEVLGVVGEGAYGVVLKCRHKETKE---IVAIKKFKDSEeNEEVKETTLRELKMLRTLKQENIVELKEAFRRrGKLYLV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRsFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYK 264
Cdd:cd07848    79 FEYVEKNMLE-LLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNAN 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1914781966 265 ASKgKLPIKWM-APESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIEN--GerlPMPPNCPPTLYS 339
Cdd:cd07848   158 YTE-YVATRWYrSPELLLGAPYGKAVDMWSVG-CILGELSDGQPLFPGESEIDQLFTIQKvlG---PLPAEQMKLFYS 230
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
156-358 1.65e-09

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


Pssm-ID: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 60.10  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 156 QEALTMRQFDHPHIVKLIGVITENP-------VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRF 228
Cdd:cd07874    65 RELVLMKCVNHKNIISLLNVFTPQKsleefqdVYLVMELMD----ANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKp 308
Cdd:cd07874   141 IHRDLKPSNIVVKSDCTLKILDFGLARTA--GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKIL- 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 309 FQGVKNNDVIGRIEngERLPMPpnCPPTLYSLMTKCWAYdPSRRPRFTEL 358
Cdd:cd07874   218 FPGRDYIDQWNKVI--EQLGTP--CPEFMKKLQPTVRNY-VENRPKYAGL 262
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
156-355 1.71e-09

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: 60.44  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 156 QEALTMRQFDHPHIVKLIGVITENP-------VWIIMELCTlgelRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRF 228
Cdd:cd07875    72 RELVLMKCVNHKNIIGLLNVFTPQKsleefqdVYIVMELMD----ANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 229 VHRDIAARNVLVSSNDCVKLGDFGLSRYMedSTYYKASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVKp 308
Cdd:cd07875   148 IHRDLKPSNIVVKSDCTLKILDFGLARTA--GTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVL- 224
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1914781966 309 FQGVKNNDVIGRIEngERLPMPpnCPPTLYSLMTKCWAYdPSRRPRF 355
Cdd:cd07875   225 FPGTDHIDQWNKVI--EQLGTP--CPEFMKKLQPTVRTY-VENRPKY 266
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
101-325 1.77e-09

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: 59.13  E-value: 1.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 101 YEIQRErielgrcIGEGQFGDV----HQGIYMSPENPALAVAIKTcknctsdsvREKFLQEALTMRQFDHPHIVKLIGVI 176
Cdd:cd14107     4 YEVKEE-------IGRGTFGFVkrvtHKGNGECCAAKFIPLRSST---------RARAFQERDILARLSHRRLTCLLDQF 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 -TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSS--NDCVKLGDFGL 253
Cdd:cd14107    68 eTRKTLILILELCSSEELLDRL-FLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSptREDIKICDFGF 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 254 SRYMeDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMHGvKPFQGVKNNDVIGRIENGE 325
Cdd:cd14107   147 AQEI-TPSEHQFSKYGSP-EFVAPEIVHQEPVSAATDIWALGVIAYLSLTCH-SPFAGENDRATLLNVAEGV 215
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
108-301 1.78e-09

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 59.32  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 108 IELGRcigeGQFGDVHQGIymspeNPALAVAIKTCK---NCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENP---- 180
Cdd:cd14032     7 IELGR----GSFKTVYKGL-----DTETWVEVAWCElqdRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWESCAkgkr 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 -VWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSS-NDCVKLGDFGLSRy 256
Cdd:cd14032    78 cIVLVTELMTSGTLKTYLK-RFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKIGDLGLAT- 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1914781966 257 MEDSTYYKASKGKlpIKWMAPESINfRRFTSASDVWMFGVCMWEI 301
Cdd:cd14032   156 LKRASFAKSVIGT--PEFMAPEMYE-EHYDESVDVYAFGMCMLEM 197
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
191-352 1.90e-09

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


Pssm-ID: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 59.64  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLQVRKYSLDLASLiLYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY-MEDSTYYKASKGK 269
Cdd:cd05575    81 GELFFHLQRERHFPEPRAR-FYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKEgIEPSDTTSTFCGT 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 270 lPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRIENgERLPMPPNCPPTLYSLMTKCWAYDP 349
Cdd:cd05575   160 -P-EYLAPEVLRKQPYDRTVDWWCLGAVLYE-MLYGLPPFYSRDTAEMYDNILH-KPLRLRTNVSPSARDLLEGLLQKDR 235

                  ...
gi 1914781966 350 SRR 352
Cdd:cd05575   236 TKR 238
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
145-358 1.94e-09

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 59.23  E-value: 1.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 145 CTSDSVREKFLQEALTMRQFDHPHIVKLI--GVITENP----VWIIMELCTLGELRSFLQVRK-----YSLDLASLILYa 213
Cdd:cd13986    35 CHSKEDVKEAMREIENYRLFNHPNILRLLdsQIVKEAGgkkeVYLLLPYYKRGSLQDEIERRLvkgtfFPEDRILHIFL- 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 214 yQLSTALAYL---ESKRFVHRDIAARNVLVSSNDCVKLGDFG-------------LSRYMEDSTyykASKGKLPikWMAP 277
Cdd:cd13986   114 -GICRGLKAMhepELVPYAHRDIKPGNVLLSEDDEPILMDLGsmnparieiegrrEALALQDWA---AEHCTMP--YRAP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 278 ESINFRR---FTSASDVWMFGvCMWEILMHGVKPFQGV--KNNDVIGRIENGE-RLPMPPNCPPTLYSLMTKCWAYDPSR 351
Cdd:cd13986   188 ELFDVKShctIDEKTDIWSLG-CTLYALMYGESPFERIfqKGDSLALAVLSGNySFPDNSRYSEELHQLVKSMLVVNPAE 266

                  ....*..
gi 1914781966 352 RPRFTEL 358
Cdd:cd13986   267 RPSIDDL 273
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
111-311 3.14e-09

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


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 58.97  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 111 GRCIGEGQFGDVHQGI--YMSPEnpalaVAIKTCKNCTSDSvREKFLQEALTMRQFD-HPHIVKLIGVITENPV-WIIME 186
Cdd:cd14090     7 GELLGEGAYASVQTCInlYTGKE-----YAVKIIEKHPGHS-RSRVFREVETLHQCQgHPNILQLIEYFEDDERfYLVFE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 LCTLGELRSFLQVRK-YSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDC---VKLGDFGLSRYMEDSTY 262
Cdd:cd14090    81 KMRGGPLLSHIEKRVhFTEQEASLVVR--DIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLGSGIKLSST 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 263 YkASKGKLP--------IKWMAPESINFRRFTSAS-----DVWMFGVCMWeILMHGVKPFQG 311
Cdd:cd14090   159 S-MTPVTTPelltpvgsAEYMAPEVVDAFVGEALSydkrcDLWSLGVILY-IMLCGYPPFYG 218
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
210-321 3.93e-09

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: 58.52  E-value: 3.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 210 ILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSAS 289
Cdd:cd05605   105 VFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGRVGT--VGYMAPEVVKNERYTFSP 182
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1914781966 290 DVWMFGVCMWEILMhGVKPFQG----VKNNDVIGRI 321
Cdd:cd05605   183 DWWGLGCLIYEMIE-GQAPFRArkekVKREEVDRRV 217
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
112-328 4.32e-09

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: 58.85  E-value: 4.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 112 RCI---GEGQFGDVHQGIYMSPENpalAVAIKTCKNC---TSDSVR----EKFLQEALT-MRqfdHPHIVKLIGVI-TEN 179
Cdd:cd05589     2 RCIavlGRGHFGKVLLAEYKPTGE---LFAIKALKKGdiiARDEVEslmcEKRIFETVNsAR---HPFLVNLFACFqTPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 180 PVWIIMELCTLGELRSFLQVRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymED 259
Cdd:cd05589    76 HVCFVMEYAAGGDLMMHIHEDVFSEPRA--VFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCK--EG 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 260 -------STYYKASKgklpikWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRIENGE-RLP 328
Cdd:cd05589   152 mgfgdrtSTFCGTPE------FLAPEVLTDTSYTRAVDWWGLGVLIYEMLV-GESPFPGDDEEEVFDSIVNDEvRYP 221
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
177-415 4.46e-09

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: 58.56  E-value: 4.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQ-VRKYSLDLAslILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSR 255
Cdd:cd05587    68 TMDRLYFVMEYVNGGDLMYHIQqVGKFKEPVA--VFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 256 --YMEDSTyYKASKGKlPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQGVKNNDVIGRI-ENGERLP--MP 330
Cdd:cd05587   146 egIFGGKT-TRTFCGT-P-DYIAPEIIAYQPYGKSVDWWAYGVLLYEMLA-GQPPFDGEDEDELFQSImEHNVSYPksLS 221
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 331 PNCPPTLYSLMTKcwayDPSRRPRFTelkaqlstileeEKAQQEERMRMESRRqatVSWDSGGSDEAPPkPSRPGYPSPR 410
Cdd:cd05587   222 KEAVSICKGLLTK----HPAKRLGCG------------PTGERDIKEHPFFRR---IDWEKLERREIQP-PFKPKIKSPR 281

                  ....*
gi 1914781966 411 SSEGF 415
Cdd:cd05587   282 DAENF 286
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
155-323 5.24e-09

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


Pssm-ID: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 57.60  E-value: 5.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 155 LQEALTMRQFDHPHIVKLIGVITE-NPVWIIMELCTLGELRSFLqvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDI 233
Cdd:cd14108    46 RRELALLAELDHKSIVRFHDAFEKrRVVIIVTELCHEELLERIT--KRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 234 AARNVLV--SSNDCVKLGDFGLSRYME-DSTYYkaSKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPFQ 310
Cdd:cd14108   124 KPENLLMadQKTDQVRICDFGNAQELTpNEPQY--CKYGTP-EFVAPEIVNQSPVSKVTDIWPVGVIAY-LCLTGISPFV 199
                         170
                  ....*....|...
gi 1914781966 311 GVKNNDVIGRIEN 323
Cdd:cd14108   200 GENDRTTLMNIRN 212
pknD PRK13184
serine/threonine-protein kinase PknD;
106-367 5.67e-09

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 59.78  E-value: 5.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGiymspENPALA--VAIKTCKNCTSDS--VREKFLQEALTMRQFDHPHIVKLIGVITE-NP 180
Cdd:PRK13184    2 QRYDIIRLIGKGGMGEVYLA-----YDPVCSrrVALKKIREDLSENplLKKRFLREAKIAADLIHPGIVPVYSICSDgDP 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIM---ELCTLGE-LRSFLQVRKYSLDLA------SLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGD 250
Cdd:PRK13184   77 VYYTMpyiEGYTLKSlLKSVWQKESLSKELAektsvgAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 251 FGLSRY--------------MEDSTYYKASK-GKL--PIKWMAPESINFRRFTSASDVWMFGVCMWEILMHGVkPFQGVK 313
Cdd:PRK13184  157 WGAAIFkkleeedlldidvdERNICYSSMTIpGKIvgTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSF-PYRRKK 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1914781966 314 nndviGR-IENGERLPMPP------NCPPTLYSLMTKCWAYDPSRRPR-FTELKAQLSTILE 367
Cdd:PRK13184  236 -----GRkISYRDVILSPIevapyrEIPPFLSQIAMKALAVDPAERYSsVQELKQDLEPHLQ 292
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
210-325 6.16e-09

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: 58.06  E-value: 6.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 210 ILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlpIKWMAPESINFRRFTSAS 289
Cdd:cd05632   107 LFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGT--VGYMAPEVLNNQRYTLSP 184
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1914781966 290 DVWMFGVCMWEiLMHGVKPFQG----VKNNDVIGRIENGE 325
Cdd:cd05632   185 DYWGLGCLIYE-MIEGQSPFRGrkekVKREEVDRRVLETE 223
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
138-302 8.75e-09

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: 57.41  E-value: 8.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 138 AIKT----CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITEN--PVWIIMELC--TLGELrsfLQVRKYSLD---L 206
Cdd:cd14001    32 AVKKinskCDKGQRSLYQERLKEEAKILKSLNHPNIVGFRAFTKSEdgSLCLAMEYGgkSLNDL---IEERYEAGLgpfP 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 207 ASLIL-YAYQLSTALAYLES-KRFVHRDIAARNVLVSSN-DCVKLGDFGLS-RYMEDSTYYKASK----GKLPikWMAPE 278
Cdd:cd14001   109 AATILkVALSIARALEYLHNeKKILHGDIKSGNVLIKGDfESVKLCDFGVSlPLTENLEVDSDPKaqyvGTEP--WKAKE 186
                         170       180
                  ....*....|....*....|....*
gi 1914781966 279 SINFRR-FTSASDVWMFGVCMWEIL 302
Cdd:cd14001   187 ALEEGGvITDKADIFAYGLVLWEMM 211
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
161-321 8.97e-09

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: 57.69  E-value: 8.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 161 MRQFDHPHIVKLIGVITENP-------VWIIMELctLG-ELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRD 232
Cdd:cd07851    68 LKHMKHENVIGLLDVFTPASsledfqdVYLVTHL--MGaDLNNIVKCQKLSDDHIQFLVY--QILRGLKYIHSAGIIHRD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 233 IAARNVLVSSNDCVKLGDFGLSRYMEDS-TYYKASkgklpiKW-MAPESI-NFRRFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd07851   144 LKPSNLAVNEDCELKILDFGLARHTDDEmTGYVAT------RWyRAPEIMlNWMHYNQTVDIWSVGCIMAELLT-GKTLF 216
                         170
                  ....*....|..
gi 1914781966 310 QGVKNNDVIGRI 321
Cdd:cd07851   217 PGSDHIDQLKRI 228
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
102-301 9.11e-09

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 57.75  E-value: 9.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 102 EIQRERIELGRCIGEGQFGDVHQgIYMSPENpaLAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENP 180
Cdd:cd06649     1 ELKDDDFERISELGAGNGGVVTK-VQHKPSG--LIMARKLIHLEIKPAIRNQIIRELQVLHECNSPYIVGFYGAFySDGE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 VWIIMELCTLGELRsflQVRKYSLDLASLILYAYQLST--ALAYLESK-RFVHRDIAARNVLVSSNDCVKLGDFGLSRYM 257
Cdd:cd06649    78 ISICMEHMDGGSLD---QVLKEAKRIPEEILGKVSIAVlrGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSGQL 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1914781966 258 EDSTyykASKGKLPIKWMAPESINFRRFTSASDVWMFGVCMWEI 301
Cdd:cd06649   155 IDSM---ANSFVGTRSYMSPERLQGTHYSVQSDIWSMGLSLVEL 195
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
215-311 1.04e-08

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: 56.87  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 215 QLSTALAYLESKRFVHRDIAARNVLVSSnDC----VKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRRFTSASD 290
Cdd:cd14197   119 QILEGVSFLHNNNVVHLDLKPQNILLTS-ESplgdIKIVDFGLSRILKNSEELREIMGT-P-EYVAPEILSYEPISTATD 195
                          90       100
                  ....*....|....*....|.
gi 1914781966 291 VWMFGVCMWeILMHGVKPFQG 311
Cdd:cd14197   196 MWSIGVLAY-VMLTGISPFLG 215
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
148-309 1.19e-08

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: 56.90  E-value: 1.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 148 DSVREKFLQEALTMRQF-DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLES 225
Cdd:cd14181    56 EEVRSSTLKEIHILRQVsGHPSIITLIDSYeSSTFIFLVFDLMRRGELFDYL-TEKVTLSEKETRSIMRSLLEAVSYLHA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 226 KRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESINFRR------FTSASDVWMFGVCMW 299
Cdd:cd14181   135 NNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCGT-P-GYLAPEILKCSMdethpgYGKEVDLWACGVILF 212
                         170
                  ....*....|
gi 1914781966 300 EILMhGVKPF 309
Cdd:cd14181   213 TLLA-GSPPF 221
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
161-316 1.31e-08

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 56.79  E-value: 1.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 161 MRqfDHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVL 239
Cdd:PHA03390   65 MK--DNPNFIKLYYSVtTLKGHVLIMDYIKDGDLFDLLK-KEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 240 VS-SNDCVKLGDFGLSRY-----MEDST--YYkaskgklpikwmAPESINFRRFTSASDVWMFGVCMWEILMhGVKPFQg 311
Cdd:PHA03390  142 YDrAKDRIYLCDYGLCKIigtpsCYDGTldYF------------SPEKIKGHNYDVSFDWWAVGVLTYELLT-GKHPFK- 207

                  ....*
gi 1914781966 312 vKNND 316
Cdd:PHA03390  208 -EDED 211
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
115-332 1.42e-08

Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 57.26  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 115 GEGQFGDVHQGIymSPENPALaVAIKTCKNctsdsvREKFLQEA------LTM--RQFD---HPHIVKLIG-VITENPVW 182
Cdd:cd14212     8 GQGTFGQVVKCQ--DLKTNKL-VAVKVLKN------KPAYFRQAmleiaiLTLlnTKYDpedKHHIVRLLDhFMHHGHLC 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 IIMELctLG-ELRSFLQVRKY-SLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGlSRYME 258
Cdd:cd14212    79 IVFEL--LGvNLYELLKQNQFrGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSpeIKLIDFG-SACFE 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 259 DSTYYKASKGKLpikWMAPESINFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKNNDVIGRIEngERLPMPPN 332
Cdd:cd14212   156 NYTLYTYIQSRF---YRSPEVLLGLPYSTAIDMWSLG-CIAAELFLGLPLFPGNSEYNQLSRII--EMLGMPPD 223
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
114-301 2.26e-08

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: 56.54  E-value: 2.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIMELCTlGE 192
Cdd:cd07872    14 LGEGTYATVFKGRSKLTEN---LVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVhTDKSLTLVFEYLD-KD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 193 LRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKASKGKLPI 272
Cdd:cd07872    90 LKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLAR--AKSVPTKTYSNEVVT 167
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1914781966 273 KWMAPESI--NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd07872   168 LWYRPPDVllGSSEYSTQIDMWGVGCIFFEM 198
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
105-311 2.36e-08

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: 56.50  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITE----- 178
Cdd:cd07880    14 PDRYRDLKQVGSGAYGTV---CSALDRRTGAKVAIKKLyRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPdlsld 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 --NPVWIIMEL--CTLGELrsfLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS 254
Cdd:cd07880    91 rfHDFYLVMPFmgTDLGKL---MKHEKLSEDRIQFLVY--QMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLA 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 255 RYMEDSTyykasKGKLPIKWM-APESI-NFRRFTSASDVWMFGVCMWEILMhGVKPFQG 311
Cdd:cd07880   166 RQTDSEM-----TGYVVTRWYrAPEVIlNWMHYTQTVDIWSVGCIMAEMLT-GKPLFKG 218
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
114-318 2.73e-08

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 56.08  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpaLAVAIKTCKNctSDSVREKFLQEALTMRQF------DHPHIVKLIGVIT-ENPVWIIME 186
Cdd:cd14135     8 LGKGVFSNVVRARDLARGN--QEVAIKIIRN--NELMHKAGLKELEILKKLndadpdDKKHCIRLLRHFEhKNHLCLVFE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 187 lCTLGELRSFLQV--RKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCV-KLGDFGLSRYMEDS--T 261
Cdd:cd14135    84 -SLSMNLREVLKKygKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNTlKLCDFGSASDIGENeiT 162
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 262 YYKASKgklpiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVI 318
Cdd:cd14135   163 PYLVSR-----FYRAPEIILGLPYDYPIDMWSVGCTLYE-LYTGKILFPGKTNNHML 213
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
137-357 2.74e-08

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: 56.43  E-value: 2.74e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 137 VAIKTC-KNCTSDSVREKFLQEALTMRQFDHPHIVKL--IGVITENPVWIIMELctLG-ELRSFLQVRKYSLDLASLILY 212
Cdd:cd07856    38 VAVKKImKPFSTPVLAKRTYRELKLLKHLRHENIISLsdIFISPLEDIYFVTEL--LGtDLHRLLTSRPLEKQFIQYFLY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 213 ayQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDS-TYYKASKgklpiKWMAPE-SINFRRFTSASD 290
Cdd:cd07856   116 --QILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQmTGYVSTR-----YYRAPEiMLTWQKYDVEVD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 291 VWMFGvCMWEILMHGVKPFQGvKNN----------------DVIGRI--ENG----------ERLPMP---PNCPPTLYS 339
Cdd:cd07856   189 IWSAG-CIFAEMLEGKPLFPG-KDHvnqfsiitellgtppdDVINTIcsENTlrfvqslpkrERVPFSekfKNADPDAID 266
                         250
                  ....*....|....*...
gi 1914781966 340 LMTKCWAYDPSRRPRFTE 357
Cdd:cd07856   267 LLEKMLVFDPKKRISAAE 284
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
94-309 3.02e-08

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: 56.55  E-value: 3.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  94 TMPSTRDYEIQRERIELGRCIGEGQFGDVhQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLI 173
Cdd:cd05622    61 TINKIRDLRMKAEDYEVVKVIGRGAFGEV-QLVRHKSTRKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLF 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 174 GVITENP-VWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFG 252
Cdd:cd05622   140 YAFQDDRyLYMVMEYMPGGDLVNLMS--NYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFG 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 253 LSRYMEDSTYYKASKGKLPIKWMAPESINFR----RFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd05622   218 TCMKMNKEGMVRCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLYEMLV-GDTPF 277
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
107-367 3.43e-08

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


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 55.59  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGiymSPENPALAVAIKTCKNcTSDSVREKFLQEALTMRQFD-HPHIVKLIGVITENP----- 180
Cdd:cd14036     1 KLRIKRVIAEGGFAFVYEA---QDVGTGKEYALKRLLS-NEEEKNKAIIQEINFMKKLSgHPNIVQFCSAASIGKeesdq 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 181 ----VWIIMELCTLGELRSFLQVR-KYSLDLASLILYAYQLSTALAYLESKR--FVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd14036    77 gqaeYLLLTELCKGQLVDFVKKVEaPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGK------------LPIkWMAPESINFRR---FTSASDVWMFGvCMWEILMHGVKPFQ-GVKNndv 317
Cdd:cd14036   157 ATTEAHYPDYSWSAQKrslvedeitrntTPM-YRTPEMIDLYSnypIGEKQDIWALG-CILYLLCFRKHPFEdGAKL--- 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 318 igRIENGeRLPMPPNcpPTLYS----LMTKCWAYDPSRRPRFTELKAQLSTILE 367
Cdd:cd14036   232 --RIINA-KYTIPPN--DTQYTvfhdLIRSTLKVNPEERLSITEIVEQLQELAA 280
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
114-311 3.56e-08

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: 56.06  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIymsPENPALAVAIKT-CKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVITENPV-------WIIM 185
Cdd:cd07879    23 VGSGAYGSVCSAI---DKRTGEKVAIKKlSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSgdefqdfYLVM 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELctlgeLRSFLQ-VRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTyyk 264
Cdd:cd07879   100 PY-----MQTDLQkIMGHPLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEM--- 171
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 265 asKGKLPIKWM-APESI-NFRRFTSASDVWMFGVCMWEILmHGVKPFQG 311
Cdd:cd07879   172 --TGYVVTRWYrAPEVIlNWMHYNQTVDIWSVGCIMAEML-TGKTLFKG 217
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
109-358 4.52e-08

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: 55.00  E-value: 4.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENpalAVAIKTC-KNCTSDSVREKFL-QEALTMRQFDHPHIVKLIGVI--TENPVWII 184
Cdd:cd14163     3 QLGKTIGEGTYSKVKEAFSKKHQR---KVAIKIIdKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLesADGKIYLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 185 MELCTLGELRSFLQVRKYSLDLASLILYAyQLSTALAYLESKRFVHRDIAARNVLVSSNDcVKLGDFGLSRYMEDSTYYK 264
Cdd:cd14163    80 MELAEDGDVFDCVLHGGPLPEHRAKALFR-QLVEAIRYCHGCGVAHRDLKCENALLQGFT-LKLTDFGFAKQLPKGGREL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 265 ASKGKLPIKWMAPESIN-FRRFTSASDVWMFGVCMWEILMHGVkPFQGVKNNDVIGRIENGERLPMPPNCPPTLYSLMTK 343
Cdd:cd14163   158 SQTFCGSTAYAAPEVLQgVPHDSRKGDIWSMGVVLYVMLCAQL-PFDDTDIPKMLCQQQKGVSLPGHLGVSRTCQDLLKR 236
                         250
                  ....*....|....*
gi 1914781966 344 CWAYDPSRRPRFTEL 358
Cdd:cd14163   237 LLEPDMVLRPSIEEV 251
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
105-309 4.71e-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: 55.44  E-value: 4.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 105 RERIELGRCIGEGQFGDVhqgIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWI 183
Cdd:cd14168     9 KKIFEFKEVLGTGAFSEV---VLAEERATGKLFAVKCIPKKALKGKESSIENEIAVLRKIKHENIVALEDIYeSPNHLYL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQVRKY--SLDLASLIlyaYQLSTALAYLESKRFVHRDIAARNVLVSSND---CVKLGDFGLSRyME 258
Cdd:cd14168    86 VMQLVSGGELFDRIVEKGFytEKDASTLI---RQVLDAVYYLHRMGIVHRDLKPENLLYFSQDeesKIMISDFGLSK-ME 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1914781966 259 DSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14168   162 GKGDVMSTACGTP-GYVAPEVLAQKPYSKAVDCWSIGVIAY-ILLCGYPPF 210
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
215-358 5.42e-08

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


Pssm-ID: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 54.47  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 215 QLSTALAYLESKRFVHRDIAARNVLVSS-NDCVKLGDFGLSRYMEDSTYYKASKGKLpikWMAPESINFRRFTS-ASDVW 292
Cdd:cd14101   116 QVVEAVQHCHSKGVVHRDIKDENILVDLrTGDIKLIDFGSGATLKDSMYTDFDGTRV---YSPPEWILYHQYHAlPATVW 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1914781966 293 MFGVCMWEILMhGVKPFQgvKNNDVIgRIENGERLPMPPNCpptlYSLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14101   193 SLGILLYDMVC-GDIPFE--RDTDIL-KAKPSFNKRVSNDC----RSLIRSCLAYNPSDRPSLEQI 250
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
114-342 5.76e-08

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 54.57  E-value: 5.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCKNCTSDSVREkflQEALTMRQFD-HPHIVKLIGVITENPV-WIIMELC--T 189
Cdd:cd14017     8 IGGGGFGEIYKVRDVVDGE---EVAMKVESKSQPKQVLK---MEVAVLKKLQgKPHFCRLIGCGRTERYnYIVMTLLgpN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 190 LGELRSFLQVRKYSLdlASLILYAYQLSTALAYLESKRFVHRDIAARNVL--VSSNDC--VKLGDFGLSRymedstYYKA 265
Cdd:cd14017    82 LAELRRSQPRGKFSV--STTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAigRGPSDErtVYILDFGLAR------QYTN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 266 SKGKlpIKWMAPESINFR---RFTSAS-----------DVWMFGVCMWEiLMHGVKPFQGVKNNDVIG----RIENGERL 327
Cdd:cd14017   154 KDGE--VERPPRNAAGFRgtvRYASVNahrnkeqgrrdDLWSWFYMLIE-FVTGQLPWRKLKDKEEVGkmkeKIDHEELL 230
                         250
                  ....*....|....*
gi 1914781966 328 pmpPNCPPTLYSLMT 342
Cdd:cd14017   231 ---KGLPKEFFQILK 242
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
107-359 6.75e-08

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: 54.39  E-value: 6.75e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHqgiYMSPENPALAVAIKTCKNctSDSVREKFLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 185
Cdd:cd14662     1 RYELVKDIGSGNFGVAR---LMRNKETKELVAVKYIER--GLKIDENVQREIINHRSLRHPNIIRFKEVVlTPTHLAIVM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTLGEL-RSFLQVRKYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRYMEDSTY 262
Cdd:cd14662    76 EYAAGGELfERICNAGRFSEDEARY--FFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAprLKICDFGYSKSSVLHSQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 263 YKASKGKlPiKWMAPESINFRRFT-SASDVWMFGVCMWEILMhGVKPFQGVKN----NDVIGRIENGE-RLPMPPNCPPT 336
Cdd:cd14662   154 PKSTVGT-P-AYIAPEVLSRKEYDgKVADVWSCGVTLYVMLV-GAYPFEDPDDpknfRKTIQRIMSVQyKIPDYVRVSQD 230
                         250       260
                  ....*....|....*....|...
gi 1914781966 337 LYSLMTKCWAYDPSRRPRFTELK 359
Cdd:cd14662   231 CRHLLSRIFVANPAKRITIPEIK 253
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
114-309 9.82e-08

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: 53.81  E-value: 9.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENPalaVAIKTCKNCTSDsvREKFLQEALTMRQFDHPHIVKLIGVItENPV--WIIMELCTLG 191
Cdd:cd14115     1 IGRGRFSIVKKCLHKATRKD---VAVKFVSKKMKK--KEQAAHEAALLQHLQHPQYITLHDTY-ESPTsyILVLELMDDG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 192 ELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---SNDCVKLGDFGLSryMEDSTYYKASKG 268
Cdd:cd14115    75 RLLDYL-MNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDlriPVPRVKLIDLEDA--VQISGHRHVHHL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1914781966 269 KLPIKWMAPESINFRRFTSASDVWMFGVCMWeILMHGVKPF 309
Cdd:cd14115   152 LGNPEFAAPEVIQGTPVSLATDIWSIGVLTY-VMLSGVSPF 191
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
166-301 1.03e-07

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: 54.28  E-value: 1.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 166 HPHIVKLIGV-----ITENPVWIIMELCTLGELRSFLQVRKYSLDlaSLILYAYQLSTALAYLESK----------RFVH 230
Cdd:cd14141    48 HENILQFIGAekrgtNLDVDLWLITAFHEKGSLTDYLKANVVSWN--ELCHIAQTMARGLAYLHEDipglkdghkpAIAH 125
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1914781966 231 RDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKLPI-KWMAPE----SINFRRFTSAS-DVWMFGVCMWEI 301
Cdd:cd14141   126 RDIKSKNVLLKNNLTACIADFGLALKFEAGKSAGDTHGQVGTrRYMAPEvlegAINFQRDAFLRiDMYAMGLVLWEL 202
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
104-255 1.15e-07

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 54.05  E-value: 1.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 104 QRERIELgrcIGEGQFGDVHQGiymSPENPALAVAIKTCKNCTSDS-VREKFLQEALTMRQFDHPHIVKLIGVI-TENPV 181
Cdd:PLN00009    3 QYEKVEK---IGEGTYGVVYKA---RDRVTNETIALKKIRLEQEDEgVPSTAIREISLLKEMQHGNIVRLQDVVhSEKRL 76
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1914781966 182 WIIMELCTLGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVS-SNDCVKLGDFGLSR 255
Cdd:PLN00009   77 YLVFEYLDLDLKKHMDSSPDFAKNPRLIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDrRTNALKLADFGLAR 151
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
165-316 1.17e-07

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: 54.65  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 165 DHPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 243
Cdd:cd05618    79 NHPFLVGLHSCFqTESRLFFVIEYVNGGDLMFHMQ-RQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE 157
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1914781966 244 DCVKLGDFGLSRYMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNND 316
Cdd:cd05618   158 GHIKLTDYGMCKEGLRPGDTTSTFCGTP-NYIAPEILRGEDYGFSVDWWALGVLMFE-MMAGRSPFDIVGSSD 228
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
166-398 1.25e-07

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 54.04  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 166 HPHIVKLIGVI-TENPVWIIMELCTLGELRSFLQ-VRKYslDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSN 243
Cdd:cd05591    55 HPFLTALHSCFqTKDRLFFVMEYVNGGDLMFQIQrARKF--DEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 244 DCVKLGDFGLSR--YMEDSTyyKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIGRI 321
Cdd:cd05591   133 GHCKLADFGMCKegILNGKT--TTTFCGTP-DYIAPEILQELEYGPSVDWWALGVLMYE-MMAGQPPFEADNEDDLFESI 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 322 ENGERL-P--MPPNCPPTLYSLMTKcwayDPSRR----------------PRFTELKAQLstiLEEEKAQQEERMRMESR 382
Cdd:cd05591   209 LHDDVLyPvwLSKEAVSILKAFMTK----NPAKRlgcvasqggedairqhPFFREIDWEA---LEQRKVKPPFKPKIKTK 281
                         250
                  ....*....|....*.
gi 1914781966 383 RQATvSWDSGGSDEAP 398
Cdd:cd05591   282 RDAN-NFDQDFTKEEP 296
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
109-358 1.49e-07

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 53.43  E-value: 1.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 109 ELGRCIGEGQFGDVHQGIYMSPENPalaVAIKtckNCTSDSVRE--------KFLQEALTMRQFDHPH--IVKLIGVItE 178
Cdd:cd14100     3 QVGPLLGSGGFGSVYSGIRVADGAP---VAIK---HVEKDRVSEwgelpngtRVPMEIVLLKKVGSGFrgVIRLLDWF-E 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 179 NP---VWIIMELCTLGELRSFLQVR-KYSLDLASLilYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDC-VKLGDFGL 253
Cdd:cd14100    76 RPdsfVLVLERPEPVQDLFDFITERgALPEELARS--FFRQVLEAVRHCHNCGVLHRDIKDENILIDLNTGeLKLIDFGS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLpikWMAPESINFRRFTSAS-DVWMFGVCMWEILMhGVKPFQgvkNNDVIGRIENGERLPMPPN 332
Cdd:cd14100   154 GALLKDTVYTDFDGTRV---YSPPEWIRFHRYHGRSaAVWSLGILLYDMVC-GDIPFE---HDEEIIRGQVFFRQRVSSE 226
                         250       260
                  ....*....|....*....|....*.
gi 1914781966 333 CPptlySLMTKCWAYDPSRRPRFTEL 358
Cdd:cd14100   227 CQ----HLIKWCLALRPSDRPSFEDI 248
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
177-360 1.64e-07

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: 53.87  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLQvRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRY 256
Cdd:cd05617    87 TTSRLFLVIEYVNGGDLMFHMQ-RQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKE 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 257 MEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEiLMHGVKPFQGVKNNDVIgriengerlpmppNCPPT 336
Cdd:cd05617   166 GLGPGDTTSTFCGTP-NYIAPEILRGEEYGFSVDWWALGVLMFE-MMAGRSPFDIITDNPDM-------------NTEDY 230
                         170       180
                  ....*....|....*....|....
gi 1914781966 337 LYSLMTKcwayDPSRRPRFTELKA 360
Cdd:cd05617   231 LFQVILE----KPIRIPRFLSVKA 250
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
117-302 2.40e-07

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 53.11  E-value: 2.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 117 GQFGDVHQGIYMspeNPALAVAIKTCKNCTS-DSVREKFLQEALTmrqfdHPHIVKLI-----GVITENPVWIIMELCTL 190
Cdd:cd14140     6 GRFGCVWKAQLM---NEYVAVKIFPIQDKQSwQSEREIFSTPGMK-----HENLLQFIaaekrGSNLEMELWLITAFHDK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 191 GELRSFLqvRKYSLDLASLILYAYQLSTALAYLESK-----------RFVHRDIAARNVLVSSNDCVKLGDFGLSRYMED 259
Cdd:cd14140    78 GSLTDYL--KGNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEP 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1914781966 260 STYYKASKGKLPI-KWMAPE----SINFRRFTSAS-DVWMFGVCMWEIL 302
Cdd:cd14140   156 GKPPGDTHGQVGTrRYMAPEvlegAINFQRDSFLRiDMYAMGLVLWELV 204
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
212-334 2.57e-07

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: 53.12  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 212 YAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLS-RYMEDSTYYKASKGKLPiKWMAPESINFR-----RF 285
Cdd:cd05597   107 YLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFGSClKLREDGTVQSSVAVGTP-DYISPEILQAMedgkgRY 185
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1914781966 286 TSASDVWMFGVCMWEILmHGVKPFQGVKNNDVIGRIEN-GERLPMPPNCP 334
Cdd:cd05597   186 GPECDWWSLGVCMYEML-YGETPFYAESLVETYGKIMNhKEHFSFPDDED 234
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
107-267 2.61e-07

Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. The delta and epsilon isoforms of CK1 play important roles in circadian rhythm and cell growth. They phosphorylate PERIOD proteins (PER1-3), which are circadian clock proteins that fulfill negative regulatory functions. PER phosphorylation leads to its degradation. However, CRY proteins form a complex with PER and CK1delta/epsilon that protects PER from degradation and leads to nuclear accummulation of the complex, which inhibits BMAL1-CLOCK dependent transcription activation. CK1delta/epsilon also phosphorylate the tumor suppressor p53 and the cellular oncogene Mdm2, which are key regulators of cell growth, genome integrity, and the development of cancer. This subfamily also includes the CK1 fungal proteins Saccharomyces cerevisiae HRR25 and Schizosaccharomyces pombe HHP1. These fungal proteins are involved in DNA repair. The CK1 delta/epsilon subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 52.76  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 107 RIELGRCIGEGQFGDVHQGIYMSPENPalaVAIKTcknctsDSVREKFLQEALTMRqfdhphIVKLI--GVITENPVW-- 182
Cdd:cd14125     1 KYRLGRKIGSGSFGDIYLGTNIQTGEE---VAIKL------ESVKTKHPQLLYESK------LYKILqgGVGIPNVRWyg 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 183 -------IIMELC--TLGELRSFLQvRKYSLDlaSLILYAYQLSTALAYLESKRFVHRDIAARNVLVS---SNDCVKLGD 250
Cdd:cd14125    66 vegdynvMVMDLLgpSLEDLFNFCS-RKFSLK--TVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMGlgkKGNLVYIID 142
                         170       180
                  ....*....|....*....|..
gi 1914781966 251 FGLS-RYMEDSTY----YKASK 267
Cdd:cd14125   143 FGLAkKYRDPRTHqhipYRENK 164
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
128-352 3.14e-07

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 52.63  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 128 MSPENPALAVAIKTCKNCTSDSVREK-FLQEALTMRQFD-HPHIVKLIGVITENPVWIIMELCTLGELrsfLQVRKYSLD 205
Cdd:cd14020    23 RGADQPTSALKEFQLDHQGSQESGDYgFAKERAALEQLQgHRNIVTLYGVFTNHYSANVPSRCLLLEL---LDVSVSELL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 206 LAS--------LILY-AYQLSTALAYLESKRFVHRDIAARNVLVSSND-CVKLGDFGLS--RYMEDSTY-----YKASKG 268
Cdd:cd14020   100 LRSsnqgcsmwMIQHcARDVLEALAFLHHEGYVHADLKPRNILWSAEDeCFKLIDFGLSfkEGNQDVKYiqtdgYRAPEA 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 269 KLPIKWMAPESINFRRFTSASDVWMFGVCMWEI-----LMHGVKPfQGVKNND--VIGRIENGERLPMPPNCPPTLYSLM 341
Cdd:cd14020   180 ELQNCLAQAGLQSETECTSAVDLWSLGIVLLEMfsgmkLKHTVRS-QEWKDNSsaIIDHIFASNAVVNPAIPAYHLRDLI 258
                         250
                  ....*....|.
gi 1914781966 342 TKCWAYDPSRR 352
Cdd:cd14020   259 KSMLHNDPGKR 269
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
177-355 3.21e-07

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


Pssm-ID: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 52.58  E-value: 3.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 177 TENPVWIIMELCTLGELRSFLqvrkYSLDLAS-------LILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLG 249
Cdd:cd05608    72 TKTDLCLVMTIMNGGDLRYHI----YNVDEENpgfqeprACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRIS 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 250 DFGLSRYMEDSTYYKASKGKLPiKWMAPESINFRRFTSASDVWMFGVCMWEILMhGVKPF----QGVKNNDVIGRIENgE 325
Cdd:cd05608   148 DLGLAVELKDGQTKTKGYAGTP-GFMAPELLLGEEYDYSVDYFTLGVTLYEMIA-ARGPFrargEKVENKELKQRILN-D 224
                         170       180       190
                  ....*....|....*....|....*....|
gi 1914781966 326 RLPMPPNCPPTLYSLMTKCWAYDPSRRPRF 355
Cdd:cd05608   225 SVTYSEKFSPASKSICEALLAKDPEKRLGF 254
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
95-309 3.92e-07

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: 53.08  E-value: 3.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966  95 MPSTRDYEIQRERIELGRCIGEGQFGDVhQGIYMSPENPALAVAIKTCKNCTSDSVREKFLQEALTMRQFDHPHIVKLIG 174
Cdd:cd05621    41 VNKIRELQMKAEDYDVVKVIGRGAFGEV-QLVRHKASQKVYAMKLLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLFC 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 175 VIT-ENPVWIIMELCTLGELRSFLQvrKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGL 253
Cdd:cd05621   120 AFQdDKYLYMVMEYMPGGDLVNLMS--NYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGT 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 254 SRYMEDSTYYKASKGKLPIKWMAPESINFR----RFTSASDVWMFGVCMWEILMhGVKPF 309
Cdd:cd05621   198 CMKMDETGMVHCDTAVGTPDYISPEVLKSQggdgYYGRECDWWSVGVFLFEMLV-GDTPF 256
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
114-321 3.96e-07

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: 52.38  E-value: 3.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 114 IGEGQFGDVHQGIYMSPENpalAVAIKTCK-------NCTSdsvrekfLQEALTMRQFDHPHIVKLIGVI-TENPVWIIM 185
Cdd:cd07844     8 LGEGSYATVYKGRSKLTGQ---LVALKEIRleheegaPFTA-------IREASLLKDLKHANIVTLHDIIhTKKTLTLVF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 186 ELCTlGELRSFLQVRKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSNDCVKLGDFGLSRymEDSTYYKA 265
Cdd:cd07844    78 EYLD-TDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLAR--AKSVPSKT 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1914781966 266 SKGKLPIKWMAPESI--NFRRFTSASDVWMFGvCMWEILMHGVKPFQGVKN-NDVIGRI 321
Cdd:cd07844   155 YSNEVVTLWYRPPDVllGSTEYSTSLDMWGVG-CIFYEMATGRPLFPGSTDvEDQLHKI 212
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
106-357 4.51e-07

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 51.76  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 106 ERIELGRCIGEGQFGDVHQGIYMSPENPALAVA-IKTCKNCTSDSVREkflqeALTMRQFDHPHIVKLIGVITENPV-WI 183
Cdd:cd14112     3 GRFSFGSEIFRGRFSVIVKAVDSTTETDAHCAVkIFEVSDEASEAVRE-----FESLRTLQHENVQRLIAAFKPSNFaYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 184 IMELCTLGELRSFLQVRKYSLDLASLILYayQLSTALAYLESKRFVHRDIAARNVLVSSNDC--VKLGDFGLSRymedst 261
Cdd:cd14112    78 VMEKLQEDVFTRFSSNDYYSEEQVATTVR--QILDALHYLHFKGIAHLDVQPDNIMFQSVRSwqVKLVDFGRAQ------ 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 262 yyKASK-GKLP----IKWMAPESINFR-RFTSASDVWMFGVCMWeILMHGVKPFQG-------VKNN--DVIGRIENger 326
Cdd:cd14112   150 --KVSKlGKVPvdgdTDWASPEFHNPEtPITVQSDIWGLGVLTF-CLLSGFHPFTSeyddeeeTKENviFVKCRPNL--- 223
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1914781966 327 lpMPPNCPPTLYSLMTKCWAYDPSRRPRFTE 357
Cdd:cd14112   224 --IFVEATQEALRFATWALKKSPTRRMRTDE 252
PK_STRAD_alpha cd08227
Pseudokinase domain of STE20-related kinase adapter protein alpha; The pseudokinase domain ...
145-310 4.80e-07

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: 52.25  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 145 CTSDSVreKFLQEALTMRQ-FDHPHIVKLIGV-ITENPVWIIMELCTLGELRSFLQVrkYSLDLASLILYAYQLS---TA 219
Cdd:cd08227    38 CTNEMV--TFLQGELHVSKlFNHPNIVPYRATfIADNELWVVTSFMAYGSAKDLICT--HFMDGMSELAIAYILQgvlKA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 220 LAYLESKRFVHRDIAARNVLVSSNDCVKL----GDFGLSRYMEDST----YYKASKGKLPikWMAPESI--NFRRFTSAS 289
Cdd:cd08227   114 LDYIHHMGYVHRSVKASHILISVDGKVYLsglrSNLSMINHGQRLRvvhdFPKYSVKVLP--WLSPEVLqqNLQGYDAKS 191
                         170       180
                  ....*....|....*....|.
gi 1914781966 290 DVWMFGVCMWEiLMHGVKPFQ 310
Cdd:cd08227   192 DIYSVGITACE-LANGHVPFK 211
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
150-352 4.94e-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: 4.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 150 VREKFLQEALTMRQFD-HPHIVKLIGVITENPVW-IIMELCTLGELRSFLqVRKYSLDLASLILYAYQLSTALAYLESKR 227
Cdd:cd14182    52 LREATLKEIDILRKVSgHPNIIQLKDTYETNTFFfLVFDLMKKGELFDYL-TEKVTLSEKETRKIMRALLEVICALHKLN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1914781966 228 FVHRDIAARNVLVSSNDCVKLGDFGLSRYMEDSTYYKASKGKlPiKWMAPESI------NFRRFTSASDVWMFGVCMWEI 301
Cdd:cd14182   131 IVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGEKLREVCGT-P-GYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTL 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1914781966 302 LMhGVKPFQGVKNNDVIGRIENGERLPMPP---NCPPTLYSLMTKCWAYDPSRR 352
Cdd:cd14182   209 LA-GSPPFWHRKQMLMLRMIMSGNYQFGSPewdDRSDTVKDLISRFLVVQPQKR 261
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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